eF-site ID 2v5h-ABCDEFGHIJKL PDB Code 2v5h Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Controlling the storage of nitrogen as arginine: the complex of PII and acetylglutamate kinase from Synechococcus elongatus PCC 7942 Classification TRANSCRIPTION Compound ACETYLGLUTAMATE KINASE Source Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) (GLNB_SYNP7) Sequence A:  AGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEELK EAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEPQF HNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRAVG FCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLERG YIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLILL TDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGMIP KVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIGTM IVGS B:  AGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEELK EAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEPQF HNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRAVG FCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLERG YIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLILL TDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGMIP KVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIGTM IVGSGYHEA C:  AGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEELK EAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEPQF HNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRAVG FCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLERG YIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLILL TDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGMIP KVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIGTM IVGS D:  AGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEELK EAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEPQF HNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRAVG FCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLERG YIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLILL TDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGMIP KVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIGTM IVGSGY E:  AGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEELK EAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEPQF HNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRAVG FCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLERG YIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLILL TDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGMIP KVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIGTM IVGSGY F:  IEAGAADRVRILSEALPYLQQFAGRTVVVKYGGAAMKQEE LKEAVMRDIVFLACVGMRPVVVHGGGPEINAWLGRVGIEP QFHNGLRVTDADTMEVVEMVLVGRVNKDIVSRINTTGGRA VGFCGTDGRLVLARPHDQEGIGFVGEVNSVNSEVIEPLLE RGYIPVISSVAADENGQSFNINADTVAGEIAAALNAEKLI LLTDTRGILEDPKRPESLIPRLNIPQSRELIAQGIVGGGM IPKVDCCIRSLAQGVRAAHIIDGRIPHALLLEIFTDAGIG TMIVGSG G:  MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQK GQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAA ARTGEIGDGKIFVSPVDQTIRIRTGEKNADA H:  MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQK GQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAA ARTGEIGDGKIFVSPVDQTIRIRTGEKN I:  MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQK TERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAAAR TGEIGDGKIFVSPVDQTIRIRTGEKNADA J:  MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQK GQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAA ARTGEIGDGKIFVSPVDQTIRIRTGEKNAD K:  MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQK GQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAA ARTGEIGDGKIFVSPVDQTIRIRTGEKN L:  MKKIEAIIRPFKLDEVKIALVNAGIVGMTVSEVRGFGRQK GQTERYRGSEYTVEFLQKLKLEIVVEDAQVDTVIDKIVAA ARTGEIGDGKIFVSPVDQTIRIRTGEKNA Description Functional site 1) chain A residue 69 type sequence G description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 2) chain A residue 70 type sequence G description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 3) chain A residue 71 type sequence G description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 4) chain A residue 74 type sequence I description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 5) chain A residue 92 type sequence R description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 6) chain A residue 174 type sequence S description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 7) chain A residue 185 type sequence N description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 8) chain A residue 186 type sequence I description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 9) chain A residue 187 type sequence N description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 10) chain A residue 188 type sequence A description BINDING SITE FOR RESIDUE NLG A 1292 source : AC1 11) chain A residue 277 type sequence E description BINDING SITE FOR RESIDUE NA A 1293 source : AC2 12) chain A residue 280 type sequence T description BINDING SITE FOR RESIDUE NA A 1293 source : AC2 13) chain B residue 69 type sequence G description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 14) chain B residue 70 type sequence G description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 15) chain B residue 71 type sequence G description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 16) chain B residue 74 type sequence I description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 17) chain B residue 92 type sequence R description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 18) chain B residue 174 type sequence S description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 19) chain B residue 185 type sequence N description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 20) chain B residue 186 type sequence I description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 21) chain B residue 188 type sequence A description BINDING SITE FOR RESIDUE NLG B 1297 source : AC3 22) chain B residue 277 type sequence E description BINDING SITE FOR RESIDUE NA B 1298 source : AC4 23) chain B residue 280 type sequence T description BINDING SITE FOR RESIDUE NA B 1298 source : AC4 24) chain C residue 69 type sequence G description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 25) chain C residue 70 type sequence G description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 26) chain C residue 71 type sequence G description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 27) chain C residue 74 type sequence I description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 28) chain C residue 92 type sequence R description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 29) chain C residue 174 type sequence S description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 30) chain C residue 185 type sequence N description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 31) chain C residue 188 type sequence A description BINDING SITE FOR RESIDUE NLG C 1292 source : AC5 32) chain C residue 277 type sequence E description BINDING SITE FOR RESIDUE NA C 1293 source : AC6 33) chain C residue 280 type sequence T description BINDING SITE FOR RESIDUE NA C 1293 source : AC6 34) chain D residue 69 type sequence G description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 35) chain D residue 70 type sequence G description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 36) chain D residue 71 type sequence G description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 37) chain D residue 74 type sequence I description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 38) chain D residue 92 type sequence R description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 39) chain D residue 185 type sequence N description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 40) chain D residue 188 type sequence A description BINDING SITE FOR RESIDUE NLG D 1294 source : AC7 41) chain D residue 277 type sequence E description BINDING SITE FOR RESIDUE NA D 1295 source : AC8 42) chain D residue 280 type sequence T description BINDING SITE FOR RESIDUE NA D 1295 source : AC8 43) chain E residue 69 type sequence G description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 44) chain E residue 70 type sequence G description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 45) chain E residue 71 type sequence G description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 46) chain E residue 74 type sequence I description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 47) chain E residue 92 type sequence R description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 48) chain E residue 185 type sequence N description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 49) chain E residue 188 type sequence A description BINDING SITE FOR RESIDUE NLG E 1294 source : AC9 50) chain D residue 181 type sequence G description BINDING SITE FOR RESIDUE GOL E 1295 source : BC1 51) chain E residue 112 type sequence K description BINDING SITE FOR RESIDUE GOL E 1295 source : BC1 52) chain E residue 113 type sequence D description BINDING SITE FOR RESIDUE GOL E 1295 source : BC1 53) chain E residue 117 type sequence R description BINDING SITE FOR RESIDUE GOL E 1295 source : BC1 54) chain E residue 277 type sequence E description BINDING SITE FOR RESIDUE NA E 1296 source : BC2 55) chain E residue 280 type sequence T description BINDING SITE FOR RESIDUE NA E 1296 source : BC2 56) chain F residue 69 type sequence G description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 57) chain F residue 70 type sequence G description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 58) chain F residue 71 type sequence G description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 59) chain F residue 92 type sequence R description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 60) chain F residue 149 type sequence V description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 61) chain F residue 185 type sequence N description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 62) chain F residue 188 type sequence A description BINDING SITE FOR RESIDUE NLG F 1293 source : BC3 63) chain F residue 277 type sequence E description BINDING SITE FOR RESIDUE NA F 1294 source : BC4 64) chain F residue 280 type sequence T description BINDING SITE FOR RESIDUE NA F 1294 source : BC4 65) chain G residue 39 type sequence Q description BINDING SITE FOR RESIDUE CL G 1112 source : BC5 66) chain G residue 87 type sequence G description BINDING SITE FOR RESIDUE CL G 1112 source : BC5 67) chain G residue 88 type sequence D description BINDING SITE FOR RESIDUE CL G 1112 source : BC5 68) chain I residue 103 type sequence R description BINDING SITE FOR RESIDUE CL G 1112 source : BC5 69) chain G residue 103 type sequence R description BINDING SITE FOR RESIDUE CL H 1109 source : BC6 70) chain H residue 86 type sequence I description BINDING SITE FOR RESIDUE CL H 1109 source : BC6 71) chain H residue 87 type sequence G description BINDING SITE FOR RESIDUE CL H 1109 source : BC6 72) chain H residue 101 type sequence R description BINDING SITE FOR RESIDUE CL H 1110 source : BC7 73) chain H residue 103 type sequence R description BINDING SITE FOR RESIDUE CL H 1110 source : BC7 74) chain I residue 86 type sequence I description BINDING SITE FOR RESIDUE CL H 1110 source : BC7 75) chain I residue 87 type sequence G description BINDING SITE FOR RESIDUE CL H 1110 source : BC7 76) chain I residue 88 type sequence D description BINDING SITE FOR RESIDUE CL H 1110 source : BC7 77) chain J residue 103 type sequence R description BINDING SITE FOR RESIDUE CL J 1111 source : BC8 78) chain K residue 86 type sequence I description BINDING SITE FOR RESIDUE CL J 1111 source : BC8 79) chain K residue 87 type sequence G description BINDING SITE FOR RESIDUE CL J 1111 source : BC8 80) chain J residue 86 type sequence I description BINDING SITE FOR RESIDUE CL J 1112 source : BC9 81) chain J residue 87 type sequence G description BINDING SITE FOR RESIDUE CL J 1112 source : BC9 82) chain L residue 103 type sequence R description BINDING SITE FOR RESIDUE CL J 1112 source : BC9 83) chain K residue 101 type sequence R description BINDING SITE FOR RESIDUE CL K 1109 source : CC1 84) chain K residue 103 type sequence R description BINDING SITE FOR RESIDUE CL K 1109 source : CC1 85) chain L residue 87 type sequence G description BINDING SITE FOR RESIDUE CL K 1109 source : CC1 86) chain L residue 88 type sequence D description BINDING SITE FOR RESIDUE CL K 1109 source : CC1 87) chain G residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 88) chain D residue 70 type MOD_RES sequence G description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 89) chain D residue 92 type MOD_RES sequence R description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 90) chain D residue 185 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 91) chain E residue 70 type MOD_RES sequence G description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 92) chain E residue 92 type MOD_RES sequence R description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 93) chain E residue 185 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 94) chain F residue 70 type MOD_RES sequence G description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 95) chain F residue 92 type MOD_RES sequence R description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 96) chain F residue 185 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 97) chain H residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 98) chain I residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 99) chain J residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 100) chain K residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 101) chain L residue 49 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 102) chain C residue 70 type MOD_RES sequence G description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 103) chain C residue 92 type MOD_RES sequence R description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 104) chain C residue 185 type MOD_RES sequence N description Phosphoserine => ECO:0000269|PubMed:7592328 source Swiss-Prot : SWS_FT_FI1 105) chain G residue 51 type MOD_RES sequence Y description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 106) chain E residue 248 type MOD_RES sequence K description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 107) chain F residue 35 type MOD_RES sequence K description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 108) chain F residue 248 type MOD_RES sequence K description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 109) chain H residue 51 type MOD_RES sequence Y description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 110) chain I residue 51 type MOD_RES sequence Y description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 111) chain J residue 51 type MOD_RES sequence Y description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 112) chain K residue 51 type MOD_RES sequence Y description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 113) chain L residue 51 type MOD_RES sequence Y description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 114) chain D residue 35 type MOD_RES sequence K description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 115) chain D residue 248 type MOD_RES sequence K description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 116) chain E residue 35 type MOD_RES sequence K description O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 source Swiss-Prot : SWS_FT_FI2 117) chain G residue 46-51 type prosite sequence YRGSEY description PII_GLNB_UMP P-II protein uridylation site. YRGSEY source prosite : PS00496 118) chain G residue 83-96 type prosite sequence TGEIGDGKIFVSPV description PII_GLNB_CTER P-II protein C-terminal region signature. TgeiGDGKIFVspV source prosite : PS00638

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