eF-site ID 1dbt-ABC PDB Code 1dbt Chain A, B, C click to enlarge Title CRYSTAL STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH UMP Classification LYASE Compound OROTIDINE 5'-PHOSPHATE DECARBOXYLASE Source Bacillus subtilis (PYRF_BACSU) Sequence A:  MKNNLPIIALDFASAEETLAFLAPFQQEPLFVKVGMELFY QEGPSIVKQLKERNCELFLDLKLHDIPTTVNKAMKRLASL GVDLVNVHAAGGKKMMQAALEGLEEGTPAGKKRPSLIAVT QLTSTSEQIMKDELLIEKSLIDTVVHYSKQAEESGLDGVV CSVHEAKAIYQAVSPSFLTVTPGIRMSEDAANDQVRVATP AIAREKGSSAIVVGRSITKAEDPVKAYKAVRLEWEGI B:  NNLPIIALDFASAEETLAFLAPFQQEPLFVKVGMELFYQE GPSIVKQLKERNCELFLDLKLHDIPTTVNKAMKRLASLGV DLVNVHAAGGKKMMQAALEGLEEGTPAGKKRPSLIAVTQL TSTSEQIMKDELLIEKSLIDTVVHYSKQAEESGLDGVVCS VHEAKAIYQAVSPSFLTVTPGIRMSEDAANDQVRVATPAI AREKGSSAIVVGRSITKAEDPVKAYKAVRLEWEG C:  NNLPIIALDFASAEETLAFLAPFQQEPLFVKVGMELFYQE GPSIVKQLKERNCELFLDLKLHDIPTTVNKAMKRLASLGV DLVNVHAAGGKKMMQAALEGLEEGTPAGKKRPSLIAVTQL TSTSEQIMKDELLIEKSLIDTVVHYSKQAEESGLDGVVCS VHEAKAIYQAVSPSFLTVTPGIRMSEDAANDQVRVATPAI AREKGSSAIVVGRSITKAEDPVKAYKAVRLEWEG Description Functional site 1) chain A residue 11 type sequence D description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 2) chain A residue 33 type sequence K description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 3) chain A residue 62 type sequence K description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 4) chain A residue 122 type sequence L description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 5) chain A residue 123 type sequence T description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 6) chain A residue 160 type sequence V description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 7) chain A residue 182 type sequence P description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 8) chain A residue 185 type sequence R description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 9) chain A residue 194 type sequence Q description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 10) chain A residue 212 type sequence V description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 11) chain A residue 214 type sequence G description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 12) chain A residue 215 type sequence R description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 13) chain B residue 65 type sequence D description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 14) chain B residue 66 type sequence I description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 15) chain B residue 69 type sequence T description BINDING SITE FOR RESIDUE U5P A 250 source : AC1 16) chain A residue 65 type sequence D description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 17) chain A residue 66 type sequence I description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 18) chain A residue 69 type sequence T description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 19) chain B residue 11 type sequence D description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 20) chain B residue 33 type sequence K description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 21) chain B residue 62 type sequence K description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 22) chain B residue 122 type sequence L description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 23) chain B residue 123 type sequence T description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 24) chain B residue 160 type sequence V description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 25) chain B residue 182 type sequence P description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 26) chain B residue 185 type sequence R description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 27) chain B residue 194 type sequence Q description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 28) chain B residue 212 type sequence V description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 29) chain B residue 214 type sequence G description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 30) chain B residue 215 type sequence R description BINDING SITE FOR RESIDUE U5P B 251 source : AC2 31) chain C residue 11 type sequence D description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 32) chain C residue 33 type sequence K description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 33) chain C residue 62 type sequence K description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 34) chain C residue 65 type sequence D description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 35) chain C residue 66 type sequence I description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 36) chain C residue 69 type sequence T description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 37) chain C residue 122 type sequence L description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 38) chain C residue 123 type sequence T description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 39) chain C residue 160 type sequence V description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 40) chain C residue 182 type sequence P description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 41) chain C residue 185 type sequence R description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 42) chain C residue 194 type sequence Q description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 43) chain C residue 212 type sequence V description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 44) chain C residue 214 type sequence G description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 45) chain C residue 215 type sequence R description BINDING SITE FOR RESIDUE U5P C 252 source : AC3 46) chain A residue 11 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 47) chain B residue 33 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 48) chain B residue 60 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 49) chain B residue 123 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 50) chain B residue 185 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 51) chain B residue 194 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 52) chain B residue 214 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 53) chain B residue 215 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 54) chain C residue 11 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 55) chain C residue 33 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 56) chain C residue 60 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 57) chain A residue 33 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 58) chain C residue 123 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 59) chain C residue 185 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 60) chain C residue 194 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 61) chain C residue 214 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 62) chain C residue 215 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 63) chain A residue 60 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 64) chain A residue 123 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 65) chain A residue 185 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 66) chain A residue 194 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 67) chain A residue 214 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 68) chain A residue 215 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 69) chain B residue 11 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI2 70) chain A residue 62 type ACT_SITE sequence K description Proton donor source Swiss-Prot : SWS_FT_FI1 71) chain B residue 62 type ACT_SITE sequence K description Proton donor source Swiss-Prot : SWS_FT_FI1 72) chain C residue 62 type ACT_SITE sequence K description Proton donor source Swiss-Prot : SWS_FT_FI1 73) chain A residue 33 type catalytic sequence K description 50 source MCSA : MCSA1 74) chain A residue 60 type catalytic sequence D description 50 source MCSA : MCSA1 75) chain A residue 62 type catalytic sequence K description 50 source MCSA : MCSA1 76) chain A residue 65 type catalytic sequence D description 50 source MCSA : MCSA1 77) chain A residue 123 type catalytic sequence T description 50 source MCSA : MCSA1 78) chain A residue 215 type catalytic sequence R description 50 source MCSA : MCSA1 79) chain B residue 33 type catalytic sequence K description 50 source MCSA : MCSA2 80) chain B residue 60 type catalytic sequence D description 50 source MCSA : MCSA2 81) chain B residue 62 type catalytic sequence K description 50 source MCSA : MCSA2 82) chain B residue 65 type catalytic sequence D description 50 source MCSA : MCSA2 83) chain B residue 123 type catalytic sequence T description 50 source MCSA : MCSA2 84) chain B residue 215 type catalytic sequence R description 50 source MCSA : MCSA2 85) chain C residue 33 type catalytic sequence K description 50 source MCSA : MCSA3 86) chain C residue 60 type catalytic sequence D description 50 source MCSA : MCSA3 87) chain C residue 62 type catalytic sequence K description 50 source MCSA : MCSA3 88) chain C residue 65 type catalytic sequence D description 50 source MCSA : MCSA3 89) chain C residue 123 type catalytic sequence T description 50 source MCSA : MCSA3 90) chain C residue 215 type catalytic sequence R description 50 source MCSA : MCSA3 91) chain A residue 57-70 type prosite sequence LFLDLKLHDIPTTV description OMPDECASE Orotidine 5'-phosphate decarboxylase active site. LFlDlKlhDIPtTV source prosite : PS00156

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