eF-site ID 2yyu-AB PDB Code 2yyu Chain A, B click to enlarge Title Crystal structure of uncharacterized conserved protein from Geobacillus kaustophilus Classification LYASE Compound Orotidine 5'-phosphate decarboxylase Source Geobacillus kaustophilus (PYRF_GEOKA) Sequence A:  TPFIVALDFPSKQEVERFLRPFAGTPLFVKVGMELYYQEG PAIVAFLKEQGHAVFLDLKLHDIPNTVKQAMKGLARVGAD LVNVHAAGGRRMMEAAIEGLDAGTPSGRMRPRCIAVTQLT STDERMLHEELWISRPLVETVAHYAALAKESGLDGVVCSA NEAAFIKERCGASFLAVTPGIRFADRVVTPRKARALGSDY IVIGRSLTRAADPLRTYARLQHEWN B:  HTPFIVALDFPSKQEVERFLRPFAGTPLFVKVGMELYYQE GPAIVAFLKEQGHAVFLDLKLHDIPNTVKQAMKGLARVGA DLVNVHAAGGRRMMEAAIEGLDAGTPSGRMRPRCIAVTQL TSTDERMLHEELWISRPLVETVAHYAALAKESGLDGVVCS ANEAAFIKERCGASFLAVTPGIRFADDAARVVTPRKARAL GSDYIVIGRSLTRAADPLRTYARLQHEWN Description Functional site 1) chain A residue 12 type sequence D description BINDING SITE FOR RESIDUE C5P A 1301 source : AC1 2) chain A residue 34 type sequence K description BINDING SITE FOR RESIDUE C5P A 1301 source : AC1 3) chain A residue 124 type sequence T description BINDING SITE FOR RESIDUE C5P A 1301 source : AC1 4) chain A residue 186 type sequence R description BINDING SITE FOR RESIDUE C5P A 1301 source : AC1 5) chain A residue 215 type sequence G description BINDING SITE FOR RESIDUE C5P A 1301 source : AC1 6) chain A residue 216 type sequence R description BINDING SITE FOR RESIDUE C5P A 1301 source : AC1 7) chain B residue 10 type sequence A description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 8) chain B residue 12 type sequence D description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 9) chain B residue 34 type sequence K description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 10) chain B residue 124 type sequence T description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 11) chain B residue 183 type sequence P description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 12) chain B residue 186 type sequence R description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 13) chain B residue 215 type sequence G description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 14) chain B residue 216 type sequence R description BINDING SITE FOR RESIDUE C5P B 2301 source : AC2 15) chain A residue 12 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 34 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 61 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 124 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 186 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 215 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 216 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 34 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 61 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 124 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 186 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 215 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 216 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 12 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 63 type ACT_SITE sequence K description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 63 type ACT_SITE sequence K description Proton donor => ECO:0000255|HAMAP-Rule:MF_01200 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 58-71 type prosite sequence VFLDLKLHDIPNTV description OMPDECASE Orotidine 5'-phosphate decarboxylase active site. VFlDlKlhDIPnTV source prosite : PS00156

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