eF-site ID 1xld-AB PDB Code 1xld Chain A, B click to enlarge Title MECHANISM FOR ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE INVOLVING RING OPENING FOLLOWED BY A 1,2-HYDRIDE SHIFT Classification ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) Compound D-XYLOSE ISOMERASE Source Arthrobacter sp. (strain NRRL B3728) (XYLA_ARTS7) Sequence A:  VQPTPADHFTFGLWTVGWTGADPFGVATRKNLDPVEAVHK LAELGAYGITFHDNDLIPFDATEAEREKILGDFNQALKDT GLKVPMVTTNLFSHPVFKDGGFTSNDRSIRRFALAKVLHN IDLAAEMGAETFVMWGGREGSEYDGSKDLAAALDRMREGV DTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLF HIDLNGQRGIKYDQDLVFGHGDLTSAFFTVDLLENGFPNG GPKYTGPRHFDYKPSRTDGYDGVWDSAKANMSMYLLLKER ALAFRADPEVQEAMKTSGVFELGETTLNAGESAADLMNDS ASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR B:  VQPTPADHFTFGLWTVGWTGADPFGVATRKNLDPVEAVHK LAELGAYGITFHDNDLIPFDATEAEREKILGDFNQALKDT GLKVPMVTTNLFSHPVFKDGGFTSNDRSIRRFALAKVLHN IDLAAEMGAETFVMWGGREGSEYDGSKDLAAALDRMREGV DTAAGYIKDKGYNLRIALEPKPNEPRGDIFLPTVGHGLAF IEQLEHGDIVGLNPETGHEQMAGLNFTHGIAQALWAEKLF HIDLNGQRGIKYDQDLVFGHGDLTSAFFTVDLLENGFPNG GPKYTGPRHFDYKPSRTDGYDGVWDSAKANMSMYLLLKER ALAFRADPEVQEAMKTSGVFELGETTLNAGESAADLMNDS ASFAGFDAEAAAERNFAFIRLNQLAIEHLLGSR Description Functional site 1) chain A residue 54 type catalytic sequence D description 308 source MCSA : MCSA1 2) chain A residue 257 type catalytic sequence L description 308 source MCSA : MCSA1 3) chain A residue 293 type catalytic sequence Y description 308 source MCSA : MCSA1 4) chain A residue 57 type catalytic sequence L description 308 source MCSA : MCSA1 5) chain A residue 88 type catalytic sequence V description 308 source MCSA : MCSA1 6) chain A residue 181 type catalytic sequence P description 308 source MCSA : MCSA1 7) chain A residue 183 type catalytic sequence P description 308 source MCSA : MCSA1 8) chain A residue 217 type catalytic sequence T description 308 source MCSA : MCSA1 9) chain A residue 220 type catalytic sequence E description 308 source MCSA : MCSA1 10) chain A residue 245 type catalytic sequence L description 308 source MCSA : MCSA1 11) chain A residue 255 type catalytic sequence Q description 308 source MCSA : MCSA1 12) chain B residue 54 type catalytic sequence D description 308 source MCSA : MCSA2 13) chain B residue 257 type catalytic sequence L description 308 source MCSA : MCSA2 14) chain B residue 293 type catalytic sequence Y description 308 source MCSA : MCSA2 15) chain B residue 57 type catalytic sequence L description 308 source MCSA : MCSA2 16) chain B residue 88 type catalytic sequence V description 308 source MCSA : MCSA2 17) chain B residue 181 type catalytic sequence P description 308 source MCSA : MCSA2 18) chain B residue 183 type catalytic sequence P description 308 source MCSA : MCSA2 19) chain B residue 217 type catalytic sequence T description 308 source MCSA : MCSA2 20) chain B residue 220 type catalytic sequence E description 308 source MCSA : MCSA2 21) chain B residue 245 type catalytic sequence L description 308 source MCSA : MCSA2 22) chain B residue 255 type catalytic sequence Q description 308 source MCSA : MCSA2 23) chain A residue 54 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:2319597 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 57 type ACT_SITE sequence L description ACT_SITE => ECO:0000269|PubMed:2319597 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 54 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:2319597 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 57 type ACT_SITE sequence L description ACT_SITE => ECO:0000269|PubMed:2319597 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 181 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI2 28) chain B residue 220 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 29) chain B residue 245 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 30) chain B residue 255 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 31) chain B residue 257 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 32) chain B residue 293 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 33) chain A residue 217 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 34) chain A residue 220 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 245 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 255 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 37) chain A residue 257 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 293 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI2 39) chain B residue 181 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI2 40) chain B residue 217 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2

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