eF-site ID 1mns-A PDB Code 1mns Chain A click to enlarge Title ON THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FOR STEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE Classification RACEMASE Compound MANDELATE RACEMASE Source Pseudomonas putida (Arthrobacter siderocapsulatus) (MANR_PSEPU) Sequence A:  EVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATS AGVVGHSYLFAYTPVALKSLKQLLDDMAAMIVNEPLAPVS LEAMLAKRFCLAGYTGLIRMAAAGIDMAAWDALGKVHETP LVKLLGANARPVQAYDSHSLDGVKLATERAVTAAELGFRA VKTKIGYPALDQDLAVVRSIRQAVGDDFGIMVDYNQSLDV PAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLNVP VQMGENWLGPEEMFKALSIGACRLAMPDAMKIGGVTGWIR ASALAQQFGIPMSSHLFQEISAHLLAATPTAHWLERLDLA GSVIEPTLTFEGGNAVIPDLPGVGIIWREKEIGKYLV Description (1)  MANDELATE RACEMASE (E.C.5.1.2.2) Functional site 1) chain A residue 195 type sequence D description DIRECT METAL ION LIGANDS source : MTL 2) chain A residue 221 type sequence E description DIRECT METAL ION LIGANDS source : MTL 3) chain A residue 247 type sequence E description DIRECT METAL ION LIGANDS source : MTL 4) chain A residue 166 type sequence K description ACID/BASE CATALYSTS RESPONSIBLE FOR PROTON ABSTRACTION AND REDELIVERY IN THE RACEMIZATION REACTION source : ACT 5) chain A residue 297 type sequence H description ACID/BASE CATALYSTS RESPONSIBLE FOR PROTON ABSTRACTION AND REDELIVERY IN THE RACEMIZATION REACTION source : ACT 6) chain A residue 164 type sequence K description BINDING SITE FOR THE CARBOXYL GROUP OF SUBSTRATE. THESE RESIDUES FUNCTION, ALONG WITH THE METAL ION, AS ELECTROPHILIC CATALYSTS source : CAR 7) chain A residue 317 type sequence E description BINDING SITE FOR THE CARBOXYL GROUP OF SUBSTRATE. THESE RESIDUES FUNCTION, ALONG WITH THE METAL ION, AS ELECTROPHILIC CATALYSTS source : CAR 8) chain A residue 195 type sequence D description BINDING SITE FOR RESIDUE MG A 360 source : AC1 9) chain A residue 221 type sequence E description BINDING SITE FOR RESIDUE MG A 360 source : AC1 10) chain A residue 247 type sequence E description BINDING SITE FOR RESIDUE MG A 360 source : AC1 11) chain A residue 52 type sequence F description BINDING SITE FOR RESIDUE APG A 361 source : AC2 12) chain A residue 139 type sequence S description BINDING SITE FOR RESIDUE APG A 361 source : AC2 13) chain A residue 164 type sequence K description BINDING SITE FOR RESIDUE APG A 361 source : AC2 14) chain A residue 166 type sequence K description BINDING SITE FOR RESIDUE APG A 361 source : AC2 15) chain A residue 195 type sequence D description BINDING SITE FOR RESIDUE APG A 361 source : AC2 16) chain A residue 197 type sequence N description BINDING SITE FOR RESIDUE APG A 361 source : AC2 17) chain A residue 221 type sequence E description BINDING SITE FOR RESIDUE APG A 361 source : AC2 18) chain A residue 247 type sequence E description BINDING SITE FOR RESIDUE APG A 361 source : AC2 19) chain A residue 297 type sequence H description BINDING SITE FOR RESIDUE APG A 361 source : AC2 20) chain A residue 317 type sequence E description BINDING SITE FOR RESIDUE APG A 361 source : AC2 21) chain A residue 319 type sequence L description BINDING SITE FOR RESIDUE APG A 361 source : AC2 22) chain A residue 164 type catalytic sequence K description 187 source MCSA : MCSA1 23) chain A residue 166 type catalytic sequence K description 187 source MCSA : MCSA1 24) chain A residue 195 type catalytic sequence D description 187 source MCSA : MCSA1 25) chain A residue 197 type catalytic sequence N description 187 source MCSA : MCSA1 26) chain A residue 221 type catalytic sequence E description 187 source MCSA : MCSA1 27) chain A residue 247 type catalytic sequence E description 187 source MCSA : MCSA1 28) chain A residue 270 type catalytic sequence D description 187 source MCSA : MCSA1 29) chain A residue 297 type catalytic sequence H description 187 source MCSA : MCSA1 30) chain A residue 317 type catalytic sequence E description 187 source MCSA : MCSA1 31) chain A residue 195 type BINDING sequence D description BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 221 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 247 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 317 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 166 type ACT_SITE sequence K description Proton acceptor; specific for S-mandelate source Swiss-Prot : SWS_FT_FI1 36) chain A residue 297 type ACT_SITE sequence H description Proton acceptor; specific for R-mandelate source Swiss-Prot : SWS_FT_FI2 37) chain A residue 103-128 type prosite sequence AAAGIDMAAWDALGKVHETPLVKLLG description MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AaAGIDmAAwDAlGKvhetPLvkLLG source prosite : PS00908 38) chain A residue 192-223 type prosite sequence IMVDYNQSLDVPAAIKRSQALQQEGVTWIEEP description MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. ImvDyNqsldvpaAikrsqaLqqegvtwIEEP source prosite : PS00909

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