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Database: UniProt
Entry: S7V5A2_DESML
LinkDB: S7V5A2_DESML
Original site: S7V5A2_DESML 
ID   S7V5A2_DESML            Unreviewed;       406 AA.
AC   S7V5A2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=dsmv_1833 {ECO:0000313|EMBL:EPR41834.1};
OS   Desulfococcus multivorans DSM 2059.
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfococcaceae; Desulfococcus.
OX   NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR41834.1, ECO:0000313|Proteomes:UP000014977};
RN   [1] {ECO:0000313|EMBL:EPR41834.1, ECO:0000313|Proteomes:UP000014977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR41834.1,
RC   ECO:0000313|Proteomes:UP000014977};
RX   PubMed=23950126;
RA   Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT   "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT   bacteria.";
RL   Genome Announc. 1:e00618-e00613(2013).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC       also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPR41834.1}.
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DR   EMBL; ATHJ01000071; EPR41834.1; -; Genomic_DNA.
DR   RefSeq; WP_020876215.1; NZ_FUWN01000010.1.
DR   AlphaFoldDB; S7V5A2; -.
DR   STRING; 897.B2D07_00215; -.
DR   PATRIC; fig|1121405.3.peg.1289; -.
DR   eggNOG; COG0787; Bacteria.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000014977; Unassembled WGS sequence.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000014977}.
FT   DOMAIN          260..388
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        45
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        281
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   406 AA;  43563 MW;  3DE3373670097A1E CRC64;
     MGEERKKSLK KHVVWAEIDL GAIHHNLKAL KRLIGPAVRM LVAVKANSYG HGLIPVARQA
     LADGVDMLGV ARIDEGIQLR RAGITAPILL FGYTAPDATA DLLKYDLTPT VFSHATAKAM
     SAAALAAGKP LPVHVKLDTG MGRIGLAAPD LDILHGSDSV REIERIAHLE GLIPEGIYTH
     FASADDRDKT SAGRQFERFM TTLSELAQSG VTFPLRHAAN SGAVIDMPET HLDMVRPGIA
     VYGLYPSNDV ARSRIDLIPA MTLKARIAQI KSVPAGFQVS YGSTYTTPKP TVIATVPVGY
     ADGYPRGLSS RGIMLAGGLR VPVIGRICMD LTMLDVGDVP GIKAEDEVVI LGNQGRESIS
     ADEIAGWLGT INYEVVSSVM ARVPRVYTWR GSSVLPGDRS EDNERY
//
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