ID   G0H2Y6_METMI            Unreviewed;       373 AA.
AC   G0H2Y6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=GYY_08400 {ECO:0000313|EMBL:AEK20533.1};
OS   Methanococcus maripaludis X1.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=1053692 {ECO:0000313|Proteomes:UP000008889};
RN   [1] {ECO:0000313|EMBL:AEK20533.1, ECO:0000313|Proteomes:UP000008889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1 {ECO:0000313|EMBL:AEK20533.1,
RC   ECO:0000313|Proteomes:UP000008889};
RX   PubMed=21914896; DOI=10.1128/JB.05835-11;
RA   Wang X., Greenfield P., Li D., Hendry P., Volk H., Sutherland T.D.;
RT   "Complete Genome Sequence of a Nonculturable Methanococcus maripaludis
RT   Strain Extracted in a Metagenomic Survey of Petroleum Reservoir Fluids.";
RL   J. Bacteriol. 193:5595-5595(2011).
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, ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP002913; AEK20533.1; -; Genomic_DNA.
DR   RefSeq; WP_013999828.1; NC_015847.1.
DR   AlphaFoldDB; G0H2Y6; -.
DR   GeneID; 10983088; -.
DR   KEGG; mmd:GYY_08400; -.
DR   PATRIC; fig|1053692.7.peg.1672; -.
DR   HOGENOM; CLU_028393_2_2_2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008889; Chromosome.
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; IPR020622; Ala_racemase_pyridoxalP-BS.
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.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 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}.
FT   DOMAIN          245..372
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        37
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        266
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         37
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   373 AA;  41460 MW;  5972051191F3ECAF CRC64;
     MVSHPIWAEI DLSAIKNNIK EIRRITNPKS QVMAVVKANA YGHGSVEVSK VCLENGADRL
     AVARSTEALE LRNAGITCPI LVFGYVTEEE ILKMVENDIT LTVYSLEIAN SIQKIAEKLG
     KHSKIHIKVD TGMSRLGFLP EKSSVETIKK IRELKNIEVE GIYTHFADAD NSDKTYTTMQ
     FSKFTSFLHD LEENGINIPI KHASNSAAII DHPETHLNMV RPGIILYGLY PSELVHKERI
     NLQPAMSLKV LVTHVKDVPE NTKISYGCTF ETKKQSKIAS LPIGYADGFT RMLKNGNVLI
     HGLRVPVVGR ICMDQCMIDV SGIENVNVGD VVTVFGKDGN EKISIEEFGN KLGTINYELV
     CMVSARVPRI YLH
//