ID   ALR_METMP               Reviewed;         373 AA.
AC   Q6LX41;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=MMP1512;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=S2 / LL;
RX   PubMed=15659675; DOI=10.1128/jb.187.3.972-979.2005;
RA   Moore B.C., Leigh J.A.;
RT   "Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for
RT   alanine dehydrogenase, alanine racemase, and alanine permease.";
RL   J. Bacteriol. 187:972-979(2005).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine.
CC       This organism is able to use both L- and D-alanine as a nitrogen
CC       source. May also prevent D-alanine from interfering with the use of L-
CC       alanine. {ECO:0000269|PubMed:15659675}.
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:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC       from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- DISRUPTION PHENOTYPE: No growth on D-alanine, however able to grow on
CC       L-alanine. Slower than wild-type growth on a mix of alanine isomers.
CC       {ECO:0000269|PubMed:15659675}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
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DR   EMBL; BX950229; CAF31068.1; -; Genomic_DNA.
DR   RefSeq; WP_011171456.1; NC_005791.1.
DR   AlphaFoldDB; Q6LX41; -.
DR   SMR; Q6LX41; -.
DR   STRING; 267377.MMP1512; -.
DR   EnsemblBacteria; CAF31068; CAF31068; MMP1512.
DR   GeneID; 2761062; -.
DR   KEGG; mmp:MMP1512; -.
DR   PATRIC; fig|267377.15.peg.1549; -.
DR   eggNOG; arCOG06677; Archaea.
DR   HOGENOM; CLU_028393_2_2_2; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 21006at2157; -.
DR   BioCyc; MMAR267377:MMP_RS07770-MON; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000590; 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   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..373
FT                   /note="Alanine racemase"
FT                   /id="PRO_0000415442"
FT   ACT_SITE        37
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   ACT_SITE        266
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT   MOD_RES         37
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
SQ   SEQUENCE   373 AA;  41536 MW;  2D611E7E744167B5 CRC64;
     MVSHPIWAEI DLSAIKNNIK EIRRITNPKS QVMAVVKANA YGHGSVEVSK ICLENGADRL
     AVARSTEALE LRDAGITCPI LVFGYVTEEE ILKMVENDIT LTVYSLEIAN SIQKIAEKLG
     KHSKIHIKVD TGMSRLGFLP EKSSVETIKK IRELENIEVE GIYTHFADAD NSDKTYTTMQ
     FSKFTSFLHD LEENGIDIPI KHASNSAAII DHPETHLNMV RPGIILYGLY PSELVHKERI
     NLQPAMSLKV LVTHVKDVPE NTKISYGCTF ETKKQSKIAS LPIGYADGFT RMLRNGNVLI
     HGLRVPVVGR ICMDQCMIDV TSIENVNVGD VVTVFGKDGT EKISIEEFGN KLGTINYELV
     CMVSARVPRI YLH