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Database: UniProt/SWISS-PROT
Entry: ALR_METMP
LinkDB: ALR_METMP
Original site: ALR_METMP 
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   05-DEC-2018, entry version 88.
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;
OC   Methanococcales; 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.,
RA   Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J.,
RA   Major T.A., Moore B.C., Porat I., Palmeiri A., Rouse G.,
RA   Saenphimmachak C., Soell D., Van Dien S., Wang T., Whitman W.B.,
RA   Xia Q., Zhang Y., Larimer F.W., Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable
RT   hydrogenotrophic 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
RT   roles for alanine dehydrogenase, alanine racemase, and alanine
RT   permease.";
RL   J. Bacteriol. 187:972-979(2005).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. This organism is able to use both L-and D-alanine as a
CC       nitrogen source. May also prevent D-alanine from interfering with
CC       the use of L-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-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- DISRUPTION PHENOTYPE: No growth on D-alanine, however able to grow
CC       on L-alanine. Slower than wild-type growth on a mix of alanine
CC       isomers. {ECO:0000269|PubMed:15659675}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; BX950229; CAF31068.1; -; Genomic_DNA.
DR   RefSeq; WP_011171456.1; NC_005791.1.
DR   ProteinModelPortal; Q6LX41; -.
DR   SMR; Q6LX41; -.
DR   STRING; 267377.MMP1512; -.
DR   PRIDE; Q6LX41; -.
DR   EnsemblBacteria; CAF31068; CAF31068; MMP1512.
DR   GeneID; 2761062; -.
DR   KEGG; mmp:MMP1512; -.
DR   PATRIC; fig|267377.15.peg.1549; -.
DR   eggNOG; arCOG06677; Archaea.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; POG093Z03IN; -.
DR   BioCyc; MMAR267377:MMP_RS07770-MONOMER; -.
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   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    373       Alanine racemase.
FT                                /FTId=PRO_0000415442.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    266    266       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     313    313       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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