GenomeNet

Database: UniProt
Entry: A8M4B3
LinkDB: A8M4B3
Original site: A8M4B3 
ID   ALR_SALAI               Reviewed;         372 AA.
AC   A8M4B3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   16-JAN-2019, entry version 72.
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=Sare_4247;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S.,
RA   Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       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: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   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; CP000850; ABW00029.1; -; Genomic_DNA.
DR   RefSeq; WP_012184266.1; NC_009953.1.
DR   ProteinModelPortal; A8M4B3; -.
DR   SMR; A8M4B3; -.
DR   STRING; 391037.Sare_4247; -.
DR   EnsemblBacteria; ABW00029; ABW00029; Sare_4247.
DR   GeneID; 5708097; -.
DR   KEGG; saq:Sare_4247; -.
DR   PATRIC; fig|391037.6.peg.4287; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; SARE391037:G1GA7-4289-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001153; 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.
FT   CHAIN         1    372       Alanine racemase.
FT                                /FTId=PRO_1000085506.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    261    261       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     309    309       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      33     33       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   372 AA;  39060 MW;  DC2D242501215038 CRC64;
     MWQAEVRVDL DAIRENVSWL RSGSAAELMA VVKGDGYGHG MVPAALAALD GGADWLGVCT
     LDEALTLRRE GITAPILAWL LAPGLPLHEG VAAGIDLGAA SVAQLDEMVQ AGRTAGRPAR
     LHLKIDTGLS RGGATVSDWP GLLTAAAKAQ ADGTVEVVGV WSHFVYADAP GHPTTDRQLA
     VFHEGLDMVE KAGLRPRYRH LANSAATLTR PDAHFDLVRP GLAVYGLSPV AGESFGLRPA
     MTARARVMLT KQVPAGAGVS YGHTYTTERD STLAVIPLGY ADGVPRSASN SGPVHLGGVR
     RTISGRVCMD QFVLDCGDDP VAPGDVAVLF GSGRNGEPTA DDWAEAVGTI NYEIVTRFGS
     TRVPRSYDGE RP
//
DBGET integrated database retrieval system