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Database: UniProt
Entry: A4XBI0
LinkDB: A4XBI0
Original site: A4XBI0 
ID   ALR_SALTO               Reviewed;         372 AA.
AC   A4XBI0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JAN-2019, entry version 75.
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=Strop_3857;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S.,
RA   Udwary D.W., Richardson P.;
RT   "Complete sequence of Salinispora tropica CNB-440.";
RL   Submitted (APR-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; CP000667; ABP56287.1; -; Genomic_DNA.
DR   RefSeq; WP_012015062.1; NC_009380.1.
DR   ProteinModelPortal; A4XBI0; -.
DR   SMR; A4XBI0; -.
DR   STRING; 369723.Strop_3857; -.
DR   PRIDE; A4XBI0; -.
DR   EnsemblBacteria; ABP56287; ABP56287; Strop_3857.
DR   GeneID; 5060335; -.
DR   KEGG; stp:Strop_3857; -.
DR   PATRIC; fig|369723.5.peg.3981; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000235; 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    372       Alanine racemase.
FT                                /FTId=PRO_1000085507.
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;  39213 MW;  C4E9E1D89EABDB68 CRC64;
     MWQAEVRVDL DAIRENVSWL RSGSAAELMA VVKGDGYGHG MVPAAHAALD GGADWLGVCT
     LDEALTLRRA GITVPVLAWL LAPGLPLHEG VTAGIDLGVA SVAQLEEMVE AGRVAGRPAR
     LHLKIDTGLS RGGATISEWP ELLDAAAKAQ ADGAVEVVGV WSHFVYADAP GHPTTDRQLA
     VFHEGLGMVE KAGLRPRYRH LANSAATLTR PDAHFDLVRP GLAVYGLSPV AGERFGLRPA
     MTARARVMLT KQVPAGAGVS YGHTYTTDRA SNLAVIPLGY ADGVPRDASN SGPVQLGGVR
     RTISGRVCMD QFVLDCGDDP VAPGDVATLF GTGRDGEPTA DDWAEAVGTI NYEIVTRFGS
     TRVPRCYDGE RP
//
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