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Database: UniProt
Entry: Q83D71
LinkDB: Q83D71
Original site: Q83D71 
ID   ALR_COXBU               Reviewed;         364 AA.
AC   Q83D71;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 93.
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=CBU_0869;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90402.1; -; Genomic_DNA.
DR   RefSeq; NP_819888.1; NC_002971.3.
DR   RefSeq; WP_005772336.1; NC_002971.4.
DR   ProteinModelPortal; Q83D71; -.
DR   SMR; Q83D71; -.
DR   STRING; 227377.CBU_0869; -.
DR   PRIDE; Q83D71; -.
DR   EnsemblBacteria; AAO90402; AAO90402; CBU_0869.
DR   GeneID; 1208762; -.
DR   KEGG; cbu:CBU_0869; -.
DR   PATRIC; fig|227377.7.peg.854; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; CBUR227377:G1G0B-861-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002671; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    364       Alanine racemase.
FT                                /FTId=PRO_1000065985.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    259    259       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     129    129       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     307    307       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   364 AA;  39962 MW;  38DD172C79E0E8DA CRC64;
     MNRATATINV TALKHNLSQI KALAPKSLAW AMIKSNGYGH GLVRVAKALS DANAFGVACI
     DEALTLREVG IKSPIIVMKG FYNEAELSQF ARHRLGAVIH CSDQVSLLEK TNLTSSLSVW
     LKIDTGMNRL GFSVEQSPAV YNQLKTSSSI QKPIGLMTHL ADADNENKTF TELQIKRFFS
     VTEKMIGPKS IVNSAGFFAY PNALVDWIRP GIILYGISPF GINYNSFKEK IEKKFRPVMT
     LSAKIIAIKN RRQNDSVGYG CTWSCPEDMP IAIVSIGYGD GYPRHAPSGT PVLLNGKICP
     LIGRVSMDMI AIDLRSQPNA QVGDDVILWG EGLPVEIIAE KAGTIAYELL CKITQRVQFI
     EIEK
//
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