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Database: UniProt
Entry: Q9KUY6
LinkDB: Q9KUY6
Original site: Q9KUY6 
ID   ALR1_VIBCH              Reviewed;         361 AA.
AC   Q9KUY6;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   05-DEC-2018, entry version 118.
DE   RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr1; OrderedLocusNames=VC_0372;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE003852; AAF93545.1; ALT_INIT; Genomic_DNA.
DR   PIR; H82329; H82329.
DR   RefSeq; NP_230026.1; NC_002505.1.
DR   ProteinModelPortal; Q9KUY6; -.
DR   SMR; Q9KUY6; -.
DR   STRING; 243277.VC0372; -.
DR   DNASU; 2615051; -.
DR   EnsemblBacteria; AAF93545; AAF93545; VC_0372.
DR   GeneID; 2615051; -.
DR   KEGG; vch:VC0372; -.
DR   PATRIC; fig|243277.26.peg.348; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; SGAAMYH; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008784; F:alanine racemase activity; ISS:TIGR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; ISS:TIGR.
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    361       Alanine racemase 1.
FT                                /FTId=PRO_0000114591.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    254    254       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     302    302       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   361 AA;  39349 MW;  EBD185735204A735 CRC64;
     MKAATAYINL EALQHNLQRV KQQAPESKIM AVVKANGYGH GLRHIARHAL GADAFGVARI
     EEALQLRASG VVKPILLLEG FYSPGDLPVL VTNNIQTVVH CEEQLQALEQ AQLETPVMVW
     LKVDSGMHRL GVRPEQYQDF VARLHQCENV AKPLRYMSHF GCADELDKST TVEQTELFLS
     LTQGCQGERS LAASAGLLAW PQSQLEWVRP GIIMYGVSPF VEKSAVQLGY QPVMTLKSHL
     IAVREVKAGE SVGYGGTWTS QRDTKIGVIA IGYGDGYPRT APNGTPVVVN GRRVPIAGRV
     SMDMLTVDLG PDACDRVGDE AMLWGNELPV EEVAAHIGTI GYELVTKLTS RVEMSYYGAG
     V
//
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