GenomeNet

Database: UniProt
Entry: Q72DH4
LinkDB: Q72DH4
Original site: Q72DH4 
ID   ALR_DESVH               Reviewed;         376 AA.
AC   Q72DH4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 97.
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=DVU_0955;
OS   Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 /
OS   NCIMB 8303).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D.,
RA   Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R.,
RA   Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS95435.1; -; Genomic_DNA.
DR   RefSeq; WP_010938254.1; NC_002937.3.
DR   RefSeq; YP_010176.1; NC_002937.3.
DR   ProteinModelPortal; Q72DH4; -.
DR   SMR; Q72DH4; -.
DR   STRING; 882.DVU0955; -.
DR   PaxDb; Q72DH4; -.
DR   EnsemblBacteria; AAS95435; AAS95435; DVU_0955.
DR   GeneID; 2795151; -.
DR   KEGG; dvu:DVU0955; -.
DR   PATRIC; fig|882.5.peg.899; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   PhylomeDB; Q72DH4; -.
DR   BioCyc; DVUL882:G1GT1-983-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002194; 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    376       Alanine racemase.
FT                                /FTId=PRO_1000164592.
FT   ACT_SITE     36     36       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     134    134       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     314    314       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   376 AA;  39406 MW;  F41CD32773346D72 CRC64;
     MPISYNKASV VVSLQSIIAN YRRIRTVAQR PMPVIKSDAY GHGLEAVGMA LEAEGARECA
     VGTVGEGAKL RKAGFGADIV ALLGALDRED AQLAASSGII PTVLDIAGLE RLAAQGTPER
     PVRVALKFDT GMARLGFTEH DVSALCERLR TLPSVRPVMA VSHLAVADDP TQSAFTMAQG
     AAFARIMAGL RSNFPDIMGS LSNSAATLAH PQLHWDVQRP GIALYGSNPL RGTALARHGE
     GLLPAMSVSV PVLQVHPLPA GRSISYGRTY TATKDATVAI IAAGYADNYS RALSGRGVAV
     AGGRRVPVLG RVCMQTTAID VTDVPGIATG DRVWLLGGPG PATVSADELA DLWGTISYEV
     LCLLGMNPRR HDDSVE
//
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