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Database: UniProt/TrEMBL
Entry: G4Q3V8_ACIIR
LinkDB: G4Q3V8_ACIIR
Original site: G4Q3V8_ACIIR 
ID   G4Q3V8_ACIIR            Unreviewed;       381 AA.
AC   G4Q3V8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-SEP-2017, entry version 44.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:AEQ23024.1};
GN   OrderedLocusNames=Acin_1813 {ECO:0000313|EMBL:AEQ23024.1};
OS   Acidaminococcus intestini (strain RyC-MR95).
OC   Bacteria; Firmicutes; Negativicutes; Acidaminococcales;
OC   Acidaminococcaceae; Acidaminococcus.
OX   NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ23024.1, ECO:0000313|Proteomes:UP000007093};
RN   [1] {ECO:0000313|EMBL:AEQ23024.1, ECO:0000313|Proteomes:UP000007093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ23024.1,
RC   ECO:0000313|Proteomes:UP000007093};
RX   PubMed=22123762; DOI=10.1128/JB.06301-11;
RA   D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA   Latorre A.;
RT   "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a
RT   Gram-negative bacterium from the phylum Firmicutes.";
RL   J. Bacteriol. 193:7008-7009(2011).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP003058; AEQ23024.1; -; Genomic_DNA.
DR   RefSeq; WP_009015859.1; NC_016077.1.
DR   ProteinModelPortal; G4Q3V8; -.
DR   STRING; 568816.Acin_1813; -.
DR   EnsemblBacteria; AEQ23024; AEQ23024; Acin_1813.
DR   KEGG; ain:Acin_1813; -.
DR   PATRIC; fig|568816.4.peg.1761; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007093; 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 {ECO:0000313|Proteomes:UP000007093};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007093}.
FT   DOMAIN      243    368       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     37     37       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    264    264       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     135    135       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   381 AA;  41804 MW;  3FA4181A234C02DF CRC64;
     MRARNVWAEV DLSAIAHNVQ VTRKVLKPGT KICAVVKADA YGHGAVPVAT AALAAGVNYL
     AVSMTQEALE LREAGIMAPI LILGTMTEEH EKALVDYNIT QTVYDLAVAQ ELSAAALQEN
     KVAKVHLAVD TGMNRIGCRP EEAADLAEAI SKLPHVELEG MFSHFASADE MDKSFAESQY
     RKFMEADRAI KDRGIQIPLV HIDNSAGITE MKHTECDMVR QGITLYGLWP SDDVERCLDL
     KPALSLKAEV VFVKDVPAGE KIGYGCTYET KAPMKVATIP LGYADGYSRA LSNRGYITIR
     GYKAPVVGRI CMDQFMVDVT NVPGVHKGDE AVIFGPGGVS LDQLAKWVGT IPYELMCLLS
     TRVPRKYTYT YTIKHYENNR F
//
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