GenomeNet

Database: UniProt
Entry: Q8RGA2
LinkDB: Q8RGA2
Original site: Q8RGA2 
ID   ALR_FUSNN               Reviewed;         354 AA.
AC   Q8RGA2;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   05-DEC-2018, entry version 107.
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=FN0406;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP
OS   101130 / JCM 8532 / LMG 13131).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131;
RX   PubMed=11889109; DOI=10.1128/JB.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L.,
RA   Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A.,
RA   Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R.,
RA   Fonstein M., Kyrpides N.C., Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium
RT   nucleatum strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL94609.1; -; Genomic_DNA.
DR   RefSeq; NP_603310.1; NC_003454.1.
DR   RefSeq; WP_011016367.1; NC_003454.1.
DR   ProteinModelPortal; Q8RGA2; -.
DR   SMR; Q8RGA2; -.
DR   STRING; 190304.FN0406; -.
DR   EnsemblBacteria; AAL94609; AAL94609; FN0406.
DR   GeneID; 991792; -.
DR   KEGG; fnu:FN0406; -.
DR   PATRIC; fig|190304.8.peg.981; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   InParanoid; Q8RGA2; -.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; FNUC190304:G1FZS-1000-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002521; 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    354       Alanine racemase.
FT                                /FTId=PRO_0000114520.
FT   ACT_SITE     33     33       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    251    251       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     127    127       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     299    299       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   354 AA;  39835 MW;  A6BFD3D8D049F0E4 CRC64;
     MRTWIEIDKE NLKYNVLKLK EIANNKEILG VVKANAYGLG SIEIAKILKE VEVKLFGVAN
     LEEAIELQEA GIKDKILILG ASFEDELVEA TKRGVHVAIS SMGQLQFLVS KNLNPNIHLK
     FDTGMTRLGF EVDDAEKVIE YCKNNNLNLV GIFSHLSDSD GNTIETKNFT LEQIEKFKKI
     VNSLNLEYIH ISNSAGITNF HNDILGNLVR LGIGMYSFTG NKKTPYLKNI FTIKSKILFI
     KKVKKDSFVS YGRHYTLPAD STYAVLPIGY ADGLKKYLSK GGYVLINNHR CEIIGNICMD
     MTMIRVPKEI ENSIKIGDEV TVINADILDN LNIPELCVWE FMTGIGRRVK RIIV
//
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