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Database: UniProt/TrEMBL
Entry: B3E7F8_GEOLS
LinkDB: B3E7F8_GEOLS
Original site: B3E7F8_GEOLS 
ID   B3E7F8_GEOLS            Unreviewed;       380 AA.
AC   B3E7F8;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-SEP-2017, entry version 79.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   OrderedLocusNames=Glov_2762 {ECO:0000313|EMBL:ACD96475.1};
OS   Geobacter lovleyi (strain ATCC BAA-1151 / DSM 17278 / SZ).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=398767 {ECO:0000313|EMBL:ACD96475.1, ECO:0000313|Proteomes:UP000002420};
RN   [1] {ECO:0000313|EMBL:ACD96475.1, ECO:0000313|Proteomes:UP000002420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1151 / DSM 17278 / SZ
RC   {ECO:0000313|Proteomes:UP000002420};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L.,
RA   Brettin T., Detter J.C., Han C., Tapia R., Kuske C.R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sung Y.,
RA   Fletcher K.E., Ritalahti K.M., Loeffler F.E., Richardson P.;
RT   "Complete sequence of chromosome of Geobacter lovleyi SZ.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001089; ACD96475.1; -; Genomic_DNA.
DR   RefSeq; WP_012470804.1; NC_010814.1.
DR   ProteinModelPortal; B3E7F8; -.
DR   STRING; 398767.Glov_2762; -.
DR   EnsemblBacteria; ACD96475; ACD96475; Glov_2762.
DR   KEGG; glo:Glov_2762; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; GLOV398767:GH32-2777-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002420; 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:UP000002420};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ACD96475.1};
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:UP000002420}.
FT   DOMAIN      247    376       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   380 AA;  41444 MW;  5F0E2EF1D97C0177 CRC64;
     MFDSRPTFAE IDLGALRENY SVVRSSVPSR SAVLAVVKAD AYGHGFLEVS KELERQGVDA
     FGVAFLAEAI QLRKAGIDKP VLLLGGIYPG QERKCVGYGI SSAVFSLEQL KALDLAAGKL
     YRKALVHLKV DTGMGRLGIP YDQVPALLNA LKLLPNIYLE GVISHFASAD ELDESGQYFT
     RLQGERFGWA VEQIRKAGFS PRYIHIANSA GALLNDYPFC NLVRPGIALY GALPSPDFQG
     RLSLRPVMRL KSKIAMLKWV EPATTISYGR RFTAEQRTLI ASVPVGYADG YPRALTNKGQ
     VLVRGERAQV SGTVCMDWLM LDVTHIPGVA VGDDVTLIGE DRKGNTVFAE EVAHWAGTIP
     YELLCGISKR VPRVYLGAGK
//
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