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Database: UniProt/TrEMBL
Entry: D3T4E6_THEIA
LinkDB: D3T4E6_THEIA
Original site: D3T4E6_THEIA 
ID   D3T4E6_THEIA            Unreviewed;       385 AA.
AC   D3T4E6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   28-FEB-2018, entry version 63.
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=Thit_1856 {ECO:0000313|EMBL:ADD03098.1};
OS   Thermoanaerobacter italicus (strain DSM 9252 / Ab9).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=580331 {ECO:0000313|EMBL:ADD03098.1, ECO:0000313|Proteomes:UP000001552};
RN   [1] {ECO:0000313|EMBL:ADD03098.1, ECO:0000313|Proteomes:UP000001552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9252 / Ab9 {ECO:0000313|Proteomes:UP000001552};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter italicus Ab9.";
RL   Submitted (FEB-2010) 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; CP001936; ADD03098.1; -; Genomic_DNA.
DR   RefSeq; WP_012995809.1; NC_013921.1.
DR   ProteinModelPortal; D3T4E6; -.
DR   STRING; 580331.Thit_1856; -.
DR   EnsemblBacteria; ADD03098; ADD03098; Thit_1856.
DR   KEGG; tit:Thit_1856; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   OrthoDB; POG091H022F; -.
DR   BioCyc; TITA580331:G1GHL-1889-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001552; 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; -; 2.
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:UP000001552};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADD03098.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456}.
FT   DOMAIN      246    374       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   385 AA;  43263 MW;  84290DA878A3FB2A CRC64;
     MFDNIRPTRA EIYLDNIVHN LSEVKRWVGK KVKIMGVVKA NAYGHGACHV AKVLVENGVC
     YLGVATIEEA LELRECGINI PILVFGYTPL TQAEELIVHN ITQTVFDINY VEDLEKIALK
     VGKKAKVHVK IDTGMGRIGY TDLKVAEKEI EKMMEMEGVE VEGIFSHFAT SDEKDKSYAE
     QQFDMFKKLL ERLKEKGINI PLKHMANSGA IIDLKYTYLD MVRPGIVLYG SYPSEEVKRP
     LDLKQTMGFK TKIVYIKEVP EGTSISYGKT FITKRKSKIA TLPVGYADGF NRLLSNNYHV
     LVKGKYAAVV GRICMDQTMI DVTDIEGVEV GDDVIIFGNQ EGEKITAEEI AKKLNTIPYE
     VYCGISSRVP RIYIYKGKVV GEKII
//
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