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Database: UniProt/TrEMBL
Entry: D7ARI7_THEM3
LinkDB: D7ARI7_THEM3
Original site: D7ARI7_THEM3 
ID   D7ARI7_THEM3            Unreviewed;       385 AA.
AC   D7ARI7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-SEP-2017, entry version 60.
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=Tmath_1831 {ECO:0000313|EMBL:ADH61529.1};
OS   Thermoanaerobacter mathranii subsp. mathranii (strain DSM 11426 / CIP
OS   108742 / A3).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=583358 {ECO:0000313|EMBL:ADH61529.1, ECO:0000313|Proteomes:UP000002064};
RN   [1] {ECO:0000313|EMBL:ADH61529.1, ECO:0000313|Proteomes:UP000002064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11426 / CIP 108742 / A3
RC   {ECO:0000313|Proteomes:UP000002064};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhou J., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter mathranii subsp. mathranii
RT   mathranii str. A3.";
RL   Submitted (MAY-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; CP002032; ADH61529.1; -; Genomic_DNA.
DR   RefSeq; WP_013150747.1; NC_014209.1.
DR   ProteinModelPortal; D7ARI7; -.
DR   EnsemblBacteria; ADH61529; ADH61529; Tmath_1831.
DR   KEGG; tmt:Tmath_1831; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   BioCyc; TMAT583358:GHOX-1797-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002064; 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:UP000002064};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:ADH61529.1};
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;  43348 MW;  A129114359CE70E4 CRC64;
     MFDNIRPTRA EIYLDNIAHN LSEVKRWVGK KVKIMGVVKA NAYGHGACHV AKVLVENGVC
     YLGVATIEEA LELRECGINI PILVFGYTPL TQAEELIVHN ITQTVFDINY VEDLEKIALN
     VGKKAKVHVK IDTGMGRIGY TDLKVAEKEI EKMMEMEGVE VEGIFSHFAT SDEKDKSYAE
     QQFDMFKKLL ERLKEKRINI PLKHMANSGA IIDLKYTYLD MVRPGIVLYG SYPSEEVKRP
     LDLRQTMGFK TKIVYIKEVP EGTSISYGKT FITKRKSKIA TLPVGYADGF NRLLSNNYHV
     LVKGKYAAVV GRICMDQTMI DVTDIEGVEV GDDVIIFGNQ EGEKITAEEI AKKLNTIPYE
     VYCGISSRVP RIYIYKGKVV GEKII
//
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