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Database: UniProt
Entry: Q97DY9
LinkDB: Q97DY9
Original site: Q97DY9 
ID   ALR2_CLOAB              Reviewed;         395 AA.
AC   Q97DY9;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JAN-2019, entry version 110.
DE   RecName: Full=Alanine racemase 2 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr2; OrderedLocusNames=CA_C3331;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG
OS   5710 / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81263.1; -; Genomic_DNA.
DR   PIR; D97309; D97309.
DR   RefSeq; NP_349923.1; NC_003030.1.
DR   RefSeq; WP_010966603.1; NC_003030.1.
DR   ProteinModelPortal; Q97DY9; -.
DR   SMR; Q97DY9; -.
DR   STRING; 272562.CA_C3331; -.
DR   EnsemblBacteria; AAK81263; AAK81263; CA_C3331.
DR   GeneID; 1119513; -.
DR   KEGG; cac:CA_C3331; -.
DR   PATRIC; fig|272562.8.peg.3511; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; VHLEYEN; -.
DR   OrthoDB; 859043at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000814; 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    395       Alanine racemase 2.
FT                                /FTId=PRO_0000114510.
FT   ACT_SITE     60     60       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    288    288       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     158    158       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     332    332       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      60     60       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   395 AA;  44613 MW;  1A13F287C5C7CE43 CRC64;
     MEKKTVYNIT NSIAISEEEA VNCNIPEVNK AEINLSQLKR NFDIIQGFLK PNTKFMAVLK
     GDAYGHGIRP IAKELINLKC DVFGVVRLIE AFTLRKAGIK TPIMLLAPIS PSQAAWVIRY
     NIIPMVDSEE IVEALDQSAS QNDTIVKLHV KINTGLNRYG VNPENAVKFI REIHEKYLHV
     QVDGVYTHFQ DPDYNPDFTH KQIECFNNII FQLQKQKLRP RIIHAANSTG IIRYPEAHYD
     MVRCGTLLFG LEHEQGQRNM PKGIKTLMEL KGRIMKVRTI RAGEAGGYGS TFVAKKDSKV
     AIIAFGYGDG ISRGWKEVLV AGKRVPVVNY FMDGLMVDIS NIDETVKELD EAVIVGNQGD
     ESITWLEACK SLGSYVDEQI QCITERVPKK YFYEK
//
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