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Database: UniProt/TrEMBL
Entry: A5I7C2_CLOBH
LinkDB: A5I7C2_CLOBH
Original site: A5I7C2_CLOBH 
ID   A5I7C2_CLOBH            Unreviewed;       386 AA.
AC   A5I7C2; A7G8K6;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   27-SEP-2017, entry version 93.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=alr {ECO:0000313|EMBL:CAL84957.1};
GN   OrderedLocusNames=CBO3397 {ECO:0000313|EMBL:CAL84957.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL84957.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J.,
RA   Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T.,
RA   Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N.,
RA   Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E.,
RA   Sanders M., Simmonds M., White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum
RT   strain Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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; AM412317; CAL84957.1; -; Genomic_DNA.
DR   RefSeq; WP_012048315.1; NC_009698.1.
DR   RefSeq; YP_001255879.1; NC_009495.1.
DR   RefSeq; YP_001389121.1; NC_009698.1.
DR   ProteinModelPortal; A5I7C2; -.
DR   GeneID; 5186557; -.
DR   GeneID; 5401733; -.
DR   KEGG; cbh:CLC_3341; -.
DR   KEGG; cbo:CBO3397; -.
DR   PATRIC; fig|413999.7.peg.3373; -.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001986; 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:UP000001986};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647, ECO:0000313|EMBL:CAL84957.1};
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:UP000001986}.
FT   DOMAIN      246    374       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    267    267       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     315    315       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   386 AA;  43175 MW;  712F9A140EF3F3A3 CRC64;
     MFRNLRAVWA EIDLDNLQHN LKQIKKICGN KEIIGVIKAN AYGHGAMEIA PTLLENGVSR
     LAVAVLSEAM ELRMSGVKEP IMILGYTPWA LGDMLLDNDI EQSVYSYNDA LELSKIAVLK
     RKILKIHIVV DTGMGRIGFL PTKESVEDVY KISKLPNIEI EGIFSHFSSA DESDKDYTLY
     QMNKYNAFIN KLEEKNIQVP IKHIANSAAI IDLENTHLDA VRAGIIMYGY YPSNYVLRNN
     INLKPVMSLK TSIVHIKKVS SGEYISYGRT FKTKRESIIA TLPIGYADGY NRLLSNKGKV
     IVNGKLAPVI GRVCMDQCMI DVTFIENLKV GDVVTIMGEE NGVSYTAEDI ASQIGTISYE
     VICNVNKRVP RVYKKDGKII NVVNYI
//
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