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Database: UniProt/SWISS-PROT
Entry: ALR1_CLOAB
LinkDB: ALR1_CLOAB
Original site: ALR1_CLOAB 
ID   ALR1_CLOAB              Reviewed;         386 AA.
AC   Q97LR2;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   28-FEB-2018, entry version 105.
DE   RecName: Full=Alanine racemase 1 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr1; OrderedLocusNames=CA_C0492;
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: L-alanine = D-alanine. {ECO:0000255|HAMAP-
CC       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; AAK78472.1; -; Genomic_DNA.
DR   PIR; E96960; E96960.
DR   RefSeq; NP_347132.1; NC_003030.1.
DR   RefSeq; WP_010963814.1; NC_003030.1.
DR   ProteinModelPortal; Q97LR2; -.
DR   SMR; Q97LR2; -.
DR   STRING; 272562.CA_C0492; -.
DR   EnsemblBacteria; AAK78472; AAK78472; CA_C0492.
DR   GeneID; 1116675; -.
DR   KEGG; cac:CA_C0492; -.
DR   PATRIC; fig|272562.8.peg.691; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; WRGPILL; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
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; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    386       Alanine racemase 1.
FT                                /FTId=PRO_0000114509.
FT   ACT_SITE     38     38       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    267    267       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     136    136       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     315    315       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      38     38       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   386 AA;  43736 MW;  3EBADBE597A4D41B CRC64;
     MFRHIRPVWA EIDLDNIAYN MQQIRRCSKS DEIIGVVKAD AYGHGAVDVA PVLLENGANR
     LAVAVISEAV ELRKSGIQCP IMILGYTPLS LVDSIIKYSI EQTVFSYDYA EKLSEAARQK
     NITLRIHIAL DTGMGRIGFL PTEESVWEVY KISKLSNIII EGIFSHFSTS DETNKEYTYA
     QLKKFEWFYN ELRKKNIKIN IRHIGNSAAI MELPETHFEA TRPGIILYGY YPSNEVDKNK
     LNLKPIMTLK TNVVHIKKMM PGEYVSYGRK FKCERESIIA TLPVGYADGY TRMLSGKAKV
     IINGNYAPVI GRICMDQCMI DITDLPSVQV GDEVVIMGES DDKKFTADDM AEIIGTINYE
     VICMISKRVP RVYIKNGEVV KIRNYV
//
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