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Database: UniProt
Entry: A0PY95
LinkDB: A0PY95
Original site: A0PY95 
ID   ALR_CLONN               Reviewed;         387 AA.
AC   A0PY95;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JAN-2019, entry version 76.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=NT01CX_1264;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A.,
RA   Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W.,
RA   Vogelstein B., Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium
RT   novyi-NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61810.1; -; Genomic_DNA.
DR   RefSeq; WP_011721355.1; NC_008593.1.
DR   ProteinModelPortal; A0PY95; -.
DR   SMR; A0PY95; -.
DR   STRING; 386415.NT01CX_1264; -.
DR   PRIDE; A0PY95; -.
DR   EnsemblBacteria; ABK61810; ABK61810; NT01CX_1264.
DR   GeneID; 4540795; -.
DR   KEGG; cno:NT01CX_1264; -.
DR   PATRIC; fig|386415.7.peg.374; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; CNOV386415:G1G6M-394-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008220; 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    387       Alanine racemase.
FT                                /FTId=PRO_1000065979.
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   387 AA;  43171 MW;  523B69FF5F59C7D3 CRC64;
     MFKHLRPVWA EINLDNLASN MKHIKELSNT KEIIGIVKAD AYGHGALDIV PTLIENGATA
     LAVAVVSEGV ELRRGGIECP IMVLGFTPPS LIDMLLKHDI EQTVFSLDYA KELSKAAEKM
     HKVAKIHIAV DTGMGRIGFL PNEQSIQDVK AISMLPNIKI KGMFSHFSTA DEKNKEYSAY
     QLNQFNKFYE GLKRENVNIE TRHISNSAAI MDLPETIFEG VRPGIILYGY YPSNEVDKTK
     LELKPVMQLK TNVVHIKKIP SGEYISYGRK FKTDRESLIA TLPVGYADGY TRLLFGKAKV
     IINGQLAPVV GRICMDQCMV DITDIKGDIK VGEEVILIGE KNGVKIDADD IAEMLGTINY
     EVICMISKRV PRVYIKNGEV IKVRNYI
//
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