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Database: UniProt
Entry: Q8X5V2
LinkDB: Q8X5V2
Original site: Q8X5V2 
ID   ALR1_ECO57              Reviewed;         359 AA.
AC   Q8X5V2;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   13-FEB-2019, entry version 120.
DE   RecName: Full=Alanine racemase, biosynthetic;
DE            EC=5.1.1.1;
GN   Name=alr; OrderedLocusNames=Z5651, ECs5035;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. Provides the D-alanine required for cell wall
CC       biosynthesis (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000305}.
DR   EMBL; AE005174; AAG59251.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38458.1; -; Genomic_DNA.
DR   PIR; C91258; C91258.
DR   PIR; G86098; G86098.
DR   RefSeq; NP_313062.1; NC_002695.1.
DR   RefSeq; WP_001147332.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; Q8X5V2; -.
DR   SMR; Q8X5V2; -.
DR   STRING; 155864.Z5651; -.
DR   EnsemblBacteria; AAG59251; AAG59251; Z5651.
DR   EnsemblBacteria; BAB38458; BAB38458; BAB38458.
DR   GeneID; 914300; -.
DR   KEGG; ece:Z5651; -.
DR   KEGG; ecs:ECs5035; -.
DR   PATRIC; fig|386585.9.peg.5258; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031446; -.
DR   KO; K01775; -.
DR   BioCyc; ECOO157:ALR-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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   Cell shape; Cell wall biogenesis/degradation; Complete proteome;
KW   Isomerase; Peptidoglycan synthesis; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    359       Alanine racemase, biosynthetic.
FT                                /FTId=PRO_0000114516.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000250}.
FT   ACT_SITE    255    255       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000250}.
FT   BINDING     129    129       Substrate. {ECO:0000250}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   359 AA;  39195 MW;  1CB591F0CE42B948 CRC64;
     MQAATVVINR RALRHNLQRL RELAPASKMV AVVKANAYGH GLLETARTLP DADAFGVARL
     EEALRLRAGG ITKPVLLLEG FFDARDLPTI SAQHFHTAVH NEEQLAALEE ASLDEPVTVW
     MKLDTGMHRL GVRPEQAEAF YHRLTQCKNV RQPVNIVSHF ARADEPKCGA TEKQLAIFNT
     FCEGKPGQRS IAASGGILLW PQSHFDWVRP GIILYGVSPL EDRSTGADFG CQPVMSLTSS
     LIAVREHKVG EPVGYGGTWI SERDTRLGVV AMGYGDGYPR AAPSGTPVLV NGREVPIVGR
     VAMDMICVDL GPQAQDKAGD PVILWGEGLP VERIAEMTKV SAYELITRLT SRVAMKYVD
//
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