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Database: UniProt
Entry: Q9EZ08
LinkDB: Q9EZ08
Original site: Q9EZ08 
ID   ALR2_STAA8              Reviewed;         361 AA.
AC   Q9EZ08; Q2FYN5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   13-FEB-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; Synonyms=dal; OrderedLocusNames=SAOUHSC_01400;
OS   Staphylococcus aureus (strain NCTC 8325).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11447207; DOI=10.1128/IAI.69.8.5198-5202.2001;
RA   Wiltshire M.D., Foster S.J.;
RT   "Identification and analysis of Staphylococcus aureus components
RT   expressed by a model system of growth in serum.";
RL   Infect. Immun. 69:5198-5202(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA   Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
RL   Washington D.C. (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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG42250.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF306669; AAG42250.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP000253; ABD30494.1; -; Genomic_DNA.
DR   RefSeq; WP_000127593.1; NZ_LS483365.1.
DR   RefSeq; YP_499927.1; NC_007795.1.
DR   ProteinModelPortal; Q9EZ08; -.
DR   STRING; 93061.SAOUHSC_01400; -.
DR   PRIDE; Q9EZ08; -.
DR   EnsemblBacteria; ABD30494; ABD30494; SAOUHSC_01400.
DR   GeneID; 3920690; -.
DR   KEGG; sao:SAOUHSC_01400; -.
DR   PATRIC; fig|93061.5.peg.1281; -.
DR   eggNOG; ENOG4108XFP; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000280025; -.
DR   KO; K01775; -.
DR   OMA; VHLEYEN; -.
DR   BioCyc; GCF_000013425:G1I0R-1308-MONOMER; -.
DR   BioCyc; SAUR93061:G1G5Y-1308-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   PRO; PR:Q9EZ08; -.
DR   Proteomes; UP000008816; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    361       Alanine racemase 2.
FT                                /FTId=PRO_0000114579.
FT   ACT_SITE     30     30       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    256    256       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     122    122       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     303    303       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      30     30       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   361 AA;  41410 MW;  1EB1C133B086F5CA CRC64;
     MTATWSVNKK IFLQNAITVK NNQPLMAVVK NNAYHYDLEF AVTQFIHAGI DTFSTTSLRE
     AIQIRQLAPD ATIFLMNAVY EFDLVREHQI HMTLPSLTYY YNHKNDLAGI HVHLEFENLL
     HRSGFKDLNE IKEVLKDHHH NQNAKMIISG LWTHFGYADE FDVSDYNVER SQWMEIVEAL
     LSEGYQFDLI HAQNSASFYR EGQILLPHHT HARVGIALYG SRPYSSLNQH DIVQSLTLKA
     HVIQVREVQA GDYCGYSFAF EVTKNNTKLA VVDIGYGDGI LRTRAKHEAL INGKRYPIRA
     LMMSHMFVEV DGNVHAQDEV ILYNNDIRID EYTFKGVGAN SEQLSAMNHD SLKKEYISND
     C
//
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