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Database: UniProt
Entry: Q9ZAH5
LinkDB: Q9ZAH5
Original site: Q9ZAH5 
ID   ALR1_STAA8              Reviewed;         382 AA.
AC   Q9ZAH5; Q2FWI6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   13-FEB-2019, entry version 119.
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; Synonyms=alr; OrderedLocusNames=SAOUHSC_02305;
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=9756984; DOI=10.1016/S0378-1119(98)00404-1;
RA   Kullik I., Jenni R., Berger-Baechi B.;
RT   "Sequence of the putative alanine racemase operon in Staphylococcus
RT   aureus: insertional interruption of this operon reduces D-alanine
RT   substitution of lipoteichoic acid and autolysis.";
RL   Gene 219:9-17(1998).
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}.
DR   EMBL; Y16431; CAA76221.1; -; Genomic_DNA.
DR   EMBL; CP000253; ABD31339.1; -; Genomic_DNA.
DR   RefSeq; WP_001281145.1; NZ_LS483365.1.
DR   RefSeq; YP_500784.1; NC_007795.1.
DR   ProteinModelPortal; Q9ZAH5; -.
DR   SMR; Q9ZAH5; -.
DR   STRING; 93061.SAOUHSC_02305; -.
DR   PRIDE; Q9ZAH5; -.
DR   EnsemblBacteria; ABD31339; ABD31339; SAOUHSC_02305.
DR   GeneID; 3920930; -.
DR   KEGG; sao:SAOUHSC_02305; -.
DR   PATRIC; fig|93061.5.peg.2089; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031444; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   BioCyc; GCF_000013425:G1I0R-2177-MONOMER; -.
DR   BioCyc; SAUR93061:G1G5Y-2177-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   PRO; PR:Q9ZAH5; -.
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; 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    382       Alanine racemase 1.
FT                                /FTId=PRO_0000114573.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   382 AA;  42823 MW;  52B3C88E9811956D CRC64;
     MSDKYYRSAY MNVDLNAVAS NFKVFSTLHP NKTVMAVVKA NAYGLGSVKV ARHLMENGAT
     FFAVATLDEA IELRMHGITA KILVLGVLPA KDIDKAIQHR VALTVPSKQW LKEAIKNISG
     EQEKKLWLHI KLDTGMGRLG IKDTKTYQEV IEIIQQYEQL VFEGVFTHFA CADEPGDMTT
     EQYQRFKDMV NEAIKPEYIH CQNSAGSLLM DCQFCNAIRP GISLYGYYPS EYVQQKVKVH
     LKPSVQLIAN VVQTKTLQAG ESVSYGATYT ATDPTTIALL PIGYADGYLR IMQGSFVNVN
     GHQCEVIGRV CMDQTIVKVP DQVKAGDSVI LIDNHRESPQ SVEVVAEKQH TINYEVLCNL
     SRRLPRIYHD GDQRFVTNEL LK
//
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