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Database: UniProt
Entry: Q9ZE52
LinkDB: Q9ZE52
Original site: Q9ZE52 
ID   ALR_RICPR               Reviewed;         404 AA.
AC   Q9ZE52;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   05-DEC-2018, entry version 116.
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=RP095;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O.,
RA   Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K.,
RA   Eriksson A.-S., Winkler H.H., Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
RN   [2]
RP   DOMAIN RPE1.
RX   PubMed=11030655; DOI=10.1126/science.290.5490.347;
RA   Ogata H., Audic S., Barbe V., Artiguenave F., Fournier P.-E.,
RA   Raoult D., Claverie J.-M.;
RT   "Selfish DNA in protein-coding genes of Rickettsia.";
RL   Science 290:347-350(2000).
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; AJ235270; CAA14565.1; -; Genomic_DNA.
DR   PIR; F71718; F71718.
DR   RefSeq; NP_220488.1; NC_000963.1.
DR   RefSeq; WP_004599740.1; NC_000963.1.
DR   ProteinModelPortal; Q9ZE52; -.
DR   SMR; Q9ZE52; -.
DR   STRING; 272947.RP095; -.
DR   EnsemblBacteria; CAA14565; CAA14565; CAA14565.
DR   GeneID; 883682; -.
DR   KEGG; rpr:RP095; -.
DR   PATRIC; fig|272947.5.peg.95; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; SGAAMYH; -.
DR   BioCyc; RPRO272947:G1GT0-96-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000002480; 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; -; 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   InterPro; IPR005728; Rickett_RPE.
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; TIGR01045; RPE1; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    404       Alanine racemase.
FT                                /FTId=PRO_0000114557.
FT   DOMAIN      226    273       RPE1 insert.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    298    298       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     133    133       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     346    346       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      34     34       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   404 AA;  44730 MW;  FEA23D86698256DA CRC64;
     MSLCTLEINL SAIKNNYRLL QDICKTALVG AVVKANGYGL GAMQIAKALI KENCQYFFVA
     TSEEGINLRK VLNNDITILV LNGVFTHDAL ELIQYNLTPV LNNLSQIEIW QKFSNLKGKI
     LPCYLHFNTG LNRFGLNSDE IEQLINDRDL LKGLDLQYII SHLAASEETG NPYNLIQLNR
     FKVYLEYFPN VKASFANSGG IFLGQDYHFD LARPGAALYG LNSLIEVSSN LSYTEEFESN
     TAALTTTACI NKCPDVSVRL TPKLPLKGSY TVRLQNPVTL KAPIIDLQNL TLDSHIGYNM
     TFTTKRDSVI ATLPLGYADG FSRNFSSQGE VFINSCSVPI VGRVSMDLIN IDVTDLPPSE
     VFLGQEAEII GNYCTPDKIA SIIGTIGYEV LTSLGSRYKR KYIS
//
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