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Database: UniProt
Entry: Q4UNC8
LinkDB: Q4UNC8
Original site: Q4UNC8 
ID   ALR_RICFE               Reviewed;         462 AA.
AC   Q4UNC8;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JAN-2019, entry version 84.
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=RF_0079;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY60930.1; -; Genomic_DNA.
DR   RefSeq; WP_011270434.1; NC_007109.1.
DR   ProteinModelPortal; Q4UNC8; -.
DR   STRING; 315456.RF_0079; -.
DR   PRIDE; Q4UNC8; -.
DR   EnsemblBacteria; AAY60930; AAY60930; RF_0079.
DR   KEGG; rfe:RF_0079; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   OMA; VEILFIM; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; RFEL315456:G1G4G-132-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008548; 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; 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   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 2.
DR   TIGRFAMs; TIGR01045; RPE1; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate.
FT   CHAIN         1    462       Alanine racemase.
FT                                /FTId=PRO_0000272405.
FT   DOMAIN      286    332       RPE1 insert.
FT   REGION       73    132       Unknown insert.
FT   ACT_SITE     34     34       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    357    357       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     193    193       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     405    405       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   462 AA;  51764 MW;  B1739EA66F516316 CRC64;
     MSLCTLEINL SAIKNNYLLL QDICKTSLVG AAVKANGYGL GAVQISKALI EENCRHFFVA
     SSEEGVNLRK ALASWHESVF RHCEKNYTVI RRSNPVKNSV SQNFFNYFSG LQQCFAPRND
     GSSIHATTPK ALDNDVNILV LNGVFEHDAL ELIEYNLTPV LNNLKQIEIW QKFSNLKNRL
     LPCYLHFNTG INRLGLTHNE IEQLINNRDL LKGLDLQYII SHLAVSEEID NPYNLEQLNR
     FKTYLQYFPN VKASLANSGG IFLGQDYHFD LARPGAALYG LNPVIDLSNN LSYKEEFEGD
     TERRTAAYIN VREDSSTGST YKLPLEGGYS RGLQNPVTLK APIIHLQNLT LDSHIGYNMT
     FTTERDSVIA TLPLGYADGF SRNFSNQGEV FINGRSVPIV GRISMDLINI DVTDLPPLDI
     FLGQEAEIIG NYCTPDKIAS IIGTIGYEVL TSLGSRYKRI YK
//
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