GenomeNet

Database: UniProt
Entry: Q8Z300
LinkDB: Q8Z300
Original site: Q8Z300 
ID   ALR3_SALTI              Reviewed;         368 AA.
AC   Q8Z300;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 1.
DT   13-FEB-2019, entry version 119.
DE   RecName: Full=Alanine racemase 3 {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr3; OrderedLocusNames=STY3763, t3513;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA   Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA   Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA   Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA   Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA   Whitehead S., Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella
RT   enterica serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA   Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT   and CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD09518.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71021.1; -; Genomic_DNA.
DR   RefSeq; NP_457948.1; NC_003198.1.
DR   RefSeq; WP_000976816.1; NZ_UFRG01000003.1.
DR   ProteinModelPortal; Q8Z300; -.
DR   SMR; Q8Z300; -.
DR   STRING; 220341.STY3763; -.
DR   EnsemblBacteria; AAO71021; AAO71021; t3513.
DR   EnsemblBacteria; CAD09518; CAD09518; CAD09518.
DR   GeneID; 1250019; -.
DR   KEGG; stt:t3513; -.
DR   KEGG; sty:STY3763; -.
DR   PATRIC; fig|220341.7.peg.3838; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000031445; -.
DR   KO; K01775; -.
DR   BioCyc; GCF_001048035:AC754_RS23865-MONOMER; -.
DR   BioCyc; GCF_001048375:AC768_RS24065-MONOMER; -.
DR   BioCyc; GCF_001079465:ADV44_RS24635-MONOMER; -.
DR   BioCyc; GCF_001088345:AEZ18_RS00115-MONOMER; -.
DR   BioCyc; GCF_001095585:AD238_RS23465-MONOMER; -.
DR   BioCyc; GCF_001104165:AE704_RS22935-MONOMER; -.
DR   BioCyc; GCF_001104885:AEZ38_RS06575-MONOMER; -.
DR   BioCyc; GCF_001106745:AE121_RS24660-MONOMER; -.
DR   BioCyc; GCF_001118185:AE086_RS23745-MONOMER; -.
DR   BioCyc; GCF_001119245:AE140_RS23635-MONOMER; -.
DR   BioCyc; GCF_001121865:AE338_RS03065-MONOMER; -.
DR   BioCyc; GCF_001127485:AE735_RS24125-MONOMER; -.
DR   BioCyc; GCF_001135805:AEG73_RS23925-MONOMER; -.
DR   BioCyc; GCF_001148125:AEN24_RS22735-MONOMER; -.
DR   BioCyc; GCF_001148305:AEN67_RS00120-MONOMER; -.
DR   BioCyc; GCF_001157245:AER93_RS23235-MONOMER; -.
DR   BioCyc; GCF_001163025:AFA50_RS24410-MONOMER; -.
DR   BioCyc; GCF_001165785:AFA97_RS23945-MONOMER; -.
DR   BioCyc; GCF_001240865:ALC23_RS00145-MONOMER; -.
DR   BioCyc; GCF_001356455:AQJ76_RS23935-MONOMER; -.
DR   BioCyc; GCF_001357935:AQL34_RS14030-MONOMER; -.
DR   BioCyc; GCF_001359015:AQL50_RS13940-MONOMER; -.
DR   BioCyc; GCF_001360555:AQK88_RS23735-MONOMER; -.
DR   BioCyc; GCF_001361075:AQM75_RS01275-MONOMER; -.
DR   BioCyc; GCF_001362095:AQO19_RS24250-MONOMER; -.
DR   BioCyc; GCF_001362135:AQN73_RS00235-MONOMER; -.
DR   BioCyc; GCF_001362175:AQN68_RS23935-MONOMER; -.
DR   BioCyc; GCF_001362195:AQN87_RS11835-MONOMER; -.
DR   BioCyc; GCF_001362335:AQN99_RS00340-MONOMER; -.
DR   BioCyc; GCF_001364695:AQQ97_RS14565-MONOMER; -.
DR   BioCyc; GCF_900185485:CDZ80_RS00895-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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.
FT   CHAIN         1    368       Alanine racemase 3.
FT                                /FTId=PRO_0000114562.
FT   ACT_SITE     42     42       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    262    262       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     141    141       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     310    310       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      42     42       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   368 AA;  39778 MW;  1338A6D2936004B3 CRC64;
     MMKLAEIQAA CGVLCVDLAA VVDNYQTLAR HVAPAQCGAV LKANGYGLGA EAIAPALYAA
     NCRIFFVAQL SEGVALRNIL SADAMVVLLN GVMPQAMPFC CAQQITPLLN SVDQVMTWLA
     LQEARSQRRP VLIQLDSGMS RLGVTPEQLA RLAAIFRQRG WAAPDYIISH LANADRPDHA
     LNVYQHTLLQ QAKKAFPTSR YSLANSCGMF LHPAWREDLC RPGVALFGVA QPWFSTPLKP
     AFTLTLTILR VQDVPVGTPI GYGSTVTTTR PLRIATVSAG YADGIPRNLR PPAGVCWRGV
     RLPVLGRVCM DSFMVDASAI MPTSGDVVEF IGVSQTLEEV AAACDTIPYE IMARLGARFR
     RIMQPAEA
//
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