ALR3_SALTI
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 03-AUG-2022, entry version 131.
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., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT 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., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000255|HAMAP-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-alanine
CC from L-alanine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000255|HAMAP-
CC Rule:MF_01201}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_WSUR01000010.1.
DR AlphaFoldDB; Q8Z300; -.
DR SMR; Q8Z300; -.
DR STRING; 220341.16504635; -.
DR EnsemblBacteria; AAO71021; AAO71021; t3513.
DR KEGG; stt:t3513; -.
DR KEGG; sty:STY3763; -.
DR PATRIC; fig|220341.7.peg.3838; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_1_1_6; -.
DR OMA; HMTHFSD; -.
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 Isomerase; Pyridoxal phosphate.
FT CHAIN 1..368
FT /note="Alanine racemase 3"
FT /id="PRO_0000114562"
FT ACT_SITE 42
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT ACT_SITE 262
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01201"
FT MOD_RES 42
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="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
