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Database: UniProt
Entry: P9WQA8
LinkDB: P9WQA8
Original site: P9WQA8 
ID   ALR_MYCTO               Reviewed;         386 AA.
AC   P9WQA8; L0TFK3; P0A4X2; Q50705;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   16-JAN-2019, entry version 24.
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=MT3532;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE000516; AAK47870.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70738; D70738.
DR   ProteinModelPortal; P9WQA8; -.
DR   SMR; P9WQA8; -.
DR   EnsemblBacteria; AAK47870; AAK47870; MT3532.
DR   KEGG; mtc:MT3532; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001020; 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    386       Alanine racemase.
FT                                /FTId=PRO_0000426808.
FT   ACT_SITE     44     44       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    273    273       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     142    142       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     321    321       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      44     44       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   386 AA;  40926 MW;  806225696ACB0BFE CRC64;
     MAMTPISQTP GLLAEAMVDL GAIEHNVRVL REHAGHAQLM AVVKADGYGH GATRVAQTAL
     GAGAAELGVA TVDEALALRA DGITAPVLAW LHPPGIDFGP ALLADVQVAV SSLRQLDELL
     HAVRRTGRTA TVTVKVDTGL NRNGVGPAQF PAMLTALRQA MAEDAVRLRG LMSHMVYADK
     PDDSINDVQA QRFTAFLAQA REQGVRFEVA HLSNSSATMA RPDLTFDLVR PGIAVYGLSP
     VPALGDMGLV PAMTVKCAVA LVKSIRAGEG VSYGHTWIAP RDTNLALLPI GYADGVFRSL
     GGRLEVLING RRCPGVGRIC MDQFMVDLGP GPLDVAEGDE AILFGPGIRG EPTAQDWADL
     VGTIHYEVVT SPRGRITRTY REAENR
//
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