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Database: UniProt
Entry: P9WQA9
LinkDB: P9WQA9
Original site: P9WQA9 
ID   ALR_MYCTU               Reviewed;         386 AA.
AC   P9WQA9; L0TFK3; P0A4X2; Q50705;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   13-FEB-2019, entry version 34.
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=Rv3423c; ORFNames=MTCY78.06;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11267762; DOI=10.1111/j.1574-6968.2001.tb10547.x;
RA   Strych U., Penland R.L., Jimenez M., Krause K.L., Benedik M.J.;
RT   "Characterization of the alanine racemases from two Mycobacteria.";
RL   FEMS Microbiol. Lett. 196:93-98(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, SUBUNIT, COFACTOR, AND PYRIDOXAL PHOSPHATE AT LYS-44.
RX   PubMed=15683232; DOI=10.1021/bi0486583;
RA   LeMagueres P., Im H., Ebalunode J., Strych U., Benedik M.J.,
RA   Briggs J.M., Kohn H., Krause K.L.;
RT   "The 1.9 A crystal structure of alanine racemase from Mycobacterium
RT   tuberculosis contains a conserved entryway into the active site.";
RL   Biochemistry 44:1471-1481(2005).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. D-alanine plays a key role in peptidoglycan cross-
CC       linking. {ECO:0000269|PubMed:11267762}.
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         ECO:0000269|PubMed:11267762};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201,
CC         ECO:0000269|PubMed:15683232};
CC   -!- ACTIVITY REGULATION: Inhibited by the antituberculous drug D-
CC       cycloserine (DCS), which is a structural analog of D-alanine.
CC       {ECO:0000269|PubMed:11267762}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 mM for D-alanine {ECO:0000269|PubMed:11267762};
CC         KM=1.2 mM for L-alanine {ECO:0000269|PubMed:11267762};
CC         Vmax=0.46 umol/min/mg enzyme toward D-alanine
CC         {ECO:0000269|PubMed:11267762};
CC         Vmax=0.51 umol/min/mg enzyme toward L-alanine
CC         {ECO:0000269|PubMed:11267762};
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:0000269|PubMed:15683232}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD51033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CCP46245.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AF172731; AAD51033.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL123456; CCP46245.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70738; D70738.
DR   RefSeq; NP_217940.1; NC_000962.3.
DR   PDB; 1XFC; X-ray; 1.90 A; A/B=3-386.
DR   PDBsum; 1XFC; -.
DR   ProteinModelPortal; P9WQA9; -.
DR   SMR; P9WQA9; -.
DR   STRING; 83332.Rv3423c; -.
DR   ChEMBL; CHEMBL2031; -.
DR   PaxDb; P9WQA9; -.
DR   EnsemblBacteria; CCP46245; CCP46245; Rv3423c.
DR   GeneID; 887634; -.
DR   KEGG; mtu:Rv3423c; -.
DR   PATRIC; fig|83332.12.peg.3820; -.
DR   TubercuList; Rv3423c; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   BioCyc; MTBH37RV:G185E-7700-MONOMER; -.
DR   BRENDA; 5.1.1.1; 3445.
DR   UniPathway; UPA00042; UER00497.
DR   PRO; PR:P9WQA9; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IDA:MTBBASE.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:MTBBASE.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IDA:MTBBASE.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:MTBBASE.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Isomerase; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN         1    386       Alanine racemase.
FT                                /FTId=PRO_0000114539.
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:0000269|PubMed:15683232}.
FT   STRAND       14     19       {ECO:0000244|PDB:1XFC}.
FT   HELIX        20     34       {ECO:0000244|PDB:1XFC}.
FT   STRAND       37     42       {ECO:0000244|PDB:1XFC}.
FT   HELIX        44     48       {ECO:0000244|PDB:1XFC}.
FT   HELIX        52     61       {ECO:0000244|PDB:1XFC}.
FT   STRAND       66     70       {ECO:0000244|PDB:1XFC}.
FT   HELIX        72     80       {ECO:0000244|PDB:1XFC}.
FT   STRAND       87     89       {ECO:0000244|PDB:1XFC}.
FT   HELIX        99    103       {ECO:0000244|PDB:1XFC}.
FT   STRAND      107    110       {ECO:0000244|PDB:1XFC}.
FT   HELIX       113    126       {ECO:0000244|PDB:1XFC}.
FT   STRAND      130    136       {ECO:0000244|PDB:1XFC}.
FT   STRAND      142    145       {ECO:0000244|PDB:1XFC}.
FT   TURN        147    149       {ECO:0000244|PDB:1XFC}.
FT   HELIX       150    162       {ECO:0000244|PDB:1XFC}.
FT   STRAND      165    172       {ECO:0000244|PDB:1XFC}.
FT   HELIX       184    202       {ECO:0000244|PDB:1XFC}.
FT   STRAND      208    211       {ECO:0000244|PDB:1XFC}.
FT   HELIX       215    220       {ECO:0000244|PDB:1XFC}.
FT   HELIX       222    224       {ECO:0000244|PDB:1XFC}.
FT   STRAND      227    229       {ECO:0000244|PDB:1XFC}.
FT   HELIX       233    236       {ECO:0000244|PDB:1XFC}.
FT   HELIX       242    244       {ECO:0000244|PDB:1XFC}.
FT   STRAND      253    258       {ECO:0000244|PDB:1XFC}.
FT   STRAND      261    265       {ECO:0000244|PDB:1XFC}.
FT   STRAND      270    272       {ECO:0000244|PDB:1XFC}.
FT   HELIX       273    275       {ECO:0000244|PDB:1XFC}.
FT   STRAND      283    288       {ECO:0000244|PDB:1XFC}.
FT   HELIX       292    294       {ECO:0000244|PDB:1XFC}.
FT   HELIX       298    300       {ECO:0000244|PDB:1XFC}.
FT   TURN        301    303       {ECO:0000244|PDB:1XFC}.
FT   STRAND      305    308       {ECO:0000244|PDB:1XFC}.
FT   STRAND      311    317       {ECO:0000244|PDB:1XFC}.
FT   STRAND      324    332       {ECO:0000244|PDB:1XFC}.
FT   STRAND      340    344       {ECO:0000244|PDB:1XFC}.
FT   HELIX       354    361       {ECO:0000244|PDB:1XFC}.
FT   HELIX       365    369       {ECO:0000244|PDB:1XFC}.
FT   STRAND      376    381       {ECO:0000244|PDB:1XFC}.
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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