GenomeNet

Database: UniProt
Entry: Q73NQ7
LinkDB: Q73NQ7
Original site: Q73NQ7 
ID   ALR_TREDE               Reviewed;         379 AA.
AC   Q73NQ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 89.
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=TDE_1095;
OS   Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / CIP 103919 / DSM 14222;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H.,
RA   Selengut J., Ren Q., Brinkac L.M., Madupu R., Kolonay J.F.,
RA   Durkin S.A., Daugherty S.C., Shetty J., Shvartsbeyn A.,
RA   Gebregeorgis E., Geer K., Tsegaye G., Malek J.A., Ayodeji B.,
RA   Shatsman S., McLeod M.P., Smajs D., Howell J.K., Pal S., Amin A.,
RA   Vashisth P., McNeill T.Z., Xiang Q., Sodergren E., Baca E.,
RA   Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola
RT   with other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS11584.1; -; Genomic_DNA.
DR   RefSeq; NP_971703.1; NC_002967.9.
DR   RefSeq; WP_002682404.1; NC_002967.9.
DR   ProteinModelPortal; Q73NQ7; -.
DR   SMR; Q73NQ7; -.
DR   STRING; 243275.TDE1095; -.
DR   EnsemblBacteria; AAS11584; AAS11584; TDE_1095.
DR   GeneID; 2740225; -.
DR   KEGG; tde:TDE1095; -.
DR   PATRIC; fig|243275.7.peg.1054; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   KO; K01775; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; TDEN243275:G1G0Q-1110-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000008212; 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; Reference proteome.
FT   CHAIN         1    379       Alanine racemase.
FT                                /FTId=PRO_1000066059.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    265    265       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     133    133       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     312    312       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   379 AA;  42227 MW;  6958BE9EEA85D48C CRC64;
     MRATKAIIHL DNLQYNIKEI KKRLNKNVKI CLPVKADAYG HGAVRVAVAA IRAGVSYLAV
     ASIQEAVELR EAGIVAPIIS LSLPVLEEIP ELLKYDIEPL VIDEEFINDL NRFAKKLNKK
     AWVHLKIDTG MRRIGCSPME AVKLAVQIDR AENLELKGVC THFAVSDSTD EKNIKFTKKQ
     ISVFKDSIKE IKKAGINPGL IHAANSGSVL QYPEAQFDMV RPGILVYGYA PSPSLNSLID
     LKPVMELVTQ VVLIKKIEKD TSVSYDRCWT AEKETFVATL PIGYADGLMR SLSGLKVRIG
     KDFFPIIGRI CMDQCMIDIG ASPWVQRWDE VCIFGPVSKE HPKNNTAQDL AKIAGTIPYE
     LTCDINKRVP RIFIDETIQ
//
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