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DescriptionRecName: Full=2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; EC=1.3.1.28;
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MyHits synonymsENTA_ECOLI , P15047 , P77100 , Q2MBK5 , E840488335AD317B
match map segment
ipat:ADH_SHORT  
Legends: 1, ACT_SITE Proton acceptor (By similarity); 2, BINDING Substrate (By similarity); 3, NP_BIND NAD (By similarity); 4, ipat:ADH_SHORT [T]; 5, STRAND; 6, HELIX; 7, TURN.
ID   ENTA_ECOLI              Reviewed;         248 AA.
AC   P15047; P77100; Q2MBK5;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-NOV-2009, entry version 86.
DE   RecName: Full=2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase;
DE            EC=1.3.1.28;
GN   Name=entA; OrderedLocusNames=b0596, JW0588;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-14.
RX   MEDLINE=89123155; PubMed=2521622;
RA   Liu J., Duncan K., Walsh C.T.;
RT   "Nucleotide sequence of a cluster of Escherichia coli enterobactin
RT   biosynthesis genes: identification of entA and purification of its
RT   product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
RL   J. Bacteriol. 171:791-798(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89123154; PubMed=2521621;
RA   Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT   "Nucleotide sequence and transcriptional organization of the
RT   Escherichia coli enterobactin biosynthesis cistrons entB and entA.";
RL   J. Bacteriol. 171:784-790(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- CATALYTIC ACTIVITY: 2,3-dihydro-2,3-dihydroxybenzoate + NAD(+) =
CC       2,3-dihydroxybenzoate + NADH.
CC   -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC   -!- SUBUNIT: Homooctamer.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; M24148; AAA16103.1; -; Unassigned_DNA.
DR   EMBL; M24143; AAA76836.1; -; Genomic_DNA.
DR   EMBL; U82598; AAB40796.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73697.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76351.1; -; Genomic_DNA.
DR   PIR; A91904; DEECDB.
DR   RefSeq; AP_001243.1; -.
DR   RefSeq; NP_415128.1; -.
DR   PDB; 2FWM; X-ray; 2.00 A; X=1-248.
DR   PDBsum; 2FWM; -.
DR   DIP; DIP:9511N; -.
DR   STRING; P15047; -.
DR   GeneID; 945284; -.
DR   GenomeReviews; AP009048_GR; JW0588.
DR   GenomeReviews; U00096_GR; b0596.
DR   KEGG; ecj:JW0588; -.
DR   KEGG; eco:b0596; -.
DR   EchoBASE; EB0255; -.
DR   EcoGene; EG10259; entA.
DR   HOGENOM; P15047; -.
DR   OMA; HASHITL; -.
DR   BioCyc; EcoCyc:ENTA-MON; -.
DR   BioCyc; MetaCyc:ENTA-MON; -.
DR   Genevestigator; P15047; -.
DR   GO; GO:0008667; F:2,3-dihydro-2,3-dihydroxybenzoate dehydroge...; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009239; P:enterobactin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR003560; DHB_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR01397; DHBDHDRGNASE.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Enterobactin biosynthesis; Ion transport; Iron; Iron transport; NAD;
KW   Oxidoreductase; Transport.
FT   CHAIN         1    248       2,3-dihydro-2,3-dihydroxybenzoate
FT                                dehydrogenase.
FT                                /FTId=PRO_0000054659.
FT   NP_BIND       9     33       NAD (By similarity).
FT   ACT_SITE    144    144       Proton acceptor (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   STRAND        7     12
FT   HELIX        16     27
FT   STRAND       31     37
FT   STRAND       45     50
FT   HELIX        56     69
FT   STRAND       75     78
FT   TURN         88     90
FT   HELIX        93    103
FT   HELIX       105    121
FT   STRAND      125    129
FT   HELIX       132    134
FT   HELIX       142    162
FT   HELIX       163    165
FT   STRAND      168    174
FT   HELIX       215    226
FT   HELIX       228    230
FT   STRAND      237    241
FT   TURN        242    247
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CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       131    159       ipat:ADH_SHORT [T]
SQ   SEQUENCE   248 AA;  26250 MW;  E840488335AD317B CRC64;
     MDFSGKNVWV TGAGKGIGYA TALAFVEAGA KVTGFDQAFT QEQYPFATEV MDVADAAQVA
     QVCQRLLAET ERLDALVNAA GILRMGATDQ LSKEDWQQTF AVNVGGAFNL FQQTMNQFRR
     QRGGAIVTVA SDAAHTPRIG MSAYGASKAA LKSLALSVGL ELAGSGVRCN VVSPGSTDTD
     MQRTLWVSDD AEEQRIRGFG EQFKLGIPLG KIARPQEIAN TILFLASDLA SHITLQDIVV
     DGGSTLGA
//