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EDD_ECO57
ID   EDD_ECO57               Reviewed;         603 AA.
AC   P0ADF7; P25530;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phosphogluconate dehydratase {ECO:0000255|HAMAP-Rule:MF_02094};
DE            EC=4.2.1.12 {ECO:0000255|HAMAP-Rule:MF_02094};
GN   Name=edd {ECO:0000255|HAMAP-Rule:MF_02094};
GN   OrderedLocusNames=Z2903, ECs2561;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-
CC       dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000255|HAMAP-
CC       Rule:MF_02094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-
CC         gluconate + H2O; Xref=Rhea:RHEA:17277, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57569, ChEBI:CHEBI:58759; EC=4.2.1.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02094};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02094};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_02094};
CC   -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC       {ECO:0000255|HAMAP-Rule:MF_02094}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC       Rule:MF_02094, ECO:0000305}.
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DR   EMBL; AE005174; AAG56841.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35984.1; -; Genomic_DNA.
DR   PIR; A98949; A98949.
DR   RefSeq; NP_310588.1; NC_002695.1.
DR   RefSeq; WP_001069467.1; NZ_SWKA01000004.1.
DR   AlphaFoldDB; P0ADF7; -.
DR   SMR; P0ADF7; -.
DR   STRING; 155864.EDL933_2824; -.
DR   EnsemblBacteria; AAG56841; AAG56841; Z2903.
DR   EnsemblBacteria; BAB35984; BAB35984; ECs_2561.
DR   GeneID; 67415450; -.
DR   GeneID; 912867; -.
DR   KEGG; ece:Z2903; -.
DR   KEGG; ecs:ECs_2561; -.
DR   PATRIC; fig|386585.9.peg.2684; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_1_2_6; -.
DR   OMA; CANIAHV; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004456; F:phosphogluconate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009255; P:Entner-Doudoroff pathway through 6-phosphogluconate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.30.80; -; 1.
DR   HAMAP; MF_02094; Edd; 1.
DR   InterPro; IPR004786; 6-phosphgluc_deHydtase.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43661:SF1; PTHR43661:SF1; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; SSF143975; 1.
DR   TIGRFAMs; TIGR01196; edd; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Carbohydrate metabolism; Gluconate utilization; Iron; Iron-sulfur;
KW   Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..603
FT                   /note="Phosphogluconate dehydratase"
FT                   /id="PRO_0000103554"
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02094"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   603 AA;  64639 MW;  D046405193BFC185 CRC64;
     MNPQLLRVTN RIIERSRETR SAYLARIEQA KTSTVHRSQL ACGNLAHGFA ACQPEDKASL
     KSMLRNNIAI ITSYNDMLSA HQPYEHYPEI IRKALHEANA VGQVAGGVPA MCDGVTQGQD
     GMELSLLSRE VIAMSAAVGL SHNMFDGALF LGVCDKIVPG LTMAALSFGH LPAVFVPSGP
     MASGLPNKEK VRIRQLYAEG KVDRMALLES EAASYHAPGT CTFYGTANTN QMVVEFMGMQ
     LPGSSFVHPD SPLRDALTAA AARQVTRMTG NGNEWMPIGK MIDEKVVVNG IVALLATGGS
     TNHTMHLVAM ARAAGIQINW DDFSDLSDVV PLMARLYPNG PADINHFQAA GGVPVLVREL
     LKAGLLHEDV NTVAGFGLSR YTLEPWLNNG ELDWREGAEK SLDSNVIASF EQPFSHHGGT
     KVLSGNLGRA VMKTSAVPVE NQVIEAPAVV FESQHDVMPA FEAGLLDRDC VVVVRHQGPK
     ANGMPELHKL MPPLGVLLDR CFKIALVTDG RLSGASGKVP SAIHVTPEAY DGGLLAKVRD
     GDIIRVNGQT GELTLLVDEA ELAAREPHIP DLSASRVGTG RELFSALREK LSGAEQGATC
     ITF
 
 
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