(data stored in ACNUC7421 zone)

SWISSPROT: GMHA_ECODH

ID   GMHA_ECODH              Reviewed;         192 AA.
AC   B1XD84;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Phosphoheptose isomerase {ECO:0000255|HAMAP-Rule:MF_00067};
DE            EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067};
DE   AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00067};
GN   Name=gmhA {ECO:0000255|HAMAP-Rule:MF_00067};
GN   OrderedLocusNames=ECDH10B_0204;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate
CC       in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00067}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-
CC         heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-
CC         phosphate; Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:60203, ChEBI:CHEBI:60204; EC=5.3.1.28;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00067};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00067};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00067};
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-
CC       phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-
CC       phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from
CC       sedoheptulose 7-phosphate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00067}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- MISCELLANEOUS: The reaction produces a racemic mixture of D-
CC       glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-
CC       manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC   -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00067}.
DR   EMBL; CP000948; ACB01393.1; -; Genomic_DNA.
DR   RefSeq; WP_000284050.1; NC_010473.1.
DR   SMR; B1XD84; -.
DR   EnsemblBacteria; ACB01393; ACB01393; ECDH10B_0204.
DR   KEGG; ecd:ECDH10B_0204; -.
DR   eggNOG; ENOG4105F55; Bacteria.
DR   eggNOG; COG0279; LUCA.
DR   HOGENOM; HOG000237571; -.
DR   KO; K03271; -.
DR   OMA; FLAHKEA; -.
DR   BioCyc; ECOL316385:ECDH10B_RS01030-MONOMER; -.
DR   UniPathway; UPA00041; UER00436.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05006; SIS_GmhA; 1.
DR   HAMAP; MF_00067; GmhA; 1.
DR   InterPro; IPR035461; GmhA/DiaA.
DR   InterPro; IPR004515; Phosphoheptose_Isoase.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF13580; SIS_2; 1.
DR   TIGRFAMs; TIGR00441; gmhA; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1XD84.
DR   SWISS-2DPAGE; B1XD84.
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding; Zinc.
FT   CHAIN         1    192       Phosphoheptose isomerase.
FT                                /FTId=PRO_1000092271.
FT   DOMAIN       37    192       SIS. {ECO:0000255|HAMAP-Rule:MF_00067}.
FT   REGION       52     54       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00067}.
FT   REGION       93     94       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00067}.
FT   REGION      119    121       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00067}.
FT   METAL        61     61       Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}.
FT   METAL        65     65       Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}.
FT   METAL       172    172       Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}.
FT   METAL       180    180       Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}.
FT   BINDING      65     65       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00067}.
FT   BINDING     124    124       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00067}.
FT   BINDING     172    172       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00067}.
SQ   SEQUENCE   192 AA;  20815 MW;  7A2C05E1079108B4 CRC64;
     MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC GNGGSHCDAM
     HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI FSRYVEAVGR EGDVLLGIST
     SGNSANVIKA IAAAREKGMK VITLTGKDGG KMAGTADIEI RVPHFGYADR IQEIHIKVIH
     ILIQLIEKEM VK
//

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