(data stored in ACNUC7421 zone)

SWISSPROT: GMHA_ECO27

ID   GMHA_ECO27              Reviewed;         192 AA.
AC   B7UJB5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, 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=E2348C_0219;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS07767.1; -; Genomic_DNA.
DR   RefSeq; WP_012578839.1; NC_011601.1.
DR   SMR; B7UJB5; -.
DR   PRIDE; B7UJB5; -.
DR   EnsemblBacteria; CAS07767; CAS07767; E2348C_0219.
DR   KEGG; ecg:E2348C_0219; -.
DR   KO; K03271; -.
DR   OMA; FLAHKEA; -.
DR   BioCyc; ECOL574521:E2348C_RS01160-MONOMER; -.
DR   UniPathway; UPA00041; UER00436.
DR   Proteomes; UP000008205; Chromosome.
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; B7UJB5.
DR   SWISS-2DPAGE; B7UJB5.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase;
KW   Metal-binding; Zinc.
FT   CHAIN         1    192       Phosphoheptose isomerase.
FT                                /FTId=PRO_1000196999.
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;  20829 MW;  1767E5F5B8D5F65E CRC64;
     MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAALLLADS FKAGGKVLSC GNGGSHCDAM
     HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI FSRYVEAVGR EGDVLLGIST
     SGNSANVIKA IAAAREKGMK VITLTGKDGG KMAGTADIEI RVPHFGYADR IQEIHIKVIH
     ILIQLIEKEM VK
//

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