(data stored in ACNUC7421 zone)

SWISSPROT: GMHA_ECO57

ID   GMHA_ECO57              Reviewed;         192 AA.
AC   P63225; P51001;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   30-AUG-2017, entry version 88.
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}; Synonyms=lpcA;
GN   OrderedLocusNames=Z0280, ECs0249;
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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: D-sedoheptulose 7-phosphate = D-glycero-D-
CC       manno-heptose 7-phosphate. {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   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
CC       biosynthesis.
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; AE005174; AAG54547.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33672.1; -; Genomic_DNA.
DR   PIR; A90660; A90660.
DR   PIR; G85510; G85510.
DR   RefSeq; NP_308276.1; NC_002695.1.
DR   RefSeq; WP_000284050.1; NZ_MWVM01000023.1.
DR   ProteinModelPortal; P63225; -.
DR   SMR; P63225; -.
DR   STRING; 155864.Z0280; -.
DR   EnsemblBacteria; AAG54547; AAG54547; Z0280.
DR   EnsemblBacteria; BAB33672; BAB33672; BAB33672.
DR   GeneID; 914335; -.
DR   KEGG; ece:Z0280; -.
DR   KEGG; ecs:ECs0249; -.
DR   PATRIC; fig|386585.9.peg.349; -.
DR   eggNOG; ENOG4105F55; Bacteria.
DR   eggNOG; COG0279; LUCA.
DR   HOGENOM; HOG000237571; -.
DR   KO; K03271; -.
DR   UniPathway; UPA00041; UER00436.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009244; P:lipopolysaccharide core region 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; P63225.
DR   SWISS-2DPAGE; P63225.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase;
KW   Lipopolysaccharide biosynthesis; Metal-binding; Zinc.
FT   CHAIN         1    192       Phosphoheptose isomerase.
FT                                /FTId=PRO_0000136527.
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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