(data stored in ACNUC10821 zone)

SWISSPROT: C8U1V4_ECO10

ID   C8U1V4_ECO10            Unreviewed;       192 AA.
AC   C8U1V4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Phosphoheptose isomerase {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846111};
DE            EC=5.3.1.28 {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846105};
DE   AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00067};
GN   Name=lpcA {ECO:0000313|EMBL:BAI29112.1};
GN   Synonyms=gmhA {ECO:0000256|HAMAP-Rule:MF_00067};
GN   OrderedLocusNames=ECO103_0238 {ECO:0000313|EMBL:BAI29112.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29112.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29112.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate
CC       in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00067, ECO:0000256|SAAS:SAAS00846114}.
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:0000256|HAMAP-Rule:MF_00067,
CC         ECO:0000256|SAAS:SAAS01116330};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00067};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_00067, ECO:0000256|SAAS:SAAS00846100}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00067}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00067,
CC       ECO:0000256|SAAS:SAAS00846118}.
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:0000256|HAMAP-Rule:MF_00067}.
CC   -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846117}.
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DR   EMBL; AP010958; BAI29112.1; -; Genomic_DNA.
DR   RefSeq; WP_000284050.1; NC_013353.1.
DR   SMR; C8U1V4; -.
DR   EnsemblBacteria; BAI29112; BAI29112; ECO103_0238.
DR   KEGG; eoh:ECO103_0238; -.
DR   HOGENOM; HOG000237571; -.
DR   KO; K03271; -.
DR   OMA; FLAHKEA; -.
DR   BioCyc; ECOL585395:ECO103_RS01255-MONOMER; -.
DR   UniPathway; UPA00041; UER00436.
DR   Proteomes; UP000000959; 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; C8U1V4.
DR   SWISS-2DPAGE; C8U1V4.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846094};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846120};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846084, ECO:0000313|EMBL:BAI29112.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00067,
KW   ECO:0000256|SAAS:SAAS00846086};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00067, ECO:0000256|SAAS:SAAS00846090}.
FT   DOMAIN       37    192       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   REGION       52     54       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00067}.
FT   REGION       93     94       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00067}.
FT   REGION      119    121       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00067}.
FT   METAL        61     61       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   METAL        65     65       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   METAL       172    172       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   METAL       180    180       Zinc. {ECO:0000256|HAMAP-Rule:MF_00067}.
FT   BINDING      65     65       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00067}.
FT   BINDING     124    124       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00067}.
FT   BINDING     172    172       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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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