(data stored in SCRATCH3701 zone)

SWISSPROT: GMHA_ECOBW

ID   GMHA_ECOBW              Reviewed;         192 AA.
AC   C4ZRV8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 57.
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}; OrderedLocusNames=BWG_0208;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC       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-phosphate;
CC         Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203,
CC         ChEBI:CHEBI:60204; EC=5.3.1.28; Evidence={ECO:0000255|HAMAP-
CC         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-Rule:MF_00067};
CC   -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-
CC       phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and
CC       D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-
CC       phosphate: step 1/1. {ECO:0000255|HAMAP-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-glycero-
CC       alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-
CC       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; CP001396; ACR63005.1; -; Genomic_DNA.
DR   RefSeq; WP_000284050.1; NC_012759.1.
DR   SMR; C4ZRV8; -.
DR   PRIDE; C4ZRV8; -.
DR   EnsemblBacteria; ACR63005; ACR63005; BWG_0208.
DR   KEGG; ebw:BWG_0208; -.
DR   HOGENOM; HOG000237571; -.
DR   KO; K03271; -.
DR   OMA; FLAHKEA; -.
DR   BioCyc; ECOL595496:BWG_RS01135-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; C4ZRV8.
DR   SWISS-2DPAGE; C4ZRV8.
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding; Zinc.
FT   CHAIN           1..192
FT                   /note="Phosphoheptose isomerase"
FT                   /id="PRO_1000202418"
FT   DOMAIN          37..192
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   REGION          52..54
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   REGION          93..94
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   REGION          119..121
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   METAL           61
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   METAL           65
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   METAL           172
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   METAL           180
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         65
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         124
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         172
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-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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