GMHA_PROMH
ID GMHA_PROMH Reviewed; 192 AA.
AC B4EUT1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=PMI0349;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM942759; CAR40905.1; -; Genomic_DNA.
DR RefSeq; WP_004244807.1; NC_010554.1.
DR AlphaFoldDB; B4EUT1; -.
DR SMR; B4EUT1; -.
DR STRING; 529507.PMI0349; -.
DR EnsemblBacteria; CAR40905; CAR40905; PMI0349.
DR GeneID; 6800936; -.
DR KEGG; pmr:PMI0349; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_4_0_6; -.
DR OMA; FLAHKEA; -.
DR UniPathway; UPA00041; UER00436.
DR Proteomes; UP000008319; 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_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00441; gmhA; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..192
FT /note="Phosphoheptose isomerase"
FT /id="PRO_1000092284"
FT DOMAIN 37..192
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 52..54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 119..121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
SQ SEQUENCE 192 AA; 20852 MW; 93C044E549B39254 CRC64;
MYQDLIRGEL TEAADTLSRF LQDDANIEAI QKAAVLLADS FKAGGKVLSC GNGGSHCDAM
HFAEELTGRY RENRPGYPAI AISDVSHISC VSNDFGYEYV FSRYVEAVGK EGDVLLGIST
SGNSGNIIKA ISAAREKGMK VITLTGKDGG KMAGSADIEI RVPHFGYADR IQEIHIKVIH
ILIQLIEKEM EK
