ID GMHA_COLP3 Reviewed; 196 AA.
AC Q47VU0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
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=CPS_4434;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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}.
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DR EMBL; CP000083; AAZ28650.1; -; Genomic_DNA.
DR RefSeq; WP_011045163.1; NC_003910.7.
DR PDB; 5BY2; X-ray; 2.80 A; A=1-196.
DR PDBsum; 5BY2; -.
DR AlphaFoldDB; Q47VU0; -.
DR SMR; Q47VU0; -.
DR STRING; 167879.CPS_4434; -.
DR KEGG; cps:CPS_4434; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_3_1_6; -.
DR UniPathway; UPA00041; UER00436.
DR Proteomes; UP000000547; 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 PANTHER; PTHR30390:SF6; DNAA INITIATOR-ASSOCIATING PROTEIN DIAA; 1.
DR PANTHER; PTHR30390; SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding;
KW Zinc.
FT CHAIN 1..196
FT /note="Phosphoheptose isomerase"
FT /id="PRO_1000196994"
FT DOMAIN 34..192
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 49..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 117..119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 122
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"
FT HELIX 1..22
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:5BY2"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:5BY2"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:5BY2"
FT HELIX 168..190
FT /evidence="ECO:0007829|PDB:5BY2"
SQ SEQUENCE 196 AA; 20922 MW; 209B4F651FF2AF93 CRC64;
MLEQIKNNFT ESIQTQIAAS ELLGPSIEHA GMMMVQCLLG GNKIISCGNG GSAGHAQHFC
AQLLNKYETE RPSLPAISLN SDISTITSIA NDYQYDEVFS KQIRALGHNG DVLLAISTSG
NSRNVVKAIE SAVSRDIPII ALTGFDGGDI SGLLGEGDVE IRVPSARTSR IQEVHLVVLH
SLCEIIDTTL FPQGDS
//
