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GMHA_COLP3
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   03-AUG-2022, entry version 87.
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; Proteobacteria; 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   EnsemblBacteria; AAZ28650; AAZ28650; CPS_4434.
DR   KEGG; cps:CPS_4434; -.
DR   eggNOG; COG0279; Bacteria.
DR   HOGENOM; CLU_080999_3_1_6; -.
DR   OMA; DVHICVP; -.
DR   OrthoDB; 1571626at2; -.
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   Pfam; PF13580; SIS_2; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Metal-binding;
KW   Reference proteome; 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
 
 
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