位置:首页 > 蛋白库 > GMHA_METJA
GMHA_METJA
ID   GMHA_METJA              Reviewed;         187 AA.
AC   Q58731;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable 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=MJ1335;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
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   -!- 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   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99342.1; Type=Frameshift; Evidence={ECO:0000305};
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; L77117; AAB99342.1; ALT_FRAME; Genomic_DNA.
DR   PIR; F64466; F64466.
DR   AlphaFoldDB; Q58731; -.
DR   SMR; Q58731; -.
DR   STRING; 243232.MJ_1335; -.
DR   EnsemblBacteria; AAB99342; AAB99342; MJ_1335.
DR   KEGG; mja:MJ_1335; -.
DR   eggNOG; arCOG05355; Archaea.
DR   HOGENOM; CLU_080999_4_1_2; -.
DR   InParanoid; Q58731; -.
DR   OMA; DVHICVP; -.
DR   PhylomeDB; Q58731; -.
DR   UniPathway; UPA00041; UER00436.
DR   Proteomes; UP000000805; 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..187
FT                   /note="Probable phosphoheptose isomerase"
FT                   /id="PRO_0000136552"
FT   DOMAIN          32..187
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         47..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         115..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
SQ   SEQUENCE   187 AA;  20399 MW;  38440D7520757DB4 CRC64;
     MIMKKYFEES ANVKLKFIEE DEEKLKKAIE VIYNALKNGN KILICGNGGS AANSQHFAAE
     IVGRFKLERK GLPAIALTTD ISILTAIGND YGFDRIFERQ VEALGKEGDV LAGISTSGNS
     ENVIKAANKA KEMGIYTIGL LGKGGGKLKD IVDLALVVPS NDTARIQECH LTIYHVICEE
     VEKKLVK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024