位置:首页 > 蛋白库 > GMHBA_CLOAB
GMHBA_CLOAB
ID   GMHBA_CLOAB             Reviewed;         181 AA.
AC   Q97EQ5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE            EC=3.1.3.83;
DE   AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE            Short=HBP phosphatase;
GN   Name=gmhB; OrderedLocusNames=CA_C3053;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
RN   [2]
RP   BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX   PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA   Valvano M.A., Messner P., Kosma P.;
RT   "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT   heptose precursors of bacterial glycoproteins and cell surface
RT   polysaccharides.";
RL   Microbiology 148:1979-1989(2002).
CC   -!- FUNCTION: Converts the D-glycero-alpha-D-manno-heptose 1,7-bisphosphate
CC       intermediate into D-glycero-alpha-D-manno-heptose 1-phosphate by
CC       removing the phosphate group at the C-7 position. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glycero-alpha-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC         glycero-alpha-D-manno-heptose 1-phosphate + phosphate;
CC         Xref=Rhea:RHEA:28522, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60207, ChEBI:CHEBI:61574; EC=3.1.3.83;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-D-glycero-alpha-D-manno-
CC       heptose biosynthesis; GDP-D-glycero-alpha-D-manno-heptose from D-
CC       glycero-alpha-D-manno-heptose 7-phosphate: step 2/3.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Is probably involved in the capsular polysaccharide
CC       (CPS) biosynthesis.
CC   -!- SIMILARITY: Belongs to the GmhB family. {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; AE001437; AAK80993.1; -; Genomic_DNA.
DR   PIR; F97275; F97275.
DR   RefSeq; NP_349653.1; NC_003030.1.
DR   RefSeq; WP_010966334.1; NC_003030.1.
DR   AlphaFoldDB; Q97EQ5; -.
DR   SMR; Q97EQ5; -.
DR   STRING; 272562.CA_C3053; -.
DR   EnsemblBacteria; AAK80993; AAK80993; CA_C3053.
DR   GeneID; 44999540; -.
DR   KEGG; cac:CA_C3053; -.
DR   PATRIC; fig|272562.8.peg.3236; -.
DR   eggNOG; COG0241; Bacteria.
DR   HOGENOM; CLU_085077_2_1_9; -.
DR   OMA; EHQICLE; -.
DR   OrthoDB; 1472357at2; -.
DR   BRENDA; 3.1.3.82; 1452.
DR   UniPathway; UPA00543; UER00607.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034200; F:D,D-heptose 1,7-bisphosphate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR004446; Heptose_bisP_phosphatase.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR013954; PNK3P.
DR   PANTHER; PTHR42891; PTHR42891; 1.
DR   Pfam; PF08645; PNK3P; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00213; GmhB_yaeD; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Carbohydrate metabolism; Cytoplasm;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..181
FT                   /note="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000209388"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         8..10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         16..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            50
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
FT   SITE            107
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            108
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   181 AA;  20962 MW;  14D79C4114814F38 CRC64;
     MNKAVFLDRD GTINVEKNYL YKIEDFEFTE GAVEAIKLLN QNEYKVIVIS NQAGVARGYY
     TEEAVDKLHE YIQKQLKKYD AHIDAFYYCP HHPIHGVGKY KLQCKCRKPE DGLYKRAIKD
     FNIDVEKSYA VGDKLSDLIP AVDNNIKSFL VMTGYGKEEV KNIKTDMRIT KNLYSFVTEI
     I
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024