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GMHBB_NEIMB
ID   GMHBB_NEIMB             Reviewed;         187 AA.
AC   Q9JXI5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase;
DE            EC=3.1.3.82;
DE   AltName: Full=D,D-heptose 1,7-bisphosphate phosphatase;
DE            Short=HBP phosphatase;
GN   Name=gmhB; Synonyms=gmhX; OrderedLocusNames=NMB2033;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   ROLE IN HEPTOSE ASSEMBLY.
RC   STRAIN=NMB / Serogroup B;
RX   PubMed=11496013; DOI=10.1099/00221287-147-8-2367;
RA   Shih G.C., Kahler C.M., Carlson R.W., Rahman M.M., Stephens D.S.;
RT   "gmhX, a novel gene required for the incorporation of L-glycero-D-manno-
RT   heptose into lipooligosaccharide in Neisseria meningitidis.";
RL   Microbiology 147:2367-2377(2001).
RN   [3]
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-beta-D-manno-heptose 1,7-bisphosphate
CC       intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by
CC       removing the phosphate group at the C-7 position.
CC       {ECO:0000305|PubMed:11496013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-
CC         glycero-beta-D-manno-heptose 1-phosphate + phosphate;
CC         Xref=Rhea:RHEA:28518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:60208, ChEBI:CHEBI:61593; EC=3.1.3.82;
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; ADP-L-glycero-beta-D-manno-
CC       heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-
CC       glycero-beta-D-manno-heptose 7-phosphate: step 2/4.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LOS core biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
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DR   EMBL; AE002098; AAF42354.1; -; Genomic_DNA.
DR   PIR; F81013; F81013.
DR   RefSeq; NP_275024.1; NC_003112.2.
DR   RefSeq; WP_002224688.1; NC_003112.2.
DR   AlphaFoldDB; Q9JXI5; -.
DR   SMR; Q9JXI5; -.
DR   STRING; 122586.NMB2033; -.
DR   PaxDb; Q9JXI5; -.
DR   EnsemblBacteria; AAF42354; AAF42354; NMB2033.
DR   KEGG; nme:NMB2033; -.
DR   PATRIC; fig|122586.8.peg.2592; -.
DR   HOGENOM; CLU_085077_2_0_4; -.
DR   OMA; EHQICLE; -.
DR   UniPathway; UPA00356; UER00438.
DR   UniPathway; UPA00976; -.
DR   Proteomes; UP000000425; 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:0097171; P:ADP-L-glycero-beta-D-manno-heptose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IMP:CACAO.
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   PANTHER; PTHR42891; PTHR42891; 1.
DR   PIRSF; PIRSF004682; GmhB; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
DR   TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..187
FT                   /note="D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000209399"
FT   ACT_SITE        7
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        9
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7..9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         7
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         15..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         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         100..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   SITE            50
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
FT   SITE            100
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            101
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   187 AA;  20713 MW;  0E4D689BEC2017AF CRC64;
     MKLIILDRDG VINQDRDDFV KSVDEWIPVE GSMDAVAFLT QAGYTVAVAT NQSGIGRKYF
     TVQNLTEMHA KMHRLVRQAG GEINGIWFCP HTDADNCNCR KPKPGMIEDI IGRFNAQASE
     TWLVGDSLRD LQAIDAVGGK PALVLTGKGK KTLSQHGHEL PEHTQVFDTL LDFSQYIMQE
     NTAPQAD
 
 
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