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GMHBA_MYCTO
ID   GMHBA_MYCTO             Reviewed;         190 AA.
AC   P9WMV2; L0T2I2; O53636;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
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=MT0122.1;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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   -!- SIMILARITY: Belongs to the GmhB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK44345.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK44345.1; ALT_INIT; Genomic_DNA.
DR   PIR; E70840; E70840.
DR   RefSeq; WP_003400840.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMV2; -.
DR   SMR; P9WMV2; -.
DR   EnsemblBacteria; AAK44345; AAK44345; MT0122.
DR   GeneID; 45424079; -.
DR   KEGG; mtc:MT0122; -.
DR   PATRIC; fig|83331.31.peg.129; -.
DR   HOGENOM; CLU_066606_0_0_11; -.
DR   UniPathway; UPA00543; UER00607.
DR   Proteomes; UP000001020; 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   PANTHER; PTHR42891; PTHR42891; 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   Zinc.
FT   CHAIN           1..190
FT                   /note="D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-
FT                   phosphatase"
FT                   /id="PRO_0000427237"
FT   ACT_SITE        15
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        17
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         15..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         23..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         100
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         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7WG29"
FT   SITE            59
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
FT   SITE            109
FT                   /note="Contributes to substrate recognition"
FT                   /evidence="ECO:0000250"
FT   SITE            110
FT                   /note="Stabilizes the phosphoryl group"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  20511 MW;  4A5A06E97EB8B812 CRC64;
     MVAERAGHQW CLFLDRDGVI NRQVVGDYVR NWRQFEWLPG AARALKKLRA WAPYIVVVTN
     QQGVGAGLMS AVDVMVIHRH LQMQLASDGV LIDGFQVCPH HRSQRCGCRK PRPGLVLDWL
     GRHPDSEPLL SIVVGDSLSD LELAHNVAAA AGACASVQIG GASSGGVADA SFDSLWEFAV
     AVGHARGERG
 
 
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