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P46452

- GMHBB_HAEIN

UniProt

P46452 - GMHBB_HAEIN

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Protein
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
Gene
gmhB, HI_0621.1
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position By similarity.

Catalytic activityi

D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate.

Cofactori

Magnesium By similarity.
Zinc By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Nucleophile By similarity
Metal bindingi8 – 81Magnesium By similarity
Active sitei10 – 101Proton donor By similarity
Metal bindingi10 – 101Magnesium; via carbonyl oxygen By similarity
Sitei50 – 501Stabilizes the phosphoryl group By similarity
Metal bindingi89 – 891Zinc By similarity
Metal bindingi91 – 911Zinc; via amide nitrogen By similarity
Metal bindingi103 – 1031Zinc By similarity
Metal bindingi105 – 1051Zinc By similarity
Sitei106 – 1061Contributes to substrate recognition By similarity
Sitei107 – 1071Stabilizes the phosphoryl group By similarity
Metal bindingi132 – 1321Magnesium By similarity
Metal bindingi133 – 1331Magnesium By similarity
Binding sitei133 – 1331Substrate By similarity

GO - Molecular functioni

  1. D,D-heptose 1,7-bisphosphate phosphatase activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. ADP-L-glycero-beta-D-manno-heptose biosynthetic process Source: UniProtKB-UniPathway
  2. carbohydrate metabolic process Source: UniProtKB-KW
  3. dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00356; UER00438.
UPA00976.

Names & Taxonomyi

Protein namesi
Recommended name:
D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC:3.1.3.82)
Alternative name(s):
D,D-heptose 1,7-bisphosphate phosphatase
Short name:
HBP phosphatase
Gene namesi
Name:gmhB
Ordered Locus Names:HI_0621.1
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
PRO_0000209392Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

STRINGi71421.HI0621.1.

Structurei

3D structure databases

ProteinModelPortaliP46452.
SMRiP46452. Positions 4-181.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 103Substrate binding By similarity
Regioni16 – 194Substrate binding By similarity
Regioni50 – 534Substrate binding By similarity
Regioni106 – 1072Substrate binding By similarity

Sequence similaritiesi

Belongs to the GmhB family.

Phylogenomic databases

eggNOGiCOG0241.
KOiK03273.
OMAiFMQLTEW.
OrthoDBiEOG6QG8GT.
PhylomeDBiP46452.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR004446. Heptose_bisP_phosphatase.
IPR006543. Histidinol-phos.
[Graphical view]
PIRSFiPIRSF004682. GmhB. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR00213. GmhB_yaeD. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.

Sequencei

Sequence statusi: Complete.

P46452-1 [UniParc]FASTAAdd to Basket

« Hide

MNKAIFLDRD GTLNIDYGYV HEIDNFKFID GVIDALRELK KMGYMLVLVT    50
NQSGIARGYF SEDQFLQLTE WMDWSLAEQD VDLDGIYYCP HHSEGKGEYK 100
EDCDCRKPKS GMLLQAIKEL KIDPTQSIMV GDKVEDLKAG IGAKVKMNVL 150
VRTGKPVTGE GEGIADYVLD SIVDLPRILK RLKK 184
Length:184
Mass (Da):20,810
Last modified:November 1, 1995 - v1
Checksum:i49D1D56DA6DF3DBD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22281.1.
RefSeqiNP_438781.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22281; AAC22281; HI_0621.1.
GeneIDi949688.
KEGGihin:HI0621.1.
PATRICi20189829. VBIHaeInf48452_0647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22281.1 .
RefSeqi NP_438781.1. NC_000907.1.

3D structure databases

ProteinModelPortali P46452.
SMRi P46452. Positions 4-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI0621.1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC22281 ; AAC22281 ; HI_0621.1 .
GeneIDi 949688.
KEGGi hin:HI0621.1.
PATRICi 20189829. VBIHaeInf48452_0647.

Phylogenomic databases

eggNOGi COG0241.
KOi K03273.
OMAi FMQLTEW.
OrthoDBi EOG6QG8GT.
PhylomeDBi P46452.

Enzyme and pathway databases

UniPathwayi UPA00356 ; UER00438 .
UPA00976 .

Family and domain databases

Gene3Di 3.40.50.1000. 1 hit.
InterProi IPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR004446. Heptose_bisP_phosphatase.
IPR006543. Histidinol-phos.
[Graphical view ]
PIRSFi PIRSF004682. GmhB. 1 hit.
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR00213. GmhB_yaeD. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Koonin E.V., Rudd K.E.
    Submitted (SEP-1995) to UniProtKB
    Cited for: IDENTIFICATION.
  3. "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides."
    Valvano M.A., Messner P., Kosma P.
    Microbiology 148:1979-1989(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.

Entry informationi

Entry nameiGMHBB_HAEIN
AccessioniPrimary (citable) accession number: P46452
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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