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Protein

D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase

Gene

gmhB

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81NucleophileBy similarity
Metal bindingi8 – 81MagnesiumBy similarity
Active sitei10 – 101Proton donorBy similarity
Metal bindingi10 – 101Magnesium; via carbonyl oxygenBy similarity
Sitei50 – 501Stabilizes the phosphoryl groupBy similarity
Metal bindingi89 – 891ZincBy similarity
Metal bindingi91 – 911Zinc; via pros nitrogenBy similarity
Metal bindingi103 – 1031ZincBy similarity
Metal bindingi105 – 1051ZincBy similarity
Sitei106 – 1061Contributes to substrate recognitionBy similarity
Sitei107 – 1071Stabilizes the phosphoryl groupBy similarity
Metal bindingi132 – 1321MagnesiumBy similarity
Binding sitei133 – 1331SubstrateBy 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

BRENDAi3.1.3.82. 2529.
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 Componenti: Chromosome

Subcellular locationi

  1. 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-phosphatasePRO_0000209392Add
BLAST

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi71421.HI0621.1.

Structurei

3D structure databases

ProteinModelPortaliP46452.
SMRiP46452. Positions 4-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the GmhB family.Curated

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

        10         20         30         40         50
MNKAIFLDRD GTLNIDYGYV HEIDNFKFID GVIDALRELK KMGYMLVLVT
60 70 80 90 100
NQSGIARGYF SEDQFLQLTE WMDWSLAEQD VDLDGIYYCP HHSEGKGEYK
110 120 130 140 150
EDCDCRKPKS GMLLQAIKEL KIDPTQSIMV GDKVEDLKAG IGAKVKMNVL
160 170 180
VRTGKPVTGE GEGIADYVLD SIVDLPRILK RLKK
Length:184
Mass (Da):20,810
Last modified:November 1, 1995 - v1
Checksum:i49D1D56DA6DF3DBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22281.1.
RefSeqiNP_438781.1. NC_000907.1.

3D structure databases

ProteinModelPortaliP46452.
SMRiP46452. Positions 4-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0621.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0241.
KOiK03273.
OMAiFMQLTEW.
OrthoDBiEOG6QG8GT.
PhylomeDBiP46452.

Enzyme and pathway databases

UniPathwayiUPA00356; UER00438.
UPA00976.
BRENDAi3.1.3.82. 2529.

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.
ProtoNetiSearch...

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: April 1, 2015
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.