Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P46452 (GMHBB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:gmhB
Ordered Locus Names:HI_0621.1
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Magnesium By similarity.

Zinc By similarity.

Pathway

Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4.

Bacterial outer membrane biogenesis; LOS core biosynthesis.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the GmhB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase
PRO_0000209392

Regions

Region8 – 103Substrate binding By similarity
Region16 – 194Substrate binding By similarity
Region50 – 534Substrate binding By similarity
Region106 – 1072Substrate binding By similarity

Sites

Active site81Nucleophile By similarity
Active site101Proton donor By similarity
Metal binding81Magnesium By similarity
Metal binding101Magnesium; via carbonyl oxygen By similarity
Metal binding891Zinc By similarity
Metal binding911Zinc; via amide nitrogen By similarity
Metal binding1031Zinc By similarity
Metal binding1051Zinc By similarity
Metal binding1321Magnesium By similarity
Metal binding1331Magnesium By similarity
Binding site1331Substrate By similarity
Site501Stabilizes the phosphoryl group By similarity
Site1061Contributes to substrate recognition By similarity
Site1071Stabilizes the phosphoryl group By similarity

Sequences

Sequence LengthMass (Da)Tools
P46452 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 49D1D56DA6DF3DBD

FASTA18420,810
        10         20         30         40         50         60 
MNKAIFLDRD GTLNIDYGYV HEIDNFKFID GVIDALRELK KMGYMLVLVT NQSGIARGYF 

        70         80         90        100        110        120 
SEDQFLQLTE WMDWSLAEQD VDLDGIYYCP HHSEGKGEYK EDCDCRKPKS GMLLQAIKEL 

       130        140        150        160        170        180 
KIDPTQSIMV GDKVEDLKAG IGAKVKMNVL VRTGKPVTGE GEGIADYVLD SIVDLPRILK 


RLKK 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC22281.1.
RefSeqNP_438781.1. NC_000907.1.

3D structure databases

ProteinModelPortalP46452.
SMRP46452. Positions 4-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0621.1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC22281; AAC22281; HI_0621.1.
GeneID949688.
KEGGhin:HI0621.1.
PATRIC20189829. VBIHaeInf48452_0647.

Phylogenomic databases

eggNOGCOG0241.
KOK03273.
OMAFMQLTEW.
OrthoDBEOG6QG8GT.
PhylomeDBP46452.

Enzyme and pathway databases

UniPathwayUPA00356; UER00438.
UPA00976.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR004446. Heptose_bisP_phosphatase.
IPR006543. Histidinol-phos.
[Graphical view]
PIRSFPIRSF004682. GmhB. 1 hit.
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR00213. GmhB_yaeD. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGMHBB_HAEIN
AccessionPrimary (citable) accession number: P46452
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names