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Protein

Phosphoheptose isomerase

Gene

gmhA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.By similarity

Catalytic activityi

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: D-glycero-D-manno-heptose 7-phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Phosphoheptose isomerase (gmhA)
This subpathway is part of the pathway D-glycero-D-manno-heptose 7-phosphate biosynthesis, which is itself part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate, the pathway D-glycero-D-manno-heptose 7-phosphate biosynthesis and in Carbohydrate biosynthesis.

Pathwayi: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi60ZincBy similarity1
Metal bindingi64ZincBy similarity1
Binding sitei64Substrate1
Binding sitei124Substrate1
Metal bindingi174ZincBy similarity1
Binding sitei174Substrate1
Metal bindingi182ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi5.3.1.28. 5087.
UniPathwayiUPA00041; UER00436.
UPA00958.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoheptose isomerase (EC:5.3.1.28)
Alternative name(s):
Sedoheptulose 7-phosphate isomerase
Gene namesi
Name:gmhA
Ordered Locus Names:PA4425
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4425.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001365421 – 197Phosphoheptose isomeraseAdd BLAST197

Proteomic databases

PaxDbiQ9HVZ0.
PRIDEiQ9HVZ0.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi208964.PA4425.

Structurei

Secondary structure

1197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 24Combined sources22
Helixi26 – 41Combined sources16
Beta strandi46 – 49Combined sources4
Helixi53 – 66Combined sources14
Beta strandi69 – 71Combined sources3
Beta strandi78 – 80Combined sources3
Helixi85 – 94Combined sources10
Helixi97 – 99Combined sources3
Helixi102 – 108Combined sources7
Beta strandi114 – 118Combined sources5
Beta strandi120 – 122Combined sources3
Helixi125 – 136Combined sources12
Beta strandi140 – 145Combined sources6
Helixi150 – 155Combined sources6
Beta strandi161 – 164Combined sources4
Helixi170 – 193Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X92X-ray2.30A/B1-197[»]
3BJZX-ray2.40A/B/C/D1-197[»]
ProteinModelPortaliQ9HVZ0.
SMRiQ9HVZ0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HVZ0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini36 – 197SISAdd BLAST162

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni51 – 53Substrate binding3
Regioni93 – 94Substrate bindingBy similarity2
Regioni119 – 121Substrate binding3

Sequence similaritiesi

Belongs to the SIS family. GmhA subfamily.Curated
Contains 1 SIS domain.Curated

Phylogenomic databases

eggNOGiENOG4105F55. Bacteria.
COG0279. LUCA.
HOGENOMiHOG000237572.
InParanoidiQ9HVZ0.
KOiK03271.
OMAiLHEEVYA.
PhylomeDBiQ9HVZ0.

Family and domain databases

HAMAPiMF_00067. GmhA. 1 hit.
InterProiIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamiPF13580. SIS_2. 1 hit.
[Graphical view]
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HVZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMQHRIRQL FQASIETKQQ ALEVLPPYIE QASLVMVNAL LNEGKILSCG
60 70 80 90 100
NGGSAGDAQH FSSELLNRFE RERPSLPAVA LTTDSSTITS IANDYSYNEV
110 120 130 140 150
FSKQIRALGQ PGDVLLAIST SGNSANVIQA IQAAHDREML VVALTGRDGG
160 170 180 190
GMASLLLPED VEIRVPSKIT ARIQEVHLLA IHCLCDLIDR QLFGSEE
Length:197
Mass (Da):21,413
Last modified:March 1, 2001 - v1
Checksum:iCF48D9DF28634BB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG07813.1.
PIRiA83092.
RefSeqiNP_253115.1. NC_002516.2.
WP_003094149.1. NZ_ASJY01000727.1.

Genome annotation databases

EnsemblBacteriaiAAG07813; AAG07813; PA4425.
GeneIDi881196.
KEGGipae:PA4425.
PATRICi19843575. VBIPseAer58763_4634.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG07813.1.
PIRiA83092.
RefSeqiNP_253115.1. NC_002516.2.
WP_003094149.1. NZ_ASJY01000727.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X92X-ray2.30A/B1-197[»]
3BJZX-ray2.40A/B/C/D1-197[»]
ProteinModelPortaliQ9HVZ0.
SMRiQ9HVZ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4425.

Proteomic databases

PaxDbiQ9HVZ0.
PRIDEiQ9HVZ0.

Protocols and materials databases

DNASUi881196.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07813; AAG07813; PA4425.
GeneIDi881196.
KEGGipae:PA4425.
PATRICi19843575. VBIPseAer58763_4634.

Organism-specific databases

PseudoCAPiPA4425.

Phylogenomic databases

eggNOGiENOG4105F55. Bacteria.
COG0279. LUCA.
HOGENOMiHOG000237572.
InParanoidiQ9HVZ0.
KOiK03271.
OMAiLHEEVYA.
PhylomeDBiQ9HVZ0.

Enzyme and pathway databases

UniPathwayiUPA00041; UER00436.
UPA00958.
BRENDAi5.3.1.28. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9HVZ0.

Family and domain databases

HAMAPiMF_00067. GmhA. 1 hit.
InterProiIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamiPF13580. SIS_2. 1 hit.
[Graphical view]
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGMHA_PSEAE
AccessioniPrimary (citable) accession number: Q9HVZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.