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Q0K5T5 (Q0K5T5_CUPNH) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoheptose isomerase HAMAP-Rule MF_00067
EC=5.3.1.28 HAMAP-Rule MF_00067
Alternative name(s):
Sedoheptulose 7-phosphate isomerase HAMAP-Rule MF_00067
Gene names
Name:gmhA2 EMBL CAJ94636.1
Synonyms:gmhA HAMAP-Rule MF_00067
Ordered Locus Names:H16_A3578 EMBL CAJ94636.1
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP] EMBL CAJ94636.1
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus ›

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate By similarity. SAAS SAAS004515 HAMAP-Rule MF_00067

Catalytic activity

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. SAAS SAAS004515 HAMAP-Rule MF_00067

Cofactor

Binds 1 zinc ion per subunit By similarity. SAAS SAAS004515 HAMAP-Rule MF_00067

Pathway

Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. SAAS SAAS004515 HAMAP-Rule MF_00067

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00067

Subcellular location

Cytoplasm By similarity SAAS SAAS004515 HAMAP-Rule MF_00067.

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. HAMAP-Rule MF_00067

Sequence similarities

Belongs to the SIS family. GmhA subfamily. HAMAP-Rule MF_00067

Contains 1 SIS domain. SAAS SAAS004515 HAMAP-Rule MF_00067

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain35 – 195161SIS By similarity HAMAP-Rule MF_00067
Region50 – 523Substrate binding By similarity HAMAP-Rule MF_00067
Region92 – 932Substrate binding By similarity HAMAP-Rule MF_00067
Region118 – 1203Substrate binding By similarity HAMAP-Rule MF_00067

Sites

Metal binding591Zinc By similarity HAMAP-Rule MF_00067
Metal binding631Zinc By similarity HAMAP-Rule MF_00067
Metal binding1731Zinc By similarity HAMAP-Rule MF_00067
Metal binding1811Zinc By similarity HAMAP-Rule MF_00067
Binding site631Substrate By similarity HAMAP-Rule MF_00067
Binding site1231Substrate By similarity HAMAP-Rule MF_00067
Binding site1731Substrate By similarity HAMAP-Rule MF_00067

Sequences

Sequence LengthMass (Da)Tools
Q0K5T5 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: DA260D40C8BF351B

FASTA19520,356
        10         20         30         40         50         60 
MSIDSIQQQF LDSAETKRQA AAVMAPYIDA AVERMVGALT SGNKILACGN GGSAADAQHF 

        70         80         90        100        110        120 
AAELVGRFER ERPGLAAIAL TTDSSILTAI GNDYDFSKVF SKQVEALGQP GDILLALSTS 

       130        140        150        160        170        180 
GNSANVIAAI EAARQREMAV VALTGKGGGT IAGLLDEFDI HLCVPSERTA RIQEVHLLTL 

       190 
HCLCDGIDEA LLGEA

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References

[1]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM260479 Genomic DNA. Translation: CAJ94636.1.
RefSeqYP_728004.1. NC_008313.1.

3D structure databases

ProteinModelPortalQ0K5T5.
SMRQ0K5T5. Positions 6-193.
ModBaseSearch...

Protein-protein interaction databases

STRING381666.H16_A3578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ94636; CAJ94636; H16_A3578.
GeneID4248403.
KEGGreh:H16_A3578.
PATRIC35236709. VBIRalEut6770_3964.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0279.
HOGENOMHOG000237572.
KOK03271.
OMAPHIEQAS.
ProtClustDBCLSK939671.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-3542-MONOMER.
UniPathwayUPA00041; UER00436.

Family and domain databases

HAMAPMF_00067. GmhA.
InterProIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamPF13580. SIS_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00441. gmhA. 1 hit.
PROSITEPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ0K5T5_CUPNH
AccessionPrimary (citable) accession number: Q0K5T5
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2006
Last sequence update: October 3, 2006
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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