Skip Header

Contribute Send feedback
Read comments (?) or add your own

B8E9A1 (B8E9A1_SHEB2) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 32. Feed History...

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

Names and origin

Protein namesRecommended name:
Imidazole glycerol phosphate synthase subunit HisH HAMAP-Rule MF_00278
EC=2.4.2.- HAMAP-Rule MF_00278
Alternative name(s):
IGP synthase glutamine amidotransferase subunit HAMAP-Rule MF_00278
IGP synthase subunit HisH HAMAP-Rule MF_00278
ImGP synthase subunit HisH HAMAP-Rule MF_00278
Gene names
Name:hisH HAMAP-Rule MF_00278
Ordered Locus Names:Sbal223_1929 EMBL ACK46434.1
OrganismShewanella baltica (strain OS223) [Complete proteome] [HAMAP] EMBL ACK46434.1
Taxonomic identifier407976 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella ›

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR By similarity. SAAS SAAS010139 HAMAP-Rule MF_00278

Catalytic activity

5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide + L-glutamine = imidazole-glycerol phosphate + 5-aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H2O. SAAS SAAS010139 HAMAP-Rule MF_00278

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. SAAS SAAS010139 HAMAP-Rule MF_00278

Subunit structure

Heterodimer of HisH and HisF By similarity. SAAS SAAS010139 HAMAP-Rule MF_00278

Subcellular location

Cytoplasm By similarity SAAS SAAS010139 HAMAP-Rule MF_00278.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain. SAAS SAAS010139 HAMAP-Rule MF_00278

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain22 – 241220Glutamine amidotransferase type-1 By similarity HAMAP-Rule MF_00278

Sites

Active site971Nucleophile By similarity HAMAP-Rule MF_00278
Active site2161 By similarity HAMAP-Rule MF_00278
Active site2181 By similarity HAMAP-Rule MF_00278

Sequences

Sequence LengthMass (Da)Tools
B8E9A1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: B07D381F9B90EC7B

FASTA26428,131
        10         20         30         40         50         60 
MQQDTLLTAG QQLTANESPD AETVIIDTGC ANLSSVRFAF ERLGAKVLVT DDKAKIKAAK 

        70         80         90        100        110        120 
RVVLPGVGTA GVAMASLHEK GLVELIQGLT QPVLGVCLGM QMLAAISKER GGKGQDYECL 

       130        140        150        160        170        180 
GIIPTDICEL DTQLLKAESL PLPHMGWNQL KLTTNSQGAN SPNVHPLFAG IEDGSYVYFV 

       190        200        210        220        230        240 
HSYRAPLSEF TLAECTYGEG FSAAIGKGNF MGVQFHPEKS AAVGAQILRN FLQMDELQMN 

       250        260 
EALMNEALQS SSADGQAGVK KADQ

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS223."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS223.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001252 Genomic DNA. Translation: ACK46434.1.
RefSeqYP_002357857.1. NC_011663.1.

3D structure databases

ProteinModelPortalB8E9A1.
ModBaseSearch...

Protein-protein interaction databases

STRING407976.Sbal223_1929.

Protein family/group databases

MEROPSC26.965.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK46434; ACK46434; Sbal223_1929.
GeneID7090096.
KEGGsbp:Sbal223_1929.
PATRIC23480064. VBISheBal125792_1989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0118.
HOGENOMHOG000025030.
KOK02501.
OMAYGLGNLR.
ProtClustDBPRK13170.

Enzyme and pathway databases

BioCycSBAL407976:GJ6Y-2006-MONOMER.
UniPathwayUPA00031; UER00010.

Family and domain databases

HAMAPMF_00278. HisH.
InterProIPR017926. GATASE.
IPR010139. Imidazole-glycPsynth_HisH.
[Graphical view]
PfamPF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01855. IMP_synth_hisH. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB8E9A1_SHEB2
AccessionPrimary (citable) accession number: B8E9A1
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: May 29, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info