G7TPI5 (G7TPI5_VIBCL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended 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 EMBL AET26248.1
ORF Names:	Vch1786_I0640 EMBL AET26248.1

Organism

Vibrio cholerae O1 str. 2010EL-1786 EMBL AET26248.1

Taxonomic identifier

914149 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio cholerae › Vibrio cholerae O1

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Protein existence	Inferred 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

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis SAAS SAAS010139 HAMAP-Rule MF_00278
Cellular component	Cytoplasm SAAS SAAS010139 HAMAP-Rule MF_00278
Domain	Glutamine amidotransferase SAAS SAAS010139 HAMAP-Rule MF_00278
Molecular function	Glycosyltransferase EMBL AET26248.1 Transferase
Gene Ontology (GO)
Biological_process	glutamine metabolic process Inferred from electronic annotation. Source: HAMAP histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	imidazoleglycerol-phosphate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Domain	4 – 203	200	Glutamine amidotransferase type-1 By similarity HAMAP-Rule MF_00278
Sites
	Active site	79	1	Nucleophile By similarity HAMAP-Rule MF_00278
	Active site	185	1	By similarity HAMAP-Rule MF_00278
	Active site	187	1	By similarity HAMAP-Rule MF_00278

Sequences

	Sequence		Length	Mass (Da)
	G7TPI5 [UniParc]. Last modified January 25, 2012. Version 1. Checksum: 2FE3C1D485995700	FASTA	203	22,274
	10 20 30 40 50 60 MTQNVVIIDT GCANISSVKF AIERLGYAVT ISRDPQVVLA ADKLFLPGVG TASEAMKNLT 70 80 90 100 110 120 ERDLIELVKR VEKPLLGICL GMQLLGKLSE EKGQKADEIV QCLGLVDGEV RLLQTGDLPL 130 140 150 160 170 180 PHMGWNTVQV KEGHPLFNGI EPDAYFYFVH SFAMPVGDYT IAQCEYGQPF SAAIQAGNYY 190 200 GVQFHPERSS KAGARLIQNF LEL

References

[1]	Balajee S.A., Besser J., Fields P., Frace A.M., Freeman M., Govil D., Humphrys M., Neuhaus E., Olsen-Rasmussen M., Ribot E., Rowe L., Sammons S., Seenu S., Talkington D., Tang K., Tarr C., Gerner-Smidt P. Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 2010EL-1786 EMBL AET26248.1.
[2]	"Comparative Genomics of Vibrio cholerae from Haiti, Asia, and Africa." Reimer A.R., Domselaar G.V., Stroika S., Walker M., Kent H., Tarr C., Talkington D., Rowe L., Olsen-Rasmussen M., Frace M., Sammons S., Dahourou G.A., Boncy J., Smith A.M., Mabon P., Petkau A., Graham M., Gilmour M.W., Gerner-Smidt P. Emerg. Infect. Dis. 17:2113-2121(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 2010EL-1786 EMBL AET26248.1.
[3]	V. cholerae Outbreak Genomics Task Force Reimer A.R., Van Domselaar G., Stroika S., Walker M., Kent H., Tarr C., Talkington D., Rowe L., Olsen-Rasmussen M., Frace M., Sammons S., Dahourou G.A., Boncy J., Smith A.M., Mabon P., Petkau A., Graham M., Gilmour M.W., Gerner-Smidt P. Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 2010EL-1786 EMBL AET26248.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003069 Genomic DNA. Translation: AET26248.1.
RefSeq	YP_004936802.1. NC_016445.1.
3D structure databases
ProteinModelPortal	G7TPI5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AET26248; AET26248; Vch1786_I0640.
GeneID	11460459.
KEGG	vce:Vch1786_I0640.
Phylogenomic databases
KO	K02501.
Enzyme and pathway databases
UniPathway	UPA00031; UER00010.
Family and domain databases
HAMAP	MF_00278. HisH.
InterPro	IPR017926. GATASE_1. IPR010139. Imidazole-glycPsynth_HisH. [Graphical view]
Pfam	PF00117. GATase. 1 hit. [Graphical view]
PIRSF	PIRSF000495. Amidotransf_hisH. 1 hit.
TIGRFAMs	TIGR01855. IMP_synth_hisH. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G7TPI5_VIBCL

Accession

Primary (citable) accession number: G7TPI5

Entry history

Integrated into UniProtKB/TrEMBL:	January 25, 2012
Last sequence update:	January 25, 2012
Last modified:	April 3, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)