P44340 (HIS5_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Imidazole glycerol phosphate synthase subunit HisH
EC=2.4.2.-

Alternative name(s):
IGP synthase glutamine amidotransferase subunit
IGP synthase subunit HisH
ImGP synthase subunit HisH
Short name=IGPS subunit HisH

Gene names

Name:	hisH
Ordered Locus Names:	HI_0472

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	199 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. 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. HAMAP-Rule MF_00278
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. HAMAP-Rule MF_00278
Subunit structure	Heterodimer of HisH and HisF By similarity. HAMAP-Rule MF_00278
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00278.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
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
Molecule processing
	Chain	1 – 199	199	Imidazole glycerol phosphate synthase subunit HisH HAMAP-Rule MF_00278		PRO_0000152379
Regions
	Domain	3 – 199	197	Glutamine amidotransferase type-1
Sites
	Active site	78	1	Nucleophile By similarity
	Active site	178	1	By similarity
	Active site	180	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44340 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: C79126E93E1B55D9	FASTA	199	22,048
	10 20 30 40 50 60 MINITIIDTG CANLSSVKFA FDRLGYNTEI TFDLNKIKSA DKLILPGVGT ANAAMYNLQE 70 80 90 100 110 120 RQLIETIQNL TQPVLGICLG MQLMTEFSEE GNVPTLNLIS GKTNRIPDTG LPLPQMGWNR 130 140 150 160 170 180 VQFVKNCPLF DGIVQNSHFY FVHSYAVSPN EHSVAISNYG VNFSAAIAKE NFYGVQFHPE 190 RSGKNGALLL KNFVEKVPF

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. , 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22131.1.
PIR	G64070.
RefSeq	NP_438633.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44340.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0472.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22131; AAC22131; HI_0472.
GeneID	949532.
KEGG	hin:HI0472.
PATRIC	20189499. VBIHaeInf48452_0492.
Phylogenomic databases
eggNOG	COG0118.
KO	K02501.
OMA	YSEEDDI.
ProtClustDB	PRK13170.
Enzyme and pathway databases
UniPathway	UPA00031; UER00010.
Family and domain databases
HAMAP	MF_00278. HisH.
InterPro	IPR017926. GATASE. 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

HIS5_HAEIN

Accession

Primary (citable) accession number: P44340

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program