P58237 (HIS5_ECO57) 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:	Z3185, ECs2824

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	196 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
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 – 196	196	Imidazole glycerol phosphate synthase subunit HisH HAMAP-Rule MF_00278		PRO_0000152375
Regions
	Domain	2 – 196	195	Glutamine amidotransferase type-1
Sites
	Active site	77	1	Nucleophile By similarity
	Active site	178	1	By similarity
	Active site	180	1	By similarity
Experimental info
	Sequence conflict	7	1	G → D in BAA77742. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P58237 [UniParc]. Last modified August 14, 2001. Version 1. Checksum: 1B944DDECF810ED1	FASTA	196	21,595
	10 20 30 40 50 60 MNVVILGTGC ANLNSVKSAI ARHGYEPKVS RDPDVVLLAD KLFLPGVGTA QAAMDQVRER 70 80 90 100 110 120 ELFDLIKACT QPVLGICLGM QLLGRRSEES NGVDLLGIID EDVPKMTDFG LPLPHMGWNR 130 140 150 160 170 180 VYPQAGNRLF QGIEDGAYFY FVHSYAMPVN PWTIAQCNYG EPFTAAVQKD NFYGVQFHPE 190 RSGAAGAKLL KNFLEM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157." Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y. Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O157:H- / 184 / EHEC.
[2]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB008676 Genomic DNA. Translation: BAA77742.1. AE005174 Genomic DNA. Translation: AAG57082.1. BA000007 Genomic DNA. Translation: BAB36247.1.
PIR	F85827. H90981.
RefSeq	NP_288528.1. NC_002655.2. NP_310851.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P58237.
SMR	P58237. Positions 1-195.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z3185.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG57082; AAG57082; Z3185. BAB36247; BAB36247; BAB36247.
GeneID	913853. 962081.
KEGG	ece:Z3185. ecs:ECs2824.
PATRIC	18355036. VBIEscCol44059_2719.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0118.
HOGENOM	HOG000025030.
KO	K02501.
OMA	YGLGNLR.
ProtClustDB	PRK13170.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-2788-MONOMER.
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_ECO57

Accession

Primary (citable) accession number: P58237

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program