P0A1R4 (HIS5_SALTY) 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:	STM2075

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

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.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Contains 1 glutamine amidotransferase type-1 domain.
Sequence caution	The sequence AAL20979.1 differs from that shown. Reason: Erroneous initiation.

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 – 196	196	Imidazole glycerol phosphate synthase subunit HisH HAMAP-Rule MF_00278		PRO_0000152419
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	9	1	Missing in CAA31826. Ref.1
	Sequence conflict	20 – 30	11	VARHGYTPVVS → GAPRLHPGGQ in CAA31826. Ref.1
	Sequence conflict	57	1	L → V in CAA31826. Ref.1
	Sequence conflict	125	1	A → R in CAA31826. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0A1R4 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 0F870A5696A71E85	FASTA	196	21,704
	10 20 30 40 50 60 MNVVILDTGC ANLSSVKSAV ARHGYTPVVS REAEIVLRAD KLFLPGVGTA QAAMDQLRER 70 80 90 100 110 120 ELIDLIKACT QPVLGICLGM QLLGRRSEET RGVDLLNIIE QDVPKMTDFG LPLPHMGWNR 130 140 150 160 170 180 VYPQAGNRLF QGIEDGAYFY FVHSYAMPVN PWTIAQCNYG EPFTAAVQKD NFFGVQFHPE 190 RSGAAGAQLL KNFLEM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B. J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13464 Genomic DNA. Translation: CAA31826.1. AE006468 Genomic DNA. Translation: AAL20979.1. Different initiation.
PIR	XQEBHT. JS0160.
RefSeq	NP_461020.2. NC_003197.1.
3D structure databases
ProteinModelPortal	P0A1R4.
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM2075.
Proteomic databases
PRIDE	P0A1R4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL20979; AAL20979; STM2075.
GeneID	1253596.
KEGG	stm:STM2075.
PATRIC	32382733. VBISalEnt20916_2197.
Phylogenomic databases
HOGENOM	HOG000025030.
KO	K02501.
OMA	YGLGNLR.
ProtClustDB	PRK13170.
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

HIS5_SALTY

Accession

Primary (citable) accession number: P0A1R4
Secondary accession number(s): P10376

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	May 1, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program