Q9K0H2 (HIS5_NEIMB) 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:	NMB0630

Organism

Neisseria meningitidis serogroup B

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	212 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 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 MF_00278
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. HAMAP MF_00278
Subunit structure	Heterodimer of HisH and HisF By similarity. HAMAP MF_00278
Subcellular location	Cytoplasm By similarity HAMAP 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: UniProtKB-KW histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	transferase activity, transferring pentosyl groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 212	212	Imidazole glycerol phosphate synthase subunit HisH HAMAP MF_00278		PRO_0000152398
Regions
	Domain	2 – 212	211	Glutamine amidotransferase type-1
Sites
	Active site	85	1	Nucleophile By similarity
	Active site	194	1	By similarity
	Active site	196	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K0H2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 959B2F21BB5DF77B	FASTA	212	23,773
	10 20 30 40 50 60 MQTAIIDYGM GNLHSVLKSV RTAGQLAGKN TEIFLSGDPD RVSRADKVIF PGQGAMPDCM 70 80 90 100 110 120 AALKRDGLDE AVKDALKNKP FFGICVGAQL LFDHSEEGNT DGLGWFGGKV RRFERDLRDP 130 140 150 160 170 180 QGCRLKVPHM GWNTVRQTQN HPLFKDIPQD TRFYFVHSYY FAPENPETIL GESDYPSPFA 190 200 210 CIVGKDNVFA TQFHTEKSHD AGLTMLKNFL NW

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF41055.1.
PIR	B81177.
RefSeq	NP_273673.1. NC_003112.2.
3D structure databases
ProteinModelPortal	Q9K0H2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000010639; EBNEIP00000010259; EBNEIG00000010639.
GeneID	902743.
GenomeReviews	Gene locus NMB0630 in contig AE002098_GR.
KEGG	nme:NMB0630.
NMPDR	fig|122586.1.peg.607.
PATRIC	20356557. VBINeiMen85645_0798.
TIGR	NMB0630.
Phylogenomic databases
GeneTree	EBGT00050000020555.
HOGENOM	HBG292341.
OMA	SVRFAFE.
ProtClustDB	PRK13146.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_0630-MONOMER.
Family and domain databases
HAMAP	MF_00278. HisH. [Tree]
InterPro	IPR017926. GATASE_1. IPR010139. Imidazole-glycPsynth_HisH. [Graphical view]
KO	K02501.
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_NEIMB

Accession

Primary (citable) accession number: Q9K0H2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program