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Protein

Imidazole glycerol phosphate synthase subunit HisH

Gene

hisH

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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.

Pathwayi: L-histidine biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Putative histidinol dehydrogenase 2 (hisD2), Histidinol dehydrogenase 1 (hisD1)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei87NucleophileBy similarity1
Active sitei192By similarity1
Active sitei194By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00031; UER00010.

Names & Taxonomyi

Protein namesi
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 namesi
Name:hisH
Ordered Locus Names:RHOS4_08320
ORF Names:RSP_2245
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002703 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001524171 – 212Imidazole glycerol phosphate synthase subunit HisHAdd BLAST212

Interactioni

Subunit structurei

Heterodimer of HisH and HisF.By similarity

Protein-protein interaction databases

STRINGi272943.RSP_2245.

Structurei

3D structure databases

ProteinModelPortaliO33565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 212Glutamine amidotransferase type-1Add BLAST211

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4108UJE. Bacteria.
COG0118. LUCA.
HOGENOMiHOG000025030.
KOiK02501.
OMAiGMQMLLT.
OrthoDBiPOG091H03NT.
PhylomeDBiO33565.

Family and domain databases

CDDicd01748. GATase1_IGP_Synthase. 1 hit.
Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010139. Imidazole-glycPsynth_HisH.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
PIRSFiPIRSF000495. Amidotransf_hisH. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01855. IMP_synth_hisH. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O33565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTVLVDYDS GNLHSAEKAF QRMATETGAG QVLVSDRPED VARADRIVLP
60 70 80 90 100
GDGAFPACRR ALGSYGGLSE AIEEAVTRRA RPFLGICIGM QMMATRGLEH
110 120 130 140 150
EETPGFGWIA GEVVRIAPSD PHLKVPHMGW NDLTVDHPHP VLTGIETGDH
160 170 180 190 200
AYFVHSYHFQ VAHDAERLAH ADYGADITAI VGRDTMVGTQ FHPEKSQKTG
210
LRLIANFLTW KP
Length:212
Mass (Da):23,207
Last modified:January 24, 2006 - v2
Checksum:i20295625CFC3C4DE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti111G → A in CAA60713 (Ref. 1) Curated1
Sequence conflicti131 – 132ND → ER in CAA60713 (Ref. 1) Curated2
Sequence conflicti200 – 202GLR → AA in CAA60713 (Ref. 1) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87256 Genomic DNA. Translation: CAA60713.1.
CP000143 Genomic DNA. Translation: ABA78400.1.
RefSeqiWP_011337344.1. NZ_AKVW01000001.1.
YP_352301.1. NC_007493.2.

Genome annotation databases

EnsemblBacteriaiABA78400; ABA78400; RSP_2245.
GeneIDi3719775.
KEGGirsp:RSP_2245.
PATRICi23151508. VBIRhoSph57909_1148.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87256 Genomic DNA. Translation: CAA60713.1.
CP000143 Genomic DNA. Translation: ABA78400.1.
RefSeqiWP_011337344.1. NZ_AKVW01000001.1.
YP_352301.1. NC_007493.2.

3D structure databases

ProteinModelPortaliO33565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_2245.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA78400; ABA78400; RSP_2245.
GeneIDi3719775.
KEGGirsp:RSP_2245.
PATRICi23151508. VBIRhoSph57909_1148.

Phylogenomic databases

eggNOGiENOG4108UJE. Bacteria.
COG0118. LUCA.
HOGENOMiHOG000025030.
KOiK02501.
OMAiGMQMLLT.
OrthoDBiPOG091H03NT.
PhylomeDBiO33565.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00010.

Family and domain databases

CDDicd01748. GATase1_IGP_Synthase. 1 hit.
Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010139. Imidazole-glycPsynth_HisH.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
PIRSFiPIRSF000495. Amidotransf_hisH. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01855. IMP_synth_hisH. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS5_RHOS4
AccessioniPrimary (citable) accession number: O33565
Secondary accession number(s): Q3J484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.