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Protein

Imidazole glycerol phosphate synthase subunit HisH

Gene

hisH

Organism
Buchnera aphidicola subsp. Diuraphis noxia
Status
Reviewed-Annotation score: -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), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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 cyclase subunit (ATN01_00515), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Imidazoleglycerol-phosphate dehydratase (hisB)
  9. Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD)
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 sitei78NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processAmino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

UniPathwayi
UPA00031;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
OrganismiBuchnera aphidicola subsp. Diuraphis noxia
Taxonomic identifieri118101 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001523571 – ›175Imidazole glycerol phosphate synthase subunit HisHAdd BLAST›175

Interactioni

Subunit structurei

Heterodimer of HisH and HisF.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ84I56
SMRiQ84I56
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – ›175Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST›173

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

Gene3Di3.40.50.880, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR017926 GATASE
IPR010139 Imidazole-glycPsynth_HisH
PANTHERiPTHR42701 PTHR42701, 1 hit
PfamiView protein in Pfam
PF00117 GATase, 1 hit
PIRSFiPIRSF000495 Amidotransf_hisH, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
TIGRFAMsiTIGR01855 IMP_synth_hisH, 1 hit
PROSITEiView protein in PROSITE
PS51273 GATASE_TYPE_1, 1 hit

Sequencei

Sequence statusi: Fragment.

Q84I56-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKIIILNTD CANFTSIKSA IEKLGYCCMI TAEPSIVKNA KKIILPGVGT
60 70 80 90 100
ALAAMNFLSQ KKLVDIIKTF TNPILGICLG MQIFCNFSEE SNGVKTIGVV
110 120 130 140 150
KTSVLHLKTN NLPLPHIGWN QISFNKCHAL FKDIPNNSRF YFVHSYIVPV
160 170
NKYTLSVTNY GMNFSSVIQK NNFWR
Length:175
Mass (Da):19,540
Last modified:June 1, 2003 - v1
Checksum:iE50851BA299D89C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei1751

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF465524 Genomic DNA Translation: AAO33042.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF465524 Genomic DNA Translation: AAO33042.1

3D structure databases

ProteinModelPortaliQ84I56
SMRiQ84I56
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00031;UER00010

Family and domain databases

Gene3Di3.40.50.880, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR017926 GATASE
IPR010139 Imidazole-glycPsynth_HisH
PANTHERiPTHR42701 PTHR42701, 1 hit
PfamiView protein in Pfam
PF00117 GATase, 1 hit
PIRSFiPIRSF000495 Amidotransf_hisH, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
TIGRFAMsiTIGR01855 IMP_synth_hisH, 1 hit
PROSITEiView protein in PROSITE
PS51273 GATASE_TYPE_1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHIS5_BUCDN
AccessioniPrimary (citable) accession number: Q84I56
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: June 1, 2003
Last modified: December 20, 2017
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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