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Protein

Imidazole glycerol phosphate synthase subunit HisH

Gene

hisH

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidinol-phosphatase (hisN)
  9. 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821NucleophileBy similarity
Active sitei192 – 1921By similarity
Active sitei194 – 1941By similarity

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:Cgl2097, cg2300
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Imidazole glycerol phosphate synthase subunit HisHPRO_0000152370Add
BLAST

Interactioni

Subunit structurei

Heterodimer of HisH and HisF.By similarity

Protein-protein interaction databases

STRINGi196627.cg2300.

Structurei

3D structure databases

ProteinModelPortaliO69043.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 211208Glutamine amidotransferase type-1Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4108UJE. Bacteria.
COG0118. LUCA.
HOGENOMiHOG000025030.
KOiK02501.
OMAiGMQMLLT.
OrthoDBiEOG69KV05.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH.
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.

O69043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTVALLDY GSGNLRSAQR ALERAGAEVI VSSDPEVCTN ADGLLVPGVG
60 70 80 90 100
AFDACMKGLK NVFGHRIIGQ RLAGGRPVMG ICVGMQILFD EGDEHGIKSA
110 120 130 140 150
GCGEWPGKVE RLQAEILPHM GWNTLEMPTN SPMFEGISPD ERFYFVHSYG
160 170 180 190 200
VRKWTLETDD LTTPPEVVWA KHENDRFVAA VENGTLWATQ FHPEKSGDAG
210
AQLLRNWINY I
Length:211
Mass (Da):23,173
Last modified:August 13, 2002 - v2
Checksum:i73FB994AB5200C85
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 247AQRALER → LRRTRAL in AAC15231 (Ref. 1) Curated
Sequence conflicti28 – 292EV → SMF in AAC15231 (Ref. 1) Curated
Sequence conflicti34 – 418DPEVCTNA → IQKLHPTH in AAC15231 (Ref. 1) Curated
Sequence conflicti64 – 696GHRIIG → DIAYR in AAC15231 (Ref. 1) Curated
Sequence conflicti165 – 1706PEVVWA → QSCVG in AAC15231 (Ref. 1) Curated
Sequence conflicti174 – 1763NDR → VS in AAC15231 (Ref. 1) Curated
Sequence conflicti198 – 21114DAGAQ…WINYI → EQGXSYCETGSTTSNR (Ref. 1) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060558 Genomic DNA. Translation: AAC15231.1.
BA000036 Genomic DNA. Translation: BAB99490.1.
BX927154 Genomic DNA. Translation: CAF20433.1.
RefSeqiNP_601296.1. NC_003450.3.
WP_011014877.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99490; BAB99490; BAB99490.
CAF20433; CAF20433; cg2300.
GeneIDi1020048.
KEGGicgb:cg2300.
cgl:NCgl2016.
PATRICi21496194. VBICorGlu203724_2033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060558 Genomic DNA. Translation: AAC15231.1.
BA000036 Genomic DNA. Translation: BAB99490.1.
BX927154 Genomic DNA. Translation: CAF20433.1.
RefSeqiNP_601296.1. NC_003450.3.
WP_011014877.1. NC_006958.1.

3D structure databases

ProteinModelPortaliO69043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99490; BAB99490; BAB99490.
CAF20433; CAF20433; cg2300.
GeneIDi1020048.
KEGGicgb:cg2300.
cgl:NCgl2016.
PATRICi21496194. VBICorGlu203724_2033.

Phylogenomic databases

eggNOGiENOG4108UJE. Bacteria.
COG0118. LUCA.
HOGENOMiHOG000025030.
KOiK02501.
OMAiGMQMLLT.
OrthoDBiEOG69KV05.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00010.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00278. HisH.
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...

Publicationsi

« Hide 'large scale' publications
  1. Jung S.I., Han M.S., Park Y.J., Lee S.K., Lee M.-S.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
  2. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiHIS5_CORGL
AccessioniPrimary (citable) accession number: O69043
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: August 13, 2002
Last modified: November 11, 2015
This is version 113 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.