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Protein

Histidinol dehydrogenase

Gene

his2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.By similarity

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: L-histidine biosynthesis

This protein is involved in step 9 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 (his1)
  2. Histidine biosynthesis bifunctional protein his7 (his7)
  3. Histidine biosynthesis bifunctional protein his7 (his7)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (SPAC3F10.09)
  5. Imidazole glycerol phosphate synthase hisHF (his4)
  6. Imidazoleglycerol-phosphate dehydratase (his5)
  7. Histidinol-phosphate aminotransferase (his3)
  8. Probable histidinol-phosphatase (SPCC1672.01)
  9. Histidinol dehydrogenase (his2)
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
Binding sitei132NADBy similarity1
Binding sitei194NADBy similarity1
Binding sitei217NADBy similarity1
Binding sitei244SubstrateBy similarity1
Metal bindingi266ZincBy similarity1
Binding sitei266SubstrateBy similarity1
Metal bindingi269ZincBy similarity1
Binding sitei269SubstrateBy similarity1
Active sitei335Proton acceptorBy similarity1
Active sitei336Proton acceptorBy similarity1
Binding sitei336SubstrateBy similarity1
Metal bindingi369ZincBy similarity1
Binding sitei369SubstrateBy similarity1
Binding sitei423SubstrateBy similarity1
Metal bindingi428ZincBy similarity1
Binding sitei428SubstrateBy similarity1

GO - Molecular functioni

  • histidinol dehydrogenase activity Source: PomBase
  • NAD binding Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • histidine biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:his2
ORF Names:SPBC1711.13
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1711.13.
PomBaseiSPBC1711.13. his2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001359081 – 439Histidinol dehydrogenaseAdd BLAST439

Proteomic databases

MaxQBiQ9P777.
PRIDEiQ9P777.

Interactioni

Protein-protein interaction databases

BioGridi276205. 3 interactors.
DIPiDIP-59120N.
MINTiMINT-4704831.

Structurei

3D structure databases

ProteinModelPortaliQ9P777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

HOGENOMiHOG000243914.
InParanoidiQ9P777.
KOiK14152.
OMAiGGTARFY.
OrthoDBiEOG092C2FQP.
PhylomeDBiQ9P777.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P777-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEYEIQVPS YRAAALTAEE RTRLLARPIQ NTQKIRTIVQ PIIEDVKSRG
60 70 80 90 100
EASLIDYASK FEKVQLKSAV LKAPFDDDLM KISPMIKEDI DIAFNNIFAF
110 120 130 140 150
HSSQLRPTIA VQTMRGVVCQ RMSRPINRVG LYIPGGTAVL PSTALMLGVP
160 170 180 190 200
AKVAGCPHVV ISTPVRKDGT VAPEIVYIAN KIGAEAIILA GGAQAIAAMA
210 220 230 240 250
YGISGVPKVN KIFGPGNQFV TAAKMHVQND YGALVAIDLP AGPSEVLVIA
260 270 280 290 300
DETCNPESVA LDLLSQAEHG LDSQIILLTV SLSPEMFDRI QKAINDHALR
310 320 330 340 350
LSRSYIIKHA IKKSVIVQVD NVDQAFEWSN LYGPEHLVLH LKNASSYIPK
360 370 380 390 400
IDNAGSVFVG PWSPVSMGDY ASGTNHTLPT YGYASSYSGV STDSFLKYIT
410 420 430
TQELTEEGIQ RLGPTVIRLA ELEGLTAHAD AVRVRGVRL
Length:439
Mass (Da):47,554
Last modified:October 1, 2000 - v1
Checksum:i7B054B5DBDAB2DEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB88243.1.
RefSeqiNP_595886.1. NM_001021792.2.

Genome annotation databases

EnsemblFungiiSPBC1711.13.1; SPBC1711.13.1:pep; SPBC1711.13.
GeneIDi2539650.
KEGGispo:SPBC1711.13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB88243.1.
RefSeqiNP_595886.1. NM_001021792.2.

3D structure databases

ProteinModelPortaliQ9P777.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276205. 3 interactors.
DIPiDIP-59120N.
MINTiMINT-4704831.

Proteomic databases

MaxQBiQ9P777.
PRIDEiQ9P777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1711.13.1; SPBC1711.13.1:pep; SPBC1711.13.
GeneIDi2539650.
KEGGispo:SPBC1711.13.

Organism-specific databases

EuPathDBiFungiDB:SPBC1711.13.
PomBaseiSPBC1711.13. his2.

Phylogenomic databases

HOGENOMiHOG000243914.
InParanoidiQ9P777.
KOiK14152.
OMAiGGTARFY.
OrthoDBiEOG092C2FQP.
PhylomeDBiQ9P777.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Miscellaneous databases

PROiQ9P777.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHISX_SCHPO
AccessioniPrimary (citable) accession number: Q9P777
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 1, 2000
Last modified: October 5, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

In contrast to other fungi who have a single histidine biosynthesis trifunctional protein, 2 proteins are present in S.pombe to ensure these functions: his7 (phosphoribosyl-AMP cyclohydrolase and phosphoribosyl-ATP pyrophosphatase activities) and his2 (histidinol dehydrogenase activity).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.