Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321NADBy similarity
Binding sitei194 – 1941NADBy similarity
Binding sitei217 – 2171NADBy similarity
Binding sitei244 – 2441SubstrateBy similarity
Metal bindingi266 – 2661ZincBy similarity
Binding sitei266 – 2661SubstrateBy similarity
Metal bindingi269 – 2691ZincBy similarity
Binding sitei269 – 2691SubstrateBy similarity
Active sitei335 – 3351Proton acceptorBy similarity
Active sitei336 – 3361Proton acceptorBy similarity
Binding sitei336 – 3361SubstrateBy similarity
Metal bindingi369 – 3691ZincBy similarity
Binding sitei369 – 3691SubstrateBy similarity
Binding sitei423 – 4231SubstrateBy similarity
Metal bindingi428 – 4281ZincBy similarity
Binding sitei428 – 4281SubstrateBy similarity

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: PomBase
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. 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
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

PomBaseiSPBC1711.13.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439Histidinol dehydrogenasePRO_0000135908Add
BLAST

Proteomic databases

MaxQBiQ9P777.
PaxDbiQ9P777.

Interactioni

Protein-protein interaction databases

BioGridi276205. 4 interactions.
DIPiDIP-59120N.
MINTiMINT-4704831.
STRINGi4896.SPBC1711.13-1.

Structurei

3D structure databases

ProteinModelPortaliQ9P777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ9P777.
KOiK14152.
OMAiLSVQSFL.
OrthoDBiEOG7DJSVM.
PhylomeDBiQ9P777.

Family and domain databases

HAMAPiMF_01024. HisD.
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. 4 interactions.
DIPiDIP-59120N.
MINTiMINT-4704831.
STRINGi4896.SPBC1711.13-1.

Proteomic databases

MaxQBiQ9P777.
PaxDbiQ9P777.

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

PomBaseiSPBC1711.13.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ9P777.
KOiK14152.
OMAiLSVQSFL.
OrthoDBiEOG7DJSVM.
PhylomeDBiQ9P777.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Miscellaneous databases

NextBioi20800804.
PROiQ9P777.

Family and domain databases

HAMAPiMF_01024. HisD.
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...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

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: April 1, 2015
This is version 98 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

External Data

Dasty 3

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 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.