Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9P777 (HISX_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase

Short name=HDH
EC=1.1.1.23
Gene names
Name:his2
ORF Names:SPBC1711.13
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

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).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 439439Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135908

Sites

Active site3351Proton acceptor By similarity
Active site3361Proton acceptor By similarity
Metal binding2661Zinc By similarity
Metal binding2691Zinc By similarity
Metal binding3691Zinc By similarity
Metal binding4281Zinc By similarity
Binding site1321NAD By similarity
Binding site1941NAD By similarity
Binding site2171NAD By similarity
Binding site2441Substrate By similarity
Binding site2661Substrate By similarity
Binding site2691Substrate By similarity
Binding site3361Substrate By similarity
Binding site3691Substrate By similarity
Binding site4231Substrate By similarity
Binding site4281Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9P777 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7B054B5DBDAB2DEA

FASTA43947,554
        10         20         30         40         50         60 
MPEYEIQVPS YRAAALTAEE RTRLLARPIQ NTQKIRTIVQ PIIEDVKSRG EASLIDYASK 

        70         80         90        100        110        120 
FEKVQLKSAV LKAPFDDDLM KISPMIKEDI DIAFNNIFAF HSSQLRPTIA VQTMRGVVCQ 

       130        140        150        160        170        180 
RMSRPINRVG LYIPGGTAVL PSTALMLGVP AKVAGCPHVV ISTPVRKDGT VAPEIVYIAN 

       190        200        210        220        230        240 
KIGAEAIILA GGAQAIAAMA YGISGVPKVN KIFGPGNQFV TAAKMHVQND YGALVAIDLP 

       250        260        270        280        290        300 
AGPSEVLVIA DETCNPESVA LDLLSQAEHG LDSQIILLTV SLSPEMFDRI QKAINDHALR 

       310        320        330        340        350        360 
LSRSYIIKHA IKKSVIVQVD NVDQAFEWSN LYGPEHLVLH LKNASSYIPK IDNAGSVFVG 

       370        380        390        400        410        420 
PWSPVSMGDY ASGTNHTLPT YGYASSYSGV STDSFLKYIT TQELTEEGIQ RLGPTVIRLA 

       430 
ELEGLTAHAD AVRVRGVRL 

« Hide

References

[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. expand/collapse author list , 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(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAB88243.1.
RefSeqNP_595886.1. NM_001021792.2.

3D structure databases

ProteinModelPortalQ9P777.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276205. 5 interactions.
DIPDIP-59120N.
MINTMINT-4704831.
STRING4896.SPBC1711.13-1.

Proteomic databases

MaxQBQ9P777.
PaxDbQ9P777.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC1711.13.1; SPBC1711.13.1:pep; SPBC1711.13.
GeneID2539650.
KEGGspo:SPBC1711.13.

Organism-specific databases

PomBaseSPBC1711.13.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPRGDFAS.
OrthoDBEOG7DJSVM.
PhylomeDBQ9P777.

Enzyme and pathway databases

UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800804.
PROQ9P777.

Entry information

Entry nameHISX_SCHPO
AccessionPrimary (citable) accession number: Q9P777
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways