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Q8ZFX5 (HISX_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:hisD
Ordered Locus Names:YPO1548, y2621, YP_1437
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length443 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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135887

Sites

Active site3291Proton acceptor By similarity
Active site3301Proton acceptor By similarity
Metal binding2621Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding3631Zinc By similarity
Metal binding4221Zinc By similarity
Binding site1331NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2401Substrate By similarity
Binding site2621Substrate By similarity
Binding site2651Substrate By similarity
Binding site3301Substrate By similarity
Binding site3631Substrate By similarity
Binding site4171Substrate By similarity
Binding site4221Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZFX5 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E4841C0ACE54772C

FASTA44347,233
        10         20         30         40         50         60 
MQPTNFNTLI NWQQCSEEQQ KALLSRPAIN ASERITAAVS DILDRVKAEG DSALRDFSQR 

        70         80         90        100        110        120 
FDHVQVADIR ITASEIAAAS ARLSDDVKHA MAQAVRNIEI FHNAQKMPVV DVETQPGVRC 

       130        140        150        160        170        180 
QQITRPIASV GLYIPGGSAP LPSTVLMLGT PARIAGCQRV VLCSPPPIAD EILYAAQLCG 

       190        200        210        220        230        240 
IQEVFQIGGA QAIAAMAFGS ESVPKVHKIF GPGNAYVTEA KRQVSQRLDG AAIDMPAGPS 

       250        260        270        280        290        300 
EVLVIADSGA TPAFIAADLL SQAEHGPDSQ VILLTPDAAI AQAVAVEVEQ QLALLSRADI 

       310        320        330        340        350        360 
ARQALESSRL IVTNDLQQCI DISNAYGPEH LILQIRQPEE IIDQIDNAGS VFMGDWSPES 

       370        380        390        400        410        420 
AGDYASGTNH VLPTYGYTST YSSLGLADFV KRMTVQQLTP QGLLGLASTI ETLAQAEQLT 

       430        440 
AHKNAVTLRV TALNNALTAV NKE 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM10+ / Biovar Mediaevalis.
[3]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL20194.1.
AE009952 Genomic DNA. Translation: AAM86175.1.
AE017042 Genomic DNA. Translation: AAS61678.1.
PIRAH0188.
RefSeqNP_669924.1. NC_004088.1.
NP_992801.1. NC_005810.1.
YP_002346564.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZFX5.
SMRQ8ZFX5. Positions 5-433.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8ZFX5. 10 interactions.
STRING214092.YPO1548.

Proteomic databases

PRIDEQ8ZFX5.

Protocols and materials databases

DNASU1147568.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM86175; AAM86175; y2621.
AAS61678; AAS61678; YP_1437.
GeneID1147568.
1174387.
2765680.
KEGGype:YPO1548.
ypk:y2621.
ypm:YP_1437.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycYPES214092:GKDD-1529-MONOMER.
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...

Entry information

Entry nameHISX_YERPE
AccessionPrimary (citable) accession number: Q8ZFX5
Secondary accession number(s): Q0WGM4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways