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Q4QN74 (HISX_HAEI8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:NTHI0600
OrganismHaemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]
Taxonomic identifier281310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length427 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete 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 – 427427Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135778

Sites

Active site3211Proton acceptor By similarity
Active site3221Proton acceptor By similarity
Metal binding2541Zinc By similarity
Metal binding2571Zinc By similarity
Metal binding3551Zinc By similarity
Metal binding4141Zinc By similarity
Binding site1271NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2321Substrate By similarity
Binding site2541Substrate By similarity
Binding site2571Substrate By similarity
Binding site3221Substrate By similarity
Binding site3551Substrate By similarity
Binding site4091Substrate By similarity
Binding site4141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4QN74 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: B30E2B902B4C659B

FASTA42746,312
        10         20         30         40         50         60 
MQTIIWNHLS ETEKRKVIMR PVQQNGENIQ QAVNAIRENV AYNGDRALFE LCEKFDGVKL 

        70         80         90        100        110        120 
DKLIVSADEI QAASSRISVK LRNAIEQAKT NIEAFHKAQQ NQEIDLEIQE GVRCQVVTRP 

       130        140        150        160        170        180 
ISCVGLYIPG GSAPLFSTVL MLAIPAKIAG CKKIVLCSPP PISDEILYTA HLCGVETIYA 

       190        200        210        220        230        240 
IGGAQAVFAM AQGTESVAKV DKIFGPGNAF VTEAKRQVAQ NSTAIDMPAG PSEVLVIADE 

       250        260        270        280        290        300 
SADPEFVASD LLSQAEHGAD SQVILVATCE TLAKETALAI ERQLALLPRA ETARKALNHS 

       310        320        330        340        350        360 
RIFIAESLEQ AVEISNEYAP EHLIVQTKNA RKLLPYLDNA GSIFLGAYSP ESMGDYASGT 

       370        380        390        400        410        420 
NHVLPTYGYT KTYSSLGLAD FSKRMTVQEL TPKGFKNLAE TVEVMAEAEQ LAAHKMAVSV 


RLAKLNI 

« Hide

References

[1]"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 86-028NP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000057 Genomic DNA. Translation: AAX87523.1.
RefSeqYP_248183.1. NC_007146.2.

3D structure databases

ProteinModelPortalQ4QN74.
SMRQ4QN74. Positions 4-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281310.NTHI0600.

Proteomic databases

PRIDEQ4QN74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX87523; AAX87523; NTHI0600.
GeneID3429910.
KEGGhit:NTHI0600.
PATRIC20181357. VBIHaeInf100748_0552.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycHINF281310:GJ89-562-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_HAEI8
AccessionPrimary (citable) accession number: Q4QN74
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 19, 2005
Last modified: May 14, 2014
This is version 64 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