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Q9F854 (HISX_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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:VC_1133
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length431 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135874

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site1271NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9F854 [UniParc].

Last modified March 25, 2003. Version 2.
Checksum: 435CDAF188C4926C

FASTA43146,127
        10         20         30         40         50         60 
MRTVVWQSLS EAQQESILER PAITEGANIT AAVAQVIAKV RSEGDAALFE LTEKFDRVKP 

        70         80         90        100        110        120 
ASLRVSREEM DAAAARLSET MKQALEQAYN NISKFHKAQK AQPIKVETMP GVVCEQVTRP 

       130        140        150        160        170        180 
INKVGLYIPG GSAPLPSTVL MLGVPAQIAG CRKVVLCSPP PIADEILYVA KLCNIDEVYN 

       190        200        210        220        230        240 
LGGGQAIAAM AYGTETVTKV DKIFGPGNAY VTEAKRQVSN DFRGAAIDMP AGPSEVLVIA 

       250        260        270        280        290        300 
DETADANFIA ADLLSQAEHG PDSQVVLVTP SPVLADQVTD AVQKQLKVLS RASIAEKALA 

       310        320        330        340        350        360 
SSLIIIAESL TQAVSISNYY GPEHLIVQTR NPRELVPLLD NAGSIFLGDW SPESVGDYAS 

       370        380        390        400        410        420 
GTNHVLPTYG YTRTYSSLGL ADFSKRMTVQ ELTADGLQLL APTVVTMAEA EGLDAHKRAV 

       430 
TIRVEKLQKA Q 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF94292.1.
AF261153 Genomic DNA. Translation: AAG16130.1.
PIRH82237.
RefSeqNP_230778.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9F854.
SMRQ9F854. Positions 6-429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC1133.

Protocols and materials databases

DNASU2614403.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94292; AAF94292; VC_1133.
GeneID2614403.
KEGGvch:VC1133.
PATRIC20081358. VBIVibCho83274_1082.

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycVCHO:VC1133-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_VIBCH
AccessionPrimary (citable) accession number: Q9F854
Secondary accession number(s): Q9KSX3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 25, 2003
Last modified: May 14, 2014
This is version 90 of the entry and version 2 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