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Q5LAZ8 (HISX_BACFN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:BF3029
OrganismBacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]
Taxonomic identifier272559 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length428 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 – 428428Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135731

Sites

Active site3221Proton acceptor By similarity
Active site3231Proton acceptor By similarity
Metal binding2551Zinc By similarity
Metal binding2581Zinc By similarity
Metal binding3561Zinc By similarity
Metal binding4151Zinc By similarity
Binding site1241NAD By similarity
Binding site1861NAD By similarity
Binding site2091NAD By similarity
Binding site2331Substrate By similarity
Binding site2551Substrate By similarity
Binding site2581Substrate By similarity
Binding site3231Substrate By similarity
Binding site3561Substrate By similarity
Binding site4101Substrate By similarity
Binding site4151Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LAZ8 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 731DC2A51FA3930E

FASTA42846,535
        10         20         30         40         50         60 
MKLIKYPDRS QWNEILKRPV LETENLFDTV RNIINRVRAG GDRVVMEYEA VFDKAELTSL 

        70         80         90        100        110        120 
AVTSAEIEEA EKEVPIELKA AIYLAKRNIE TFHSAQRFEG KKVDTMEGVT CWQKAVAIEK 

       130        140        150        160        170        180 
VGLYIPGGTA PLFSTVLMLA IPAKIAGCKE IVLCTPPDKN GKVHPAILFA ARLAGVSKIF 

       190        200        210        220        230        240 
KAGGVQAIAA MAYGTESIPK VYKIFGPGNQ YVTAAKQLVS LRDVAIDMPA GPSEVEVLAD 

       250        260        270        280        290        300 
ESANPVFVAA DLLSQAEHGV DSQAMLVTTS EKLQTEVVYE VERQLGYLTR RDIAEKSLAS 

       310        320        330        340        350        360 
SKLILVKDME EALELTNAYA PEHLIIETKD YMEVAGQIVN AGSVFLGAFS PESAGDYASG 

       370        380        390        400        410        420 
TNHTLPTNGY AKAYSGVSLD SFIRKITFQE ILPSGMSAIG PAIEVMAANE HLDAHKNAVT 


VRLEEIRK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR626927 Genomic DNA. Translation: CAH08724.1.
RefSeqYP_212643.1. NC_003228.3.

3D structure databases

ProteinModelPortalQ5LAZ8.
SMRQ5LAZ8. Positions 8-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272559.BF3029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH08724; CAH08724; BF9343_2943.
GeneID3289178.
KEGGbfs:BF3029.
PATRIC21042676. VBIBacFra29119_3058.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAWALMIER.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycBFRA272559:GKF0-2985-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_BACFN
AccessionPrimary (citable) accession number: Q5LAZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 21, 2005
Last modified: May 14, 2014
This is version 65 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