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Q4FNE2 (HISX1_PELUB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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 1

Short name=HDH 1
EC=1.1.1.23
Gene names
Name:hisD1
Ordered Locus Names:SAR11_0475
OrganismPelagibacter ubique (strain HTCC1062) [Complete proteome] [HAMAP]
Taxonomic identifier335992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSAR11 clusterCandidatus Pelagibacter

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 1 HAMAP-Rule MF_01024
PRO_0000135809

Sites

Active site3241Proton acceptor By similarity
Active site3251Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3581Zinc By similarity
Metal binding4171Zinc By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3251Substrate By similarity
Binding site3581Substrate By similarity
Binding site4121Substrate By similarity
Binding site4171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FNE2 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 87F54F17177A8658

FASTA42847,310
        10         20         30         40         50         60 
MIKILDSKNK NFDKTLDALL SKRKNKVQLN SVSVIKIIKD VKKNGDKAIL KYEKRFNKNS 

        70         80         90        100        110        120 
IIAPSIKQIN RAIQSLDQKV KKAIDLAYDR IYKFHSLQKF KNISYTDKLK NKLEYKYVPI 

       130        140        150        160        170        180 
ESVAIYVPGS TASYPSSVLM NAVPAIVAGV KRLVMVNPGQ KGKQNPAVLY AAKKCKIKEI 

       190        200        210        220        230        240 
YSIGGPSAIA AVAYGTKKIK KVDKIIGPGN SYVAAAKKEV FGDVGIEGMI AGPSEVTIVC 

       250        260        270        280        290        300 
DKFSNPEWIA SDLIGQAEHD NLAQCILISK DKSIIKKVNY EIINQLKELP RAVIAKNSLL 

       310        320        330        340        350        360 
NNGILIYMPS DQKIINTVNK IAPEHLELNT KNYKKVVSKI KNAGSICLGK YAVMAMTDYN 

       370        380        390        400        410        420 
VGSNHVLPTN SSARYSSGVS VNEFYKRISY INLSKKGIET LGPSVITLAN YEGLVGHAKS 


VEKRIRRK 

« Hide

References

[1]"Genome streamlining in a cosmopolitan oceanic bacterium."
Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.
Science 309:1242-1245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC1062.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000084 Genomic DNA. Translation: AAZ21297.1.
RefSeqYP_265900.1. NC_007205.1.

3D structure databases

ProteinModelPortalQ4FNE2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335992.SAR11_0475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ21297; AAZ21297; SAR11_0475.
GeneID3517238.
KEGGpub:SAR11_0475.
PATRIC31990417. VBICanPel5618_0474.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycCPEL335992:GH3Z-481-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 nameHISX1_PELUB
AccessionPrimary (citable) accession number: Q4FNE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 30, 2005
Last modified: February 19, 2014
This is version 71 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