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Q4FMH0 (HISX2_PELUB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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 2

Short name=HDH 2
EC=1.1.1.23
Gene names
Name:hisD2
Ordered Locus Names:SAR11_0801
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 2 HAMAP-Rule MF_01024
PRO_0000135810

Sites

Active site3201Proton acceptor By similarity
Active site3211Proton acceptor By similarity
Metal binding2501Zinc By similarity
Metal binding2531Zinc By similarity
Metal binding3541Zinc By similarity
Metal binding4131Zinc By similarity
Binding site2281Substrate By similarity
Binding site2501Substrate By similarity
Binding site2531Substrate By similarity
Binding site3211Substrate By similarity
Binding site3541Substrate By similarity
Binding site4081Substrate By similarity
Binding site4131Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FMH0 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 0DE1C63534A76B41

FASTA42846,658
        10         20         30         40         50         60 
MAITYLKKSP KTSSTDDTKT TGIVQDLLKN IETTKEQGCI DLTKKFDKYD GEIIVSKERI 

        70         80         90        100        110        120 
EEIKKTLDQK TKDDVQFSYE RVRKFAEAQL KNYGQDFEVE LSDGLFAGQK LIPVNTAGCY 

       130        140        150        160        170        180 
VPGGRYAHIA SAVMSVTTAK VAGVKNVIAC SPPKEGVGAH PTIIYTADLC GADVILNLGG 

       190        200        210        220        230        240 
VPAIAAMTNG LFNNPPADII VGPGNQFVAE AKRILFGKVG IDLFAGPTEI GIIADAKADP 

       250        260        270        280        290        300 
EIVAVDLVGQ AEHGYNSPCW LYTTSKELAE KVMKRVPELI AELPEVPRTN ADAAWRDYGE 

       310        320        330        340        350        360 
VILCDTDEEM ATISDEYAPE HLEVQTENLE WFHKRLTNYG SLFIGEETTV AYGDKCSGTN 

       370        380        390        400        410        420 
HILPTKGAGR YTGGLFVGKF VKTLSFQRMT KESTELVGAA AARISRYEGM EAHARTGDVR 


LKKYGYSS 

« 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: AAZ21619.1.
RefSeqYP_266222.1. NC_007205.1.

3D structure databases

ProteinModelPortalQ4FMH0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335992.SAR11_0801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ21619; AAZ21619; SAR11_0801.
GeneID3516715.
KEGGpub:SAR11_0801.
PATRIC31991087. VBICanPel5618_0800.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK15509.
OMAISRLEGM.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycCPEL335992:GH3Z-811-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 nameHISX2_PELUB
AccessionPrimary (citable) accession number: Q4FMH0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 30, 2005
Last modified: May 14, 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