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Q483H8 (HISX2_COLP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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 2

Short name=HDH 2
EC=1.1.1.23
Gene names
Name:hisD2
Ordered Locus Names:CPS_2061
OrganismColwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio psychroerythus) [Complete proteome] [HAMAP]
Taxonomic identifier167879 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeColwellia

Protein attributes

Sequence length446 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

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
   LigandNAD
   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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Histidinol dehydrogenase 2 HAMAP-Rule MF_01024
PRO_0000135758

Sites

Active site3341Proton acceptor By similarity
Active site3351Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q483H8 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 4B8C883BF8A096FA

FASTA44648,236
        10         20         30         40         50         60 
MTHKVKIHRL SDLSAEQRNK LLQRTESNLD NFIDIVKPII ENVKLNGDKA LSEYAKKFDK 

        70         80         90        100        110        120 
AEVSTDQIQV TQAEFDEAFT LVDEEVIQTL SYSIDNIKKF HEAQMPEEMW MKQIRPGCYA 

       130        140        150        160        170        180 
GDRFTPINAV ACYIPRGKGS FPSVAIMTAV PAIVAGVPTA IIITPPGTDG KVDAATLVVA 

       190        200        210        220        230        240 
KLVGIDKVFK CGGAQGIAAV AYGTNTVPKC DKVVGPGSPF VVAAKKLLAD IIHPGTPAGP 

       250        260        270        280        290        300 
SEAIVLADDT ANPKLAALDL LVEAEHGPDS SAFLVTNSKE LAEQAQVAIN EYWQHMDRLR 

       310        320        330        340        350        360 
VDFSSTVLSG DNGGIVLTST FEEAVDFCND YAAEHLLILS KSPFDHLGKI INAGEILLGE 

       370        380        390        400        410        420 
NTPISIANYT LGPNAVLPTS MAAKTASPLS VFDYLKSCSI GYLTREGYEE LAPHTYRFAK 

       430        440 
YEGFDAHANA VSHLRDEAIK SEKKIK 

« Hide

References

[1]"The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses."
Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X., Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M., Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A., Zhou L., Davidsen T.M. expand/collapse author list , Wu M., Huston A.L., Lewis M., Weaver B., Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 34H / ATCC BAA-681.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000083 Genomic DNA. Translation: AAZ25938.1.
RefSeqYP_268789.1. NC_003910.7.

3D structure databases

ProteinModelPortalQ483H8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167879.CPS_2061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ25938; AAZ25938; CPS_2061.
GeneID3520186.
KEGGcps:CPS_2061.
PATRIC21467245. VBIColPsy94388_1863.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAWVVAAKR.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycCPSY167879:GI48-2061-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_COLP3
AccessionPrimary (citable) accession number: Q483H8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 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