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Q7NL02 (HISX_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:gll1324
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length445 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
Reference 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 – 445445Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135775

Sites

Active site3281Proton acceptor By similarity
Active site3291Proton acceptor By similarity
Metal binding2601Zinc By similarity
Metal binding2631Zinc By similarity
Metal binding3621Zinc By similarity
Metal binding4211Zinc By similarity
Binding site1301NAD By similarity
Binding site1921NAD By similarity
Binding site2151NAD By similarity
Binding site2381Substrate By similarity
Binding site2601Substrate By similarity
Binding site2631Substrate By similarity
Binding site3291Substrate By similarity
Binding site3621Substrate By similarity
Binding site4161Substrate By similarity
Binding site4211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NL02 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: E74D1ABE35BBFDC7

FASTA44548,032
        10         20         30         40         50         60 
MLRLITQLSE AQTEIKRIAA RTHSEQVQHQ EATVREILQN VRRQGDEALL RYTLEFDQVR 

        70         80         90        100        110        120 
LAPGDLVVGA AELDAAYQRV STSLLKAIRL AKQRIEQFHR ERICKSWVQF QDRGIVLGRR 

       130        140        150        160        170        180 
YTPVDAAGLY IPGGRASYPS SVLMSAIPAV VAGVPRIVLV TPPNPEGKIN PAVLVAAQES 

       190        200        210        220        230        240 
GVHEIYRIGG AQAIGALTYG TRTIAPVSVI AGPGNIYVTL AKKLVYGEVG IDSLAGPSEV 

       250        260        270        280        290        300 
LIIADSTANP VFLAADMLAQ AEHDSLASAI LITPDGRLAE RTIEAVDRQL ENHPRRTLTE 

       310        320        330        340        350        360 
KSLANYGLVI VTADLAEAAA LSNLFAPEHL ELEVEDPWEL LEKVRHAGAI FLGHATPEAV 

       370        380        390        400        410        420 
GDYLAGPSHI LPTSGTARYA SGVGVETFQK CSSLVQYTPQ ALAEVGEAID ALTAAEGLPS 

       430        440 
HGDSVRLRLQ QYENPHSPTQ QQQEE 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC89265.1.
RefSeqNP_924270.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NL02.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gvip194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC89265; BAC89265; BAC89265.
GeneID2598786.
KEGGgvi:gvip194.
PATRIC22042073. VBIGloVio86258_1351.

Phylogenomic databases

eggNOGCOG0141.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-1338-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_GLOVI
AccessionPrimary (citable) accession number: Q7NL02
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 76 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