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Q8NNT5 (HISX_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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:Cgl2102, cg2305
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length442 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.

Sequence caution

The sequence AAF80392.1 differs from that shown. Reason: Frameshift at positions 97, 136 and 147.

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 – 442442Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135761

Sites

Active site3321Proton acceptor By similarity
Active site3331Proton acceptor By similarity
Metal binding2631Zinc By similarity
Metal binding2661Zinc By similarity
Metal binding3661Zinc By similarity
Metal binding4251Zinc By similarity
Binding site1291NAD By similarity
Binding site1931NAD By similarity
Binding site2181NAD By similarity
Binding site2411Substrate By similarity
Binding site2631Substrate By similarity
Binding site2661Substrate By similarity
Binding site3331Substrate By similarity
Binding site3661Substrate By similarity
Binding site4201Substrate By similarity
Binding site4251Substrate By similarity

Experimental info

Sequence conflict372 – 3809Missing Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8NNT5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D696294519F95838

FASTA44246,771
        10         20         30         40         50         60 
MLNVTDLRGQ TPSKSDIRRA LPRGGTDVWS VLPIVQPVVE DVQNRGAEAA LDYGEKFDHI 

        70         80         90        100        110        120 
RPASVRVPAE VIAAAENTLD PLVRESIEES IRRVRKVHAE QKPSEHTTEL SPGGTVTERF 

       130        140        150        160        170        180 
MPIDRVGLYV PGGNAVYPSS VIMNTVPAQE AGVNSLVVAS PPQAEHGGWP HPTILAACSI 

       190        200        210        220        230        240 
LGVDEVWAVG GGQAVALLAY GDDAAGLEPV DMITGPGNIF VTAAKRLVRG VVGTDSEAGP 

       250        260        270        280        290        300 
TEIAVLADAS ANAVNVAYDL ISQAEHDVMA ASVLITDSEQ LAKDVNREIE ARYSITRNAE 

       310        320        330        340        350        360 
RVAEALRGAQ SGIVLVDDIS VGIQVADQYA AEHLEIHTEN ARAVAEQITN AGAIFVGDFS 

       370        380        390        400        410        420 
PVPLGDYSAG SNHVLPTSGS ARFSAGLSTH TFLRPVNLIE YDEAALKDVS QVVINFANAE 

       430        440 
DLPAHGEAIR ARFENLPTTD EA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of hisD gene from Corynebacterium glutamicum."
Chun J.Y., Han M.S., Sim J.K., Lee M.-S.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF160480 Genomic DNA. Translation: AAF80392.1. Frameshift.
BA000036 Genomic DNA. Translation: BAB99495.1.
BX927154 Genomic DNA. Translation: CAF20438.1.
RefSeqNP_601301.1. NC_003450.3.
YP_226339.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NNT5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2305.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99495; BAB99495; BAB99495.
CAF20438; CAF20438; cg2305.
GeneID1020053.
KEGGcgb:cg2305.
cgl:NCgl2021.
PATRIC21496206. VBICorGlu203724_2039.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAQKSLHAV.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

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_CORGL
AccessionPrimary (citable) accession number: Q8NNT5
Secondary accession number(s): Q9KJU2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 89 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