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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidinol-phosphatase (hisN)
  9. Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei129NADUniRule annotation1
Binding sitei193NADUniRule annotation1
Binding sitei218NADUniRule annotation1
Binding sitei241SubstrateUniRule annotation1
Metal bindingi263ZincUniRule annotation1
Binding sitei263SubstrateUniRule annotation1
Metal bindingi266ZincUniRule annotation1
Binding sitei266SubstrateUniRule annotation1
Active sitei332Proton acceptorUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Binding sitei333SubstrateUniRule annotation1
Metal bindingi366ZincUniRule annotation1
Binding sitei366SubstrateUniRule annotation1
Binding sitei420SubstrateUniRule annotation1
Metal bindingi425ZincUniRule annotation1
Binding sitei425SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciCORYNE:G18NG-11694-MONOMER.
UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:Cgl2102, cg2305
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357611 – 442Histidinol dehydrogenaseAdd BLAST442

Interactioni

Protein-protein interaction databases

STRINGi196627.cg2305.

Structurei

3D structure databases

ProteinModelPortaliQ8NNT5.
SMRiQ8NNT5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NNT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNVTDLRGQ TPSKSDIRRA LPRGGTDVWS VLPIVQPVVE DVQNRGAEAA
60 70 80 90 100
LDYGEKFDHI RPASVRVPAE VIAAAENTLD PLVRESIEES IRRVRKVHAE
110 120 130 140 150
QKPSEHTTEL SPGGTVTERF MPIDRVGLYV PGGNAVYPSS VIMNTVPAQE
160 170 180 190 200
AGVNSLVVAS PPQAEHGGWP HPTILAACSI LGVDEVWAVG GGQAVALLAY
210 220 230 240 250
GDDAAGLEPV DMITGPGNIF VTAAKRLVRG VVGTDSEAGP TEIAVLADAS
260 270 280 290 300
ANAVNVAYDL ISQAEHDVMA ASVLITDSEQ LAKDVNREIE ARYSITRNAE
310 320 330 340 350
RVAEALRGAQ SGIVLVDDIS VGIQVADQYA AEHLEIHTEN ARAVAEQITN
360 370 380 390 400
AGAIFVGDFS PVPLGDYSAG SNHVLPTSGS ARFSAGLSTH TFLRPVNLIE
410 420 430 440
YDEAALKDVS QVVINFANAE DLPAHGEAIR ARFENLPTTD EA
Length:442
Mass (Da):46,771
Last modified:October 1, 2002 - v1
Checksum:iD696294519F95838
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti372 – 380Missing (Ref. 1) Curated9

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160480 Genomic DNA. Translation: AAF80392.1. Frameshift.
BA000036 Genomic DNA. Translation: BAB99495.1.
BX927154 Genomic DNA. Translation: CAF20438.1.
RefSeqiNP_601301.1. NC_003450.3.
WP_011014881.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99495; BAB99495; BAB99495.
CAF20438; CAF20438; cg2305.
GeneIDi1020053.
KEGGicgb:cg2305.
cgl:NCgl2021.
PATRICi21496206. VBICorGlu203724_2039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160480 Genomic DNA. Translation: AAF80392.1. Frameshift.
BA000036 Genomic DNA. Translation: BAB99495.1.
BX927154 Genomic DNA. Translation: CAF20438.1.
RefSeqiNP_601301.1. NC_003450.3.
WP_011014881.1. NC_006958.1.

3D structure databases

ProteinModelPortaliQ8NNT5.
SMRiQ8NNT5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2305.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99495; BAB99495; BAB99495.
CAF20438; CAF20438; cg2305.
GeneIDi1020053.
KEGGicgb:cg2305.
cgl:NCgl2021.
PATRICi21496206. VBICorGlu203724_2039.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciCORYNE:G18NG-11694-MONOMER.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHISX_CORGL
AccessioniPrimary (citable) accession number: Q8NNT5
Secondary accession number(s): Q9KJU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2002
Last modified: November 2, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.