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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
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 regulatory subunit (hisZ), 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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Probable histidinol-phosphatase (hisK)
  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 sitei131NADUniRule annotation1
Binding sitei193NADUniRule annotation1
Binding sitei216NADUniRule annotation1
Binding sitei239SubstrateUniRule annotation1
Metal bindingi261ZincUniRule annotation1
Binding sitei261SubstrateUniRule annotation1
Metal bindingi264ZincUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Active sitei329Proton acceptorUniRule annotation1
Active sitei330Proton acceptorUniRule annotation1
Binding sitei330SubstrateUniRule annotation1
Metal bindingi363ZincUniRule annotation1
Binding sitei363SubstrateUniRule annotation1
Binding sitei417SubstrateUniRule annotation1
Metal bindingi422ZincUniRule annotation1
Binding sitei422SubstrateUniRule 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

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:CA_C0937
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000814 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357561 – 431Histidinol dehydrogenaseAdd BLAST431

Interactioni

Protein-protein interaction databases

STRINGi272562.CA_C0937.

Structurei

3D structure databases

ProteinModelPortaliQ97KI2.
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.

Q97KI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDIIRIIQD GSLDGEKYFQ SLKERQGKEN AEIIKTVKFI IDNVKENGDK
60 70 80 90 100
ALIEYTSKFD KVELQSIEVT KEEIKAAYSK VENDFICALK TAKENIEEYH
110 120 130 140 150
SKQVQNSYVI TKENGIVMGR TVRGLDKVGI YVPGGTAAYP SSVIMNAVPA
160 170 180 190 200
KVAGVNKIIM TTPPMKDGFV NPSILVAADL AGVDKIYKVG GAQAIAALAF
210 220 230 240 250
GTETIDKVDK IVGPGNIFVA MAKKSVYGFV DIDMIAGPSE ILVISDETGN
260 270 280 290 300
PKFIAADLMS QAEHDTLASS ILVTTSKELI GKVIEEIKLQ VEGLSRKEII
310 320 330 340 350
LEALRNFGAI ILVDSISRAI EIGNVVAPEH LEIITPNPFE YLNDIKNAGS
360 370 380 390 400
IFLGSYSPEP LGDYMAGPNH VLPTSGTARF SSPLSVDDFV KKSSYLYYSE
410 420 430
KALRNVNDKV VKIAETEGLT AHANSIKVRF K
Length:431
Mass (Da):46,930
Last modified:October 1, 2001 - v1
Checksum:i70AFA3CB1946DF19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK78913.1.
PIRiF97015.
RefSeqiNP_347573.1. NC_003030.1.
WP_010964255.1. NC_003030.1.

Genome annotation databases

EnsemblBacteriaiAAK78913; AAK78913; CA_C0937.
GeneIDi1117120.
KEGGicac:CA_C0937.
PATRICi32036255. VBICloAce74127_1147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001437 Genomic DNA. Translation: AAK78913.1.
PIRiF97015.
RefSeqiNP_347573.1. NC_003030.1.
WP_010964255.1. NC_003030.1.

3D structure databases

ProteinModelPortaliQ97KI2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272562.CA_C0937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK78913; AAK78913; CA_C0937.
GeneIDi1117120.
KEGGicac:CA_C0937.
PATRICi32036255. VBICloAce74127_1147.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

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_CLOAB
AccessioniPrimary (citable) accession number: Q97KI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2001
Last modified: November 2, 2016
This is version 96 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.