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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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. no protein annotated in this organism
  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 sitei124NADUniRule annotation1
Binding sitei186NADUniRule annotation1
Binding sitei209NADUniRule annotation1
Binding sitei232SubstrateUniRule annotation1
Metal bindingi254ZincUniRule annotation1
Binding sitei254SubstrateUniRule annotation1
Metal bindingi257ZincUniRule annotation1
Binding sitei257SubstrateUniRule annotation1
Active sitei322Proton acceptorUniRule annotation1
Active sitei323Proton acceptorUniRule annotation1
Binding sitei323SubstrateUniRule annotation1
Metal bindingi356ZincUniRule annotation1
Binding sitei356SubstrateUniRule annotation1
Binding sitei410SubstrateUniRule annotation1
Metal bindingi415ZincUniRule annotation1
Binding sitei415SubstrateUniRule 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:Moth_2035
OrganismiMoorella thermoacetica (strain ATCC 39073 / JCM 9320)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
Proteomesi
  • UP000007053 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002298581 – 424Histidinol dehydrogenaseAdd BLAST424

Proteomic databases

PRIDEiQ2RGV8.

Interactioni

Protein-protein interaction databases

STRINGi264732.Moth_2035.

Structurei

3D structure databases

ProteinModelPortaliQ2RGV8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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.

Q2RGV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPLIDGKEV KRRWSGRLLA REGVAARVRE IIAAVKREGQ AAVERYTLEL
60 70 80 90 100
DGVDLKEAGF RVTREEIGAA YRAVSPDLLE ALRIARDNIA TYHRRQPRGS
110 120 130 140 150
WMETAADGTI LGQICRPLGR VGLYVPGGTA AYPSSVLMTA VPARVAGVRE
160 170 180 190 200
IALATPPRRD GTLPPLLLVA AAEAGVEEIY KMGGAQAVAA LAYGTEKVAP
210 220 230 240 250
VDKIAGPGNI YVTLAKKEVY GQVDIDMLAG PSEIVVIADG KARPDWVAAD
260 270 280 290 300
LLSQAEHDAL AGAVLITPDA GLARAVGEEV TRQLEALPRR EIASRSLADY
310 320 330 340 350
GAAVVVTGLD AAMDLANSLA PEHLELYVSE PWSWLGRVEN AGAIFLGPYS
360 370 380 390 400
SEPLGDYLAG PSHVLPTGGT ARFYSPLSVD TFLKKSSLIA CNRAGFRAAA
410 420
GYIQALARAE GLEGHARAIE LREE
Length:424
Mass (Da):45,045
Last modified:January 24, 2006 - v1
Checksum:i79066A42F74907AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA. Translation: ABC20331.1.
RefSeqiWP_011393531.1. NC_007644.1.
YP_430874.1. NC_007644.1.

Genome annotation databases

EnsemblBacteriaiABC20331; ABC20331; Moth_2035.
GeneIDi3831410.
KEGGimta:Moth_2035.
PATRICi22641484. VBIMooThe6753_2210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA. Translation: ABC20331.1.
RefSeqiWP_011393531.1. NC_007644.1.
YP_430874.1. NC_007644.1.

3D structure databases

ProteinModelPortaliQ2RGV8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264732.Moth_2035.

Proteomic databases

PRIDEiQ2RGV8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC20331; ABC20331; Moth_2035.
GeneIDi3831410.
KEGGimta:Moth_2035.
PATRICi22641484. VBIMooThe6753_2210.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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_MOOTA
AccessioniPrimary (citable) accession number: Q2RGV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 72 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.