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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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 (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 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), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Probable histidinol-phosphatase (hisK)
  9. Histidinol dehydrogenase (hisD), 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 sitei232SubstrateUniRule annotation1
Metal bindingi254ZincUniRule annotation1
Binding sitei254SubstrateUniRule annotation1
Metal bindingi257ZincUniRule annotation1
Binding sitei257SubstrateUniRule annotation1
Active sitei324Proton acceptorUniRule annotation1
Active sitei325Proton acceptorUniRule annotation1
Binding sitei325SubstrateUniRule annotation1
Metal bindingi358ZincUniRule annotation1
Binding sitei358SubstrateUniRule annotation1
Binding sitei412SubstrateUniRule annotation1
Metal bindingi417ZincUniRule annotation1
Binding sitei417SubstrateUniRule 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:TM_1041
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358691 – 428Histidinol dehydrogenaseAdd BLAST428

Proteomic databases

PRIDEiQ9X0D1.

Interactioni

Protein-protein interaction databases

STRINGi243274.TM1041.

Structurei

3D structure databases

ProteinModelPortaliQ9X0D1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
InParanoidiQ9X0D1.
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.

Q9X0D1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILMNNPGDK EVLRLLKQRM ESVSQVEETV KEIIRRVKEE GDRALEEFLK
60 70 80 90 100
RFEKHPVGIE NLRVTEKEIS EAQVEEEFVE TIKIVIEDLK EFHRRQEERS
110 120 130 140 150
FFFTTKGGSF LGEMVVPLES VGIYVPGGKV PYFSTLLMCA VPAIVAGVER
160 170 180 190 200
IAVTTPPNEN GGISPYILKT CEILGLKEIY RMGGAHAVAA LTYGTETVKP
210 220 230 240 250
VDKIVGPGGV FVTLAKKHVY GDVGIDSIAG PSEIAIVTDG SADLDLIAAD
260 270 280 290 300
FLSQAEHDEN AMSVVITTSK EVFEKLPQVI ERHLEALPEE RRKTARISTE
310 320 330 340 350
NFGTIILTDS LKRAFEISNL IAPEHLEVLV ENPFEPLGHI KNAGSVFLGK
360 370 380 390 400
YTCESVGDYG AGPNHVLPTF RSARFSSGLR VSDFTKKIFI THLSEEDFRR
410 420
KSELYSKMAR WEGFEAHARA IDVRREKL
Length:428
Mass (Da):47,749
Last modified:November 1, 1999 - v1
Checksum:iA7A765F2C298B45C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36118.1.
PIRiH72304.
RefSeqiNP_228847.1. NC_000853.1.
WP_004080480.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36118; AAD36118; TM_1041.
GeneIDi897023.
KEGGitma:TM1041.
PATRICi23937011. VBITheMar51294_1054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36118.1.
PIRiH72304.
RefSeqiNP_228847.1. NC_000853.1.
WP_004080480.1. NZ_CP011107.1.

3D structure databases

ProteinModelPortaliQ9X0D1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1041.

Proteomic databases

PRIDEiQ9X0D1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36118; AAD36118; TM_1041.
GeneIDi897023.
KEGGitma:TM1041.
PATRICi23937011. VBITheMar51294_1054.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
InParanoidiQ9X0D1.
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_THEMA
AccessioniPrimary (citable) accession number: Q9X0D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: November 1, 1999
Last modified: October 5, 2016
This is version 111 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.