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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
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

Pathway: 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 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271NADUniRule annotation
Binding sitei190 – 1901NADUniRule annotation
Binding sitei213 – 2131NADUniRule annotation
Binding sitei238 – 2381SubstrateUniRule annotation
Metal bindingi260 – 2601ZincUniRule annotation
Binding sitei260 – 2601SubstrateUniRule annotation
Metal bindingi263 – 2631ZincUniRule annotation
Binding sitei263 – 2631SubstrateUniRule annotation
Active sitei329 – 3291Proton acceptorUniRule annotation
Active sitei330 – 3301Proton acceptorUniRule annotation
Binding sitei330 – 3301SubstrateUniRule annotation
Metal bindingi363 – 3631ZincUniRule annotation
Binding sitei363 – 3631SubstrateUniRule annotation
Binding sitei417 – 4171SubstrateUniRule annotation
Metal bindingi422 – 4221ZincUniRule annotation
Binding sitei422 – 4221SubstrateUniRule annotation

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:MK0711
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
ProteomesiUP000001826 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Histidinol dehydrogenasePRO_0000135895Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi190192.MK0711.

Structurei

3D structure databases

ProteinModelPortaliQ8TXG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.

Family and domain databases

HAMAPiMF_01024. HisD.
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.

Q8TXG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLVRPEEE ELERVLRRSE MDVTEVLPDV ERIFEDVVER GDEALLEYTE
60 70 80 90 100
RFDGVKLEAE DLRVSEDDFE VARELVDERT VEALEEAAHR IEEFHRKTLP
110 120 130 140 150
RVDRITFDVE GTECGLTLRP IPRVGCYVPG GRAAYPSTAL MTVIPARVAG
160 170 180 190 200
CREVVVCTPP ADNDVRASPE VLVAVEIAGA DAVYRVGGAQ AIAALAAGTE
210 220 230 240 250
TVLRVDKIVG PGNVYVTAAK LLAYSRGLTD VDMPAGPSEV FVIADDSANP
260 270 280 290 300
DWLARDLIAQ AEHDPHAAAV LATDSEEIAR AVKERVEELL DAGIEREEIV
310 320 330 340 350
LKALDRNGWI VVLDSLEECV RLANRYAPEH LQLCVENPEE LLQDVENAGA
360 370 380 390 400
VFVGHLTAVP FGDYATGPNH VLPTGGFARA RGALGTWDFV KIIPIQRLRE
410 420 430
GDVERLAPIV EELAEREGLP NHAEAVRARR S
Length:431
Mass (Da):47,335
Last modified:June 1, 2002 - v1
Checksum:i50DD46829C9EB5DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009439 Genomic DNA. Translation: AAM01925.1.
RefSeqiNP_613995.1. NC_003551.1.
WP_011019080.1. NC_003551.1.

Genome annotation databases

EnsemblBacteriaiAAM01925; AAM01925; MK0711.
GeneIDi1476812.
KEGGimka:MK0711.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009439 Genomic DNA. Translation: AAM01925.1.
RefSeqiNP_613995.1. NC_003551.1.
WP_011019080.1. NC_003551.1.

3D structure databases

ProteinModelPortaliQ8TXG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01925; AAM01925; MK0711.
GeneIDi1476812.
KEGGimka:MK0711.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

HAMAPiMF_01024. HisD.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Entry informationi

Entry nameiHISX_METKA
AccessioniPrimary (citable) accession number: Q8TXG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2002
Last modified: May 27, 2015
This is version 87 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

External Data

Dasty 3

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 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.