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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
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 (hisC1)
  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 sitei240SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Metal bindingi265ZincUniRule annotation1
Binding sitei265SubstrateUniRule annotation1
Active sitei331Proton acceptorUniRule annotation1
Active sitei332Proton acceptorUniRule annotation1
Binding sitei332SubstrateUniRule annotation1
Metal bindingi365ZincUniRule annotation1
Binding sitei365SubstrateUniRule annotation1
Binding sitei419SubstrateUniRule annotation1
Metal bindingi424ZincUniRule annotation1
Binding sitei424SubstrateUniRule 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:Lxx15120
OrganismiLeifsonia xyli subsp. xyli (strain CTCB07)
Taxonomic identifieri281090 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrobacteriaceaeLeifsonia
Proteomesi
  • UP000001306 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357871 – 436Histidinol dehydrogenaseAdd BLAST436

Interactioni

Protein-protein interaction databases

STRINGi281090.Lxx15120.

Structurei

3D structure databases

ProteinModelPortaliQ6AE76.
SMRiQ6AE76.
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.

Q6AE76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTIDLRGVQ PTRTAFERLV PRPVVDVQAA MTVAADLIAD VRKRGAAALR
60 70 80 90 100
EQAERFDGGV PASVRVPVAE IVAAVDALPG GVREALEEAI ARVREATAAQ
110 120 130 140 150
VPPAAVTRIG PGAVIEQRWQ PVERAGLYVP GGKAVYPSSV VMNAVPAQVA
160 170 180 190 200
GVASIALASP PQREFGGAVH PTILGAAGLL GIDEVYAMGG AGAIGALAWG
210 220 230 240 250
VGELGLEPVQ VITGPGNIYV AAAKRVVRGQ TGIDSEAGTT EILVIADDTA
260 270 280 290 300
DPRYVAADLI SQAEHDEAAA SLLVTDSPAF VGRVAAELET LAASTRYAER
310 320 330 340 350
VRAALGGQQS AVVLVDDLDA AAAFSNAYGP EHLELQTADA EAVLARIQNA
360 370 380 390 400
GAIFVGPHAP VSLGDYLAGS NHVLPTGGQA RFSPGLGAYS FLRPQQVIRY
410 420 430
DREALRAVAG RIVALSGAED LSAHGEAVTL RFEERA
Length:436
Mass (Da):44,916
Last modified:September 13, 2004 - v1
Checksum:i5E0CE3756C5ED756
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016822 Genomic DNA. Translation: AAT89320.1.

Genome annotation databases

EnsemblBacteriaiAAT89320; AAT89320; Lxx15120.
KEGGilxx:Lxx15120.
PATRICi22336666. VBILeiXyl11655_1575.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016822 Genomic DNA. Translation: AAT89320.1.

3D structure databases

ProteinModelPortaliQ6AE76.
SMRiQ6AE76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi281090.Lxx15120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT89320; AAT89320; Lxx15120.
KEGGilxx:Lxx15120.
PATRICi22336666. VBILeiXyl11655_1575.

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_LEIXX
AccessioniPrimary (citable) accession number: Q6AE76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 13, 2004
Last modified: November 2, 2016
This is version 88 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.