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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Thiobacillus denitrificans (strain ATCC 25259)
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 2 (hisC2), Histidinol-phosphate aminotransferase 1 (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 sitei133NADUniRule annotation1
Binding sitei194NADUniRule annotation1
Binding sitei217NADUniRule annotation1
Binding sitei240SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Metal bindingi265ZincUniRule annotation1
Binding sitei265SubstrateUniRule annotation1
Active sitei330Proton acceptorUniRule annotation1
Active sitei331Proton acceptorUniRule annotation1
Binding sitei331SubstrateUniRule annotation1
Metal bindingi364ZincUniRule annotation1
Binding sitei364SubstrateUniRule annotation1
Binding sitei418SubstrateUniRule annotation1
Metal bindingi423ZincUniRule annotation1
Binding sitei423SubstrateUniRule 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:Tbd_1713
OrganismiThiobacillus denitrificans (strain ATCC 25259)
Taxonomic identifieri292415 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus
Proteomesi
  • UP000008291 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358721 – 434Histidinol dehydrogenaseAdd BLAST434

Interactioni

Protein-protein interaction databases

STRINGi292415.Tbd_1713.

Structurei

3D structure databases

ProteinModelPortaliQ3SI67.
SMRiQ3SI67.
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.

Q3SI67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTLTRLDSA QPDFQARLAR LLQFDDATDA SIEEAVATIL HAVKTRGDAA
60 70 80 90 100
VLEYTERFDR LPAPSAASLE LGAAELAAAL AGLPEDTRAA LEAAADRVRR
110 120 130 140 150
YHEKQLQGSW TYTEDDGTVL GQKVTPLDRV GLYVPGGKAA YPSSVLMNAI
160 170 180 190 200
PAKVAGVAEL VMVVPTPGGE RNALVLAAAA IAGVDRVFTI GGAQAVAALA
210 220 230 240 250
YGTETVPQVD KIVGPGNAYV AAAKRRVFGT VGIDMIAGPS EILVIADGST
260 270 280 290 300
PAEWVAMDLF SQAEHDELAQ SILLSPDPDY LDAVAAAIDQ LIVEMPRAEV
310 320 330 340 350
IRTSLTNRGA LIRTHDLHDA AAIANAIAPE HLELAVSDPE ALLPKLRHAG
360 370 380 390 400
AIFMGKNTCE ALGDYCAGPN HVLPTSRTAR FSSPLGVYDF QKRTSLIHVS
410 420 430
EAGAQTLGRI AATLAYGEGL QAHARSAEYR LTHK
Length:434
Mass (Da):45,762
Last modified:October 11, 2005 - v1
Checksum:iE319DE59B7083FC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000116 Genomic DNA. Translation: AAZ97666.1.
RefSeqiWP_011312225.1. NC_007404.1.

Genome annotation databases

EnsemblBacteriaiAAZ97666; AAZ97666; Tbd_1713.
KEGGitbd:Tbd_1713.
PATRICi23969587. VBIThiDen82923_1696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000116 Genomic DNA. Translation: AAZ97666.1.
RefSeqiWP_011312225.1. NC_007404.1.

3D structure databases

ProteinModelPortaliQ3SI67.
SMRiQ3SI67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi292415.Tbd_1713.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ97666; AAZ97666; Tbd_1713.
KEGGitbd:Tbd_1713.
PATRICi23969587. VBIThiDen82923_1696.

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_THIDA
AccessioniPrimary (citable) accession number: Q3SI67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 78 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.