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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
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. no protein annotated in this organism
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. no protein annotated in this organism
  5. Related to bifunctional histidine biosynthesis protein (HisHF) (DP2167)
  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 sitei242SubstrateUniRule annotation1
Metal bindingi264ZincUniRule annotation1
Binding sitei264SubstrateUniRule annotation1
Metal bindingi267ZincUniRule annotation1
Binding sitei267SubstrateUniRule annotation1
Active sitei332Proton acceptorUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Binding sitei333SubstrateUniRule annotation1
Metal bindingi366ZincUniRule annotation1
Binding sitei366SubstrateUniRule annotation1
Binding sitei420SubstrateUniRule annotation1
Metal bindingi425ZincUniRule annotation1
Binding sitei425SubstrateUniRule 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:DP1282
OrganismiDesulfotalea psychrophila (strain LSv54 / DSM 12343)
Taxonomic identifieri177439 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfobacteralesDesulfobulbaceaeDesulfotalea
Proteomesi
  • UP000000602 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357671 – 434Histidinol dehydrogenaseAdd BLAST434

Interactioni

Protein-protein interaction databases

STRINGi177439.DP1282.

Structurei

3D structure databases

ProteinModelPortaliQ6ANR3.
SMRiQ6ANR3.
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.

Q6ANR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIEPKMIGS SEGQALLESL LNRFQIGDSG CQSAVEDILT AVRQEGDAAV
60 70 80 90 100
VKYCRRFDCP DMTASALAVT AAEIAAAYEL VDAAFLETLA AAIERIHSFH
110 120 130 140 150
EREMEDSWMQ TREDGTIVGR LVRPVDSAGL YVPGGTGGST PLVSSVLMNG
160 170 180 190 200
IPAGIAGVTT RVMVTPPGKD GKISPHLLVA ATEIGITEIY KAGSAWGIAA
210 220 230 240 250
LAYGTATIPR VDVIVGPGNQ FVTEAKRLVS GMVRIDMIAG PSEVLIVADE
260 270 280 290 300
TADPVYIAAD MLAQAEHDPQ ALSILLTTDR QVAEAVPAEI ERQLKTLSRA
310 320 330 340 350
EIAEKSIVDR AVILVVADIE EAIGLANDIA IEHLELMIVD PWAQVPHIRH
360 370 380 390 400
AGAIFLGSHT PEAAGDYFAG PNHVLPTMGT ARFASALGVE TFLKKSSIIS
410 420 430
YSQTALQNDA EHIQRLANLE GLTAHANSVA VRVK
Length:434
Mass (Da):45,998
Last modified:September 13, 2004 - v1
Checksum:i6282B79273F5C856
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR522870 Genomic DNA. Translation: CAG36011.1.
RefSeqiWP_011188523.1. NC_006138.1.

Genome annotation databases

EnsemblBacteriaiCAG36011; CAG36011; DP1282.
KEGGidps:DP1282.
PATRICi21712341. VBIDesPsy67261_1387.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR522870 Genomic DNA. Translation: CAG36011.1.
RefSeqiWP_011188523.1. NC_006138.1.

3D structure databases

ProteinModelPortaliQ6ANR3.
SMRiQ6ANR3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi177439.DP1282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG36011; CAG36011; DP1282.
KEGGidps:DP1282.
PATRICi21712341. VBIDesPsy67261_1387.

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_DESPS
AccessioniPrimary (citable) accession number: Q6ANR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: September 13, 2004
Last modified: November 2, 2016
This is version 83 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.