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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
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. 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 (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

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-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:DVU_0796
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001357681 – 436Histidinol dehydrogenaseAdd BLAST436

Proteomic databases

PaxDbiP62457.

Interactioni

Protein-protein interaction databases

STRINGi882.DVU0796.

Structurei

3D structure databases

ProteinModelPortaliP62457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG093N00U8.
PhylomeDBiP62457.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiView protein in InterPro
IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
PfamiView protein in Pfam
PF00815. Histidinol_dh. 1 hit.
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiView protein in PROSITE
PS00611. HISOL_DEHYDROGENASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P62457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPCRILTLQS EAQWPLLGDM LAGRYDPDDA VEPVVRDILA AVRSKGDEAL
60 70 80 90 100
AEYTRRFDCP DFTPALLHVT SEEVAQAVAS VPADDIAIIR QAADNIRSFH
110 120 130 140 150
EAQKERSWFV THDDGTILGQ KVTPVDRAGL YVPGGKGGDT PLLSSLLMNA
160 170 180 190 200
IPAQVAGVTS ITVASPPRPD GTLNPHLLAA AHILGITDII RAGSAWAVAA
210 220 230 240 250
FAFGTQTIAP VDVIAGPGNI FVTTAKRMVQ GRVAIDMIAG PSEILILADA
260 270 280 290 300
TARPDWVAAD MLSQAEHDPL ASSILVTTEP ALAEAVTAEL ERQLATLPRA
310 320 330 340 350
DIARKALADW GAVVVVPDMD VAVAIANRVA PEHLEVLTAQ PWELAGSLRH
360 370 380 390 400
AGALFLGPYS PEPLGDYFAG PNHVLPTMGT ARFSSALSVQ TFCKRTSIIA
410 420 430
ASRAFAERNA DAVARLARLE GLEAHARSAA SRNSQQ
Length:436
Mass (Da):46,131
Last modified:July 5, 2004 - v1
Checksum:i070577443146D3A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017285 Genomic DNA. Translation: AAS95276.1.
RefSeqiWP_010938097.1. NC_002937.3.
YP_010017.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS95276; AAS95276; DVU_0796.
GeneIDi2794518.
KEGGidvu:DVU0796.
PATRICi32061518. VBIDesVul119526_0747.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017285 Genomic DNA. Translation: AAS95276.1.
RefSeqiWP_010938097.1. NC_002937.3.
YP_010017.1. NC_002937.3.

3D structure databases

ProteinModelPortaliP62457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU0796.

Proteomic databases

PaxDbiP62457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS95276; AAS95276; DVU_0796.
GeneIDi2794518.
KEGGidvu:DVU0796.
PATRICi32061518. VBIDesVul119526_0747.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG093N00U8.
PhylomeDBiP62457.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiView protein in InterPro
IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
PfamiView protein in Pfam
PF00815. Histidinol_dh. 1 hit.
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiView protein in PROSITE
PS00611. HISOL_DEHYDROGENASE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHISX_DESVH
AccessioniPrimary (citable) accession number: P62457
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: February 15, 2017
This is version 91 of the entry and version 1 of the sequence. See 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.