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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / 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

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. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei242 – 2421SubstrateUniRule annotation
Metal bindingi264 – 2641ZincUniRule annotation
Binding sitei264 – 2641SubstrateUniRule annotation
Metal bindingi267 – 2671ZincUniRule annotation
Binding sitei267 – 2671SubstrateUniRule annotation
Active sitei332 – 3321Proton acceptorUniRule annotation
Active sitei333 – 3331Proton acceptorUniRule annotation
Binding sitei333 – 3331SubstrateUniRule annotation
Metal bindingi366 – 3661ZincUniRule annotation
Binding sitei366 – 3661SubstrateUniRule annotation
Binding sitei420 – 4201SubstrateUniRule annotation
Metal bindingi425 – 4251ZincUniRule annotation
Binding sitei425 – 4251SubstrateUniRule 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

BioCyciDVUL882:GJIL-820-MONOMER.
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 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
ProteomesiUP000002194 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Histidinol dehydrogenasePRO_0000135768Add
BLAST

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

eggNOGiCOG0141.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.
PhylomeDBiP62457.

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.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0141.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.
PhylomeDBiP62457.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciDVUL882:GJIL-820-MONOMER.

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: Hildenborough / ATCC 29579 / NCIMB 8303.

Entry informationi

Entry nameiHISX_DESVH
AccessioniPrimary (citable) accession number: P62457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
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.