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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
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:iL-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. Histidine biosynthesis bifunctional protein HisIE (hisIE)
  3. Histidine biosynthesis bifunctional protein HisIE (hisIE)
  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 sitei131 – 1311NADUniRule annotation
Binding sitei192 – 1921NADUniRule annotation
Binding sitei215 – 2151NADUniRule annotation
Binding sitei238 – 2381SubstrateUniRule annotation
Metal bindingi260 – 2601ZincUniRule annotation
Binding sitei260 – 2601SubstrateUniRule annotation
Metal bindingi263 – 2631ZincUniRule annotation
Binding sitei263 – 2631SubstrateUniRule annotation
Active sitei328 – 3281Proton acceptorUniRule annotation
Active sitei329 – 3291Proton acceptorUniRule annotation
Binding sitei329 – 3291SubstrateUniRule annotation
Metal bindingi362 – 3621ZincUniRule annotation
Binding sitei362 – 3621SubstrateUniRule annotation
Binding sitei416 – 4161SubstrateUniRule annotation
Metal bindingi421 – 4211ZincUniRule annotation
Binding sitei421 – 4211SubstrateUniRule 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

BioCyciASP62977:GJVV-626-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:ACIAD0663
OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Taxonomic identifieri62977 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
ProteomesiUP000000430 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Histidinol dehydrogenasePRO_0000135713Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi62977.ACIAD0663.

Structurei

3D structure databases

ProteinModelPortaliQ6FEC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

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.

Q6FEC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRRLSTQDQ SFKQVFADLL AFETVNDPEL LKTVDQIIAD VRQYGDEHVL
60 70 80 90 100
KLTQQFDRHP AHQFSDLELT QEQLKTAFEA LTAEIREALE LAAERIRSFH
110 120 130 140 150
QAQKQEGWSY VDALGNTLGQ KVTPLDRVGI YVPGGLASYP SSVLMNAIPA
160 170 180 190 200
HVAGVPEIIM VVPAPNGELN SLVLAAAYLA GVSRIFTIGG AQAVAALAYG
210 220 230 240 250
TQTIPAVDKI TGPGNRFVAA AKRAVFGQVG IDMIAGPSEI LVYAEGQNNA
260 270 280 290 300
KWLAMDLLSQ AEHDTVAQAI FITPDEALLD EVAQAIEEHL AALPKADIAR
310 320 330 340 350
TSIANRGALV LVKDRDEAIE LINQVAPEHL ELCLDESEAM SQKIRHAGAI
360 370 380 390 400
FMGRYTPEAI GDYCAGPNHV LPTSGTARFS SPLGVYDFQK RSSLIMCSQE
410 420 430
GVKSLAKAAD VLAQQENLDA HARSARYRYQ
Length:430
Mass (Da):46,671
Last modified:July 19, 2004 - v1
Checksum:i75B7CFF03AB94510
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR543861 Genomic DNA. Translation: CAG67580.1.

Genome annotation databases

EnsemblBacteriaiCAG67580; CAG67580; ACIAD0663.
KEGGiaci:ACIAD0663.
PATRICi20739230. VBIAciSp98416_0585.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR543861 Genomic DNA. Translation: CAG67580.1.

3D structure databases

ProteinModelPortaliQ6FEC8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi62977.ACIAD0663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG67580; CAG67580; ACIAD0663.
KEGGiaci:ACIAD0663.
PATRICi20739230. VBIAciSp98416_0585.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciASP62977:GJVV-626-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. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
    Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
    Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33305 / BD413 / ADP1.

Entry informationi

Entry nameiHISX_ACIAD
AccessioniPrimary (citable) accession number: Q6FEC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 19, 2004
Last modified: July 22, 2015
This is version 81 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.