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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. Phosphoribosyl isomerase A (priA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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 sitei240 – 2401SubstrateUniRule annotation
Metal bindingi262 – 2621ZincUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Metal bindingi265 – 2651ZincUniRule annotation
Binding sitei265 – 2651SubstrateUniRule 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

BioCyciSAVE227882:GJU1-6233-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:SAV_6153
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
ProteomesiUP000000428 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Histidinol dehydrogenasePRO_0000135859Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi227882.SAV_6153.

Structurei

3D structure databases

ProteinModelPortaliQ82AA6.
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.

Q82AA6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISRIDLRGD ALPEGSALRD LLPRADFDVS AALEKVRPIC EAVHHRGDAA
60 70 80 90 100
LIDFAEKFDG VRLESVRVPA RALADALEQL DPAVRAALEE SIRRARLVHR
110 120 130 140 150
EQRRTTHTTQ VVPGGSVTEK WVPVDRVGLY APGGRSVYPS SVVMNVVPAQ
160 170 180 190 200
EAGVESIALA SPAQAEFGGL PHPTILAACA LLGVDEVYAA GGATAVAMFA
210 220 230 240 250
YGTESCAPAD MVTGPGNIWV AAAKRYFTGK IGIDAEAGPT EIAVLADSTA
260 270 280 290 300
DPVHVASDLI SQAEHDPLAA AVLVTDSVEL ADAVEKELEP QVAATKHIDD
310 320 330 340 350
RIVPALKGRQ SAIVLVDGVD EGLRVVDAYG AEHLEIQTAD AAAVADRVRN
360 370 380 390 400
AGAIFIGPWA PVSLGDYAAG SNHVLPTGGC ACHSSGLSVQ SFLRGIHIVD
410 420 430 440
YTKDALADVA HHVVTLAEAE DLPAHGAAIK ARFGWKVPES K
Length:441
Mass (Da):46,169
Last modified:June 1, 2003 - v1
Checksum:i1D3872AE734D0EB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC73864.1.
RefSeqiNP_827329.1. NC_003155.4.
WP_010987554.1. NZ_BAVY01000017.1.

Genome annotation databases

EnsemblBacteriaiBAC73864; BAC73864; SAV_6153.
KEGGisma:SAV_6153.
PATRICi23726344. VBIStrAve112782_6525.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC73864.1.
RefSeqiNP_827329.1. NC_003155.4.
WP_010987554.1. NZ_BAVY01000017.1.

3D structure databases

ProteinModelPortaliQ82AA6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227882.SAV_6153.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC73864; BAC73864; SAV_6153.
KEGGisma:SAV_6153.
PATRICi23726344. VBIStrAve112782_6525.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciSAVE227882:GJU1-6233-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. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
    Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
    Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
  2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
    Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
    Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Entry informationi

Entry nameiHISX_STRAW
AccessioniPrimary (citable) accession number: Q82AA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 86 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.