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Protein

Histidinol dehydrogenase 1

Gene

hisD1

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  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. Putative histidinol dehydrogenase 2 (hisD2), Histidinol dehydrogenase 1 (hisD1)
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 sitei130NADUniRule annotation1
Binding sitei191NADUniRule annotation1
Binding sitei214NADUniRule annotation1
Binding sitei237SubstrateUniRule annotation1
Metal bindingi259ZincUniRule annotation1
Binding sitei259SubstrateUniRule annotation1
Metal bindingi262ZincUniRule annotation1
Binding sitei262SubstrateUniRule annotation1
Active sitei327Proton acceptorUniRule annotation1
Active sitei328Proton acceptorUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Metal bindingi361ZincUniRule annotation1
Binding sitei361SubstrateUniRule annotation1
Binding sitei415SubstrateUniRule annotation1
Metal bindingi420ZincUniRule annotation1
Binding sitei420SubstrateUniRule 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 dehydrogenase 1UniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDH 1UniRule annotation
Gene namesi
Name:hisD1UniRule annotation
Ordered Locus Names:RHOS4_22370
ORF Names:RSP_0632
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002703 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002298631 – 434Histidinol dehydrogenase 1Add BLAST434

Interactioni

Protein-protein interaction databases

STRINGi272943.RSP_0632.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.
PhylomeDBiQ3J079.

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.

Q3J079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQFLDTRRP GFEADFTALL GMKREDSPDV DAVVAGIIAD VRARGDAAVI
60 70 80 90 100
ELTARFDRLE LTPERLAFSE AEIEAEIATV SAEDRAALEL AAERIRAYHA
110 120 130 140 150
RQMPENARWT DAAGAELGWR WGPIASAGLY VPGGLASYPS SVLMNAIPAR
160 170 180 190 200
VAGVERLVVA CPTPGGVVNP LVLLAARLAG VDAVYRIGGA QAVAALAYGT
210 220 230 240 250
ETIRPVDKIT GPGNAYVAAA KRRVFGRVGI DMIAGPSEIL VIAEGAVDPD
260 270 280 290 300
WIALDLLSQA EHDESAQSIL VTPDEALGRA VVQAVEARLE TLERRAIAGA
310 320 330 340 350
SWRDYGAVIV TRDLEEAAAL SDRVAPEHLE LCVADPEALA ARIRHAGAIF
360 370 380 390 400
LGGWTPEAIG DYVGGPNHVL PTARSARFSS GLSVMDFLKR TTLARMTPAA
410 420 430
LRAVGPAAER LAISESLEAH GLSVRARLDR LNEG
Length:434
Mass (Da):45,962
Last modified:November 8, 2005 - v1
Checksum:i5B5E5AE935E404B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000143 Genomic DNA. Translation: ABA79805.1.
RefSeqiWP_011338373.1. NZ_AKVW01000001.1.
YP_353706.1. NC_007493.2.

Genome annotation databases

EnsemblBacteriaiABA79805; ABA79805; RSP_0632.
GeneIDi3718260.
KEGGirsp:RSP_0632.
PATRICi23154415. VBIRhoSph57909_2579.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000143 Genomic DNA. Translation: ABA79805.1.
RefSeqiWP_011338373.1. NZ_AKVW01000001.1.
YP_353706.1. NC_007493.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_0632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA79805; ABA79805; RSP_0632.
GeneIDi3718260.
KEGGirsp:RSP_0632.
PATRICi23154415. VBIRhoSph57909_2579.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.
PhylomeDBiQ3J079.

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 nameiHISX1_RHOS4
AccessioniPrimary (citable) accession number: Q3J079
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: November 2, 2016
This is version 73 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.