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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Rhodopirellula baltica (strain SH1)
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 (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. 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 sitei269 – 2691SubstrateUniRule annotation
Metal bindingi291 – 2911ZincUniRule annotation
Binding sitei291 – 2911SubstrateUniRule annotation
Metal bindingi294 – 2941ZincUniRule annotation
Binding sitei294 – 2941SubstrateUniRule annotation
Active sitei358 – 3581Proton acceptorUniRule annotation
Active sitei359 – 3591Proton acceptorUniRule annotation
Binding sitei359 – 3591SubstrateUniRule annotation
Metal bindingi392 – 3921ZincUniRule annotation
Binding sitei392 – 3921SubstrateUniRule annotation
Binding sitei446 – 4461SubstrateUniRule annotation
Metal bindingi451 – 4511ZincUniRule annotation
Binding sitei451 – 4511SubstrateUniRule 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

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:RB1584
OrganismiRhodopirellula baltica (strain SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
ProteomesiUP000001025 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 460460Histidinol dehydrogenasePRO_0000135834Add
BLAST

Proteomic databases

PRIDEiQ7UX39.

Interactioni

Protein-protein interaction databases

STRINGi243090.RB1584.

Structurei

3D structure databases

ProteinModelPortaliQ7UX39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ7UX39.
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.

Q7UX39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRIVAVPEF SIQTVDARDP SSSEAAETLA ALREKLSPRG DLVSPRGREL
60 70 80 90 100
TLKVFGKALS PIEVVETICK DVQSQGTEAL LRYTKSLDGA ELTADTLRVP
110 120 130 140 150
EEDLKAAHAV ADPKLIETIG RIRDNIATFQ SAILHRDVTI TPRPGVSLTQ
160 170 180 190 200
RYVPIPRVGI CVPGGAAAYP STVMMTAIPA QVAGVDEIAV VAPPTPFGAY
210 220 230 240 250
NTDMLATCHE LGIKEVYRCG GAQAVAAMAY GCDALPAVDK IVGPGNLFVA
260 270 280 290 300
LAKKHVFGTV DIDSFAGPSE VIVIADESAN AAFVASDLLA QAEHSPGSAI
310 320 330 340 350
LITWDESLLT SVQAELSRQL GELERGDLAR DALSDFGALV LARDADHACE
360 370 380 390 400
LTDSFAPEHL QIETREPESL IAKIRHSGAA FLGHHTPVAL GDYAAGPSHV
410 420 430 440 450
LPTGGTCRWA AGLSANSFLR SGSVTQFDQS ALSAIAQDVI TVAEKEGLTA
460
HARSISIRTE
Length:460
Mass (Da):48,514
Last modified:October 1, 2003 - v1
Checksum:i507E4E5DAE69E1BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294135 Genomic DNA. Translation: CAD72173.1.
RefSeqiNP_864492.1. NC_005027.1.
WP_011118440.1. NC_005027.1.

Genome annotation databases

EnsemblBacteriaiCAD72173; CAD72173; RB1584.
GeneIDi1789901.
KEGGirba:RB1584.
PATRICi23242901. VBIRhoBal59814_0740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294135 Genomic DNA. Translation: CAD72173.1.
RefSeqiNP_864492.1. NC_005027.1.
WP_011118440.1. NC_005027.1.

3D structure databases

ProteinModelPortaliQ7UX39.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243090.RB1584.

Proteomic databases

PRIDEiQ7UX39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD72173; CAD72173; RB1584.
GeneIDi1789901.
KEGGirba:RB1584.
PATRICi23242901. VBIRhoBal59814_0740.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ7UX39.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

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: SH1.

Entry informationi

Entry nameiHISX_RHOBA
AccessioniPrimary (citable) accession number: Q7UX39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: May 27, 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.