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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Chlorobium luteolum (strain DSM 273 / 2530) (Pelodictyon luteolum)
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. 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)DescriptionActionsGraphical viewLength
Binding sitei141NADUniRule annotation1
Binding sitei203NADUniRule annotation1
Binding sitei226NADUniRule annotation1
Binding sitei249SubstrateUniRule annotation1
Metal bindingi271ZincUniRule annotation1
Binding sitei271SubstrateUniRule annotation1
Metal bindingi274ZincUniRule annotation1
Binding sitei274SubstrateUniRule annotation1
Active sitei339Proton acceptorUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Binding sitei340SubstrateUniRule annotation1
Metal bindingi373ZincUniRule annotation1
Binding sitei373SubstrateUniRule annotation1
Binding sitei427SubstrateUniRule annotation1
Metal bindingi432ZincUniRule annotation1
Binding sitei432SubstrateUniRule 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 dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
Ordered Locus Names:Plut_0554
OrganismiChlorobium luteolum (strain DSM 273 / 2530) (Pelodictyon luteolum)
Taxonomic identifieri319225 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon
Proteomesi
  • UP000002709 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002298601 – 443Histidinol dehydrogenaseAdd BLAST443

Interactioni

Protein-protein interaction databases

STRINGi319225.Plut_0554.

Structurei

3D structure databases

ProteinModelPortaliQ3B5E3.
SMRiQ3B5E3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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.

Q3B5E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPVHYRTST STIVAVLKLY RFLDDRDALF RQIGRSVDFD PEVQRAVTDI
60 70 80 90 100
LEAVRLRGDM AVLEYTERFQ GAVLTSMQVP EEDILRAREE ADPAFIRVLE
110 120 130 140 150
EAWENILRFH RHEVENSFFY EGEGGVVLGQ RVTPMDRAML YVPGGKASYP
160 170 180 190 200
SSVLMNAAPA RVAGVGEIFM TTPCDASGAV SPHILAAASV AGVTSVYRLG
210 220 230 240 250
GAQAVAAFAY GTQTIPKVDI ITGPGNKYVA LAKKQVFGHV AIDSIAGPSE
260 270 280 290 300
VVVVADDDAD AEFITMDLFA QAEHDPDASS VLITPSMRLA EEVRDLAAAR
310 320 330 340 350
VGSMLRGEVI AEALSNNGAI VVVADIEEAC RVSDMIAPEH LELHVLHPWE
360 370 380 390 400
LLASIRHAGA VFMGGYSCET VGDYYAGPNH TLPTNGTARF FSPLSVRDFV
410 420 430 440
KHTSIISYTR RQIMACGERI ASFADHEGLE AHAEAVRARL KKG
Length:443
Mass (Da):48,062
Last modified:November 22, 2005 - v1
Checksum:i7A4C8C653019BE3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000096 Genomic DNA. Translation: ABB23438.1.

Genome annotation databases

EnsemblBacteriaiABB23438; ABB23438; Plut_0554.
KEGGiplt:Plut_0554.
PATRICi21378590. VBIChlLut1287_0577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000096 Genomic DNA. Translation: ABB23438.1.

3D structure databases

ProteinModelPortaliQ3B5E3.
SMRiQ3B5E3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi319225.Plut_0554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB23438; ABB23438; Plut_0554.
KEGGiplt:Plut_0554.
PATRICi21378590. VBIChlLut1287_0577.

Phylogenomic databases

eggNOGiCOG0141. LUCA.
HOGENOMiHOG000243914.
KOiK00013.
OMAiGGTARFY.
OrthoDBiPOG091H03YX.

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 nameiHISX_CHLL7
AccessioniPrimary (citable) accession number: Q3B5E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: November 2, 2016
This is version 76 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.