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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Prochlorococcus marinus (strain MIT 9313)
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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit hisF1 (hisF1), Imidazole glycerol phosphate synthase subunit HisH 2 (hisH2), Imidazole glycerol phosphate synthase subunit HisH 1 (hisH1), Putative imidazole glycerol phosphate synthase subunit hisF2 (hisF2)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. no protein annotated in this organism
  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 sitei142NADUniRule annotation1
Binding sitei204NADUniRule annotation1
Binding sitei227NADUniRule annotation1
Binding sitei250SubstrateUniRule annotation1
Metal bindingi272ZincUniRule annotation1
Binding sitei272SubstrateUniRule annotation1
Metal bindingi275ZincUniRule annotation1
Binding sitei275SubstrateUniRule annotation1
Active sitei340Proton acceptorUniRule annotation1
Active sitei341Proton acceptorUniRule annotation1
Binding sitei341SubstrateUniRule annotation1
Metal bindingi374ZincUniRule annotation1
Binding sitei374SubstrateUniRule annotation1
Binding sitei428SubstrateUniRule annotation1
Metal bindingi433ZincUniRule annotation1
Binding sitei433SubstrateUniRule 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:PMT_1510
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001423 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358141 – 442Histidinol dehydrogenaseAdd BLAST442

Interactioni

Protein-protein interaction databases

STRINGi74547.PMT1510.

Structurei

3D structure databases

ProteinModelPortaliQ7V5N9.
SMRiQ7V5N9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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.

Q7V5N9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQSGQAESE TPSTLIHCVR DRQQAKRELE RLANRSTGNS QKQAMATVED
60 70 80 90 100
ILDTVRSQGD QALITLTERF DGFRPEPLTV APEELEDAWR KTPQKLQSAL
110 120 130 140 150
ELAYRRIQDF HQHQRPNDLM VQGIHGEQLG RRWRPVQKAG IYIPGGRAAY
160 170 180 190 200
PSTVLMNAVP AQVAGVEQLV MTSPAGRDGQ INRTVLAAAH LAGIREVLRL
210 220 230 240 250
GGAQAIAALA FGTETVPKVD VISGPGNLYV TLAKKAVYGQ VGIDSLAGPS
260 270 280 290 300
EVLVIADQSA RVEQVAADLL AQSEHDPLAA AVLLTTEASL AEQLPSHLEA
310 320 330 340 350
QLKGHPREQI CRASLSNWGL VVICESLERC AQLSDHFAPE HLELLVEHPH
360 370 380 390 400
AIADCIKNAG AIFIGPWTPE AVGDYLAGPN HTLPTCGTAR FSGALSVETF
410 420 430 440
LRHTSLIEFN RSALEATANA VRELASSEGL HSHAESVRIR FE
Length:442
Mass (Da):47,869
Last modified:October 1, 2003 - v1
Checksum:iD3A84859545793C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE21685.1.
RefSeqiWP_011130878.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE21685; CAE21685; PMT_1510.
KEGGipmt:PMT_1510.
PATRICi23011587. VBIProMar135351_1937.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE21685.1.
RefSeqiWP_011130878.1. NC_005071.1.

3D structure databases

ProteinModelPortaliQ7V5N9.
SMRiQ7V5N9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74547.PMT1510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE21685; CAE21685; PMT_1510.
KEGGipmt:PMT_1510.
PATRICi23011587. VBIProMar135351_1937.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. LUCA.
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_PROMM
AccessioniPrimary (citable) accession number: Q7V5N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 90 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.