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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Pseudomonas syringae pv. syringae (strain B728a)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  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)DescriptionActionsGraphical viewLength
Binding sitei136NADUniRule annotation1
Binding sitei197NADUniRule annotation1
Binding sitei220NADUniRule annotation1
Binding sitei243SubstrateUniRule annotation1
Metal bindingi265ZincUniRule annotation1
Binding sitei265SubstrateUniRule annotation1
Metal bindingi268ZincUniRule annotation1
Binding sitei268SubstrateUniRule annotation1
Active sitei333Proton acceptorUniRule annotation1
Active sitei334Proton acceptorUniRule annotation1
Binding sitei334SubstrateUniRule annotation1
Metal bindingi367ZincUniRule annotation1
Binding sitei367SubstrateUniRule annotation1
Binding sitei421SubstrateUniRule annotation1
Metal bindingi426ZincUniRule annotation1
Binding sitei426SubstrateUniRule 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:Psyr_4133
OrganismiPseudomonas syringae pv. syringae (strain B728a)
Taxonomic identifieri205918 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae
Proteomesi
  • UP000000426 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001358231 – 448Histidinol dehydrogenaseAdd BLAST448

Interactioni

Protein-protein interaction databases

STRINGi205918.Psyr_4133.

Structurei

3D structure databases

ProteinModelPortaliQ4ZNV9.
SMRiQ4ZNV9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. 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.

Q4ZNV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPTAIRRL DAADPDFARH LDHLLSWESV SDDSVNQRVL DIIKAVRERG
60 70 80 90 100
DAALVEFTQK FDGLQVASMA DLILPRERLE LALTRITPGQ REALEKAAER
110 120 130 140 150
VRSYHEKQKQ DSWSYTEADG TVLGQKVTPL DRAGLYVPGG KASYPSSVLM
160 170 180 190 200
NAIPAKVAGV TEVVMVVPTP RGEINELVLA AACIAGVDRV FTIGGAQAVA
210 220 230 240 250
ALAYGTESVP KVDKVVGPGN IYVATAKRHV FGQVGIDMIA GPSEILVVCD
260 270 280 290 300
GQTDPDWIAM DLFSQAEHDE DAQAILVSPD AEFLDKVAAS ITRLLPTMER
310 320 330 340 350
AAIVETSING RGALIKVADM AQAIEVANRI APEHLELSVA DPEAWLPQIR
360 370 380 390 400
HAGAIFMGRH TSEALGDYCA GPNHVLPTSG TARFSSPLGV YDFQKRSSII
410 420 430 440
YCSPQGASEL GKTASVLARG ESLSGHARSA EYRITDPDWT AGNKEDGK
Length:448
Mass (Da):48,073
Last modified:June 7, 2005 - v1
Checksum:i719C1316F740E440
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000075 Genomic DNA. Translation: AAY39163.1.
RefSeqiWP_011268859.1. NC_007005.1.
YP_237201.1. NC_007005.1.

Genome annotation databases

EnsemblBacteriaiAAY39163; AAY39163; Psyr_4133.
GeneIDi3369670.
KEGGipsb:Psyr_4133.
PATRICi19989010. VBIPseSyr42314_4253.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000075 Genomic DNA. Translation: AAY39163.1.
RefSeqiWP_011268859.1. NC_007005.1.
YP_237201.1. NC_007005.1.

3D structure databases

ProteinModelPortaliQ4ZNV9.
SMRiQ4ZNV9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi205918.Psyr_4133.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAY39163; AAY39163; Psyr_4133.
GeneIDi3369670.
KEGGipsb:Psyr_4133.
PATRICi19989010. VBIPseSyr42314_4253.

Phylogenomic databases

eggNOGiENOG4105CEK. Bacteria.
COG0141. 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_PSEU2
AccessioniPrimary (citable) accession number: Q4ZNV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 79 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

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.