Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
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 regulatory subunit (hisZ), 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 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei125 – 1251NADUniRule annotation
Binding sitei186 – 1861NADUniRule annotation
Binding sitei209 – 2091NADUniRule annotation
Binding sitei234 – 2341SubstrateUniRule annotation
Metal bindingi256 – 2561ZincUniRule annotation
Binding sitei256 – 2561SubstrateUniRule annotation
Metal bindingi259 – 2591ZincUniRule annotation
Binding sitei259 – 2591SubstrateUniRule annotation
Active sitei325 – 3251Proton acceptorUniRule annotation
Active sitei326 – 3261Proton acceptorUniRule annotation
Binding sitei326 – 3261SubstrateUniRule annotation
Metal bindingi359 – 3591ZincUniRule annotation
Binding sitei359 – 3591SubstrateUniRule annotation
Binding sitei413 – 4131SubstrateUniRule annotation
Metal bindingi419 – 4191ZincUniRule annotation
Binding sitei419 – 4191SubstrateUniRule 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

BioCyciLINT189518:GJBB-2055-MONOMER.
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:LA_2515
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifieri189518 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira
ProteomesiUP000001408 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Histidinol dehydrogenasePRO_0000135788Add
BLAST

Proteomic databases

PaxDbiQ8F393.

Interactioni

Protein-protein interaction databases

STRINGi189518.LA_2515.

Structurei

3D structure databases

ProteinModelPortaliQ8F393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ8F393.
KOiK00013.
OMAiIETFHNA.
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.

Q8F393-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIQIFKVGL KDHSVLDPVL KRAREDLSST LALVKPIVED VKNRGDSALR
60 70 80 90 100
EYTQKFDEVI PPKSFVLEIS KLNPKIDPKL KTALVKAAKN IRNFHKIQIP
110 120 130 140 150
ENKEIIIHGN KLGILHTPIE SVSVYAPGGK ALYPSTILMG VIPAKLAGVK
160 170 180 190 200
NIQIVTPPRK GTLPDGLIAA AKIAGADRIV MAGGAQGIAA VSYGTESIPS
210 220 230 240 250
SEFVVGPGNK FVTAAKVYLS GQGVIGIDSP AGPSEVLIIA DDSADPMWVA
260 270 280 290 300
ADLLSQAEHG EDSVAILCTN SLSLAQKVKE EVEKALIERP KRGEMKRKSI
310 320 330 340 350
KDHGKIFVFS NLEECFVFSN LFAPEHLEIQ TKNFKKDLKK VKHAGSVFLG
360 370 380 390 400
NYSPVAMGDY ISGTNHILPT AGAARIYSSL GVSTFLKRVT WQEVSKKSIQ
410 420
NLYPHVKVLS EFEGLDEEHG NSVRIRR
Length:427
Mass (Da):46,380
Last modified:March 1, 2003 - v1
Checksum:i2FA9AB963E5D48ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010300 Genomic DNA. Translation: AAN49714.1.
RefSeqiNP_712696.1. NC_004342.2.
WP_001007465.1. NC_004342.2.

Genome annotation databases

EnsemblBacteriaiAAN49714; AAN49714; LA_2515.
GeneIDi1151858.
KEGGilil:LA_2515.
PATRICi22385862. VBILepInt91350_2497.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010300 Genomic DNA. Translation: AAN49714.1.
RefSeqiNP_712696.1. NC_004342.2.
WP_001007465.1. NC_004342.2.

3D structure databases

ProteinModelPortaliQ8F393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi189518.LA_2515.

Proteomic databases

PaxDbiQ8F393.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN49714; AAN49714; LA_2515.
GeneIDi1151858.
KEGGilil:LA_2515.
PATRICi22385862. VBILepInt91350_2497.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
InParanoidiQ8F393.
KOiK00013.
OMAiIETFHNA.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciLINT189518:GJBB-2055-MONOMER.

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: 56601.

Entry informationi

Entry nameiHISX_LEPIN
AccessioniPrimary (citable) accession number: Q8F393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 93 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.