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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. no protein annotated in this organism
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF)
  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 sitei124NADUniRule annotation1
Binding sitei185NADUniRule annotation1
Binding sitei208NADUniRule annotation1
Binding sitei233SubstrateUniRule annotation1
Metal bindingi255ZincUniRule annotation1
Binding sitei255SubstrateUniRule annotation1
Metal bindingi258ZincUniRule annotation1
Binding sitei258SubstrateUniRule annotation1
Active sitei324Proton acceptorUniRule annotation1
Active sitei325Proton acceptorUniRule annotation1
Binding sitei325SubstrateUniRule annotation1
Metal bindingi358ZincUniRule annotation1
Binding sitei358SubstrateUniRule annotation1
Binding sitei412SubstrateUniRule annotation1
Metal bindingi418ZincUniRule annotation1
Binding sitei418SubstrateUniRule 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:LBF_1772
OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Taxonomic identifieri355278 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001354381 – 430Histidinol dehydrogenaseAdd BLAST430

Structurei

3D structure databases

ProteinModelPortaliB0S9F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

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.

B0S9F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIPILHCDR NSKELYSRFL QGAREDLTTA TDRILPILES VRTQGDQALF
60 70 80 90 100
SYTEMFDGIK LSQLTIDPKK IKTNVDEKTK EAFLRAKSNI EAFHMEQKRE
110 120 130 140 150
SWSKVIDGNR LGVKYTPIPS LAVYAPGGKA LYPSSVLMGI IPAKIAGVPS
160 170 180 190 200
IQLITPPQKD GIPEILVWLA QIMDIDRIVT VGGAQGIAAA AYGTESVPKS
210 220 230 240 250
EFIVGPGNAY VAAAKSYLSG QGLIGIESPA GPSEVCIIAD ENANPKWIAC
260 270 280 290 300
DMLSQAEHGE DSSAILLTTD LTLAKRVSEE LEIAFSERPK RLQMKQTAIY
310 320 330 340 350
ENSSILVFPT LDDCIWFSNE LAPEHLEIQT KDYESVFAKI EHAGSVFLGP
360 370 380 390 400
YSPVAMGDYI SGTNHILPTA RGSRIYSSLG VDTFLKRVTF QEVTKESLEN
410 420 430
LYPFVKLMSE LEGLDEEHGT SVKVRTRQFQ
Length:430
Mass (Da):47,347
Last modified:April 8, 2008 - v1
Checksum:i3D0CA083966873FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000777 Genomic DNA. Translation: ABZ94279.1.
RefSeqiWP_012388809.1. NC_010842.1.

Genome annotation databases

EnsemblBacteriaiABZ94279; ABZ94279; LBF_1772.
KEGGilbf:LBF_1772.
PATRICi22342647. VBILepBif95142_1879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000777 Genomic DNA. Translation: ABZ94279.1.
RefSeqiWP_012388809.1. NC_010842.1.

3D structure databases

ProteinModelPortaliB0S9F2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABZ94279; ABZ94279; LBF_1772.
KEGGilbf:LBF_1772.
PATRICi22342647. VBILepBif95142_1879.

Phylogenomic databases

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_LEPBA
AccessioniPrimary (citable) accession number: B0S9F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: November 2, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.