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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandMetal-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
SMRiB0S9F2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000243914
KOiK00013
OMAiQAEHDPM
OrthoDBiPOG091H03YX

Family and domain databases

CDDicd06572 Histidinol_dh, 1 hit
HAMAPiMF_01024 HisD, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR001692 Histidinol_DH_CS
IPR022695 Histidinol_DH_monofunct
IPR012131 Hstdl_DH
PANTHERiPTHR21256 PTHR21256, 1 hit
PfamiView protein in Pfam
PF00815 Histidinol_dh, 1 hit
PIRSFiPIRSF000099 Histidinol_dh, 1 hit
PRINTSiPR00083 HOLDHDRGNASE
SUPFAMiSSF53720 SSF53720, 1 hit
TIGRFAMsiTIGR00069 hisD, 1 hit
PROSITEiView protein in PROSITE
PS00611 HISOL_DEHYDROGENASE, 1 hit

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
GeneIDi35831324
KEGGilbf:LBF_1772

Similar proteinsi

Entry informationi

Entry nameiHISX_LEPBA
AccessioniPrimary (citable) accession number: B0S9F2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 8, 2008
Last modified: April 25, 2018
This is version 72 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health