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B0S9F2

- HISX_LEPBA

UniProt

B0S9F2 - HISX_LEPBA

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Protein

Histidinol dehydrogenase

Gene

hisD

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241NADUniRule annotation
Binding sitei185 – 1851NADUniRule annotation
Binding sitei208 – 2081NADUniRule annotation
Binding sitei233 – 2331SubstrateUniRule annotation
Metal bindingi255 – 2551ZincUniRule annotation
Binding sitei255 – 2551SubstrateUniRule annotation
Metal bindingi258 – 2581ZincUniRule annotation
Binding sitei258 – 2581SubstrateUniRule annotation
Active sitei324 – 3241Proton acceptorUniRule annotation
Active sitei325 – 3251Proton acceptorUniRule annotation
Binding sitei325 – 3251SubstrateUniRule annotation
Metal bindingi358 – 3581ZincUniRule annotation
Binding sitei358 – 3581SubstrateUniRule annotation
Binding sitei412 – 4121SubstrateUniRule annotation
Metal bindingi418 – 4181ZincUniRule annotation
Binding sitei418 – 4181SubstrateUniRule annotation

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-HAMAP
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciLBIF355278:GHTJ-1770-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:LBF_1772
OrganismiLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Taxonomic identifieri355278 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000001846: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430Histidinol dehydrogenasePRO_1000135438Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi355278.LBF_1772.

Structurei

3D structure databases

ProteinModelPortaliB0S9F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiAHERIRR.
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.

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.
YP_001962857.1. NC_010842.1.

Genome annotation databases

EnsemblBacteriaiABZ94279; ABZ94279; LBF_1772.
GeneIDi6387233.
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 .
RefSeqi WP_012388809.1. NC_010842.1.
YP_001962857.1. NC_010842.1.

3D structure databases

ProteinModelPortali B0S9F2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 355278.LBF_1772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABZ94279 ; ABZ94279 ; LBF_1772 .
GeneIDi 6387233.
KEGGi lbf:LBF_1772.
PATRICi 22342647. VBILepBif95142_1879.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K00013.
OMAi AHERIRR.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci LBIF355278:GHTJ-1770-MONOMER.

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
    Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A.
    , Davies J.K., Medigue C., Adler B.
    PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Patoc 1 / Ames.

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 26, 2014
This is version 58 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

External Data

Dasty 3