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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391NADUniRule annotation
Binding sitei200 – 2001NADUniRule annotation
Binding sitei223 – 2231NADUniRule annotation
Binding sitei246 – 2461SubstrateUniRule annotation
Metal bindingi268 – 2681ZincUniRule annotation
Binding sitei268 – 2681SubstrateUniRule annotation
Metal bindingi271 – 2711ZincUniRule annotation
Binding sitei271 – 2711SubstrateUniRule annotation
Active sitei336 – 3361Proton acceptorUniRule annotation
Active sitei337 – 3371Proton acceptorUniRule annotation
Binding sitei337 – 3371SubstrateUniRule annotation
Metal bindingi370 – 3701ZincUniRule annotation
Binding sitei370 – 3701SubstrateUniRule annotation
Binding sitei424 – 4241SubstrateUniRule annotation
Metal bindingi429 – 4291ZincUniRule annotation
Binding sitei429 – 4291SubstrateUniRule 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

BioCyciBPAR257311:BPP4267-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:BPP4267
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001421: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Histidinol dehydrogenasePRO_0000135737Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257311.BPP4267.

Structurei

3D structure databases

ProteinModelPortaliQ7W2Y4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
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.

Q7W2Y4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQYHDAMALI NRLDSRDPGF KTALSQLLAF EAEQDESIDQ AAAGILADVR
60 70 80 90 100
RRGDAALLEY TQRFDRLAVD DATALEIPQA DWHAALDSLP AAQRQALEAA
110 120 130 140 150
AARVRAYHER QRGETWTYTE ADGTMLGQQI TALDRVGLYV PGGKAAYPSS
160 170 180 190 200
VLMNAIPAKV AGVPELIMVT PTPDGVRNPI VLAAAAIAGV DRAFAIGGAQ
210 220 230 240 250
AVGALAYGTA TVPAVDKIVG PGNAYVAAAK RRVFGTVGID MIAGPSEILV
260 270 280 290 300
ICDGKTPADW IAMDLFSQAE HDELAQSILL CPDAAFLAEV EAAIERLLPG
310 320 330 340 350
MPRADILRVS LANRGALILV RDLEEACAIA NDIAPEHLEI STEQPQRWTA
360 370 380 390 400
LIRHAGAIFM GRYSSEALGD YCAGPNHVLP TSRTARFSSP LGVYDFQKRS
410 420 430 440
SLIQVSREGA QTLGRIAAEL ALGEGLQAHA ASAQYRLDQP
Length:440
Mass (Da):46,882
Last modified:October 1, 2003 - v1
Checksum:iD8FC76AF462F129A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640436 Genomic DNA. Translation: CAE39546.1.
RefSeqiNP_886396.1. NC_002928.3.

Genome annotation databases

EnsemblBacteriaiCAE39546; CAE39546; BPP4267.
GeneIDi1667362.
KEGGibpa:BPP4267.
PATRICi21152644. VBIBorPar43418_4478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640436 Genomic DNA. Translation: CAE39546.1.
RefSeqiNP_886396.1. NC_002928.3.

3D structure databases

ProteinModelPortaliQ7W2Y4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257311.BPP4267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE39546; CAE39546; BPP4267.
GeneIDi1667362.
KEGGibpa:BPP4267.
PATRICi21152644. VBIBorPar43418_4478.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciBPAR257311:BPP4267-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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Entry informationi

Entry nameiHISX_BORPA
AccessioniPrimary (citable) accession number: Q7W2Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: January 7, 2015
This is version 80 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

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.