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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
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 sitei133 – 1331NADUniRule annotation
Binding sitei194 – 1941NADUniRule annotation
Binding sitei217 – 2171NADUniRule annotation
Binding sitei240 – 2401SubstrateUniRule annotation
Metal bindingi262 – 2621ZincUniRule annotation
Binding sitei262 – 2621SubstrateUniRule annotation
Metal bindingi265 – 2651ZincUniRule annotation
Binding sitei265 – 2651SubstrateUniRule annotation
Active sitei330 – 3301Proton acceptorUniRule annotation
Active sitei331 – 3311Proton acceptorUniRule annotation
Binding sitei331 – 3311SubstrateUniRule annotation
Metal bindingi364 – 3641ZincUniRule annotation
Binding sitei364 – 3641SubstrateUniRule annotation
Binding sitei418 – 4181SubstrateUniRule annotation
Metal bindingi423 – 4231ZincUniRule annotation
Binding sitei423 – 4231SubstrateUniRule 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

BioCyciBPER257313:BP3768-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:BP3768
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000002676: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Histidinol dehydrogenasePRO_0000135738Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257313.BP3768.

Structurei

3D structure databases

ProteinModelPortaliQ7VSZ1.
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.

Q7VSZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALINRLDSR DPGFKTALSQ LLAFEAEQDE SIDQAAAGIL ADVRRRGDAA
60 70 80 90 100
LLEYTQRFDR LAVDDATALE IPQADWHAAL DSLPAAQRQA LEAAAARVRA
110 120 130 140 150
YHERQRGETW TYTEADGTML GQQITALDRV GLYVPGGKAA YPSSVLMNAI
160 170 180 190 200
PAKVAGVPEL IMVTPTPDGV RNPIVLAAAA IAGVDRAFAI GGAQAVGALA
210 220 230 240 250
YGTATVPAVD KIVGPGNAYV AAAKRRVFGT VGIDMIAGPS EILVICDGKT
260 270 280 290 300
PADWIAMDLF SQAEHDELAQ SILLCPDAAF LAEVEAAIER LLPGMPRADI
310 320 330 340 350
LRVSLANRGA LILVRDLEEA CAIANDIAPE HLEISTEQPQ RWTALIRHAG
360 370 380 390 400
AIFMGRYSSE ALGDYCAGPN HVLPTSRTAR FSSPLGVYDF QKRSSLIQVS
410 420 430
REGAQTLGRI AAELALGEGL QAHAASAQYR LDQP
Length:434
Mass (Da):46,136
Last modified:October 1, 2003 - v1
Checksum:iD2D494FB6AE5EB6A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640422 Genomic DNA. Translation: CAE44024.1.
RefSeqiNP_882269.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE44024; CAE44024; BP3768.
GeneIDi2665051.
KEGGibpe:BP3768.
PATRICi21161216. VBIBorPer7866_4072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640422 Genomic DNA. Translation: CAE44024.1.
RefSeqiNP_882269.1. NC_002929.2.

3D structure databases

ProteinModelPortaliQ7VSZ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP3768.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE44024; CAE44024; BP3768.
GeneIDi2665051.
KEGGibpe:BP3768.
PATRICi21161216. VBIBorPer7866_4072.

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiLSVQSFL.
OrthoDBiEOG6CVVCR.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.
BioCyciBPER257313:BP3768-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: Tohama I / ATCC BAA-589 / NCTC 13251.

Entry informationi

Entry nameiHISX_BORPE
AccessioniPrimary (citable) accession number: Q7VSZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: January 7, 2015
This is version 77 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.