Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7VSZ1

- HISX_BORPE

UniProt

Q7VSZ1 - HISX_BORPE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
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

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.
OMAiCAIANRI.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BX640422 Genomic DNA. Translation: CAE44024.1 .
RefSeqi NP_882269.1. NC_002929.2.

3D structure databases

ProteinModelPortali Q7VSZ1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257313.BP3768.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE44024 ; CAE44024 ; BP3768 .
GeneIDi 2665051.
KEGGi bpe:BP3768.
PATRICi 21161216. VBIBorPer7866_4072.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci BPER257313:BP3768-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. "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: October 1, 2014
This is version 75 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