Skip Header

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

Q845V3

- HISX_BURM1

UniProt

Q845V3 - HISX_BURM1

(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
Burkholderia multivorans (strain ATCC 17616 / 249)
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 sitei138 – 1381NADUniRule annotation
Binding sitei199 – 1991NADUniRule annotation
Binding sitei222 – 2221NADUniRule annotation
Binding sitei245 – 2451SubstrateUniRule annotation
Metal bindingi267 – 2671ZincUniRule annotation
Binding sitei267 – 2671SubstrateUniRule annotation
Metal bindingi270 – 2701ZincUniRule annotation
Binding sitei270 – 2701SubstrateUniRule annotation
Active sitei335 – 3351Proton acceptorUniRule annotation
Active sitei336 – 3361Proton acceptorUniRule annotation
Binding sitei336 – 3361SubstrateUniRule annotation
Metal bindingi369 – 3691ZincUniRule annotation
Binding sitei369 – 3691SubstrateUniRule annotation
Binding sitei423 – 4231SubstrateUniRule annotation
Metal bindingi428 – 4281ZincUniRule annotation
Binding sitei428 – 4281SubstrateUniRule 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

BioCyciBMUL395019:GIYO-2924-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:Bmul_0328, BMULJ_02926
OrganismiBurkholderia multivorans (strain ATCC 17616 / 249)
Taxonomic identifieri395019 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000007064: Chromosome 1, UP000008815: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Histidinol dehydrogenasePRO_0000135749Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi395019.Bmul_0328.

Structurei

3D structure databases

ProteinModelPortaliQ845V3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
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.

Q845V3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSITIRKLDS TSEGFDAALR AVLAFEASED EAIERSVAQI LADVKSRGDA
60 70 80 90 100
AVLEYTNRFD RLNADSVAAL ELPQDALQAA LDGLEPKARA ALEAAAARVR
110 120 130 140 150
GYHEKQKIEC GTHSWQYTES DGTVLGQKIT PLDRVGLYVP GGKAAYPSSV
160 170 180 190 200
LMNAIPARVA GVGEIVMVVP TPDGVKNDLV LAAALLGGVD RVFTIGGAQA
210 220 230 240 250
VGALAYGTAT VPAVDKICGP GNAYVASAKR RVFGTVGIDM IAGPSEILVL
260 270 280 290 300
CDGTTDPSWV AMDLFSQAEH DELAQSILLC PDASFIERVE KAIAELLPSM
310 320 330 340 350
PRQDVIRASL EGRGALIKVR DMTEACRIAN DIAPEHLEIS ALEPQQWSQQ
360 370 380 390 400
IRHAGAIFLG RYTSESLGDY CAGPNHVLPT SRTARFSSPL GVYDFIKRSS
410 420 430
LIEVSAEGAH TLGEIAAELA YGEGLQAHAK SAEFRMKG
Length:438
Mass (Da):46,515
Last modified:September 2, 2008 - v2
Checksum:i8F702C8C7E014B1D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 10112AALEA…ARVRG → GRAGSGCRTRAR in BAC65270. (PubMed:12754231)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091436 Genomic DNA. Translation: BAC65270.1.
CP000868 Genomic DNA. Translation: ABX14023.1.
AP009385 Genomic DNA. Translation: BAG44811.1.
RefSeqiYP_001578520.1. NC_010084.1.
YP_001947347.1. NC_010804.1.

Genome annotation databases

EnsemblBacteriaiABX14023; ABX14023; Bmul_0328.
BAG44811; BAG44811; BMULJ_02926.
GeneIDi5765433.
6359505.
KEGGibmj:BMULJ_02926.
bmu:Bmul_0328.
PATRICi19167814. VBIBurMul203716_3956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091436 Genomic DNA. Translation: BAC65270.1 .
CP000868 Genomic DNA. Translation: ABX14023.1 .
AP009385 Genomic DNA. Translation: BAG44811.1 .
RefSeqi YP_001578520.1. NC_010084.1.
YP_001947347.1. NC_010804.1.

3D structure databases

ProteinModelPortali Q845V3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395019.Bmul_0328.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX14023 ; ABX14023 ; Bmul_0328 .
BAG44811 ; BAG44811 ; BMULJ_02926 .
GeneIDi 5765433.
6359505.
KEGGi bmj:BMULJ_02926.
bmu:Bmul_0328.
PATRICi 19167814. VBIBurMul203716_3956.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci BMUL395019:GIYO-2924-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

« Hide 'large scale' publications
  1. "Distribution and organization of auxotrophic genes on the multichromosomal genome of Burkholderia multivorans ATCC 17616."
    Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.
    J. Bacteriol. 185:3333-3343(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC 17616."
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17616 / 249.
  3. "Complete genome sequence of Burkholderia multivorans ATCC 17616."
    Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
    Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17616 / 249.

Entry informationi

Entry nameiHISX_BURM1
AccessioniPrimary (citable) accession number: Q845V3
Secondary accession number(s): A9AE01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: September 2, 2008
Last modified: November 26, 2014
This is version 80 of the entry and version 2 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