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Q8UH56

- BETB_AGRT5

UniProt

Q8UH56 - BETB_AGRT5

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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Agrobacterium tumefaciens (strain C58 / ATCC 33970)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid.UniRule annotation

Catalytic activityi

Betaine aldehyde + NAD+ + H2O = betaine + NADH.UniRule annotation

Cofactori

K(+)UniRule annotationNote: Binds 2 potassium ions per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi32 – 321Potassium 1UniRule annotation
Metal bindingi33 – 331Potassium 1; via carbonyl oxygenUniRule annotation
Metal bindingi99 – 991Potassium 1UniRule annotation
Active sitei168 – 1681Charge relay systemUniRule annotation
Metal bindingi250 – 2501Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei256 – 2561Proton acceptorUniRule annotation
Binding sitei290 – 2901NAD/NADPUniRule annotation
Binding sitei390 – 3901NAD/NADPUniRule annotation
Metal bindingi460 – 4601Potassium 2; via carbonyl oxygenUniRule annotation
Metal bindingi463 – 4631Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei467 – 4671Charge relay systemUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 1594NAD/NADPUniRule annotation
Nucleotide bindingi182 – 1854NAD/NADPUniRule annotation
Nucleotide bindingi234 – 2396NAD/NADPUniRule annotation

GO - Molecular functioni

  1. betaine-aldehyde dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glycine betaine biosynthetic process from choline Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, NADP, Potassium

Enzyme and pathway databases

BioCyciAGRO:ATU0829-MONOMER.
UniPathwayiUPA00529; UER00386.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD/NADP-dependent betaine aldehyde dehydrogenaseUniRule annotation (EC:1.2.1.8UniRule annotation)
Short name:
BADHUniRule annotation
Gene namesi
Name:betBUniRule annotation
Ordered Locus Names:Atu0829
ORF Names:AGR_C_1515
OrganismiAgrobacterium tumefaciens (strain C58 / ATCC 33970)
Taxonomic identifieri176299 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
ProteomesiUP000000813: Chromosome circular

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_0000056535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei290 – 2901Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi176299.Atu0829.

Structurei

Secondary structure

1
493
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176Combined sources
Beta strandi20 – 223Combined sources
Beta strandi29 – 335Combined sources
Turni35 – 373Combined sources
Beta strandi40 – 456Combined sources
Helixi49 – 6820Combined sources
Helixi71 – 8717Combined sources
Helixi89 – 10012Combined sources
Helixi104 – 1107Combined sources
Helixi112 – 12918Combined sources
Beta strandi134 – 1363Combined sources
Beta strandi138 – 14811Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi158 – 1603Combined sources
Helixi161 – 17414Combined sources
Beta strandi178 – 1825Combined sources
Helixi190 – 20011Combined sources
Beta strandi207 – 2104Combined sources
Helixi217 – 2226Combined sources
Beta strandi227 – 2348Combined sources
Helixi236 – 24813Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi261 – 2655Combined sources
Helixi271 – 28212Combined sources
Helixi287 – 2904Combined sources
Beta strandi294 – 2996Combined sources
Helixi300 – 3023Combined sources
Helixi303 – 31614Combined sources
Helixi335 – 35117Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi375 – 3806Combined sources
Helixi385 – 3884Combined sources
Beta strandi392 – 40110Combined sources
Helixi404 – 4129Combined sources
Beta strandi414 – 42310Combined sources
Helixi427 – 43610Combined sources
Beta strandi440 – 4467Combined sources
Helixi470 – 4756Combined sources
Beta strandi476 – 4849Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3R31X-ray2.15A/B1-493[»]
ProteinModelPortaliQ8UH56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiCEHQLVA.
OrthoDBiEOG6BS8QW.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR011264. BADH.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01804. BADH. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8UH56-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTIATPLKAQ PKASHFIDGD YVEDNTGTPF ESIFPATGEM IAKLHAATPA
60 70 80 90 100
IVERAIASAK RAQKEWAAMS PMARGRILKR AADIMRERND ALSTLETLDT
110 120 130 140 150
GKPIQETIVA DPTSGADAFE FFGGIAPSAL NGDYIPLGGD FAYTKRVPLG
160 170 180 190 200
VCVGIGAWNY PQQIACWKAA PALVAGNAMV FKPSENTPLG ALKIAEILIE
210 220 230 240 250
AGLPKGLFNV IQGDRDTGPL LVNHPDVAKV SLTGSVPTGR KVAAAAAGHL
260 270 280 290 300
KHVTMELGGK SPMIVFDDAD IESAVGGAML GNFYSSGQVC SNGTRVFVQK
310 320 330 340 350
KAKARFLENL KRRTEAMILG DPLDYATHLG PLVSKAQQEK VLSYIEKGKA
360 370 380 390 400
EGATLITGGG IPNNVAGEGA YVQPTVFADV TDDMTIAREE IFGPVMCVLD
410 420 430 440 450
FDDEDEVLAR ANATEFGLAG GVFTADLARA HRVVDGLEAG TLWINTYNLC
460 470 480 490
PVEIPFGGSK QSGFGRENSA AALEHYSELK TVYVSTGKVD APY
Length:493
Mass (Da):52,204
Last modified:June 1, 2002 - v1
Checksum:i7636ADEEB5327833
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007869 Genomic DNA. Translation: AAK86635.1.
PIRiAE2678.
B97460.
RefSeqiNP_353850.1. NC_003062.2.

Genome annotation databases

EnsemblBacteriaiAAK86635; AAK86635; Atu0829.
GeneIDi1132867.
KEGGiatu:Atu0829.
PATRICi20811367. VBIAgrTum91616_0825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007869 Genomic DNA. Translation: AAK86635.1 .
PIRi AE2678.
B97460.
RefSeqi NP_353850.1. NC_003062.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3R31 X-ray 2.15 A/B 1-493 [» ]
ProteinModelPortali Q8UH56.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176299.Atu0829.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK86635 ; AAK86635 ; Atu0829 .
GeneIDi 1132867.
KEGGi atu:Atu0829.
PATRICi 20811367. VBIAgrTum91616_0825.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271505.
KOi K00130.
OMAi CEHQLVA.
OrthoDBi EOG6BS8QW.

Enzyme and pathway databases

UniPathwayi UPA00529 ; UER00386 .
BioCyci AGRO:ATU0829-MONOMER.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPi MF_00804. BADH.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR011264. BADH.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01804. BADH. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C58 / ATCC 33970.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C58 / ATCC 33970.
  3. "Crystal structure of betaine aldehyde dehydrogenase from Agrobacterium tumefaciens."
    New York structural genomics research consortium (NYSGRC)
    Submitted (MAR-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiBETB_AGRT5
AccessioniPrimary (citable) accession number: Q8UH56
Secondary accession number(s): Q7D0K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 82 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3