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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Status
Reviewed-Annotation score: 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: betaine biosynthesis via choline pathway

This protein is involved in step 1 of the subpathway that synthesizes betaine from betaine aldehyde.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. NAD/NADP-dependent betaine aldehyde dehydrogenase (betB)
This subpathway is part of the pathway betaine biosynthesis via choline pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes betaine from betaine aldehyde, the pathway betaine biosynthesis via choline pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi32Potassium 1UniRule annotation1
Metal bindingi33Potassium 1; via carbonyl oxygenUniRule annotation1
Metal bindingi99Potassium 1UniRule annotation1
Active sitei168Charge relay systemUniRule annotation1
Metal bindingi250Potassium 2; via carbonyl oxygenUniRule annotation1
Active sitei256Proton acceptorUniRule annotation1
Binding sitei290NAD/NADPUniRule annotation1
Binding sitei390NAD/NADPUniRule annotation1
Metal bindingi460Potassium 2; via carbonyl oxygenUniRule annotation1
Metal bindingi463Potassium 2; via carbonyl oxygenUniRule annotation1
Active sitei467Charge relay systemUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi156 – 159NAD/NADPUniRule annotation4
Nucleotide bindingi182 – 185NAD/NADPUniRule annotation4
Nucleotide bindingi234 – 239NAD/NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

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 fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Taxonomic identifieri176299 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
Proteomesi
  • UP000000813 Componenti: Chromosome circular

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000565351 – 493NAD/NADP-dependent betaine aldehyde dehydrogenaseAdd BLAST493

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei290Cysteine sulfenic acid (-SOH)UniRule annotation1

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi176299.Atu0829.

Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Beta strandi20 – 22Combined sources3
Beta strandi29 – 33Combined sources5
Turni35 – 37Combined sources3
Beta strandi40 – 45Combined sources6
Helixi49 – 68Combined sources20
Helixi71 – 87Combined sources17
Helixi89 – 100Combined sources12
Helixi104 – 110Combined sources7
Helixi112 – 129Combined sources18
Beta strandi134 – 136Combined sources3
Beta strandi138 – 148Combined sources11
Beta strandi150 – 155Combined sources6
Beta strandi158 – 160Combined sources3
Helixi161 – 174Combined sources14
Beta strandi178 – 182Combined sources5
Helixi190 – 200Combined sources11
Beta strandi207 – 210Combined sources4
Helixi217 – 222Combined sources6
Beta strandi227 – 234Combined sources8
Helixi236 – 248Combined sources13
Beta strandi252 – 256Combined sources5
Beta strandi261 – 265Combined sources5
Helixi271 – 282Combined sources12
Helixi287 – 290Combined sources4
Beta strandi294 – 299Combined sources6
Helixi300 – 302Combined sources3
Helixi303 – 316Combined sources14
Helixi335 – 351Combined sources17
Beta strandi354 – 357Combined sources4
Beta strandi367 – 370Combined sources4
Beta strandi375 – 380Combined sources6
Helixi385 – 388Combined sources4
Beta strandi392 – 401Combined sources10
Helixi404 – 412Combined sources9
Beta strandi414 – 423Combined sources10
Helixi427 – 436Combined sources10
Beta strandi440 – 446Combined sources7
Helixi470 – 475Combined sources6
Beta strandi476 – 484Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3R31X-ray2.15A/B1-493[»]
ProteinModelPortaliQ8UH56.
SMRiQ8UH56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
KOiK00130.
OMAiTKSVYVG.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH. 1 hit.
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.
WP_010971179.1. 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.
PIRiAE2678.
B97460.
RefSeqiNP_353850.1. NC_003062.2.
WP_010971179.1. NC_003062.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3R31X-ray2.15A/B1-493[»]
ProteinModelPortaliQ8UH56.
SMRiQ8UH56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176299.Atu0829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
KOiK00130.
OMAiTKSVYVG.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BioCyciAGRO:ATU0829-MONOMER.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPiMF_00804. BADH. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiBETB_AGRFC
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 2, 2016
This is version 89 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

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 one 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.