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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Potassium 1UniRule annotation
Metal bindingi93 – 931Potassium 1UniRule annotation
Active sitei162 – 1621Charge relay systemUniRule annotation
Metal bindingi180 – 1801Potassium 1; via carbonyl oxygenUniRule annotation
Binding sitei209 – 2091NAD/NADP; via amide nitrogenUniRule annotation
Metal bindingi245 – 2451Potassium 2; via carbonyl oxygenUniRule annotation
Sitei247 – 2471Seems to be a necessary countercharge to the potassium cationsUniRule annotation
Active sitei251 – 2511Proton acceptorUniRule annotation
Binding sitei285 – 2851NAD/NADPUniRule annotation
Binding sitei386 – 3861NAD/NADPUniRule annotation
Metal bindingi456 – 4561Potassium 2; via carbonyl oxygenUniRule annotation
Metal bindingi459 – 4591Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei463 – 4631Charge relay systemUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1534NAD/NADPUniRule annotation
Nucleotide bindingi176 – 1794NAD/NADPUniRule annotation
Nucleotide bindingi228 – 2336NAD/NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, NADP, Potassium

Enzyme and pathway databases

BioCyciBAMB339670:GH48-4583-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:Bamb_4511
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000000662 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_1000047033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei285 – 2851Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi339670.Bamb_4511.

Structurei

3D structure databases

ProteinModelPortaliQ0B712.
SMRiQ0B712. Positions 8-489.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiHVYQNIA.
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.

Q0B712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVYGLQRLY IGGGYVDATS GKTFDTFDPA TGELLAQVQQ ASAADVDRAV
60 70 80 90 100
ASAREGQREW AAMTAMQRSR ILRRAVDLLR ERNDELAAIE TRDTGKPIGE
110 120 130 140 150
TLAVDIVTGA DVIEYYAGLA TAIEGLQVPL RAESFVYTRR EPLGVCAGIG
160 170 180 190 200
AWNYPIQIAC WKTAPALAAG NAMVFKPSEV TPLTALKLAE IYTEAGVPAG
210 220 230 240 250
VFNVVQGDGS VGALLTGHPD IAKVSFTGGV ETGKKVMSLA GASSLKEVTM
260 270 280 290 300
ELGGKSPLIV FEDADLDRAA DIAVTANFFS SGQVCTNGTR VFVHRSVKDA
310 320 330 340 350
FTQRVLERVK RIRVGKPTDA ATNFGPLVSA AQLDKVLGFI DSGKAEGAKL
360 370 380 390 400
LAGGTRLTDG HFASGQYVAP TVFGDCRDDM KIVREEIFGP VMSILDFESE
410 420 430 440 450
DEVIARANDT HYGLAAGVVT ENLSRAHRTI HRLEAGICWI NTWGESPAEM
460 470 480
PVGGYKQSGV GRENGITTLE HYTRIKSVQV ELGRYNPVF
Length:489
Mass (Da):52,326
Last modified:October 17, 2006 - v1
Checksum:i949732ECB2566C26
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000441 Genomic DNA. Translation: ABI90061.1.
RefSeqiWP_011659482.1. NC_008391.1.
YP_776395.1. NC_008391.1.

Genome annotation databases

EnsemblBacteriaiABI90061; ABI90061; Bamb_4511.
KEGGibam:Bamb_4511.
PATRICi19024943. VBIBurAmb61564_4727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000441 Genomic DNA. Translation: ABI90061.1.
RefSeqiWP_011659482.1. NC_008391.1.
YP_776395.1. NC_008391.1.

3D structure databases

ProteinModelPortaliQ0B712.
SMRiQ0B712. Positions 8-489.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_4511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI90061; ABI90061; Bamb_4511.
KEGGibam:Bamb_4511.
PATRICi19024943. VBIBurAmb61564_4727.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiHVYQNIA.
OrthoDBiEOG6BS8QW.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BioCyciBAMB339670:GH48-4583-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-244 / AMMD.

Entry informationi

Entry nameiBETB_BURCM
AccessioniPrimary (citable) accession number: Q0B712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: May 27, 2015
This is version 64 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

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.