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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Status
Reviewed-Annotation score: -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

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 bindingi27Potassium 1; via carbonyl oxygenUniRule annotation1
Metal bindingi93Potassium 1UniRule annotation1
Active sitei161Charge relay systemUniRule annotation1
Binding sitei208NAD/NADP; via amide nitrogenUniRule annotation1
Metal bindingi243Potassium 2; via carbonyl oxygenUniRule annotation1
Active sitei249Proton acceptorUniRule annotation1
Binding sitei283NAD/NADPUniRule annotation1
Binding sitei384NAD/NADPUniRule annotation1
Metal bindingi454Potassium 2; via carbonyl oxygenUniRule annotation1
Metal bindingi457Potassium 2; via carbonyl oxygenUniRule annotation1
Active sitei461Charge relay systemUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi149 – 152NAD/NADPUniRule annotation4
Nucleotide bindingi175 – 178NAD/NADPUniRule annotation4
Nucleotide bindingi227 – 232NAD/NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, NADP, Potassium

Enzyme and pathway databases

BioCyciOANT439375:G1G9F-2878-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:Oant_2710
OrganismiOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Taxonomic identifieri439375 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
Proteomesi
  • UP000002301 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000470441 – 487NAD/NADP-dependent betaine aldehyde dehydrogenaseAdd BLAST487

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei283Cysteine sulfenic acid (-SOH)UniRule annotation1

Keywords - PTMi

Oxidation

Proteomic databases

PRIDEiA6X2G8

Interactioni

Subunit structurei

Dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi439375.Oant_2710

Structurei

3D structure databases

ProteinModelPortaliA6X2G8
SMRiA6X2G8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C26 Bacteria
COG1012 LUCA
HOGENOMiHOG000271505
KOiK00130
OMAiSFGYTRR
OrthoDBiPOG091H05FS

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
HAMAPiMF_00804 BADH, 1 hit
InterProiView protein in InterPro
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
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
TIGRFAMsiTIGR01804 BADH, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

Sequencei

Sequence statusi: Complete.

A6X2G8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAQPKASHF IGGAFVEDKT GKPSPVIYPA TGEEIARLYS ATPDVIEAAY
60 70 80 90 100
AAALKAQGEW AALKPVERGR ILRRTADILR EKNKKLSKLE TLDTGKALQE
110 120 130 140 150
TLVADAASAA DALEFFGGII SGFNGEFVEL GGSFAYTRRE ALGICVGIGA
160 170 180 190 200
WNYPIQIAAW KSAPALAMGN AFIFKPSENT PLSALALAEA YKEAGLPDGL
210 220 230 240 250
FNVVQGFGDV GAALVNHRLT AKVSLTGSVP TGKRIMAQAG EHLKHVTMEL
260 270 280 290 300
GGKSPIIVFD DADIESAIGG AMLGNFYSTG QVCSNGTRVF VHKNLRERFV
310 320 330 340 350
ERLVERTRKI RIGDPLDEAT QMGPLVNRAQ RDKVLSYIEK GKAEGATLAC
360 370 380 390 400
GGGVPKLQGF DKGYFIEPTI FTDVTDDMTI AREEIFGPVM SVLEFSDEDE
410 420 430 440 450
VIARANDTEF GLAAGVFTAD IARGHRVIGQ IKAGTCWINA YNLTPVEVPF
460 470 480
GGYKQSGIGR ENGIAALAHY SQIKTVYVEM GKVDSPY
Length:487
Mass (Da):52,218
Last modified:August 21, 2007 - v1
Checksum:i62AEA5F26C712CB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000758 Genomic DNA Translation: ABS15422.1
RefSeqiWP_012092478.1, NC_009667.1

Genome annotation databases

EnsemblBacteriaiABS15422; ABS15422; Oant_2710
GeneIDi5378475
KEGGioan:Oant_2710
PATRICifig|439375.7.peg.2858

Similar proteinsi

Entry informationi

Entry nameiBETB_OCHA4
AccessioniPrimary (citable) accession number: A6X2G8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 23, 2018
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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