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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Klebsiella pneumoniae (strain 342)
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 bindingi27 – 271Potassium 1; via carbonyl oxygenUniRule 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 bindingi246 – 2461Potassium 2; via carbonyl oxygenUniRule annotation
Sitei248 – 2481Seems to be a necessary countercharge to the potassium cationsUniRule annotation
Active sitei252 – 2521Proton acceptorUniRule annotation
Binding sitei286 – 2861NAD/NADPUniRule annotation
Binding sitei387 – 3871NAD/NADPUniRule annotation
Metal bindingi457 – 4571Potassium 2; via carbonyl oxygenUniRule annotation
Metal bindingi460 – 4601Potassium 2; via carbonyl oxygenUniRule annotation
Active sitei464 – 4641Charge relay systemUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi150 – 1534NAD/NADPUniRule annotation
Nucleotide bindingi176 – 1794NAD/NADPUniRule annotation
Nucleotide bindingi229 – 2346NAD/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

BioCyciKPNE507522:GI0B-3995-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:KPK_3994
OrganismiKlebsiella pneumoniae (strain 342)
Taxonomic identifieri507522 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella
ProteomesiUP000001734 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_1000133954Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Cysteine sulfenic acid (-SOH)UniRule annotation

Keywords - PTMi

Oxidation

Interactioni

Subunit structurei

Dimer of dimers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB5Y007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiVGGYKES.
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.

B5Y007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRMAEQQLY INGGYTSATS GRTFETINPA TGEVLATVQA AGREDVDRAV
60 70 80 90 100
ESAQRGQKIW AAMTAMERSR ILRRAVDLLR QRNDELARLE TLDTGKPLSE
110 120 130 140 150
TAAVDIVTGA DVLEYYAGLI PALEGSQIPL RDSSFVYTRR EPLGVVAGIG
160 170 180 190 200
AWNYPIQIAL WKSAPALAAG NAMIFKPSEV TPLTALKLAE IYSEAGLPDG
210 220 230 240 250
VFNVLPGIGA ETGQYLTEHP GIAKISFTGG VASGKKVMAN SAASSLKEVT
260 270 280 290 300
MELGGKSPLI IADDADLDLA ADIAMMANFY SSGQVCTNGT RVFVPAKQKA
310 320 330 340 350
EFEHKILERV GRIRPGDLFA DDTNFGPLVS FPHRDNVLRY IESGKREGAR
360 370 380 390 400
LLCGGEALKG DGFDNGAWVA PTVFTDCSDE MTIVREEIFG PVMSILSYTD
410 420 430 440 450
EAEVIRRANA TEYGLAAGVV TPNLNRAHRL IHQLEAGICW INSWGESPAE
460 470 480 490
MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ VEMGKFQSIF
Length:490
Mass (Da):52,860
Last modified:November 25, 2008 - v1
Checksum:i65103D3653F15FF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000964 Genomic DNA. Translation: ACI10905.1.
RefSeqiWP_012542501.1. NC_011283.1.
YP_002239798.1. NC_011283.1.

Genome annotation databases

EnsemblBacteriaiACI10905; ACI10905; KPK_3994.
KEGGikpe:KPK_3994.
PATRICi20441266. VBIKlePne121904_3986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000964 Genomic DNA. Translation: ACI10905.1.
RefSeqiWP_012542501.1. NC_011283.1.
YP_002239798.1. NC_011283.1.

3D structure databases

ProteinModelPortaliB5Y007.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACI10905; ACI10905; KPK_3994.
KEGGikpe:KPK_3994.
PATRICi20441266. VBIKlePne121904_3986.

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiVGGYKES.
OrthoDBiEOG6BS8QW.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BioCyciKPNE507522:GI0B-3995-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 genome sequence of the N2-fixing broad host range endophyte Klebsiella pneumoniae 342 and virulence predictions verified in mice."
    Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., Methe B.A.
    PLoS Genet. 4:E1000141-E1000141(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 342.

Entry informationi

Entry nameiBETB_KLEP3
AccessioniPrimary (citable) accession number: B5Y007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: June 24, 2015
This is version 48 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.