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Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation1 Publication

Catalytic activityi

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

Cofactori

K+UniRule annotation2 PublicationsNote: Binds 2 potassium ions per subunit.UniRule annotation2 Publications

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 bindingi26Potassium 11
Metal bindingi27Potassium 1; via carbonyl oxygen1
Metal bindingi93Potassium 11
Active sitei162Charge relay systemUniRule annotation1 Publication1
Metal bindingi180Potassium 1; via carbonyl oxygen1
Binding sitei209NAD/NADP; via amide nitrogen1
Metal bindingi246Potassium 2; via carbonyl oxygen1
Sitei248Seems to be a necessary countercharge to the potassium cations1
Active sitei252Proton acceptorUniRule annotation1 Publication1
Binding sitei286NAD/NADP1
Binding sitei387NAD/NADP1
Metal bindingi457Potassium 2; via carbonyl oxygen1
Metal bindingi460Potassium 2; via carbonyl oxygen1
Active sitei464Charge relay systemUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi150 – 153NAD/NADP4
Nucleotide bindingi176 – 179NAD/NADP4
Nucleotide bindingi229 – 234NAD/NADP6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Potassium

Enzyme and pathway databases

BRENDAi1.2.1.8. 5087.
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:PA5373
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA5373.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000565461 – 490NAD/NADP-dependent betaine aldehyde dehydrogenaseAdd BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei286Cysteine sulfenic acid (-SOH)UniRule annotation1 Publication1

Keywords - PTMi

Oxidation

Proteomic databases

PaxDbiQ9HTJ1.
PRIDEiQ9HTJ1.

Interactioni

Subunit structurei

Dimer of dimers.UniRule annotation3 Publications

Protein-protein interaction databases

STRINGi208964.PA5373.

Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 16Combined sources5
Beta strandi19 – 21Combined sources3
Beta strandi23 – 27Combined sources5
Turni29 – 31Combined sources3
Beta strandi34 – 39Combined sources6
Helixi43 – 62Combined sources20
Helixi65 – 81Combined sources17
Helixi83 – 94Combined sources12
Helixi98 – 101Combined sources4
Turni102 – 104Combined sources3
Helixi105 – 119Combined sources15
Helixi120 – 122Combined sources3
Beta strandi125 – 131Combined sources7
Beta strandi134 – 142Combined sources9
Beta strandi144 – 149Combined sources6
Beta strandi152 – 154Combined sources3
Helixi155 – 168Combined sources14
Beta strandi172 – 176Combined sources5
Helixi183 – 195Combined sources13
Beta strandi201 – 204Combined sources4
Turni209 – 211Combined sources3
Helixi212 – 218Combined sources7
Beta strandi224 – 229Combined sources6
Helixi231 – 245Combined sources15
Beta strandi248 – 252Combined sources5
Beta strandi258 – 261Combined sources4
Helixi267 – 279Combined sources13
Helixi280 – 283Combined sources4
Beta strandi291 – 295Combined sources5
Helixi296 – 298Combined sources3
Helixi299 – 311Combined sources13
Helixi331 – 346Combined sources16
Beta strandi350 – 353Combined sources4
Turni360 – 362Combined sources3
Helixi363 – 365Combined sources3
Beta strandi372 – 376Combined sources5
Helixi382 – 385Combined sources4
Beta strandi390 – 400Combined sources11
Helixi401 – 409Combined sources9
Beta strandi415 – 420Combined sources6
Helixi424 – 433Combined sources10
Beta strandi437 – 442Combined sources6
Helixi457 – 459Combined sources3
Beta strandi460 – 462Combined sources3
Helixi466 – 471Combined sources6
Beta strandi474 – 482Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WMEX-ray2.10A/B/C/D/E/F/G/H1-490[»]
2WOXX-ray2.30A/B/C/D2-490[»]
2XDRX-ray2.30A/B/C/D2-490[»]
3ZQAX-ray2.45A/B/C/D1-490[»]
4CAZX-ray2.55A/B1-490[»]
4CBBX-ray1.80A/B/C/D/E/F/G/H2-490[»]
ProteinModelPortaliQ9HTJ1.
SMRiQ9HTJ1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HTJ1.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiQ9HTJ1.
KOiK00130.
OMAiTKSVYVG.
PhylomeDBiQ9HTJ1.

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.

Q9HTJ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARFEEQKLY IGGRYVEASS GATFETINPA NGEVLAKVQR ASREDVERAV
60 70 80 90 100
QSAVEGQKVW AAMTAMQRSR ILRRAVDILR ERNDELAALE TLDTGKPLAE
110 120 130 140 150
TRSVDIVTGA DVLEYYAGLV PAIEGEQIPL RETSFVYTRR EPLGVVAGIG
160 170 180 190 200
AWNYPVQIAL WKSAPALAAG NAMIFKPSEV TPLTALKLAE IYTEAGVPDG
210 220 230 240 250
VFNVLTGSGR EVGQWLTEHP LIEKISFTGG TSTGKKVMAS ASSSSLKEVT
260 270 280 290 300
MELGGKSPLI IFPDADLDRA ADIAVMANFF SSGQVCTNGT RVFIHRSQQA
310 320 330 340 350
RFEAKVLERV QRIRLGDPQD ENTNFGPLVS FPHMESVLGY IESGKAQKAR
360 370 380 390 400
LLCGGERVTD GAFGKGAYVA PTVFTDCRDD MTIVREEIFG PVMSILVYDD
410 420 430 440 450
EDEAIRRAND TEYGLAAGVV TQDLARAHRA IHRLEAGICW INTWGESPAE
460 470 480 490
MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ VELGDYASVF
Length:490
Mass (Da):53,332
Last modified:March 1, 2001 - v1
Checksum:iF48249A085E3A970
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08758.1.
PIRiF82973.
RefSeqiNP_254060.1. NC_002516.2.
WP_003114436.1. NZ_ASJY01000827.1.

Genome annotation databases

EnsemblBacteriaiAAG08758; AAG08758; PA5373.
GeneIDi881619.
KEGGipae:PA5373.
PATRICi19845617. VBIPseAer58763_5630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08758.1.
PIRiF82973.
RefSeqiNP_254060.1. NC_002516.2.
WP_003114436.1. NZ_ASJY01000827.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WMEX-ray2.10A/B/C/D/E/F/G/H1-490[»]
2WOXX-ray2.30A/B/C/D2-490[»]
2XDRX-ray2.30A/B/C/D2-490[»]
3ZQAX-ray2.45A/B/C/D1-490[»]
4CAZX-ray2.55A/B1-490[»]
4CBBX-ray1.80A/B/C/D/E/F/G/H2-490[»]
ProteinModelPortaliQ9HTJ1.
SMRiQ9HTJ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA5373.

Proteomic databases

PaxDbiQ9HTJ1.
PRIDEiQ9HTJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08758; AAG08758; PA5373.
GeneIDi881619.
KEGGipae:PA5373.
PATRICi19845617. VBIPseAer58763_5630.

Organism-specific databases

PseudoCAPiPA5373.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiQ9HTJ1.
KOiK00130.
OMAiTKSVYVG.
PhylomeDBiQ9HTJ1.

Enzyme and pathway databases

UniPathwayiUPA00529; UER00386.
BRENDAi1.2.1.8. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9HTJ1.

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_PSEAE
AccessioniPrimary (citable) accession number: Q9HTJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 106 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.