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Q9HTJ1 (BETB_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD/NADP-dependent betaine aldehyde dehydrogenase

Short name=BADH
EC=1.2.1.8
Gene names
Name:betB
Ordered Locus Names:PA5373
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. Ref.4

Catalytic activity

Betaine aldehyde + NAD+ + H2O = betaine + NADH. HAMAP-Rule MF_00804

Cofactor

Binds 2 potassium ions per subunit. Ref.2 Ref.4

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. HAMAP-Rule MF_00804

Subunit structure

Dimer of dimers. Ref.2 Ref.3 Ref.4

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490NAD/NADP-dependent betaine aldehyde dehydrogenase HAMAP-Rule MF_00804
PRO_0000056546

Regions

Nucleotide binding150 – 1534NAD/NADP HAMAP-Rule MF_00804
Nucleotide binding176 – 1794NAD/NADP HAMAP-Rule MF_00804
Nucleotide binding229 – 2346NAD/NADP HAMAP-Rule MF_00804

Sites

Active site1621Charge relay system Ref.2
Active site2521Proton acceptor Ref.2
Active site4641Charge relay system Ref.2
Metal binding261Potassium 1
Metal binding271Potassium 1; via carbonyl oxygen
Metal binding931Potassium 1
Metal binding1801Potassium 1; via carbonyl oxygen
Metal binding2461Potassium 2; via carbonyl oxygen
Metal binding4571Potassium 2; via carbonyl oxygen
Metal binding4601Potassium 2; via carbonyl oxygen
Binding site2091NAD/NADP; via amide nitrogen
Binding site2861NAD/NADP
Binding site3871NAD/NADP
Site2481Seems to be a necessary countercharge to the potassium cations

Amino acid modifications

Modified residue2861Cysteine sulfenic acid (-SOH) HAMAP-Rule MF_00804

Secondary structure

................................................................................... 490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9HTJ1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F48249A085E3A970

FASTA49053,332
        10         20         30         40         50         60 
MARFEEQKLY IGGRYVEASS GATFETINPA NGEVLAKVQR ASREDVERAV QSAVEGQKVW 

        70         80         90        100        110        120 
AAMTAMQRSR ILRRAVDILR ERNDELAALE TLDTGKPLAE TRSVDIVTGA DVLEYYAGLV 

       130        140        150        160        170        180 
PAIEGEQIPL RETSFVYTRR EPLGVVAGIG AWNYPVQIAL WKSAPALAAG NAMIFKPSEV 

       190        200        210        220        230        240 
TPLTALKLAE IYTEAGVPDG VFNVLTGSGR EVGQWLTEHP LIEKISFTGG TSTGKKVMAS 

       250        260        270        280        290        300 
ASSSSLKEVT MELGGKSPLI IFPDADLDRA ADIAVMANFF SSGQVCTNGT RVFIHRSQQA 

       310        320        330        340        350        360 
RFEAKVLERV QRIRLGDPQD ENTNFGPLVS FPHMESVLGY IESGKAQKAR LLCGGERVTD 

       370        380        390        400        410        420 
GAFGKGAYVA PTVFTDCRDD MTIVREEIFG PVMSILVYDD EDEAIRRAND TEYGLAAGVV 

       430        440        450        460        470        480 
TQDLARAHRA IHRLEAGICW INTWGESPAE MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ 

       490 
VELGDYASVF 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"The crystal structure of a ternary complex of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa Provides new insight into the reaction mechanism and shows a novel binding mode of the 2'-phosphate of NADP+ and a novel cation binding site."
Gonzalez-Segura L., Rudino-Pinera E., Munoz-Clares R.A., Horjales E.
J. Mol. Biol. 385:542-557(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP AND POTASSIUM IONS, ACTIVE SITE, REACTION MECHANISM, COFACTOR, SUBUNIT.
[3]"A novel cysteine-NADPH covalent adduct in Pseudomonas aeruginosa betaine aldehyde dehydrogenase suggests important roles for the reduced nucleotide in the reaction mechanism."
Diaz-Sanchez A.G., Gonzalez-Segura L., Rudino-Pinera E., Lira-Rocha A., Munoz-Clares R.A.
Submitted (MAY-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-490 IN COMPLEX WITH NADP AND POTASSIUM IONS, SUBUNIT.
[4]"Novel NADPH-cysteine covalent adduct found in the active site of an aldehyde dehydrogenase."
Diaz-Sanchez A.G., Gonzalez-Segura L., Rudino-Pinera E., Lira-Rocha A., Torres-Larios A., Munoz-Clares R.A.
Biochem. J. 439:443-452(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-490 OF WILD-TYPE AND MUTANT ALA-286 IN COMPLEX WITH WITH NADP AND POTASSIUM IONS, FUNCTION, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG08758.1.
PIRF82973.
RefSeqNP_254060.1. NC_002516.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9HTJ1.
SMRQ9HTJ1. Positions 2-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA5373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID881619.
KEGGpae:PA5373.
PATRIC19845617. VBIPseAer58763_5630.

Organism-specific databases

PseudoCAPPA5373.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
KOK00130.
OMAAHRTIHR.
OrthoDBEOG6BS8QW.
ProtClustDBPRK13252.

Enzyme and pathway databases

BRENDA1.2.1.8. 5087.
UniPathwayUPA00529; UER00386.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPMF_00804. BADH.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR011264. BADH.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01804. BADH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9HTJ1.

Entry information

Entry nameBETB_PSEAE
AccessionPrimary (citable) accession number: Q9HTJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways