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Q9HTJ1

- BETB_PSEAE

UniProt

Q9HTJ1 - BETB_PSEAE

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Protein
NAD/NADP-dependent betaine aldehyde dehydrogenase
Gene
betB, PA5373
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - 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.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 potassium ions per subunit.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Potassium 1
Metal bindingi27 – 271Potassium 1; via carbonyl oxygen
Metal bindingi93 – 931Potassium 1
Active sitei162 – 1621Charge relay system1 Publication
Metal bindingi180 – 1801Potassium 1; via carbonyl oxygen
Binding sitei209 – 2091NAD/NADP; via amide nitrogen
Metal bindingi246 – 2461Potassium 2; via carbonyl oxygen
Sitei248 – 2481Seems to be a necessary countercharge to the potassium cations
Active sitei252 – 2521Proton acceptor1 Publication
Binding sitei286 – 2861NAD/NADP
Binding sitei387 – 3871NAD/NADP
Metal bindingi457 – 4571Potassium 2; via carbonyl oxygen
Metal bindingi460 – 4601Potassium 2; via carbonyl oxygen
Active sitei464 – 4641Charge relay system1 Publication

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

  1. betaine-aldehyde dehydrogenase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. glycine betaine biosynthetic process from choline Source: UniProtKB-HAMAP
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 dehydrogenase (EC:1.2.1.8)
Short name:
BADH
Gene namesi
Name:betB
Ordered Locus Names:PA5373
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA5373.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490NAD/NADP-dependent betaine aldehyde dehydrogenaseUniRule annotation
PRO_0000056546Add
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.3 Publications

Protein-protein interaction databases

STRINGi208964.PA5373.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165
Beta strandi19 – 213
Beta strandi23 – 275
Turni29 – 313
Beta strandi34 – 396
Helixi43 – 6220
Helixi65 – 8117
Helixi83 – 9412
Helixi98 – 1014
Turni102 – 1043
Helixi105 – 11915
Helixi120 – 1223
Beta strandi125 – 1317
Beta strandi134 – 1429
Beta strandi144 – 1496
Beta strandi152 – 1543
Helixi155 – 16814
Beta strandi172 – 1765
Helixi183 – 19513
Beta strandi201 – 2044
Turni209 – 2113
Helixi212 – 2187
Beta strandi224 – 2296
Helixi231 – 24515
Beta strandi248 – 2525
Beta strandi258 – 2614
Helixi267 – 27913
Helixi280 – 2834
Beta strandi291 – 2955
Helixi296 – 2983
Helixi299 – 31113
Helixi331 – 34616
Beta strandi350 – 3534
Turni360 – 3623
Helixi363 – 3653
Beta strandi372 – 3765
Helixi382 – 3854
Beta strandi390 – 39910
Helixi401 – 4099
Beta strandi415 – 4206
Helixi424 – 43310
Beta strandi437 – 4426
Helixi457 – 4593
Beta strandi460 – 4623
Helixi466 – 4716
Beta strandi474 – 4829

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9HTJ1.
SMRiQ9HTJ1. Positions 2-490.

Miscellaneous databases

EvolutionaryTraceiQ9HTJ1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
KOiK00130.
OMAiCTDEMTI.
OrthoDBiEOG6BS8QW.
PhylomeDBiQ9HTJ1.

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.

Q9HTJ1-1 [UniParc]FASTAAdd to Basket

« Hide

MARFEEQKLY IGGRYVEASS GATFETINPA NGEVLAKVQR ASREDVERAV    50
QSAVEGQKVW AAMTAMQRSR ILRRAVDILR ERNDELAALE TLDTGKPLAE 100
TRSVDIVTGA DVLEYYAGLV PAIEGEQIPL RETSFVYTRR EPLGVVAGIG 150
AWNYPVQIAL WKSAPALAAG NAMIFKPSEV TPLTALKLAE IYTEAGVPDG 200
VFNVLTGSGR EVGQWLTEHP LIEKISFTGG TSTGKKVMAS ASSSSLKEVT 250
MELGGKSPLI IFPDADLDRA ADIAVMANFF SSGQVCTNGT RVFIHRSQQA 300
RFEAKVLERV QRIRLGDPQD ENTNFGPLVS FPHMESVLGY IESGKAQKAR 350
LLCGGERVTD GAFGKGAYVA PTVFTDCRDD MTIVREEIFG PVMSILVYDD 400
EDEAIRRAND TEYGLAAGVV TQDLARAHRA IHRLEAGICW INTWGESPAE 450
MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ VELGDYASVF 490
Length:490
Mass (Da):53,332
Last modified:March 1, 2001 - v1
Checksum:iF48249A085E3A970
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG08758.1.
PIRiF82973.
RefSeqiNP_254060.1. NC_002516.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG08758.1 .
PIRi F82973.
RefSeqi NP_254060.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WME X-ray 2.10 A/B/C/D/E/F/G/H 1-490 [» ]
2WOX X-ray 2.30 A/B/C/D 2-490 [» ]
2XDR X-ray 2.30 A/B/C/D 2-490 [» ]
3ZQA X-ray 2.45 A/B/C/D 1-490 [» ]
ProteinModelPortali Q9HTJ1.
SMRi Q9HTJ1. Positions 2-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA5373.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG08758 ; AAG08758 ; PA5373 .
GeneIDi 881619.
KEGGi pae:PA5373.
PATRICi 19845617. VBIPseAer58763_5630.

Organism-specific databases

PseudoCAPi PA5373.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271505.
KOi K00130.
OMAi CTDEMTI.
OrthoDBi EOG6BS8QW.
PhylomeDBi Q9HTJ1.

Enzyme and pathway databases

UniPathwayi UPA00529 ; UER00386 .
BRENDAi 1.2.1.8. 5087.

Miscellaneous databases

EvolutionaryTracei Q9HTJ1.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
HAMAPi MF_00804. BADH.
InterProi 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.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01804. BADH. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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: July 9, 2014
This is version 92 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

External Data

Dasty 3

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