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Q9HTJ1

- BETB_PSEAE

UniProt

Q9HTJ1 - BETB_PSEAE

Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

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
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid.1 PublicationUniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 2 potassium ions per subunit.2 PublicationsUniRule annotation

    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 PublicationUniRule annotation
    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 PublicationUniRule annotation
    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 PublicationUniRule annotation

    Regions

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

    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

    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 / 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 dehydrogenasePRO_0000056546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei286 – 2861Cysteine sulfenic acid (-SOH)1 PublicationUniRule annotation

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Dimer of dimers.3 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi208964.PA5373.

    Structurei

    Secondary structure

    1
    490
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HTJ1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.UniRule annotation

    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

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    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

    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, OXIDATION AT CYS-286, 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: October 1, 2014
    This is version 93 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