Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A9AN00

- BETB_BURM1

UniProt

A9AN00 - BETB_BURM1

Protein

NAD/NADP-dependent betaine aldehyde dehydrogenase

Gene

betB

Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 2 potassium ions per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi26 – 261Potassium 1UniRule 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 bindingi245 – 2451Potassium 2; via carbonyl oxygenUniRule annotation
    Sitei247 – 2471Seems to be a necessary countercharge to the potassium cationsUniRule annotation
    Active sitei251 – 2511Proton acceptorUniRule annotation
    Binding sitei285 – 2851NAD/NADPUniRule annotation
    Binding sitei386 – 3861NAD/NADPUniRule annotation
    Metal bindingi456 – 4561Potassium 2; via carbonyl oxygenUniRule annotation
    Metal bindingi459 – 4591Potassium 2; via carbonyl oxygenUniRule annotation
    Active sitei463 – 4631Charge relay systemUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi150 – 1534NAD/NADPUniRule annotation
    Nucleotide bindingi176 – 1794NAD/NADPUniRule annotation
    Nucleotide bindingi228 – 2336NAD/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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, NADP, Potassium

    Enzyme and pathway databases

    BioCyciBMUL395019:GIYO-4977-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:Bmul_3537, BMULJ_04980
    OrganismiBurkholderia multivorans (strain ATCC 17616 / 249)
    Taxonomic identifieri395019 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
    ProteomesiUP000007064: Chromosome 2, UP000008815: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 489489NAD/NADP-dependent betaine aldehyde dehydrogenasePRO_1000133943Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei285 – 2851Cysteine sulfenic acid (-SOH)UniRule annotation

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Dimer of dimers.UniRule annotation

    Protein-protein interaction databases

    STRINGi395019.Bmul_3537.

    Structurei

    3D structure databases

    ProteinModelPortaliA9AN00.
    SMRiA9AN00. Positions 8-489.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271505.
    KOiK00130.
    OMAiCTDEMTI.
    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.

    A9AN00-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVYGLQRLY IGGGYVDATS GKTFDTFDPA TGDLLAQVQQ ASAADVDRAI    50
    ASAQEGQREW AAMTAMQRSR ILRRAVELLR ERNDELAALE TRDTGKPIAE 100
    TLAVDIVTGA DVIEYYAGLA TAIEGLQVPL RADSFVYTRR EPLGVCAGIG 150
    AWNYPIQIAC WKTAPALAAG NAMVFKPSEV TPLSALKLAE IYTEAGVPAG 200
    VFNVVQGDGS VGALLTGHPD IAKVSFTGGV ETGKKVMSLA GASSLKEVTM 250
    ELGGKSPLIV FDDADLDRAA DIAVTANFFS SGQVCTNGTR VFVHRSIKDA 300
    FTQKVLERVK RIRVGKPTDA DTNFGPLVSA AQLDKVLGFI ESGKAEGAKL 350
    LAGGTRLTEG HFANGQYVAP TVFGDCRDDM KIVREEIFGP VMSILEFESE 400
    DEVIARANDT HYGLAAGVVT ENLSRAHRTI HRLEAGICWI NTWGESPAEM 450
    PVGGYKQSGV GRENGITTLE HYTRIKSVQV ELGRYNPVF 489
    Length:489
    Mass (Da):52,383
    Last modified:January 15, 2008 - v1
    Checksum:iB0F01435BDD0276C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000869 Genomic DNA. Translation: ABX17221.1.
    AP009386 Genomic DNA. Translation: BAG46826.1.
    RefSeqiYP_001583513.1. NC_010086.1.
    YP_001949362.1. NC_010805.1.

    Genome annotation databases

    EnsemblBacteriaiABX17221; ABX17221; Bmul_3537.
    BAG46826; BAG46826; BMULJ_04980.
    GeneIDi5769934.
    6361994.
    KEGGibmj:BMULJ_04980.
    bmu:Bmul_3537.
    PATRICi19172103. VBIBurMul203716_6087.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000869 Genomic DNA. Translation: ABX17221.1 .
    AP009386 Genomic DNA. Translation: BAG46826.1 .
    RefSeqi YP_001583513.1. NC_010086.1.
    YP_001949362.1. NC_010805.1.

    3D structure databases

    ProteinModelPortali A9AN00.
    SMRi A9AN00. Positions 8-489.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 395019.Bmul_3537.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX17221 ; ABX17221 ; Bmul_3537 .
    BAG46826 ; BAG46826 ; BMULJ_04980 .
    GeneIDi 5769934.
    6361994.
    KEGGi bmj:BMULJ_04980.
    bmu:Bmul_3537.
    PATRICi 19172103. VBIBurMul203716_6087.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00529 ; UER00386 .
    BioCyci BMUL395019:GIYO-4977-MONOMER.

    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. "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC 17616."
      Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.
      Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17616 / 249.
    2. "Complete genome sequence of Burkholderia multivorans ATCC 17616."
      Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 17616 / 249.

    Entry informationi

    Entry nameiBETB_BURM1
    AccessioniPrimary (citable) accession number: A9AN00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    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