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P17202

- BADH_SPIOL

UniProt

P17202 - BADH_SPIOL

Protein

Betaine aldehyde dehydrogenase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei159 – 1591Transition state stabilizerBy similarity
    Active sitei257 – 2571Proton acceptorPROSITE-ProRule annotation
    Active sitei291 – 2911NucleophilePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi235 – 2406NADBy similarity

    GO - Molecular functioni

    1. betaine-aldehyde dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. glycine betaine biosynthetic process from choline Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    UniPathwayiUPA00529; UER00386.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Betaine aldehyde dehydrogenase, chloroplastic (EC:1.2.1.8)
    Short name:
    BADH
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 77ChloroplastSequence Analysis
    Chaini8 – 497490Betaine aldehyde dehydrogenase, chloroplasticPRO_0000007182Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Blocked amino end (Arg)

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    497
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 123
    Beta strandi15 – 173
    Beta strandi24 – 285
    Turni30 – 323
    Beta strandi35 – 406
    Helixi44 – 5916
    Turni61 – 633
    Beta strandi64 – 663
    Helixi68 – 8417
    Helixi86 – 9712
    Helixi101 – 12525
    Turni126 – 1305
    Beta strandi140 – 1489
    Beta strandi150 – 1556
    Beta strandi158 – 1603
    Helixi161 – 17515
    Beta strandi178 – 1825
    Helixi189 – 20113
    Beta strandi207 – 2104
    Helixi215 – 22410
    Beta strandi230 – 2356
    Helixi237 – 24812
    Turni249 – 2513
    Beta strandi254 – 2574
    Beta strandi263 – 2664
    Beta strandi268 – 2703
    Helixi272 – 28413
    Helixi285 – 2884
    Beta strandi296 – 3005
    Helixi301 – 31616
    Helixi336 – 35217
    Beta strandi368 – 3703
    Beta strandi375 – 3795
    Helixi385 – 3884
    Beta strandi393 – 40311
    Helixi404 – 4118
    Beta strandi418 – 4236
    Helixi427 – 43610
    Beta strandi439 – 4468
    Helixi460 – 4623
    Turni469 – 4713
    Helixi472 – 4765
    Beta strandi477 – 4859

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A0MX-ray2.30A/B/C/D1-496[»]
    ProteinModelPortaliP17202.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 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.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17202-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFPIPARQL FIDGEWREPI KKNRIPVINP STEEIIGDIP AATAEDVEVA    50
    VVAARRAFRR NNWSATSGAH RATYLRAIAA KITEKKDHFV KLETIDSGKP 100
    FDEAVLDIDD VASCFEYFAG QAEALDGKQK APVTLPMERF KSHVLRQPLG 150
    VVGLISPWNY PLLMATWKIA PALAAGCTAV LKPSELASVT CLEFGEVCNE 200
    VGLPPGVLNI LTGLGPDAGA PLVSHPDVDK IAFTGSSATG SKVMASAAQL 250
    VKPVTLELGG KSPIVVFEDV DIDKVVEWTI FGCFWTNGQI CSATSRLLVH 300
    ESIAAEFVDK LVKWTKNIKI SDPFEEGCRL GPVISKGQYD KIMKFISTAK 350
    SEGATILYGG SRPEHLKKGY YIEPTIVTDI STSMQIWKEE VFGPVLCVKT 400
    FSSEDEAIAL ANDTEYGLAA AVFSNDLERC ERITKALEVG AVWVNCSQPC 450
    FVQAPWGGIK RSGFGRELGE WGIQNYLNIK QVTQDISDEP WGWYKSP 497
    Length:497
    Mass (Da):54,270
    Last modified:November 1, 1990 - v1
    Checksum:i55088240E635B22F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti424 – 4241S → F in AAB41696. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31480 mRNA. Translation: AAA34025.1.
    U69142 Genomic DNA. Translation: AAB41696.1.
    PIRiA35994.
    T51173.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31480 mRNA. Translation: AAA34025.1 .
    U69142 Genomic DNA. Translation: AAB41696.1 .
    PIRi A35994.
    T51173.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A0M X-ray 2.30 A/B/C/D 1-496 [» ]
    ProteinModelPortali P17202.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00529 ; UER00386 .

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    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.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought."
      Weretilnyk E.A., Hanson A.D.
      Proc. Natl. Acad. Sci. U.S.A. 87:2745-2749(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Strain: cv. Savoy hybrid 612.
    2. Shu W., Ai W., Chen S.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiBADH_SPIOL
    AccessioniPrimary (citable) accession number: P17202
    Secondary accession number(s): P93555
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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