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Protein

Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1

Gene

AIM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in peroxisomal fatty acid beta-oxidation. Required for wound-induced jasmonate biosynthesis. Possesses enoyl-CoA hydratase activity against short chain substrates (C4-C6) and 3-hydroxyacyl-CoA dehydrogenase activity against chains of variable sizes (C6-C16).3 Publications

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Kineticsi

  1. KM=115 µM for crotonyl-CoA1 Publication

    Pathway:ifatty acid beta-oxidation

    This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei116 – 1161NucleophileSequence Analysis
    Active sitei136 – 1361Proton acceptorSequence Analysis

    GO - Molecular functioni

    • 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
    • 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-EC
    • dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
    • enoyl-CoA hydratase activity Source: UniProtKB

    GO - Biological processi

    • fatty acid beta-oxidation Source: TAIR
    • flower development Source: TAIR
    • jasmonic acid biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:AT4G29010-MONOMER.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
    Alternative name(s):
    Protein ABNORMAL INFLORESCENCE MERISTEM 1
    Short name:
    AtAIM1
    Including the following 2 domains:
    Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3, EC:5.3.3.8)
    3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
    Gene namesi
    Name:AIM1
    Ordered Locus Names:At4g29010
    ORF Names:F19B15.40
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G29010.

    Subcellular locationi

    GO - Cellular componenti

    • cell wall Source: TAIR
    • chloroplast Source: TAIR
    • peroxisome Source: TAIR
    • plasmodesma Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Disruption phenotypei

    Reduced rosette size, twisted leaves, and abnormal and sterile flowers.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 721721Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1PRO_0000401372Add
    BLAST

    Proteomic databases

    PaxDbiQ9ZPI6.
    PRIDEiQ9ZPI6.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi14309. 1 interaction.
    STRINGi3702.AT4G29010.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZPI6.
    SMRiQ9ZPI6. Positions 9-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The epimerase and isomerase activities are contained in the N-terminal region while the dehydrogenase activity is in the C-terminal region.By similarity

    Sequence similaritiesi

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
    In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261347.
    InParanoidiQ9ZPI6.
    KOiK10527.
    OMAiQIFIDIE.
    PhylomeDBiQ9ZPI6.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ZPI6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAKKIGVTME VGNDGVAVIT ISNPPVNSLA SPIISGLKEK FRDANQRNDV
    60 70 80 90 100
    KAIVLIGNNG RFSGGFDINV FQQVHKTGDL SLMPEVSVEL VCNLMEDSRK
    110 120 130 140 150
    PVVAAVEGLA LGGGLELAMA CHARVAAPKA QLGLPELTLG VIPGFGGTQR
    160 170 180 190 200
    LPRLVGLAKA TDMILLSKSI SSEEGHKLGL IDALVPPGDV LSTSRKWALD
    210 220 230 240 250
    IAEGRKPFLQ SLHRTDKIGS LSEARAILKN SRQLAKKIAP NMPQHHACIE
    260 270 280 290 300
    VIEEGIIHGG YSGVLKEAEV FKQLVLSDTA KGLVHVFFAQ RATSKVPNVT
    310 320 330 340 350
    DVGLKPRPIK KVAVIGGGLM GSGIATALLL SNIRVVLKEI NSEFLMKGIK
    360 370 380 390 400
    SVEANMKSLV SRGKLTQDKA GKALSLFKGV LDYTEFNDVD MVIEAVIENI
    410 420 430 440 450
    QLKQNIFKEI EKVCSPHCIL ASNTSTIDLD VIGEKTNSKD RIVGAHFFSP
    460 470 480 490 500
    AHLMPLLEIV RSKNTSAQVI LDLMAVGKAI KKVPVVVGNC IGFAVNRTFF
    510 520 530 540 550
    PYSQAAHMLA NLGVDLFRID SVITSFGLPL GPFQLGDLAG HGIGLAVGPI
    560 570 580 590 600
    YAKVYGDRMF RSPMTELLLK SGRNGKINGR GYYIYEKGSK PKPDPSVLSI
    610 620 630 640 650
    VEKSRKLTNI MPGGKPISVT DKEIVEMILF PVVNEACRVL DEGVVIRASD
    660 670 680 690 700
    LDIASVLGMS FPSYRGGIVF WADTVGPKYI YERLKKLSET YGSFFKPSRY
    710 720
    LEERAMNGML LSESKSSRSK L
    Length:721
    Mass (Da):77,858
    Last modified:May 1, 1999 - v1
    Checksum:iF72FB3252B2216CF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF123253 Genomic DNA. Translation: AAD18041.1.
    AL078470 Genomic DNA. Translation: CAB43915.1.
    AL161574 Genomic DNA. Translation: CAB79659.1.
    CP002687 Genomic DNA. Translation: AEE85572.1.
    AY059815 mRNA. Translation: AAL24297.1.
    AY072072 mRNA. Translation: AAL59895.1.
    AY096659 mRNA. Translation: AAM20293.1.
    PIRiT08956.
    RefSeqiNP_194630.1. NM_119045.4.
    UniGeneiAt.3404.
    At.48915.

    Genome annotation databases

    EnsemblPlantsiAT4G29010.1; AT4G29010.1; AT4G29010.
    GeneIDi829022.
    KEGGiath:AT4G29010.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF123253 Genomic DNA. Translation: AAD18041.1.
    AL078470 Genomic DNA. Translation: CAB43915.1.
    AL161574 Genomic DNA. Translation: CAB79659.1.
    CP002687 Genomic DNA. Translation: AEE85572.1.
    AY059815 mRNA. Translation: AAL24297.1.
    AY072072 mRNA. Translation: AAL59895.1.
    AY096659 mRNA. Translation: AAM20293.1.
    PIRiT08956.
    RefSeqiNP_194630.1. NM_119045.4.
    UniGeneiAt.3404.
    At.48915.

    3D structure databases

    ProteinModelPortaliQ9ZPI6.
    SMRiQ9ZPI6. Positions 9-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14309. 1 interaction.
    STRINGi3702.AT4G29010.1.

    Proteomic databases

    PaxDbiQ9ZPI6.
    PRIDEiQ9ZPI6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G29010.1; AT4G29010.1; AT4G29010.
    GeneIDi829022.
    KEGGiath:AT4G29010.

    Organism-specific databases

    TAIRiAT4G29010.

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261347.
    InParanoidiQ9ZPI6.
    KOiK10527.
    OMAiQIFIDIE.
    PhylomeDBiQ9ZPI6.

    Enzyme and pathway databases

    UniPathwayiUPA00659.
    BioCyciMetaCyc:AT4G29010-MONOMER.

    Miscellaneous databases

    PROiQ9ZPI6.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR013328. 6PGD_dom_2.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 1 hit.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A defect in beta-oxidation causes abnormal inflorescence development in Arabidopsis."
      Richmond T.A., Bleecker A.B.
      Plant Cell 11:1911-1924(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Jasmonate biosynthesis in Arabidopsis thaliana requires peroxisomal beta-oxidation enzymes--additional proof by properties of pex6 and aim1."
      Delker C., Zolman B.K., Miersch O., Wasternack C.
      Phytochemistry 68:1642-1650(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2."
      Arent S., Christensen C.E., Pye V.E., Noergaard A., Henriksen A.
      J. Biol. Chem. 285:24066-24077(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiAIM1_ARATH
    AccessioniPrimary (citable) accession number: Q9ZPI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: May 1, 1999
    Last modified: July 22, 2015
    This is version 119 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

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.