Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9ZPI6 (AIM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. 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
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:AIM1
Ordered Locus Names:At4g29010
ORF Names:F19B15.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.5 Ref.6

Catalytic activity

(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.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subcellular location

Peroxisome Probable.

Tissue specificity

Widely expressed. Ref.1

Domain

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

Disruption phenotype

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

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=115 µM for crotonyl-CoA Ref.1

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   LigandNAD
   Molecular functionIsomerase
Lyase
Oxidoreductase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from sequence or structural similarity Ref.1. Source: TAIR

flower development

Inferred from mutant phenotype Ref.1. Source: TAIR

jasmonic acid biosynthetic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentcell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209. Source: TAIR

peroxisome

Inferred from direct assay PubMed 17951448. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

   Molecular_function3-hydroxyacyl-CoA dehydratase activity

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

3-hydroxyacyl-CoA dehydrogenase activity

Inferred from direct assay Ref.6. Source: UniProtKB

3-hydroxybutyryl-CoA epimerase activity

Inferred from electronic annotation. Source: EC

coenzyme binding

Inferred from electronic annotation. Source: InterPro

dodecenoyl-CoA delta-isomerase activity

Inferred from electronic annotation. Source: EC

enoyl-CoA hydratase activity

Inferred from direct assay Ref.6. Source: UniProtKB

mRNA binding

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
PRO_0000401372

Sites

Active site1161Nucleophile Potential
Active site1361Proton acceptor Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZPI6 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F72FB3252B2216CF

FASTA72177,858
        10         20         30         40         50         60 
MAKKIGVTME VGNDGVAVIT ISNPPVNSLA SPIISGLKEK FRDANQRNDV KAIVLIGNNG 

        70         80         90        100        110        120 
RFSGGFDINV FQQVHKTGDL SLMPEVSVEL VCNLMEDSRK PVVAAVEGLA LGGGLELAMA 

       130        140        150        160        170        180 
CHARVAAPKA QLGLPELTLG VIPGFGGTQR LPRLVGLAKA TDMILLSKSI SSEEGHKLGL 

       190        200        210        220        230        240 
IDALVPPGDV LSTSRKWALD IAEGRKPFLQ SLHRTDKIGS LSEARAILKN SRQLAKKIAP 

       250        260        270        280        290        300 
NMPQHHACIE VIEEGIIHGG YSGVLKEAEV FKQLVLSDTA KGLVHVFFAQ RATSKVPNVT 

       310        320        330        340        350        360 
DVGLKPRPIK KVAVIGGGLM GSGIATALLL SNIRVVLKEI NSEFLMKGIK SVEANMKSLV 

       370        380        390        400        410        420 
SRGKLTQDKA GKALSLFKGV LDYTEFNDVD MVIEAVIENI QLKQNIFKEI EKVCSPHCIL 

       430        440        450        460        470        480 
ASNTSTIDLD VIGEKTNSKD RIVGAHFFSP AHLMPLLEIV RSKNTSAQVI LDLMAVGKAI 

       490        500        510        520        530        540 
KKVPVVVGNC IGFAVNRTFF PYSQAAHMLA NLGVDLFRID SVITSFGLPL GPFQLGDLAG 

       550        560        570        580        590        600 
HGIGLAVGPI YAKVYGDRMF RSPMTELLLK SGRNGKINGR GYYIYEKGSK PKPDPSVLSI 

       610        620        630        640        650        660 
VEKSRKLTNI MPGGKPISVT DKEIVEMILF PVVNEACRVL DEGVVIRASD LDIASVLGMS 

       670        680        690        700        710        720 
FPSYRGGIVF WADTVGPKYI YERLKKLSET YGSFFKPSRY LEERAMNGML LSESKSSRSK 


L

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00545226.
PIRT08956.
RefSeqNP_194630.1. NM_119045.4.
UniGeneAt.3404.
At.48915.

3D structure databases

HSSPHSSP built from PDB template 3HDH based on UniProtKB P00348.
ProteinModelPortalQ9ZPI6.
SMRQ9ZPI6. Positions 9-712.
ModBaseSearch...

Proteomic databases

PaxDbQ9ZPI6.
PRIDEQ9ZPI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G29010.1; AT4G29010.1; AT4G29010.
GeneID829022.
KEGGath:AT4G29010.

Organism-specific databases

TAIRAt4g29010.

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261347.
InParanoidQ9ZPI6.
KOK10527.
OMANYEAQVK.
PhylomeDBQ9ZPI6.
ProtClustDBCLSN2916032.

Enzyme and pathway databases

BioCycMetaCyc:AT4G29010-MONOMER.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ9ZPI6.
GenevestigatorQ9ZPI6.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 2 hits.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAIM1_ARATH
AccessionPrimary (citable) accession number: Q9ZPI6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents