(data stored in SCRATCH zone)

HOGENOM: ARATH_4_PE3358

ID   ARATH_4_PE3358                       STANDARD;      PRT;   447 AA.
AC   ARATH_4_PE3358; Q9STR4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 7; Short=ACC
DE   synthase 7; EC=4.4.1 14;AltName: Full=S-adenosyl-L-methionine
DE   methylthioadenosine-lyase 7; (ARATH_4.PE3358).
GN   Name=ACS7; OrderedLocusNames=At4g26200; ORFNames=T25K17.10;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_4.PE3358.
CC       Arabidopsis thaliana chromosome 4 TAIR10 full sequence 1..18585056
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:1A17_ARATH
CC   -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes
CC       catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-
CC       aminocyclopropane-1-carboxylate (ACC), a direct precursor of
CC       ethylene.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane-
CC       1-carboxylate + methylthioadenosine.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.3 uM for AdoMet;
CC         Vmax=13.5 uM/h/mg enzyme;
CC       pH dependence:
CC         Optimum pH is 8;
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-
CC       adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step
CC       1/2.
CC   -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of
CC       heterodimerization with other ACS enzymes is however unsure (By
CC       similarity). Interacts with XBAT32.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-2356842, EBI-2356842;
CC       Q43309:ACS4; NbExp=4; IntAct=EBI-2356842, EBI-2436015;
CC   -!- TISSUE SPECIFICITY: Expressed in roots.
CC   -!- INDUCTION: By cycloheximide (CHX).
CC   -!- PTM: Ubiquitinated by XBAT32. Ubiquitination probably leads to its
CC       subsequent degradation, thus controlling ethylene production.
CC   -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation
CC       of such stability, play a central role in ethylene biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -!- GENE_FAMILY: HOG000011234 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT4G26200;AT4G26200.1;AT4G26200.1.
DR   EMBL; AF332390; - ;
DR   EMBL; AL049171; - ;
DR   EMBL; AL161564; - ;
DR   UniProtKB/Swiss-Prot; Q9STR4; -.
DR   EMBL; AL049171; CAB38949.1; -; Genomic_DNA.
DR   EMBL; AL161564; CAB79475.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85169.1; -; Genomic_DNA.
DR   EMBL; AF332390; AAG48754.1; -; mRNA.
DR   IPI; IPI00532829; -.
DR   PIR; T06004; T06004.
DR   RefSeq; NP_194350.1; NM_118753.2.
DR   UniGene; At.20362; -.
DR   ProteinModelPortal; Q9STR4; -.
DR   SMR; Q9STR4; 31-441.
DR   IntAct; Q9STR4; 4.
DR   STRING; Q9STR4; -.
DR   PRIDE; Q9STR4; -.
DR   EnsemblPlants; AT4G26200.1; AT4G26200.1; AT4G26200.
DR   GeneID; 828726; -.
DR   GenomeReviews; CT486007_GR; AT4G26200.
DR   KEGG; ath:AT4G26200; -.
DR   NMPDR; fig|3702.1.peg.20541; -.
DR   TAIR; At4g26200; -.
DR   eggNOG; KOG0256; -.
DR   GeneTree; EPGT00070000028140; -.
DR   InParanoid; Q9STR4; -.
DR   OMA; CEAGEAF; -.
DR   PhylomeDB; Q9STR4; -.
DR   ProtClustDB; PLN02607; -.
DR   ArrayExpress; Q9STR4; -.
DR   Genevestigator; Q9STR4; -.
DR   GermOnline; AT4G26200; Arabidopsis thaliana.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IDA:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016769; F:transferase activity, transferring nitrogenous groups; IEA:InterPro.
DR   GO; GO:0009693; P:ethylene biosynthetic process; TAS:TAIR.
DR   GO; GO:0009835; P:ripening; IEA:UniProtKB-KW.
DR   InterPro; IPR001176; ACC_synthase.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   HOGENOMDNA; ARATH_4.PE3358; -.
KW   AT4G26200pg.C_scaffold_1320000031; AT4G26200.1.C_scaffold_1320000031;
KW   AF332390; AL049171; AL161564;
KW   Complete proteome; Ethylene biosynthesis; Fruit ripening; Lyase;
KW   Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW   Ubl conjugation.
SQ   SEQUENCE   447 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGLPLMMERS SNNNNVELSR VAVSDTHGED SPYFAGWKAY DENPYDESHN PSGVIQMGLA
     ENQVSFDLLE TYLEKKNPEG SMWGSKGAPG FRENALFQDY HGLKTFRQAM ASFMEQIRGG
     KARFDPDRIV LTAGATAANE LLTFILADPN DALLVPTPYY PGFDRDLRWR TGVKIVPIHC
     DSSNHFQITP EALESAYQTA RDANIRVRGV LITNPSNPLG ATVQKKVLED LLDFCVRKNI
     HLVSDEIYSG SVFHASEFTS VAEIVENIDD VSVKERVHIV YSLSKDLGLP GFRVGTIYSY
     NDNVVRTARR MSSFTLVSSQ TQHMLASMLS DEEFTEKYIR INRERLRRRY DTIVEGLKKA
     GIECLKGNAG LFCWMNLGFL LEKKTKDGEL QLWDVILKEL NLNISPGSSC HCSEVGWFRV
     CFANMSENTL EIALKRIHEF MDRRRRF
//

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