ID V7B5N5_PHAVU Unreviewed; 483 AA.
AC V7B5N5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase {ECO:0000256|ARBA:ARBA00042673};
GN ORFNames=PHAVU_008G058400g {ECO:0000313|EMBL:ESW11776.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW11776.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:21744,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:58360,
CC ChEBI:CHEBI:59789; EC=4.4.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00036967};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00037888}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CM002295; ESW11776.1; -; Genomic_DNA.
DR RefSeq; XP_007139782.1; XM_007139720.1.
DR AlphaFoldDB; V7B5N5; -.
DR STRING; 3885.V7B5N5; -.
DR EnsemblPlants; ESW11776; ESW11776; PHAVU_008G058400g.
DR GeneID; 18621977; -.
DR Gramene; ESW11776; ESW11776; PHAVU_008G058400g.
DR KEGG; pvu:PHAVU_008G058400g; -.
DR eggNOG; KOG0256; Eukaryota.
DR OMA; VMSPHMM; -.
DR OrthoDB; 1328656at2759; -.
DR PhylomeDB; V7B5N5; -.
DR Proteomes; UP000000226; Chromosome 8.
DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43795:SF74; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 2; 1.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Ethylene biosynthesis {ECO:0000256|ARBA:ARBA00022666};
KW Fruit ripening {ECO:0000256|ARBA:ARBA00033478};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 48..428
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 464..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 54565 MW; EA583356321A0E07 CRC64;
MALKNTSFQL LSEIATNGNH GENSSYFDGW KAYESDPYHP TENPQGVIQM GLAENPLSLD
LIQEWILKNP KGSICTPEGV KWFKYIANFQ DYHGLPEFRN GLANYMSKVR GGRVRFDPDR
IVMGGGTTGA NELIMFCLAN GGDAFLVPSP YYPAFARDLC WRTKARLIPV ECYSINNFMV
TREALEEAYN KAIDANINVK GLIITNPSNP LGTTMDKETL KSIVGFINEK NIHLVCDEIY
AGTVFRGPRF VSVSEVMQEL EHCNKDLIHI VYSLSKDLGI PGLRVGIVYS YNDEVVNQGR
KMSSFGLVST QTQFFVAALL SDDEFVERFL AESARRLAAR YNHFTKELEK VNITCLPSNA
GLFFWMNLRG LLKEKTFEGE MMLWHVIINE VKLNVSPGSA FNCSEPGWYR VCFANMDDET
VEVALKRIRA FVGKETGKPV ELKRWKSNLR LSFSSRRFDE NVMSPHMLSP HSPMPHSPLV
RAT
//
