ID O22335_STELP Unreviewed; 498 AA.
AC O22335;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
OS Stellaria longipes (Longstalk starwort) (Alsine longipes).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Alsineae; Stellaria.
OX NCBI_TaxID=19744 {ECO:0000313|EMBL:AAC49923.1};
RN [1] {ECO:0000313|EMBL:AAC49923.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Prairie {ECO:0000313|EMBL:AAC49923.1};
RX PubMed=9484438; DOI=10.1023/A:1005994118535;
RA Kathiresan A., Nagarathna K.C., Moloney M.M., Reid D.M., Chinnappa C.C.;
RT "Differential regulation of 1-aminocyclopropane-1-carboxylate synthase gene
RT family and its role in phenotypic plasticity in Stellaria longipes.";
RL Plant Mol. Biol. 36:265-274(1998).
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}.
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DR EMBL; AF003981; AAC49923.1; -; mRNA.
DR AlphaFoldDB; O22335; -.
DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43795:SF10; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 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.
PE 2: Evidence at transcript level;
KW Lyase {ECO:0000313|EMBL:AAC49923.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 57..455
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 498 AA; 56409 MW; 0C9A6BC94C71E6E9 CRC64;
MVLPSKNNSE QVLSKMAVNF NSGEDSSYFL GWKAYNKDDN PHFHPYAEIE QNYNGVIQMG
LAENQLSSDL IEEWIKRNPD AAICVEDGIK SIFRALFQDY HGLIEFRQLV ARFMEKVRGG
RVRFDSNLVL TAGATGANET IIFCTDNPGD AFLVPTPYYA AGDRDLKWRT RAEILPICHC
SSNNFKITSK AKEAYEKAQS KYKAKKLDLN VKGLIMTNPS NPLGTTTLDR DTLKKISTFI
DQKNIHLVCD EIYAATVFKA KTVSIADILL DDHVNQDLVH ILYSLSKDLG LPGFRVVIVY
SKDEMVVSAA TKMSSFGLSS GLYIHTVIRL LQRLGECLVL PLSQTQNLLA TMLSDKKFTW
NYIKINRERL KRRYEMIING LKKVGIECLK GNGGLFCWMN LSPFLEKPTK EGELDLWSSI
VNEVKLNISP GSSCHCSNPG WFRVCFANMD ESMAVQLAMQ RLQNFVGEYV ADNMEKKQQW
KKSRLSLSFR RPSPLVRT
//
