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Database: UniProt
Entry: Q43166_SOLTU
LinkDB: Q43166_SOLTU
Original site: Q43166_SOLTU 
ID   Q43166_SOLTU            Unreviewed;       465 AA.
AC   Q43166;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000313|EMBL:CAA81748.1};
DE            EC=4.4.1.14 {ECO:0000313|EMBL:CAA81748.1};
GN   Name=ST ACS1B {ECO:0000313|EMBL:CAA81748.1};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EMBL:CAA81748.1};
RN   [1] {ECO:0000313|EMBL:CAA81748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Datura {ECO:0000313|EMBL:CAA81748.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:CAA81748.1};
RA   Van Der Straeten D.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAA81748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Datura {ECO:0000313|EMBL:CAA81748.1};
RC   TISSUE=Leaf {ECO:0000313|EMBL:CAA81748.1};
RX   PubMed=7891663; DOI=10.1007/BF00290453;
RA   Destefano-Beltran L.J., van Caeneghem W., Gielen J., Richard L.,
RA   van Montagu M., van der Straeten D.;
RT   "Characterization of three members of the ACC synthase gene family in
RT   Solanum tuberosum L.";
RL   Mol. Gen. Genet. 246:496-508(1995).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; Z27234; CAA81748.1; -; Genomic_DNA.
DR   PIR; S56176; S56176.
DR   AlphaFoldDB; Q43166; -.
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; 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:SF124; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE; 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   Lyase {ECO:0000313|EMBL:CAA81748.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          41..424
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   465 AA;  52909 MW;  76C98EB59991AFE2 CRC64;
     MKLLSKKAMC NSHGQDSSYF LGWEEYEKNP YDETRNPKGI IQMGLAENQL SFDLLESWLT
     QNPDAAAFKR NGDSIFRDLA LFQDYHGLPA FKDALVQFMS EIRGNKVSFD SNKLVLTAGA
     TSANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIQCTSSNG FRITESALEE
     AYKEAERRNL RVKGVLVTNP SNPLGTTLTK KELQLLLTFV STKQIHLISD EIYSGTVFNS
     PKFVSVMEVL IENNYMYTEV WDRVHIVYSL SKDLGLPGFR VGAIYSNDVM IVSAATKMSS
     FGLISSQTQY LLSALLSDKK FTKKYVSENQ KRLKKRHEML VGGLKQIGIR CLESNAGLFC
     WVDMRHLLSS NTFDGEMELW KKIVYEVGLN ISPGSSCHCT EPGWFRACFA NMSEDTLNIA
     IQRLKAFVDS RDNKDDIQNQ KHSNKKKSFS KWVFRLSFNE RQRER
//
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