ID A0A1S3X471_TOBAC Unreviewed; 467 AA.
AC A0A1S3X471;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
GN Name=LOC107761132 {ECO:0000313|RefSeq:XP_016434790.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016434790.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016434790.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR RefSeq; XP_016434790.1; XM_016579304.1.
DR AlphaFoldDB; A0A1S3X471; -.
DR SMR; A0A1S3X471; -.
DR STRING; 4097.A0A1S3X471; -.
DR PaxDb; 4097-A0A1S3X471; -.
DR GeneID; 107761132; -.
DR KEGG; nta:107761132; -.
DR OMA; YSYPGVK; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000084051; Unplaced.
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:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:amino acid metabolic process; IBA:GO_Central.
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: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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051}.
FT DOMAIN 41..424
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 467 AA; 52851 MW; 87121E361B5DBBC9 CRC64;
MKLLSKKVMC NSHGQDSSYF LGWQEYEKNP YDETRNPKGI IQMGLAENQL SFDLLESWLA
QNPDAAGFKR NGESIFRELA LFQDYHGLPA FKNALAQFMA EIRGNKVSFD SNKLVLTAGA
TSANETLMFC LADHGDAFLL PTPYYPGFDR DLKWRTGAEI VPIECTSSNG FRITESALEE
AYQEAKRRNL RVKGVLVTNP SNPLGTTLSN QEIQLLLTFI STKNIHLISD EIYSGAVFNS
PSFVSVMEIL IENNYMNSEV WDRVHIVYSL SKDLGLPGFR IGAIYSNDEL VVAAATKMSS
FGLISSQTQY LLSAMLSDKK FTKMYISENQ KRLKKRHEML VQGLQNAGIS CLDSNAGLFC
WVDMRHLLRS NTFDEEIELW KKIVYDVGLN ISPGSSCHCT EPGWFRACFA NMSEDTLNLA
IQRLKAFVDS TNNNIQNHHQ SSLSSKKKSF SKWVFRLSFN DGRQRER
//
