ID   1A1L1_TAKRU             Reviewed;         618 AA.
AC   Q9W698;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase-like protein 1;
DE            Short=ACC synthase-like protein 1;
GN   Name=accs;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1] {ECO:0000312|EMBL:AAD20564.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10767549; DOI=10.1016/s0378-1119(00)00091-3;
RA   Peixoto B.R., Mikawa Y., Brenner S.;
RT   "Characterization of the recombinase activating gene-1 and 2 locus in the
RT   Japanese pufferfish, Fugu rubripes.";
RL   Gene 246:275-283(2000).
RN   [2] {ECO:0000305}
RP   LACK OF ENZYME ACTIVITY.
RX   PubMed=11470512; DOI=10.1016/s0378-1119(01)00533-9;
RA   Koch K.A., Capitani G., Gruetter M.G., Kirsch J.F.;
RT   "The human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-
RT   carboxylate synthase encodes a protein lacking that activity.";
RL   Gene 272:75-84(2001).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
CC   -!- CAUTION: Similar to plant 1-aminocyclopropane-1-carboxylate synthases
CC       but lacks a number of residues which are necessary for activity.
CC       {ECO:0000269|PubMed:11470512}.
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DR   EMBL; AF108420; AAD20564.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9W698; -.
DR   SMR; Q9W698; -.
DR   STRING; 31033.ENSTRUP00000002425; -.
DR   PRIDE; Q9W698; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   InParanoid; Q9W698; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..618
FT                   /note="1-aminocyclopropane-1-carboxylate synthase-like
FT                   protein 1"
FT                   /id="PRO_0000318073"
FT   REGION          11..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         340
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   618 AA;  68909 MW;  FDA6C4DD1D8686E5 CRC64;
     MLTEALVAVR QGTQTPAAQT TCAPSTMSSS SRPPLETLQA QSVSADETPG SALPACAQPC
     ETARSATPTG GETPNRSRYL SHRGNSIRQQ QGILQEGFLL YSLDKFHETD KPDGIINLGT
     SENKLCHDLL HERLTRPDML LLDPPLLQYP DWSGHQFLRE EVAKFLTDYC CSPKPLKAEN
     VVVMNGCASL FSCIASVICD PKDAILISTP FYGAITEHLG LYSDVKLYHI HLDCEASGED
     GRLFHLTVDK LEEGLRRAEH EGFIVRGLVL MNPHNPLADI YTPKEMVGFL EFAKRNELHT
     IVDEVYMLSV FDESVTFDSV LSLESVPDPQ RTHVMWGLGK DFAMAGIRVG TLYSESRDLV
     EAVAKLGAFH GIPGTTQRQV AQLLQDREWI DTQYLPRNRS RLKAARSYVT GELRGLDVPY
     LDRSAAMFVW ADLRKFLAEP SFEEEMRLWR HFLKHKVVLS CGQAFSCSTP GWFRIVFSDQ
     DRRLKLGMKR IKEALEEYKD QITVTDCYSI KDGGPRVRAS GKDSDNAAIV GSTLPQGKSS
     DMLEEKDHTV QAGLGADELV LRDCQPSKPA EGLDSLIGTL RHQIRSSDWL EKNTPELSAG
     EDPEILDVFK ALLERARK