ID   1A1L1_BOVIN             Reviewed;         502 AA.
AC   Q5E9H2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase-like protein 1;
DE            Short=ACC synthase-like protein 1;
GN   Name=ACCS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:AAX08965.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Does not catalyze the synthesis of 1-aminocyclopropane-1-
CC       carboxylate but is capable of catalyzing the deamination of L-
CC       vinylglycine. {ECO:0000250|UniProtKB:Q96QU6}.
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:0000250|UniProtKB:Q96QU6}.
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DR   EMBL; BT020948; AAX08965.1; -; mRNA.
DR   RefSeq; NP_001015526.1; NM_001015526.1.
DR   AlphaFoldDB; Q5E9H2; -.
DR   SMR; Q5E9H2; -.
DR   PRIDE; Q5E9H2; -.
DR   GeneID; 505649; -.
DR   KEGG; bta:505649; -.
DR   CTD; 84680; -.
DR   InParanoid; Q5E9H2; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   2: Evidence at transcript level;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..502
FT                   /note="1-aminocyclopropane-1-carboxylate synthase-like
FT                   protein 1"
FT                   /id="PRO_0000318070"
FT   REGION          15..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         324
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  57066 MW;  29C9320218202334 CRC64;
     MFTLPQKEFR MTTACPGSDS IQDLPSNKGD GLERECSRKP DQKLLKFYGV GDPAAELSSS
     SPYLSSRGSV IKWFWDSAEE GYRTYHMDEY DEDKNPSGII NLGTSENKLC FDLLSRRLSQ
     SDMLQVEPAL LQYPDWRGHL FLREEVARFL SFYCRSPAPL KPENVVVLNG CASLFSALAT
     VLCEAGEAFL IPAPYYGAIT QHVYLYGNVR LVCVYLDSEV TGLETRPFQL TVEKLEMALQ
     GANSEGVKVK GLILINPQNP LGDIYSPGEL QEYLEFAKRH ELHVMVDEVY MLSVFEESAG
     YRSVLSLERL PDPQRTHVMW ATSKDFGMSG LRFGTLYTEN WAVATAVASL CRYHGLSGLV
     QYQMAQLLRD HDWINQVYLP ENHARLKAAH TYVSEDLRAL GIPFVSRGAG FFIWVDLRKY
     LPEATFEEEV LLWRRFLENK VLLSFGKAFE CKEPGWFRLV FSDKTHRLHL GMQRVRQVLE
     GQPQLADGAP PHQIQEPQGP HR