ID A0A0L1J059_ASPNO Unreviewed; 413 AA.
AC A0A0L1J059;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
GN ORFNames=ANOM_006713 {ECO:0000313|EMBL:KNG84798.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG84798.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG84798.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG84798.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG84798.1}.
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DR EMBL; JNOM01000188; KNG84798.1; -; Genomic_DNA.
DR RefSeq; XP_015405721.1; XM_015551969.1.
DR AlphaFoldDB; A0A0L1J059; -.
DR STRING; 1509407.A0A0L1J059; -.
DR GeneID; 26808517; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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:UP000037505}.
FT DOMAIN 66..413
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 413 AA; 45727 MW; E620FB4F5D9DA6D3 CRC64;
MLSRRGAQWA TIGFAHGEQN NYNAATNPKG IVSFANAENS LMHDDLTGFI NEHNDFDKRC
CAYGEGYTGT LCLRRAMAAH LNAHFHPANN IGPEEITFAA GVTYLNEAST LILCDPDQND
GIMLGRPVYG AFARDLAMRT NIHLEYVSVG DTDQFSPSCV AGFESGFEAA KARGTNIKAL
MICNPHNPLG RCYSRETLIG LLRLCASKGI HLISDEIYAL SVYERHDRES ETFTSIRAID
PTGIIDPSQV HVLYGMSKDF GASGMRLGCI ISQNEEFTRA TRATCRFSSP SQFSMDLATK
FLEDQEFVAK FLKRSHHCLL QSRLLVEDLL FQEGISYSQK GNAGFFLWLD LSAFLPLHET
GGDGWAAQRL LTDRFSKAGV IMSTGAEYRA PSPGRFRLVF CVDPDTLKEG IRR
//
