ID B8MMF0_TALSN Unreviewed; 461 AA.
AC B8MMF0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
GN ORFNames=TSTA_099560 {ECO:0000313|EMBL:EED13704.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED13704.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; EQ962658; EED13704.1; -; Genomic_DNA.
DR RefSeq; XP_002485942.1; XM_002485897.1.
DR AlphaFoldDB; B8MMF0; -.
DR STRING; 441959.B8MMF0; -.
DR GeneID; 8105399; -.
DR VEuPathDB; FungiDB:TSTA_099560; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_2_1; -.
DR InParanoid; B8MMF0; -.
DR OMA; HRISRFM; -.
DR OrthoDB; 1328656at2759; -.
DR PhylomeDB; B8MMF0; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; 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; 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.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 41..444
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 461 AA; 52062 MW; 574AE17AEC504703 CRC64;
MANFHVSQRG AYNLKYRDNF EAQSARHQEL WTPTNPNGRI FMDVAENSLL HDEVADFISR
KIKIEPNDHL TYGSGPRGSL RLKKAAASFL ENSFKGRDPV KSEDILVFPG LAGAIDAVTW
AICDEGEGVL VCLPMYNGFN VDIPTRTGAV VVEVPFHSVD GYSGLEDVFD PDTNRRALEA
AMDHAKKNGV SIRALLISQP HNPLGRCYPQ ETLLEMAAFC GRNGIHLISD EIYAHSVFDN
PALHHWPVFT SILALDISSH IDKSMVHVLY GASKDFCVNG LRLGLLYSRN AALLGAISTN
CVFSWVPHIV QDIWASMLED HEWRKTFFAK NQSIMANNYA LVIKFFKEQD IGFFHMNAAT
FVWVDLRRYM LPRNMRSRDA YPMLQVTDPN VGLYLEREAK VIRICSRNGV MIKPGSAYKT
EELGWFRVTF TLPEHVLLEG LRRIRKSLKE IEKLGGDSTR L
//
