ID Q0TYU5_PHANO Unreviewed; 411 AA.
AC Q0TYU5;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000256|ARBA:ARBA00039053};
DE EC=4.4.1.14 {ECO:0000256|ARBA:ARBA00039053};
GN ORFNames=SNOG_15367 {ECO:0000313|EMBL:EAT77300.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT77300.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445361; EAT77300.1; -; Genomic_DNA.
DR RefSeq; XP_001805517.1; XM_001805465.1.
DR AlphaFoldDB; Q0TYU5; -.
DR STRING; 321614.Q0TYU5; -.
DR EnsemblFungi; SNOT_15367; SNOT_15367; SNOG_15367.
DR GeneID; 5982446; -.
DR KEGG; pno:SNOG_15367; -.
DR VEuPathDB; FungiDB:JI435_153670; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_1_1; -.
DR InParanoid; Q0TYU5; -.
DR OMA; KIPWRYA; -.
DR OrthoDB; 1328656at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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 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:UP000001055}.
FT DOMAIN 59..400
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 411 AA; 45664 MW; 9E7C199C7F52A167 CRC64;
MLSSRGQANA DQLDIPFRFA QGTKYDHETN PDGLISFGTA ENALMQQELE EFAKKVDAGG
THLPSALATH INEYFHPHQL LVGDDIKITA AATALHSVLA YSLCSPGEAI LTTKPYYGRF
ELDFGNEAGV ELVAAETDHE KCFDEDVVVA LEQKLEACEK VGVKVRALLI VNPHNPLGRC
YSKPTLLALL SFCAKHALHI ISDEIYALSV FSNTKFPDAV PFTSLLSLDT KAIIDPDYVH
VTYGLSKDFG AAGLKIGALI TRNEQLKKAV HAVLRFHGVS GPSVAIGTAM LEDRVWCRGF
IDLARERIGE AYEFVTSRLE ELGIEYFKGA NAGFFVWIDL SRYLPPAQEG RSVFERECML
AQKLVDGGVF LHPREEHSIR PGWFRVVYTM EKVFMAEGMR RLGKVLKELQ W
//
