ID A0A364N1S2_9PLEO Unreviewed; 460 AA.
AC A0A364N1S2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=2,2-dialkylglycine decarboxylase {ECO:0000313|EMBL:RAR09686.1};
DE EC=4.1.1.64 {ECO:0000313|EMBL:RAR09686.1};
GN ORFNames=DDE83_005442 {ECO:0000313|EMBL:RAR09686.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR09686.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:RAR09686.1}.
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DR EMBL; QGDH01000073; RAR09686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364N1S2; -.
DR STRING; 183478.A0A364N1S2; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0047432; F:2,2-dialkylglycine decarboxylase (pyruvate) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Lyase {ECO:0000313|EMBL:RAR09686.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 460 AA; 49524 MW; 5A61BD43C0F85BD3 CRC64;
MSRPYDNTNI EQLQRDAGDC LLTYGTAFHP EIITSTNGIY VETASGHRMM DFTSGQMSTL
IGHGHPEVVK VINDHAQHLD HLFSGMISPP VINLAKRLTS VTPPGLDKAF FLSTGGESNE
AAIRLAKFYT GKFEIVGLAA SWHGMTGASL GAQYHTGRSG YGPNMAGNLA LPTPNSYRSI
FRNVDGTYDW KTELDYGFDL VDKQSCGSLA AVMVEPILSS GGMLELPPGY LKALKERCEK
RGMLLIVDEA QTALGRAGDM FAFTHHDEDE GVVPDILTLS KTLGNGIPLS AVLTSNAIAQ
HARDNGFLFY TTHINDPLPA AVGDKVLEIV IRDDLCARSK RLGIKLQAGL KRLQSQYGCI
GDVRGRGLMA GVEIVSDRKT KAGAPEVGAA VSRKMEKMGL WAQLATMASF GGVFRIAPPI
TVTEEQLDLA LSIIEEALRT TPGTMPLYTG DGEPVSKKPV
//
