ID N1QIF6_SPHMS Unreviewed; 645 AA.
AC N1QIF6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Aromatic amino acid aminotransferase 1 {ECO:0000313|EMBL:EMF12219.1};
GN ORFNames=SEPMUDRAFT_67907 {ECO:0000313|EMBL:EMF12219.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF12219.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF12219.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF12219.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; KB456265; EMF12219.1; -; Genomic_DNA.
DR RefSeq; XP_016760340.1; XM_016909796.1.
DR AlphaFoldDB; N1QIF6; -.
DR STRING; 692275.N1QIF6; -.
DR GeneID; 27906933; -.
DR eggNOG; KOG0634; Eukaryota.
DR HOGENOM; CLU_017584_0_5_1; -.
DR OMA; QREGILC; -.
DR OrthoDB; 5486605at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 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 PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF1; AROMATIC AMINO ACID AMINOTRANSFERASE, HYPOTHETICAL (EUROFUNG); 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EMF12219.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transferase {ECO:0000313|EMBL:EMF12219.1}.
FT DOMAIN 133..421
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 72459 MW; DD795B7F32568206 CRC64;
MADANAMDTR PEPKDLSHHL SRATKARTAS SMKAFYKYFQ IPGIGQLAGG LPNNYYFPFD
TLEAKVARPD RFSPTPNLPI DPPSDDEVLA SLSLHGQRKQ RAQNNPLDQP QDAIVVPHDS
KQPNPVKKID LSTALQYGTA QGYPPLYYFL REFTQKNLHP NTPYKGGPEV LLTCGNTDGW
SKVLTAFSNE WSEEKDWIRD REGLLVEHFA YMNAVQSAYP RGLTVTPVAI DDEGLIAEGP
GGMRDVLENW DHTKGRRPHL LYTVTMGQNP TSGVLSLARR RELYAVAKKY DVLIVEDDPY
WYLQFPSATA RNTVTTSHPS NTSFNPEQPM FANAEPHPEG WKSSGYAYLD SLVPSFLSID
TDGRVIRLDT FSKTVAPGCR LGWISAQPAL IERLLRITET STQQPSGFVQ SVVGELILGP
DHEGIKQSMR DGKGGRGGLR DGQGWKADGW VRWLEGLRGN YERRMNSMCR ILDSSKYQVK
AGRRQSLVQH EEDEDEDEWS VVEKTPLYSF DWPVGGMFLW LQVLFESHPL YKQYSKRGDA
ERLSKALWVF WTTSPYKVLV APGTMFSPTA EIAAKEGWKR FRLCFAAINE DELSGVTQRL
ADGVNAFWRI KDMKKIEDLL DEDADEASIT SKEGLVQMGM TASGC
//