ID K2SXH9_MACPH Unreviewed; 480 AA.
AC K2SXH9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Aminotransferase class-3 {ECO:0000313|EMBL:EKG21270.1};
GN ORFNames=MPH_01413 {ECO:0000313|EMBL:EKG21270.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21270.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG21270.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG21270.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG21270.1}.
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DR EMBL; AHHD01000053; EKG21270.1; -; Genomic_DNA.
DR AlphaFoldDB; K2SXH9; -.
DR STRING; 1126212.K2SXH9; -.
DR VEuPathDB; FungiDB:MPH_01413; -.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_4_0_1; -.
DR InParanoid; K2SXH9; -.
DR OrthoDB; 345661at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EKG21270.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transferase {ECO:0000313|EMBL:EKG21270.1}.
SQ SEQUENCE 480 AA; 52000 MW; CA58DC0039900DF9 CRC64;
MNFCFRACSR ARVRSVIRPQ HRANTTSAVN DFVAKSHVMH RALRSEPQSI VSGSGISFVL
ANGKTLIDAS GGPAVSCLGH HRPEVAKAVA DQINKIGYVY SVGYTSDPAE ELATMLLKDK
PGGLSRAMFF NSGSEATDAA VKLATQYWKE KGELQRRNVI SRAQSYHGNT IGALCVSGHE
SRRAMYSDWM SNNVSFVDPC YAYRAKPDGQ SDEEYLTHLI KQLDDEFHRL GPETVSAFFA
ETISGTTLGC LPALPGYFKA VRELCDKYGA LLILDEIICG MGKTGAMHAW QQEEGFRGPD
LQTIGKTLGG GFVPLSAVLV HEKVFDALAV GTGALSHGHT FQAHPTACAA AIEVQKIIGQ
ENLLENCQKM GAVLGERMKA EILPLPLVGD VRGRGLYWAA EFVMDKEAKT PFPLSDNFST
KVVAAAAELG LNILGNLGKT GLIDVEHVMI TPPYIITEDE VVKVVGLLKK AIQRASEPYL
//
