ID K2QRB7_MACPH Unreviewed; 392 AA.
AC K2QRB7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Aminotransferase class-3 {ECO:0000313|EMBL:EKG12441.1};
GN ORFNames=MPH_10397 {ECO:0000313|EMBL:EKG12441.1};
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:EKG12441.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG12441.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG12441.1,
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:EKG12441.1}.
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DR EMBL; AHHD01000450; EKG12441.1; -; Genomic_DNA.
DR AlphaFoldDB; K2QRB7; -.
DR STRING; 1126212.K2QRB7; -.
DR VEuPathDB; FungiDB:MPH_10397; -.
DR eggNOG; KOG1404; Eukaryota.
DR HOGENOM; CLU_016922_4_0_1; -.
DR InParanoid; K2QRB7; -.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EKG12441.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transferase {ECO:0000313|EMBL:EKG12441.1}.
SQ SEQUENCE 392 AA; 42032 MW; ED7861E497E76A94 CRC64;
MLPPSRSTHD DAEAAKKSGI LHRSLRTLPL KVVGASGNYL TLSNGQQIFD ATGGAAVSCL
GHGDKRVQEA VMRQMNEAAY CHSLFFSTSA AEALGNELIA GTDGEMAKAF IVSSGSEAIE
AAMKLARQYH LETTPPQPGR INFIARKESY HGTTLGSLSL GGHVARRALF EPMLLQNISR
VSPCNAYRGK KEGESDEDYV VRLAKELDDE FQRLGPESVI AFVAEPVVGA ALGCVPSVPG
YFKAVKAICD KYGALLIMDE IMSGMGRTGT LHAWQQEGVV PDIQTIGKGL GGGYAPVAGL
LINHRVVNAL YKGTGSFSHG QTYQGHPMAC AAAAEVQRII REDKLCENAM AMGKYLEELL
KNSLADHPNV GDIRGRGLFW GVSIWKSPEL TD
//
