ID E9EPU7_METRA Unreviewed; 424 AA.
AC E9EPU7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Aminotransferase class I and II {ECO:0000313|EMBL:EFZ02150.1};
GN ORFNames=MAA_01732 {ECO:0000313|EMBL:EFZ02150.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ02150.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFZ02150.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFZ02150.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EFZ02150.1}.
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DR EMBL; ADNJ02000001; EFZ02150.1; -; Genomic_DNA.
DR RefSeq; XP_007817921.1; XM_007819730.1.
DR AlphaFoldDB; E9EPU7; -.
DR GeneID; 19256018; -.
DR KEGG; maj:MAA_01732; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR OrthoDB; 176869at2759; -.
DR Proteomes; UP000002498; 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; 3.90.1150.10; 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; PTHR43807; FI04487P; 1.
DR PANTHER; PTHR43807:SF20; FI04487P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Aminotransferase {ECO:0000313|EMBL:EFZ02150.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFZ02150.1}.
FT DOMAIN 36..415
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 424 AA; 47590 MW; 57B1629C87B1894B CRC64;
MEGSSKIKPA ARVSGQKQDV WSIINEAAAA SPKQPIVNMG QGFFGYNPPD FILNAAKDAL
DRVECNQYSP TKGRPRLKKA IADAYSPFWG RKIDPETEVT ITTGANEGML SAFMAFIEPG
DEVIIFEPFF DQYISNIEMP GGKIVYVPMH PPETGATKTS SAADWTIDFA ELEKAITPRT
KMIVLNTPHN PVGKVYSRDE LQKIGDLCVK NEVIILSDEV YDRLYYVPFT RMATLSPEIE
KLTITVGSAG KNFYATGWRV GWLMGPANLI KYVSAAHTRI CYSSVSPLQE ACAVGFEQAE
SEGFWDKTIT DMKSKMDRFN EIWAELDLPY SEPEGGYFVL VNMKKVQVPA DYPFPEHVAS
RPRDFKLAWF LIQEVGVAAI PPTEFYTHAN AHLAEDYVRF AVCKDDEVLE EAKRRLRGLK
KYMQ
//