ID M2RPR9_CERS8 Unreviewed; 531 AA.
AC M2RPR9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN ORFNames=CERSUDRAFT_111028 {ECO:0000313|EMBL:EMD40422.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD40422.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD40422.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD40422.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; KB445792; EMD40422.1; -; Genomic_DNA.
DR AlphaFoldDB; M2RPR9; -.
DR STRING; 914234.M2RPR9; -.
DR HOGENOM; CLU_017584_0_5_1; -.
DR OrthoDB; 5486605at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 115..398
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 531 AA; 59732 MW; B9C21BA75D949E4E CRC64;
MAQEKREKAI DLSHHLSELS KKRQTSPLKG LAKYFGRPGL ISLAGGMPSE AYFPFANIGG
DALIPESFAV KADEQESSVS WFWKLFGKPK ERTNPITVPK FPTKPDEINL AVALQYGMST
GLPQLQKFID EFIAKVYQPA YSNCESLVQT GNTDGWSRAM QTLCNPGEMI LTEDWTYPSA
LASARPFGIE PVPVPMDKEG MKSDELRKVL AEWDEKARGA KRPHVMYTVP VGQNPSGATM
GAERKKEIYD ICVEYDVIIV EDDPYFFLQM GEYKPKSIRD QQSAATESDD QFLANLAPSF
VKFDYQGRVI RLDTFSKYIA PGSRLGFFTC NPMFSERLQR QGETSTQAPC GFGQSLIAQL
LTTWKFNGYA RWLHGLATQY TDRRNFFVDC FAEEFHLQLT TGAQGAWEGC AVYAASPKPR
GNAMSEKYSV GTKMFSFVPP TSGMFLWINM HFENHPSIQS EPEETLEMKL WTKIADAGVL
IAPGWYFAAN DDIPEAGHGH FRISFSNAEF PDLKKAVQIF SKVTREFFEE Q
//