ID   A0A0C9MLC3_9FUNG        Unreviewed;       468 AA.
AC   A0A0C9MLC3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=PLP-dependent transferase {ECO:0000313|EMBL:GAN03922.1};
GN   ORFNames=MAM1_0051d03378 {ECO:0000313|EMBL:GAN03922.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN03922.1};
RN   [1] {ECO:0000313|EMBL:GAN03922.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN03922.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; DF836340; GAN03922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9MLC3; -.
DR   STRING; 91626.A0A0C9MLC3; -.
DR   OrthoDB; 5474881at2759; -.
DR   Proteomes; UP000053815; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 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:UP000053815};
KW   Transferase {ECO:0000313|EMBL:GAN03922.1}.
FT   DOMAIN          87..429
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          27..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  52853 MW;  E767C5159D97045D CRC64;
     MSTSPLHKKP RYHFRDVALA VQNKLQQERE SKAHQTLRSY PGNENKATKA QEKGTIHGIE
     HPGSTGVIYV MDRAMKNGFT YASEGWANFG QGAPEVGPID GCFERPKHVD IPQDAYEYAP
     TSGITELRQA VADLYNEIYR QGKDSKYTHE NVCIVPGGRA GLTRVAAAIG DVNVGYFLPE
     YTAYEQMLSV FKRFVPIPTT LEEDARYHIN PDTIRKEISG RGLGVIVASN PRNPTGQVIQ
     DQELEELVQI AKERHTTLVL DEFYSSYIYD QEPGKTVSVS QFVDDVNHDP VILIDGLTKN
     FRMPGWRVCW IVGPKPVISS MESAGSFLEG GANHPLQLAA IPFLDPTKFR NEAKALQHHF
     KEKRDFVLNR LKEMGLNVKV PPNATFYIWL DLSHLPEPIN IGLNFFEECL KEKVIVVPGI
     FFDVNPSHRR ELFESPCHHF VRLSFGPPLD QLKLGLDNIE RVIKKFTK
//