ID   M7WPG7_RHOT1            Unreviewed;       852 AA.
AC   M7WPG7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:EMS19966.1};
GN   ORFNames=RHTO_03764 {ECO:0000313|EMBL:EMS19966.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19966.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS19966.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS19966.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004746}.
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DR   EMBL; KB722664; EMS19966.1; -; Genomic_DNA.
DR   RefSeq; XP_016271085.1; XM_016417433.1.
DR   AlphaFoldDB; M7WPG7; -.
DR   GeneID; 27367777; -.
DR   eggNOG; KOG1401; Eukaryota.
DR   HOGENOM; CLU_010794_0_0_1; -.
DR   OrthoDB; 5487177at2759; -.
DR   Proteomes; UP000016926; 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:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd03109; DTBS; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   Pfam; PF00202; Aminotran_3; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:EMS19966.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMS19966.1}.
FT   REGION          299..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  90717 MW;  D2FBD76843E99BED CRC64;
     MLSRHLRTHL VVAPSTSVGK SIFSTGLVRA SLALGEKVGY LKPVGTGSGD GDDELHLQRF
     APQAKTACLF HFDEPVSPHL AVERSAAGLS KAVTKATTDA EFAAAVGKYA RSFAEETAGK
     RSSLYIETAG GVHSPTLSGT SQLDAFRPLL PPTLLVASAA LGGISTTISA YESLLLRGYD
     VDAVLVFREE YYANYQYFEK WFTERGIRVG VIDQPPEQVT NAAEDAANLE AYYSKLAGSP
     LQRIVQRLQQ IHLDRMSNLA TAPRRTLDKV WWPFVQHGLV QNESDVMVID SAHGDHFSVF
     ATSSPPVEPP TPTSDPSTAP AISPSEQATS TSAATPSLPP AQSPAHPLLS PVFDGSASWW
     TQCLGHANPE LTLAAAHASG RFGHVMFPTA TNLPALELAE KLLATVGESW ADRVFFSDDG
     STGMEVALKM ALRAYADRER LSPAEGRRLA VLGLKGSYHG DTIGAMDACE GGVYSERVEW
     YEGRGYWLAA PEVRIEQGKV VVRGKGGRAT SYDSLTQLYD VDRRVQEDEL AQTYRQEIEG
     ELQKRLDKGD GIRFGALVLE PVVMGAGGMI FVDPLYQRVL IDVVRTNRQL FPAASPAPSD
     SATLAATGSN PVWQGLPVIF DEVFVGLHRL GRTTASTFLG SSTKPDIACY AKILTGGLVP
     MAVTLASDAI FRAFWSDKKV DALLHGHSYT AHAVGCGVAN KTLAILDRME KQGVYDEAKQ
     DWAAAAGSSA GGMVSGVWSL WSSSFVEAVS SHPAVDGVMA IGTVLAIHLK AADGSGYQST
     ASETVLAQLR FGTPVDSDPA AAASPTGAPF HIHARPLGNV IYFMSSLNSS PETLRSVEGS
     IVAALNAKAG AS
//