ID   A0A3B0KRM2_DROGU        Unreviewed;       941 AA.
AC   A0A3B0KRM2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Blast:Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|EMBL:SPP89299.1};
GN   ORFNames=DGUA_6G020085 {ECO:0000313|EMBL:SPP89299.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP89299.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; OUUW01000019; SPP89299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0KRM2; -.
DR   STRING; 7266.A0A3B0KRM2; -.
DR   OMA; TKFPDRE; -.
DR   OrthoDB; 1815533at2759; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR032503; FAO_M.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR13847:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16350; FAO_M; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Pyruvate {ECO:0000313|EMBL:SPP89299.1}.
FT   DOMAIN          71..430
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          434..488
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          491..775
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          803..888
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
FT   REGION          910..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   941 AA;  106195 MW;  81569B7608591CAE CRC64;
     MYRVLLGGLC RSIPAGGHVG SRSVVSTRTL SVATGHTDPA DEQVLRKRKF QPQQAPDLSE
     QLAGQLPGRA RVVICGGGIT GASVAYHLGL QGWGGETLLI EQDRVGGELP WSACGLAGRF
     EPSYTELKLA EYSIDLIKRL TKRGLPTGWR QVGSLNLARN FDRMTSFNRM KSQAVAWGMN
     CEILSPEQCQ QHCPLLSLDG IEGGLWIPED GVCDPHLVCH AYVDEARRLG VQIVEHCAIK
     KIHSEHGKVK RVETTAGDVD CEYFVNCTGF WAREVGTLSK PVVKVPLKAV EHHYLHTQPI
     DGLDPNTPFV RDFDGRIFFR ECEGHILAGG FEREAKMVYE DGVIPLSQTA RQFPPDWDHF
     HELLDALLVR VPSFRQASLD RLTNSLQVFS PDCKWILGEA PEIQNYYVAA GNKTMGVSAS
     GGIGRVLTDL ITKGSTYLDL HILDISRFLG LHNNRKFLRD RCKEAPGKHF EINYPFEEFQ
     TGRNLRMSPI YPQLKEAGAV FGQSMGYERA NYFDQQDKQD EFGLPRFRIA QTRTFGKPPW
     FDHVASEYRA CRERVGIADY SSFTKYDFWS KGNEVVELLQ YLCSNDVDVA VGSIIHTGMQ
     NHNGGYENDC SLARLSERHY MMIAPTIQQT RSMCWIRKHM PDHLRAKVNV ADVTSMYTAI
     CILGPYSRVL LSELTDTDLT PKNFPFFTYK ELDVGLADGI RVLNITHTGE LGYVLYIPNE
     YALHVYSRLY QAGHKFNIQH AGYYATRALR IEKFYAFWGQ DLDTFTTPLE CGRSWRVKFN
     KPIDFIGRNA LLKQREEGVT RMYVQLLLND HDHEVDMWCW GGEPIYRDGV YVGMTTTTGY
     GFTFEKQVCL GFVRNFDEQG RELAVTNDYI LSGHYEVEVA GVRFEAKVNL HSPNLPTKFP
     DREREAYHAT RDKPDQADLL SFSSNPMTTV TRSGGGTGGS Q
//