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
//