ID F4W6V4_ACREC Unreviewed; 896 AA.
AC F4W6V4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|EMBL:EGI70067.1};
GN ORFNames=G5I_01160 {ECO:0000313|EMBL:EGI70067.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI70067.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; GL887762; EGI70067.1; -; Genomic_DNA.
DR RefSeq; XP_011064350.1; XM_011066048.1.
DR RefSeq; XP_011064358.1; XM_011066056.1.
DR RefSeq; XP_011064363.1; XM_011066061.1.
DR AlphaFoldDB; F4W6V4; -.
DR STRING; 103372.F4W6V4; -.
DR EnsemblMetazoa; XM_011066048.1; XP_011064350.1; LOC105152020.
DR EnsemblMetazoa; XM_011066056.1; XP_011064358.1; LOC105152020.
DR EnsemblMetazoa; XM_011066061.1; XP_011064363.1; LOC105152020.
DR GeneID; 105152020; -.
DR KEGG; aec:105152020; -.
DR eggNOG; KOG2844; Eukaryota.
DR InParanoid; F4W6V4; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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:EGI70067.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT DOMAIN 50..409
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 412..467
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 470..755
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 781..869
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 896 AA; 101098 MW; 86744F8B966EFB9F CRC64;
MWKQCKLLCS RGVVQGRKIF SRSYQTRETV TKVIDVTSDD SEYVFPKEAR VVICGGGVMG
GAVAYHLSLI GLGPETILVE SGRLGGGTTW HASGLVGAFK PSLAQVKLAQ DSIALYKELE
KKGLSTGWKQ CGSLSLARTR DRMTSFRRMK AQSVSRNIEC HLVSPEEIHD LCPLLHVEDL
IGGLWIPGDG VGDPYQICLT LMQEAQQRGV RVFENCTVTK VINHSGQIEA VETTRGMIKC
QHFVNCAGFW ARNVGKLSEP HVKVPLHPVE HYYLHTKPIA NLDPMIPVIR DLDGYIYFRE
NEGRLLAGGF EPVAKPAFED GIIPESMDKR FLPEDWDHFH ILLEQMLHRI PSLGNAILER
LCNGPEAFSP DCRWIVGEAP EIRNYYIAAG MKTVGISAAG GVGRATAELI VNGSTSLDMY
ELDVSRFLGL HNNRKFLRDR VREVPGMHYA LQYPHLEFKT GRNLRMSPIY PKLRDAGAVF
GQVMGYERPS WFQPDHDCDL EFPDGFQRYK IAYTNTFGKP PWFDAVAQEY AACREAIGLS
DYSSFTKIDL WSNDTEVVDL LQYLCSNDVD VPVGSIIHTG MQNYLGGYEN DCSLARIAPN
HYMMIAPTIQ QTRCKNWIHR HLPVDGSVAV SDVTSAYTAI CIMGPATRKL LTELTDIDLN
PKNFPFFTFK ELDVGLANGI RTMNLTHTGE LGYVLYIPNE FALHVYTRLI EAGAKYGMKH
AGYYATRALR VEKFYAFWGQ DLDTFTTPLE CGRSWRVKFD KEVNFIGRDA LLKQREQGVQ
RKYVQLLLND HDLEFDTWCW GGEPIYRNGK YCGMTTTTGY GFTFKKQVCL GFVQNFDSKD
QPQEVTNEYI LSGDYEVNVA GIMYPAKCHL HSPNLPTKFP DKERDAYHAT RDQQSL
//
