ID   A0A0V0XL69_TRIPS        Unreviewed;       898 AA.
AC   A0A0V0XL69;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|EMBL:KRX88712.1};
GN   Name=PDPR {ECO:0000313|EMBL:KRX88712.1};
GN   ORFNames=T4E_1581 {ECO:0000313|EMBL:KRX88712.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88712.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX88712.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX88712.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX88712.1}.
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DR   EMBL; JYDU01000225; KRX88709.1; -; Genomic_DNA.
DR   EMBL; JYDU01000225; KRX88712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XL69; -.
DR   Proteomes; UP000054815; 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; IPR028896; GCST/YgfZ/DmdA.
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; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF9; SARCOSINE DEHYDROGENASE; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Pyruvate {ECO:0000313|EMBL:KRX88712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT   DOMAIN          65..430
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          435..488
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          490..763
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          802..875
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   898 AA;  101540 MW;  0EDEB6838DC5104C CRC64;
     MLSLHYLRAA NSKLMLMTKN AYSPRRCFRQ FASGLSVNEL NLSMSDLPFR SYEYEDLIEF
     PEKVDVLICG GGLSGLCLAY HLSAIGKHKI LLLERNSTGL LLANQTWRCH GMLDMVHFAD
     DFYNYLSKQQ DIAGYSEWSR MLLASTEATA LQLKRILSIA KASNFNGRLL SPEELKKLDK
     ECQIGETKAI NIKSDIICYA ALLLDDVRVN QYASAHVLAS MINRTGVDIV ENCAVRFVKL
     DNQCRVIGAE TDYGFVECDA FVDAAGAFSG SFFGHDVDPA IKQFPLHPLF YNSVVLEAEG
     IYSFPSTVVH DVDLNVYVSH SGRYLVCGGF DKHAFKLDNE DSLLLYGAEG SQLPEQWDFF
     VHVLEKLAKR FPALLNLPVA RQFVIGEAFT PDGLPVLGAL PSVPNYYCLT GMNGLVTTMA
     PGLSKVLAQR ICGIEPELDV DKFDVSRFIL LHCNKHYISQ RATEVAGSVF SNFNPLYEWS
     SVRRLRLSPL HEELKEAGGV FGEVMGFEQV LYFSKGDVPW MKCGESFPLG KPEWFDHVAV
     EYRACREKVA IMEMSYLSKF EVKGQDYGVI YFLQKMCSAN VDQPIGSAIF TGIQNYKGGY
     VADCTLNRFG QYEFFITAAP DQQTRLRIWM QRHLTAEDKT NIHDVTSKYT TLCILGPASR
     MLMQELTDEP LSSFASFSCR KINIGCVSGI RAVSVTHCGE LGWTLHCPNE FAQYIFEQLR
     TYGQSYDVQL AGNYAFNSLR IEKFYVRWGV DIDWMTTPNE CGRSFRVDFN KDFIGKDALL
     EEMQMCPRRL FVQLLFLGHD MRRDPWPFGN EPIYRNGYFC GFTTSTSYAF TIGCQVSLGY
     INIDGMRTAD EAADYVLDKY AVYEIEIAGK RFQVQLNLHS PDLPMVSSEH PHHYRPTQ
//