ID   A0A0V1H4M3_9BILA        Unreviewed;       911 AA.
AC   A0A0V1H4M3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|EMBL:KRZ05028.1};
GN   Name=PDPR {ECO:0000313|EMBL:KRZ05028.1};
GN   ORFNames=T11_9675 {ECO:0000313|EMBL:KRZ05028.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ05028.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ05028.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ05028.1};
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:KRZ05028.1}.
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DR   EMBL; JYDP01000148; KRZ05026.1; -; Genomic_DNA.
DR   EMBL; JYDP01000148; KRZ05028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1H4M3; -.
DR   Proteomes; UP000055024; 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:KRZ05028.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT   DOMAIN          65..443
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          448..501
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          503..776
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          807..888
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   911 AA;  102976 MW;  97AFFE6BE3287EBE CRC64;
     MLSLHYLRAA NSKLMLMMKN AYSPRRCFRQ FASGLSVNEL NLSMSDLPFR SYEYEDLIEF
     PEKVDVLICG GGLSGLCLAY HLSAIGKHKI LLLERNRLSK CATMLSTGLL LANQTWRCHG
     MLDMVHFADE FYNYLSKQQD IAGYSEWSRM LLASTEATAL QLKRILSIAK ASNFNGRLLS
     PEELNKLDKE CQIGETKAIN IKAALLLDDV RVNQYASAHV LASMINRTGV DIVENCAVRL
     VKLDNQCRVI GAETDYGFVE CDAFVDAAGA VSVYGWSVFS FSGGFFDRDV DPAIKQFPLH
     PLFYNSVVLE AEGIYTFPST VVHDVDLNVY VSHSGRYLVC GGFDKHAFKL DNEDSLLLYG
     AEGSQLPEQW DFFVHVLEKL AKRFPALLNL PVARQFVIGE AFTPDGLPVV GALPSVPNYY
     CLTGMNGLVT TMAPGLSKVL AQRICGIEPE LDVDKFDVGR FILLHCNKHY ISQRATEVAG
     SVFSNFNPLY EWSSVRRLRL SPLHEELKEA GGVFGEVMGF EQVLYFSKGD VPWMKCGESF
     PLGKPEWFDH VAVEYRACRE KVAIMEMSYL SKFEVKGQDY GVIYFLQKMC SANVDQPIGS
     AVFTGIQNYK GGYVADCTLN RFGQYEFFMT AAPDQQTRLR IWMQRHLTAE DKTSIHDVTS
     KYTTLCILGP ASRMLMQELT DEPLSSFASF SCRKINIGCV SGIRAVSVTH CGELGWTLHC
     PNEFAQYIFE QLRTYGQSYD VQLAGNYAFN SLRIEKFYVR WGVDIDWMTT PNECGRSFRV
     DFNKDFIGKD ALLEEMQMCP RRLFVQLLFL EHDMRRDPWP FGNEPIYRNG DFCGFTTSTS
     YAFTIGCQVS LGYINIDGMR TADEAADYVL DKYAVYEIEI AGKRFQVQLN LHSPDLPMVS
     SEHPHHYRPT Q
//