ID A0A0V0S3G0_9BILA Unreviewed; 904 AA.
AC A0A0V0S3G0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|EMBL:KRX21291.1};
GN Name=PDPR {ECO:0000313|EMBL:KRX21291.1};
GN ORFNames=T07_9323 {ECO:0000313|EMBL:KRX21291.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX21291.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX21291.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX21291.1};
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:KRX21291.1}.
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DR EMBL; JYDL01000040; KRX21291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0S3G0; -.
DR Proteomes; UP000054630; 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:KRX21291.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 65..436
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 441..494
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 496..769
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 808..882
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 904 AA; 102213 MW; 653B0B642D0C7AFC CRC64;
MLSLHYLRAA NSKFMLMVKN AYSPRLCFRQ FTSGLSENEL NLSMSDLPFR SYEYEDLIEF
PEKVDVLICG GGLSGLCLAY HLSAIGKHKI LLLERNSTGL LLANQTWRSH GMLDLVHFAD
DFYNYLSKQQ DIAGYSEWSR MLVASTEATA LQLKRILSIA KASNFNGRFL SPEELKKLDK
ECQIGETKAI NIESEAALLL DDVRVNQYAS AHVLASMINR TGVDIVENCA VRFVKMDNQC
RVVGAETDYG FVECDAFVDA AGAFSGGFFG HDVDPAIKQF PLHPLFYNSV VLEAEGMYTF
PSTVVHDVDL NVYVSHSGRY LICGGFDKHA FKLDNEDSLL LYGAEGSQLP EQWDFFGLRL
CFFFTAVHVL EKLAKRFPAL LNLPVARQFV IGEAFTPDGL PVVGALPSVQ NYYCLTGMNG
LVTTMAPGLS KVLAQRICGI EPELDVDKFD VGRFILLHCN KHYISQRATE VAGSVFSNFN
PLYEWSSVRR LRLSPLHEEL KEAGGVFGEV MGFEQVLYFS KGDVPWMKCG ESFPLGKPEW
FDHVAVEYRA CREKVAIMEM SYLSKFEVKG QDYGVIYFLQ KMCSANVDQP IGSAIFTGIQ
NYKGGYVADC TLNRFGQYEF FMTAAPDQQT RLRIWMQRHL TAEDQTSIHD VTSKYTTLCI
LGPASRMLMQ ELTDEPLSSF ASFSCRKINI GCVSGIRAVS VTHCGELGWT LHCPNEFAQY
IFEQLRTYGQ SYDVQLAGNY AFNSLRIEKF YVRWGVDIDW MTTPNECGRS FRVDFNKDFI
GKDALLEEMQ MCPRRLFVQL LFLGHDMRRD PWPFGNEPIY RNGDFCGFTT STAYAFTIGC
QVSLGYININ GMRTADEAAD YVLDKYAVYE IEIAGKRYQV QLNLHSPDLP MVSSEHPFHY
RPTQ
//