ID A0A0N4ZUK6_PARTI Unreviewed; 869 AA.
AC A0A0N4ZUK6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|WBParaSite:PTRK_0001226900.1};
OS Parastrongyloides trichosuri (Possum-specific nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Parastrongyloides.
OX NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0001226900.1};
RN [1] {ECO:0000313|WBParaSite:PTRK_0001226900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR AlphaFoldDB; A0A0N4ZUK6; -.
DR STRING; 131310.A0A0N4ZUK6; -.
DR WBParaSite; PTRK_0001226900.1; PTRK_0001226900.1; PTRK_0001226900.
DR Proteomes; UP000038045; Unplaced.
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;
FT DOMAIN 35..400
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 410..459
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 462..737
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 766..848
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 869 AA; 98977 MW; 2D05F3148A0BC1E5 CRC64;
MLSRYHCKRL LHYRSTFLNV RYASSFTEQG FEKADVVVCG GGIAGLSVAY HLNKLGKRVS
IFDKYCIGEG SASVINYGLI SSPYFWQNRT LMKLAERSHE FYKKLGETSN IEIEKCGKVY
FATNDEMAHE LRRIYTWAKS FGYKDVELLD CPSEMLSRWP VADTEDVTLA LNAPHDIRLD
MSSVLLELQK RLKKSGVKIY ENCKVRNVCV GNKRRIYGIQ TDLGLIETEI FVDCSGINAG
RIPVKALPNE HVMVASYPCT VNGLTTSRVN ASSLNNISPV LCDVESNIFL KTGQYDTICG
GFVEDGMKPL PNTKSDVTKD WTIPIADWDN FHPILTKLID RFPNLGSAPH GNLQLHYDTF
TPDKNPIIGE CSEVSGYYIA TGFNARGLTL APGATELLSR WICKYPIKED VSTIDVTRFL
PMHGNTKYLY QRIPEVASYV YDTTRQSFQF HSARNLRMSP IYHQLRDAGG VFGELMGYER
PLWYDKNSTQ ESHLFCGQDP LYGRPRWFEH VEKEYEACRE RVGLIDMTSF SKFEVKGEDS
ERFLQYLCSA NVNMPIGETV YTGMQNENGG YVTDCTISRL KDNHYFVIAP TVQQLRCFIW
MRKWSKKLKT DVKIIDVTGN YTALDLIGPS SRYLMQDISG ESMAPGDFPT FRMKEINIGM
GTGIRANSIS HCGELGWMLY IPNEFAQNVY DVIVESGKEY NMKHCGYYTM RALRIEKFYV
YWGQDINEQT TPVECGRSFR VDFDKENFIG KDALLKQVEE GVNKRFVQIF VENHDMDRDP
WPQGGEPIFC NGKQCGLTTS SAYGFTLKKQ ICLGYVESLE EKIEPSHITQ QNYTINISGK
EFPIKVSLHS PNLPMISSEH PVHYAPTQN
//
