ID   T1J478_STRMM            Unreviewed;       826 AA.
AC   T1J478;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0008006|Google:ProtNLM};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR008409-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR008409-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH431841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1J478; -.
DR   STRING; 126957.T1J478; -.
DR   EnsemblMetazoa; SMAR008409-RA; SMAR008409-PA; SMAR008409.
DR   eggNOG; KOG2844; Eukaryota.
DR   HOGENOM; CLU_007884_11_0_1; -.
DR   OMA; PFNVQRF; -.
DR   OrthoDB; 1815533at2759; -.
DR   PhylomeDB; T1J478; -.
DR   Proteomes; UP000014500; 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   Reference proteome {ECO:0000313|Proteomes:UP000014500}.
FT   DOMAIN          12..366
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          369..425
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          427..686
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          714..801
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   826 AA;  92614 MW;  B47FB8A8AF8D4259 CRC64;
     MMSASYLPKQ ARVVVCGAGV VGTSVAYHLA KRGCVDVVLL ESSRVGSGTS WHGSGLVSQF
     RSPSERNLIS YSAQLYEQLQ ESGHNVGWQQ CGSLNIAQSK NRWISLRRFY AQSQATDLDC
     QLLTPKEISE LHPLLNVDDI QGGVWVPSDG VAQSILLCNT LAKLAQQQGV KIIENCKVNY
     VHTNHETVSS IETAKGRIDC EYFVNCSGLW SHDVALNTDT PVRVPIHAAL HTYITTKTVD
     DVNISHLPFV QDYDGRIYVR EWKKGLLAGG HELLGKPVTP RQTLEFQHMP EDWERFKPLY
     QMMKKRFPLF GRVAIENVYT APENFTPDGK WIVGESPEVK NYFVGCGMNG NSVPGAGGLG
     KALADWIVDG ESAYYVLPFD IKRFIGLHNN KKFLSERVKE IAAKQYTLKF PMQSEFRLAR
     KLRCSPLYTL EEAAGGVFGE RMCCERALYF NPYSKGGNAA HIMGPGTFGK PDWFDFVKEE
     VITCRTGVGL IDLSSLTKME LSSNGTEVVS FLQLLCANDV DVPVNYIVQT GMLNDHGGYF
     MVCPTFQHTR IKEWLSRHLP MDGSVAFNDV TSMYTVLNVV GPKSKELMAE LTCSDMNLPP
     FTCREMNLGY ASEIMVLGFT NAAEPGYSIF VPSEYALHIY DRLRAVGRDY GLRNVGYYAV
     RFLRIEKFIP FWGEEMDCIT TPYEVNRGYK VKLEKDYFIG KMALLKQKQT GVKRRLVHFT
     FENHDLEQDY WPWGKEPILR NGQIVGLTTS SGYGVTLDKL VCMGFVHKGT GVSNEFVTGK
     NVKFEIDLAG KKCPVHASLH PPKIPVITLD STQQYSPKVR GKVQIH
//