ID   A0A3Q1HLH3_ANATE        Unreviewed;       670 AA.
AC   A0A3Q1HLH3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit {ECO:0000313|Ensembl:ENSATEP00000008199.2};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000008199.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000008199.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1HLH3; -.
DR   STRING; 64144.ENSATEP00000008199; -.
DR   Ensembl; ENSATET00000008344.2; ENSATEP00000008199.2; ENSATEG00000005675.2.
DR   GeneTree; ENSGT00940000159082; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR006222; GCV_T_N.
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   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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040}.
FT   DOMAIN          43..401
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          405..459
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          461..654
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
SQ   SEQUENCE   670 AA;  74594 MW;  28B36398EF596642 CRC64;
     LLFRLLLLPQ TGHRLSGRSL WTSPHCMAAS GDSQLLPLPN QARVVICGGG IVGTSVAYHL
     AKLGWTDIVL LEQGRLGAGT TRLCAGIVSV AKPISIECQM ANYSNNLYQR LEEETGIKTG
     YVKTGSLCLA QNQDRFISLK RLASRLKVMG ISCNIIKSKD VAKLHPLVNI HDLVGAIHLP
     SDAVVSPPDV NHAMAVAAAA QGVHILERTS VQQVLVEKGH VMAVETERGS IECEYFINCA
     GQWAYELGQA SEMKVSVPLH GCEHFYLLTK PLQEPLPANT PVVIDMDGRI YARSWQGGLL
     SGGFEKNPKP IFTEGRNQLE IQNMQEDWDH FEPILSALLR RMPGLELAEI HQLVNCPESF
     TPDMRCLMGE IPGVSGYYVL AGMNSSGLAF AGGAGKYLAE WMTYGYPTAN VWPLDIKRFG
     NLQSSRTFLR HRVMEVMPLL FELKVPRWDF QTGRQLRTSP LYDRLDTQGA RWMEKHGFER
     PKYFIPPGKD LLSLDQSKTF YKPDWFDIVG AEVKCCKEAV CVIDMSSFTK FELTSTGDQA
     LELLQYLCAN DLDVPVGHIV HTGMLNERGG YENDCSVVRL SKNSFFIISP TDQQVHCWSW
     IKKHMPNDPH LHLEDVSWKY TALNLIGPRA MDVLAELSYV SMTPDHFPSM FCKVGKKGLS
     LIRSVVCSVA
//