ID A0A2K6B2N0_MACNE Unreviewed; 879 AA.
AC A0A2K6B2N0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit {ECO:0000313|Ensembl:ENSMNEP00000005662.1};
GN Name=PDPR {ECO:0000313|Ensembl:ENSMNEP00000005662.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000005662.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000005662.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR AlphaFoldDB; A0A2K6B2N0; -.
DR STRING; 9545.ENSMNEP00000005662; -.
DR Ensembl; ENSMNET00000028244.1; ENSMNEP00000005662.1; ENSMNEG00000025756.1.
DR GeneTree; ENSGT00940000159082; -.
DR OMA; TKFPDRE; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000025756; Expressed in adult mammalian kidney and 12 other cell types or tissues.
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; IPR001763; Rhodanese-like_dom.
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.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 45..88
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 879 AA; 99451 MW; F0D01A1E96378326 CRC64;
VMFYRLLSIV GRQRASPGWQ NWSSARNSTS AAEARSMALP TQAQVVICGG GIMGTSVAYH
LSKMGWKDIV LLEQGRLAAG STRFCAGILS TARHLTIEQK MADYSNKLYH QLEQETGIQT
GYTRTGSIFL AQTQDRLISL KRINSRLNVI GIPSEIISPK KVAELHHLLN VHDLVGAMHV
PEDAVVSSAD VALALASAAS QNGVQIYDRT SVLHVMVKKG QVTGVETDKG QIECQYFVNC
AGQWAYELGL SNEEPVSIPL HACEHFYLLT RPLETPLQSS TPTIVDADGR IYIRNWQGGI
LSGGFEKNPK PIFTEGKNQL EIQNLQEDWD HFEPLLSSLL RRMPELETLE IMKLVNCPET
FTPDMRCIMG ESPAVQGYFV LAGMNSAGLS FGGGAGKYLA EWMVHGYPSE NVWELDLKRF
GALQSSRTFL RHRVMEVMPL MYDLKVPRWD FQTGRQLRTS PLYDRLDAQG ARWMEKHGFE
RPKYFVPPDK DLLALEQSKT FYKPDWFDIV ESEVKCCKEA VCVIDMSSFT KFEITSTGDQ
ALEVLQYLFS NDLDVPVGHI VHTGMLNEGG GYENDCSIAR LNKRSFFMIS PTDQQVHCWA
WLKKHMPKDS NLLLEDVTWK YTALNLIGPR AVDVLSELSY APMTPDHFPS LFCKEMSVGY
ANGIRVMSMT HTGEPGFMLY IPIEYALHVY NEVMSVGQKY GIRNAGYYAL RSLRIEKFFA
FWGQDINNLT TPLECGRESR VKLEKGMDFI GRDALLLQKQ NGVYKRLTMF ILDDHDTDLD
LWPWWGEPIY RNGQYVGKTT SSAYSYSLER HVCLGFVHNF SEDTGEEQVV TADFINRGEY
EIDIAGYRFQ AKAKLYPVAS LFTQKRRKDD MELSDLHGK
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