ID A0A2Y9EHS5_PHYMC Unreviewed; 878 AA.
AC A0A2Y9EHS5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial {ECO:0000313|RefSeq:XP_007102635.2, ECO:0000313|RefSeq:XP_007102636.2};
GN Name=PDPR {ECO:0000313|RefSeq:XP_007102635.2,
GN ECO:0000313|RefSeq:XP_007102636.2, ECO:0000313|RefSeq:XP_007102637.2,
GN ECO:0000313|RefSeq:XP_023980621.1, ECO:0000313|RefSeq:XP_054934842.1,
GN ECO:0000313|RefSeq:XP_054934843.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007102635.2};
RN [1] {ECO:0000313|RefSeq:XP_007102635.2, ECO:0000313|RefSeq:XP_007102636.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007102635.2,
RC ECO:0000313|RefSeq:XP_007102636.2};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_007102635.2; XM_007102573.4.
DR RefSeq; XP_007102636.2; XM_007102574.4.
DR RefSeq; XP_007102637.2; XM_007102575.4.
DR RefSeq; XP_023980621.1; XM_024124853.3.
DR RefSeq; XP_054934842.1; XM_055078867.1.
DR RefSeq; XP_054934843.1; XM_055078868.1.
DR STRING; 9755.ENSPCTP00005016248; -.
DR KEGG; pcad:102990415; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000248484; Chromosome 17.
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 Pyruvate {ECO:0000313|RefSeq:XP_007102635.2,
KW ECO:0000313|RefSeq:XP_007102636.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT DOMAIN 44..87
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 878 AA; 99435 MW; D6039E7F110B5FCB CRC64;
MFYRLLSVVR RPRSSQGWQK WSSARSGASA AKAHSVALPA QAQVVICGGG IMGTSVAYHL
SKMGWKDIVL LEQGRLAAGS TRFCAGILST ARHLTIEQKM ADYSNKLYHQ LEQETGIHTG
YIRTGSIFLA QTQDRLISLK RINSRLNVIG IPSEIISPKK VAELHPLLNV HDLVGAMHVP
EDAVVSSADV ALALASAASQ NGVQIYDRTS ILHVMVRKGQ VTGVETDKGQ IQCHYFVNCA
GQWAYELGLS NEEPVSIPLH ACEHFYLLTR PWETPLQSNA PTIVDADGRI YIRNWQGGIL
SGGFEKNPKP IFTEGKNQLE IQNLQEDWDH FEPLLSSLLR RMPELETLEI MKLVNCPETF
TPDMRCIMGE SPSVRGYFVL VGMNSAGLSF GGGAGRYLAE WMVHGYPSES VWELDLKRFG
ALQSSRTFLR HRVMEVMPLL YDLKVPRWDF QTGRQLRTSP LYDRLDAQGA RWMEKHGFER
PKYFVPPDKD LLALEQSKTF YKPDWFEIVE SEVKCCKEAV CVIDMSSFTK FEITSTGDQA
LEILQYLFSN DLDVPVGHIV HTGMLNEGGG YENDCSIARL SKRSFFMISP TDQQVHCWAW
LKKYMPEDSN LILEDVTWKY TALNLIGPRA VDVLSELSYA PMTPDHFPSL FCKEMSVGYA
NGIRVMSMTH TGEPGFMLYI PIEYALHVYN EVMSVGQKYG IRNAGYYALR SLRIEKFFAF
WGQDLNTLTT PLECGRESRV KLDKGMDFIG RDALLQQKQN GVYKRLTMFI LDDHDTDLDL
WPWWGEPIYR NGQYVGKTTS SAYGYTLERH VCLGFVHNFS EDTGEEQVVT ADFINRGEYE
IDIAGHRFQA KAKLYPVTSL FTHKRRKDDV ELSDLHGK
//