ID H0ZNQ2_TAEGU Unreviewed; 560 AA.
AC H0ZNQ2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial {ECO:0000256|ARBA:ARBA00040842};
DE EC=3.1.3.43 {ECO:0000256|ARBA:ARBA00038972};
DE AltName: Full=Protein phosphatase 2C {ECO:0000256|ARBA:ARBA00041989};
DE AltName: Full=Pyruvate dehydrogenase phosphatase catalytic subunit 1 {ECO:0000256|ARBA:ARBA00041690};
GN Name=PDP1 {ECO:0000313|Ensembl:ENSTGUP00000012229.1};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000012229.1, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000012229.1, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000012229.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mitochondrial enzyme that catalyzes the dephosphorylation and
CC concomitant reactivation of the alpha subunit of the E1 component of
CC the pyruvate dehydrogenase complex (PDC), thereby stimulating the
CC conversion of pyruvate into acetyl-CoA.
CC {ECO:0000256|ARBA:ARBA00043921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha
CC subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] +
CC phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-
CC COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.43;
CC Evidence={ECO:0000256|ARBA:ARBA00043727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12670;
CC Evidence={ECO:0000256|ARBA:ARBA00043727};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC subunit. {ECO:0000256|ARBA:ARBA00038577}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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DR AlphaFoldDB; H0ZNQ2; -.
DR STRING; 59729.ENSTGUP00000037158; -.
DR Ensembl; ENSTGUT00000012363.2; ENSTGUP00000012229.1; ENSTGUG00000011869.2.
DR GeneTree; ENSGT00940000156368; -.
DR HOGENOM; CLU_021928_0_0_1; -.
DR OMA; DVRTPPY; -.
DR TreeFam; TF313505; -.
DR Proteomes; UP000007754; Chromosome 2.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832:SF627; [PYRUVATE DEHYDROGENASE [ACETYL-TRANSFERRING]]-PHOSPHATASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT DOMAIN 133..547
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 560 AA; 63349 MW; C03FDF6F0FE01D27 CRC64;
MCVCPGPRRI AIPVRSSRLP LLSDAMPAPA HLFPLIRNCE ISRIGSTACY CHHKHLCCLS
SHFAHSHFRY APQKKFAALY RPKEHFNHFI HARDYASTPQ RFYLTPAQVN SILKANEYSF
KVPEFDGKNV SSVLGFDSNQ LPANAPIEDR RSAATCLQTR GMLLGVFDGH AGCACAQAVS
ERLFYYIAVS LLPHETLLEI ENAVENGRAL LPILQWHKHP NDYFSKEASK LYFNSLRTYW
QELIDLNSGE TTDVREALIN AFKRLDNDIS LEAQVGDPNS FLNYLVLRVA FSGSTACVAH
VDGVDLHIAN TGDSRAMLGV QEEDGSWSAV NLSYDHNAQN ENEVERVKME HPKSEEKSLV
KQDRLLGLLM PFRAFGDVKF KWSIELQKRV VESGPDQLND NEYTKFIPPN YHTPPYLTAE
PEVIHHKLRP QDKFLVLATD GLWETMHRQD VARIVGEYLT GVHHQQPIAV GGYKVTLGQM
HGLLTERRAK ISSVFEDQNA ATHLIRHAVG NNEFGTVDHE RLSKMLSLPE ELARMYRDDI
TIIVVQFNSH VIGAYQNEEL
//
