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Database: UniProt
Entry: A0CUD3_PARTE
LinkDB: A0CUD3_PARTE
Original site: A0CUD3_PARTE 
ID   A0CUD3_PARTE            Unreviewed;       972 AA.
AC   A0CUD3;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE            EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN   ORFNames=GSPATT00010600001 {ECO:0000313|EMBL:CAK74400.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK74400.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK74400.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK74400.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|RuleBase:RU364056}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00043839,
CC         ECO:0000256|RuleBase:RU364056};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603437-50, ECO:0000256|RuleBase:RU364056};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|RuleBase:RU364056}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC       ECO:0000256|RuleBase:RU364056}.
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DR   EMBL; CT868185; CAK74400.1; -; Genomic_DNA.
DR   RefSeq; XP_001441797.1; XM_001441760.1.
DR   AlphaFoldDB; A0CUD3; -.
DR   STRING; 5888.A0CUD3; -.
DR   EnsemblProtists; CAK74400; CAK74400; GSPATT00010600001.
DR   GeneID; 5027582; -.
DR   KEGG; ptm:GSPATT00010600001; -.
DR   eggNOG; KOG2040; Eukaryota.
DR   HOGENOM; CLU_004620_3_2_1; -.
DR   InParanoid; A0CUD3; -.
DR   OMA; DEHCHPQ; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|RuleBase:RU364056};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364056};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50,
KW   ECO:0000256|RuleBase:RU364056};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT   DOMAIN          40..464
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          478..755
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          792..912
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         726
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   972 AA;  108867 MW;  EEE5FEBD92A12AF3 CRC64;
     MLRSIRLIQR VANFSRLANP HEVNPKVPDW FKSSDYMEPR FIGSESQQVN EMLKAVEAKS
     LDELVDKIIP KEIRSEAAFQ SPDNFPDAIP ESAMVQHLQS LANKNKLYKN YIGQGFYGTH
     TPYVILRNVL EDPGWYTSYT PYQAEISQGR LEALLNYQTV ITELTGMDVS NASLLDEATA
     AGEAMFLANS WFEKKKFFVD NHVFPQSIDH IKTKAYYLGI DIVVGDAKTY DFKDADQYCG
     VLVQSPDNLG EVHDWSDLFK HTLKDAKLLK VIGTDLLSLA INKTPKDQGA NVTYGNSQRF
     GVPMGFGGPH AAFFAVEDEF KRKMPGRIIG ISKDANGKSA YRMSLQTREQ HIRREKATSN
     ICTAQALLAN MAGFYATYHG PQGLQKIANR VNCLARSFAK LAKSLGLVVK EGRIFDTVVL
     HNTETLQEYL HYNAQTNVRK IGQDTIFSFD ETHTVQDVED LFNHLQHYTK KKADFMSVIQ
     KVIPYKSERA PFLQQKVFNS LHSETEMLRY INYLRQKDVS LTKSMISLGS CTMKLNPTSF
     MLPVSFQGFS QLHPFSPLSC TQGYQELTEN VEKWLCDITQ LEAVSLMPNS GAQGEYTGLL
     CIRKYHIMNG QKDRNICLIP ISAHGTNPAS AVLAGLTVVP VNVVDGYVDL NDLNKKIKEN
     EKSLACIMIT YPSTYGVYED QTKKIIQLIH EHGGLVYMDG ANMNAQVGYT SPGYLGADVC
     HLNLHKTFSI PHGGGGPGLG PIAVNKKLAP YLPGREHSLG SVASSLFSSA SILPIPYSYF
     GQLGRQGAKK CTAMAMLNAN YLMKSLKDDY KVLFTGQNGM CAHEFIIDIR PIKQESGITE
     EDIAKRLMDY GFHAPTMSFP VPGTLMIEPT ESESKSELDR FIEAMKNIKL EIEKVKNGQY
     DKNDNPLKNA PHTQDQVINS GWSHKYSREE AAFPLPYVLQ RGKVWPTVSR INNAFGDRNL
     ICQCPSVSDY QQ
//
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