ID A0A078B105_STYLE Unreviewed; 1045 AA.
AC A0A078B105;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=Contig3514.g3755 {ECO:0000313|EMBL:CDW88016.1};
GN ORFNames=STYLEM_17131 {ECO:0000313|EMBL:CDW88016.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW88016.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW88016.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW88016.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; CCKQ01016138; CDW88016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078B105; -.
DR EnsemblProtists; CDW88016; CDW88016; STYLEM_17131.
DR InParanoid; A0A078B105; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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:UP000039865};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 84..523
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 562..823
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 866..986
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 794
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1045 AA; 116385 MW; E98C01FB093D3F0B CRC64;
MLSKHFTELK RLAINQTHTS KLLSTFQNVK LTNTQLRPFA KNVNSTLHHK NKLQVSQHIL
SKNLSYLQNN KISQALKPSD NFPQRHLGND KKNTQEILNT LGVQTIEELM DQVVPSNIRL
KSGSAFIHNG KELHGIESET MLLANLRDLA NTNKVFRSFQ GTGYYPTNLP SVIRRNVLEN
PNWYTPYTPY QAEIAQGRLE SLLNYQTMIT ELTKLDVSNA SLLDEATSAA EAMFMAYNVH
DGKRRKFFVS SSMFPQNIDV VKTKAFGLNI ELVIDEPANF DWSKANEFCG FMLQNPDNLG
NVSNISELTQ KLRDNKIVSV VIADILSLAV IKPPGEMGVD IAVGSVQRFG VPMAFGGPHP
GYMACRDEFK RKMPGRLIGV SKDSHGDKAY RMALQTREQH IRRDKATSNI CTAQALLANI
SAFFGQWYGP EGLKKQAERV QYFSEILIDE LSSLGYTIVT DKNNHFDTVT IDAKKSGVSS
SDAVLHEFEK YGINLRKIDD SLVSLAFNET TSLIDLDEVI EIFADLKGNQ TTQGFLTQEF
YEKRQYRGPS ANLKRKSAFM TQPQFNEITS ETQMMRYIQR LADKDIGLTN SMIALGSCTL
KLNSAISMIP ITWAGFAGIH PFAPKDQVKG YMKLIKELED DLVAITQYDA ISLQPNSGAN
GEYAGLMAIK KYHESRGDLQ RDICLIPVSA HGTNPASAAL CNMKIVVVKC DANGNIDVQD
LKQKAEEHKD KLAAFMITYP STHGVFEAAV IEMCDIIHKN GGQVYMDGAN FNAQMGLTSP
GFVGADVGHL NLHKTFSIPH GGGGPGVGPI GVKKHLEPFM PGHPLIPVNG RNSLAVAAAP
YGSAGILPIP YAYIKMMGKQ GLLDSSRHAI MSANYIAKQL EGDYKILYTG QNGRVAHEFI
LDMRDFKKTS DVTETDIAKR LMDYGFHAPT VSFPVPGSLM IEPTESEDKV EMDRFIDAMR
RIRQEIREIE EGKADRVDNV IKNSPHTLKH LICHDWTHSY SREKAAYPAP WLHTRGKVYP
AVGRIDNVHG DRNLICTCPP VTDFL
//
