ID A0A3Q7HQA3_SOLLC Unreviewed; 1036 AA.
AC A0A3Q7HQA3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN Name=101260070 {ECO:0000313|EnsemblPlants:Solyc08g065220.3.1};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc08g065220.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc08g065220.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc08g065220.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc08g065220.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc08g065220.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) to UniProtKB.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000256|ARBA:ARBA00003788}.
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: Homodimer (By similarity). The glycine cleavage system is
CC composed of four proteins: P, T, L and H.
CC {ECO:0000256|ARBA:ARBA00011289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC 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 RefSeq; XP_004245101.1; XM_004245053.3.
DR AlphaFoldDB; A0A3Q7HQA3; -.
DR STRING; 4081.A0A3Q7HQA3; -.
DR PaxDb; 4081-Solyc08g065220-2-1; -.
DR EnsemblPlants; Solyc08g065220.3.1; Solyc08g065220.3.1; Solyc08g065220.3.
DR GeneID; 101260070; -.
DR Gramene; Solyc08g065220.3.1; Solyc08g065220.3.1; Solyc08g065220.3.
DR KEGG; sly:101260070; -.
DR InParanoid; A0A3Q7HQA3; -.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000004994; Chromosome 8.
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 GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd00613; GDC-P; 2.
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 HAMAP; MF_00711; GcvP; 1.
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|ARBA:ARBA00023128,
KW 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:UP000004994};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 80..506
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 518..799
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 850..971
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 772
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1036 AA; 113067 MW; 0A9F94FCBF81EADC CRC64;
MERARKLANR AILKRLVSQS KQSRSNEIPS PSSLYRPSRY VSSLSPYTFQ ARNSVKSFNT
QQVRSISVEA LKPSDTFPRR HNSATPEEQT KMAEFCGFQS LDALIDATVP QSIRSESMKL
PKFDGGLTES QMIEHMQKLA SKNKVFKSYI GMGYYNTYVP PVILRNLLEN PAWYTQYTPY
QAEISQGRLE SLLNYQTMIT DLTGLPMSNA SLLDEGTAAA EAMAMCNNIL KGKKKTFLIA
NNCHPQTIEI CKTRADGFDL KVVTVDLKDI DYKSGDVCGV LVQYPGTEGE ILDYGEFIKN
AHAHGVKVVM ASDLLALTML KPPGELGADI VVGSAQRFGV PMGYGGPHAA FLATSQEYKR
MMPGRIIGLS VDSTGKPALR MAMQTREQHI RRDKATSNIC TAQALLANMA AMYAVYHGPE
GLKTIGQRVH GLAGTFSAGL KKLGTVEVQD LPFFDTVKVK CSDAKAIADV ATKNDINVRI
VDNNTITVSF DETTTLEDVD DLFKVFALGK PVPFTAQSIA QEVENLIPSG LTRETPFLTH
QIFNSYHTEH ELLRYLHKLQ SKDLSLCHSM IPLGSCTMKL NATTEMMPVT WPSFANIHPF
APTEQAAGYQ EMFDDLGALL CTITGFDSFS LQPNAGAAGE YAGLMVIRAY HMSRGDHHRN
VCIIPVSAHG TNPASAAMCG MKIVAVGTDA KGNINIEELR KAAEAHKDNL SALMVTYPST
HGVYEEGIDE ICKIIHDNGG QVYMDGANMN AQVGLTSPGF IGADVCHLNL HKTFCIPHGG
GGPGMGPIGV KKHLAPYLPS HPVVSTGGIP SPDQSKPLGA ISAAPWGSAL ILPISYTYIA
MMGSKGLTDA SKIAILSANY MAKRLEKHYP VLFRGVNGTC AHEFIIDLRG FKNTAGIEPE
DVAKRLIDYG FHGPTMSWPV PGTLMIEPTE SESKAELDRF CDALISIREE IAQIEKGNVD
INNNVLKGAP HPPSMLMADA WTKPYSREYA AYPAPWLRSA KFWPTTGRVD NVYGDRNLIC
TLLPVSEMAE EKAATA
//
