ID A0A0E0FS11_ORYNI Unreviewed; 892 AA.
AC A0A0E0FS11;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA01G32380.3};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA01G32380.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G32380.3};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA01G32380.3}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA01G32380.3};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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|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|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 AlphaFoldDB; A0A0E0FS11; -.
DR EnsemblPlants; ONIVA01G32380.3; ONIVA01G32380.3; ONIVA01G32380.
DR Gramene; ONIVA01G32380.3; ONIVA01G32380.3; ONIVA01G32380.
DR Proteomes; UP000006591; 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; 1.
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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 3.
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|RuleBase:RU364056};
KW Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 73..500
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 745..847
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 20..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 96862 MW; C8BEE467FAF463D7 CRC64;
MERARRLANR ALLRRLLAAA ASTTSPAPSR GISTLAKGSR PRAPPRPAPH QYTTGRRPVS
ASALQPSDTF PRRHNSATPA EQAAMASECG FNTLDALIDA TVPAAIRAPT MHFSGKFDAG
FTESQMIDHM QRLAAMNKAY KSFIGMGYYN THVPAVILRN LMENPAWYTQ YTPYQAEIAQ
GRLESLLNYQ TMVADLTGLP MSNASLLDEA TAAAEAMAMC NGILKSKKKT FLIASNCHPQ
TIDVCQTRAA GFDLNVIVAD AKDFDYGSGD VCGVLVQYPG TEGEVLDYAE FVRDAHAHGV
KVVMATDLLA LTSLRPPGEI GADIAVGSAQ RFGVPMGYGG PHAAFLATSQ EYKRLMPGRI
IGVSVDSSGK PALRMAMQTR EQHIRRDKAT SNICTAQALL ANMAAMYAVY HGPEGLKAIA
DRVHGLAGTF AHGLKKLGTV TVQELPFFDT VKVKVADANA IAQEACKNEM NLRVVDATTI
TVAFDETTTL EDVDKLFKVF NGGKPVNFTA ESLVSEVSSS IPSSLVRKSP YLTHPIFNMY
HTEHELLRYL HKLQSKDLSL CHSMIPLGSC TMKLNATVEM MPVTYPSFAN MHPFAPTEQA
AGYHEMFDDL GDLLCKITGF DSFSLQPNAG ASGEYAGLMV IRAYHRARGD YHRDVCIIPV
SAHGTNPASA AMCGMKIVAV GTDSKGNINI EELRKAAEAN KDNLAALMVT YPSTHGVYEE
GIDEICMIIH ENGGQVYMDG ANMNAQKHYP VLFRGVNGTV AHEFIIDLRG FKTTAGIEPE
DVAKRLMDYG FHAPTMSWPV PGTLMIEPTE SESKAELDRF CDALISIREE IAEIESGKAD
VNNNVLKVKY QYTAICFHIL DCRVDNVYGD RNLICTLQQG SQVAEEAAAA TA
//
