ID I1NR70_ORYGL Unreviewed; 1017 AA.
AC I1NR70;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
OS Oryza glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA01G0236000.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA01G0236000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; I1NR70; -.
DR STRING; 4538.I1NR70; -.
DR EnsemblPlants; ORGLA01G0236000.1; ORGLA01G0236000.1; ORGLA01G0236000.
DR Gramene; ORGLA01G0236000.1; ORGLA01G0236000.1; ORGLA01G0236000.
DR eggNOG; KOG2040; Eukaryota.
DR HOGENOM; CLU_004620_1_1_1; -.
DR OMA; RNLICTC; -.
DR Proteomes; UP000007306; 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; 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 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; 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|RuleBase:RU364056};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 75..502
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 829..951
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 20..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 110034 MW; 07739D3DC7803231 CRC64;
MERARRLANR ALLRRLLAAA ASTTSPAPSR GISTLAKAPG AGSRPRAPRP APHQYTTGRP
VSASALQPSD TFPRRHNSAT PAEQAAMASE CGFNTLDALI DATVPAAIRA PTMHFSGKFD
AGFTESQMID HMQRLAAMNK AYKSFIGMGY YNTHVPAVIL RNLMENPAWY TQYTPYQAEI
AQGRLESLLN YQTMVADLTG LPMSNASLLD EATAAAEAMA MCNGILKSKK KTFLIASNCH
PQTIDVCQTR AAGFDLNVIV ADAKDFDYSS GDVCGVLVQY PGTEGEVLDY AEFVKDAHAH
GVKVVMATDL LALTSLRPPG EIGADIAVGS AQRFGVPMGY GGPHAAFLAT SQEYKRLMPG
RIIGVSVDSS GKPALRMAMQ TREQHIRRDK ATSNICTAQA LLANMAAMYA VYHGPEGLKA
IADRVHGLAG TFAHGLKKLG TVTVQELPFF DTVKVKVADA NAIAQEACKN EMNLRVVDAT
TITVAFDETT TLEDVDKLFK VFNGGKPVNF TAESLASEVS SSIPSSLVRK SPYLTHPIFN
MYHTEHELLR YLHKLQSKDL SLCHSMIPLG SCTMKLNATV EMMPVTYPSF ANMHPFAPTE
QAAGYHEMFD DLGDLLCKIT GFDSFSLQPN AGASGEYAGL MVIRAYHRAR GDYHRDVCII
PVSAHGTNPA SAAMCGMKIV AVGTDSKGNI NIEELRKAAE ANKDNLAALM VTYPSTHGVY
EEGIDEICRI IHENGGQVYM DGANMNAQPS QDILHSTWWG GPGMGPIGVK KHLAPFLPSH
PVITTGGFPL PEKTDPLGTI SAAPWGSALI LPISYTYIAM MGSKGLTDAS KIAILNANYM
AKRLEKHYPV LFRGVNGTVA HEFIIDLRGF KTTAGIEPED VAKRLMDYGF HAPTMSWPVP
GTLMIEPTES ESKAELDRFC DALISIREEI AEIESGKADV NNNVLKQSAP HPPQLLMSDS
WTKPYSREYA AFPAAWLRGA KFWPTTCRVD NVYGDRNLIC TLQQGSQVAE EAAAATA
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