ID A0A0G4IRS1_PLABS Unreviewed; 990 AA.
AC A0A0G4IRS1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=PBRA_005963 {ECO:0000313|EMBL:CEO97849.1}, PLBR_LOCUS5284
GN {ECO:0000313|EMBL:SPQ98069.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OG Mitochondrion {ECO:0000313|EMBL:SPQ98069.1}.
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO97849.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEO97849.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEO97849.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPQ98069.1, ECO:0000313|Proteomes:UP000290189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fogelqvist J.;
RL Submitted (MAR-2018) 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; CDSF01000081; CEO97849.1; -; Genomic_DNA.
DR EMBL; OVEO01000009; SPQ98069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IRS1; -.
DR STRING; 37360.A0A0G4IRS1; -.
DR EnsemblProtists; CEO97849; CEO97849; PBRA_005963.
DR OMA; RNLICTC; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR Proteomes; UP000290189; 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; 1.
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|RuleBase:RU364056, ECO:0000313|EMBL:SPQ98069.1};
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:UP000039324};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 43..469
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 522..774
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 812..932
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 747
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 990 AA; 107896 MW; 22689FB2537D94B3 CRC64;
MHRLMAVSSA MPARAAGRCL VSRRHLSAIS MSESFLPLDT FVNRHCGSSP DEIQTMLDVV
GVNHLEGLSE QCVPKDIYLQ RLLKVPPAKG ETEALAQLHR IMSRNQVLRS HIGCGYYGTV
TPGVILRNIL ENPAWYTPYT PYQAEISQGR LEMLLNFQTM VCDLTGLPVA NASLLDEGTA
AAEAMLLAYN ACNKQAHKLL VSPKLHPQTL AVIKTRAAPF GIEVIATKPS TWPRILERGS
VFGAIVQYPS TDGVLKDWSE ECDLVHKSGG LFVVASDLLA LTVVKPPGEW GADVVVGSSQ
RFGVPMGYGG PHAAFFACRD ELKRRAPGRI IGVSRDARGQ RALRMAIQTR EQHIRRDKAT
SNICTAQALL ANVAAAYAMY HGPKGLRAIA NRAMRAAQVA RLGLEKLSYK CYGEFGSTFD
TVTFGVSDAK AFAEVGIDHG FNCRIVSDRV ASLSFDETVQ LGDLQEIYKA IGKVKDTALD
FTAADMAEVL EIDAPEACDK LYPEFVRKTP ILSHPVFNTY CNSETQMLRY LYQLQMKDLS
LASAMIPLGS CTMKLNATSE MAPITWPNVN SLHPFAPKSQ AAGYEKMLTT LKQWLCEITG
FAAVSLQPNS GAQGEYAGLL AIQAYHKSRG EAQRHVCLIP TSAHGTNPAS AALAGLSIVV
VKCDANGNVD LEDLGSKAKE HAKNLSCFMI TYPSTHGVFE STIKKCCAII HENGGQVYLD
GANMNAQVGL CRPGDYGADV CHLNLHKTFC IPHGGGGPGM GPIAVAGHLA EFLPAPEGSG
SPVASAPFSS ASILPIPWMY IRMMGPDGLR LATQMAILNA NYMATRLSKH YPILYRGENG
RVAHEFIIDL RPFKEHGVTE EDVAKRLMDY SFHGPTMSFP VPGTLMIEPT ESEPLSELDR
FCEAMISIRQ EIEDVISGRV VAEESVLKGA PHTMDVVASD NWNRKYSRET AAYPVKSLRQ
NKFWPSVARI DNVFGDRNVI CQCPPVSSYQ
//
