ID B9RRS7_RICCO Unreviewed; 1057 AA.
AC B9RRS7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=RCOM_0797460 {ECO:0000313|EMBL:EEF45787.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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|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 EMBL; EQ973807; EEF45787.1; -; Genomic_DNA.
DR RefSeq; XP_002516446.1; XM_002516400.2.
DR AlphaFoldDB; B9RRS7; -.
DR STRING; 3988.B9RRS7; -.
DR GeneID; 8275599; -.
DR KEGG; rcu:8275599; -.
DR eggNOG; KOG2040; Eukaryota.
DR InParanoid; B9RRS7; -.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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 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:UP000008311};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 100..526
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 543..819
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 870..991
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 18..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 792
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1057 AA; 114826 MW; 6BD130DA081CF60A CRC64;
MERARKLANR AILKRLVNES KPHKHHSRNE SSATTLLNSS SSPILYTPSR YVSSLSSFAS
RNPRSGSLPG TKSIGYYGIG SQVRSISVES LKPSDTFPRR HNSATAEEQS KMAELCGFDN
LDSLIDATVP KSIRIDSMKF SKFDNGLTES QMIEHMQDLA SKNKVFKSYI GMGYYNTHVP
PVILRNIMEN PAWYTQYTPY QAEISQGRLE SLLNYQTMIT DLTGLPMSNA SLLDEGTAAA
EAMAMCNNIL KGKKKTFIIA NNCHPQTIDI CKTRADGFDI KVVTMDLKDI NYKSGDVCGV
LLQYPGTEGE VLDYEEFIKN AHANGVKVVM ASDLLALTML KPPGELGADI VVGSAQRFGV
PMGYGGPHAA FLATSQEYKR LMPGRIIGLS VDSSGKPALR MAMQTREQHI RRDKATSNIC
TAQALLANMA AMFAVYHGPE GLKAIAQRVH GLAGALALGL KKLGTVEIQG LPFFDTVKIK
CANAQAIADA AYKNEINLRV VDANTITVSL DETTTLEDVD NLFKVFGDGK PVPFSAASLA
PDVQNAIPSK LIRESPFLAH PIFNMYHTEH ELLRYIHKLQ SKDLSLCHSM IPLGSCTMKL
NATAEMMPVT WPNFTNIHPF APVDQAQGFQ EMFDNLGDLL CTITGFDSFS LQPNAGAAGE
YAGLMVIRAY HKSRGDHHRN VCIIPVSAHG TNPASAAMCG MKIVAVGTDA KGNINIEELK
KAAEANRDNL SALMVTYPST HGVYEEGIDE ICKIIHDNGG QVYMDGANMN AQVGLTSPGF
IGADVCHLNL HKTFCIPHGG GGPGMGPIGV KKHLAPFLPS HPVISTGGIP APDNAQPLGT
ISAAPWGSAL ILPISYTYIA MMGSQGLTDA SKIAILNANY MAKRLENYYP VLFRGVNGTC
AHEFIIDLRG FKNTAGIEPE DVAKRLMDYG FHAPTMSWPV PGTLMIEPTE SESKAELDRF
CDALISIREE IAEIENGKAD VHNNVLKGAP HPPSLLMGDA WTKPYSREYA AFPASWLRGA
KFWPTTGRVD NVYGDRNLIC TLLPASQYVE EQAAASA
//
