ID R0F2S5_9BRAS Unreviewed; 1038 AA.
AC R0F2S5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Glycine cleavage system P protein {ECO:0000256|RuleBase:RU364056};
DE EC=1.4.4.2 {ECO:0000256|RuleBase:RU364056};
GN ORFNames=CARUB_v10004049mg {ECO:0000313|EMBL:EOA15952.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA15952.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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; KB870811; EOA15952.1; -; Genomic_DNA.
DR RefSeq; XP_006283054.1; XM_006282992.1.
DR AlphaFoldDB; R0F2S5; -.
DR STRING; 81985.R0F2S5; -.
DR GeneID; 17877678; -.
DR KEGG; crb:17877678; -.
DR eggNOG; KOG2040; Eukaryota.
DR OrthoDB; 177349at2759; -.
DR Proteomes; UP000029121; 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 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:UP000029121};
KW Transit peptide {ECO:0000256|RuleBase:RU364056}.
FT DOMAIN 83..509
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 523..802
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 853..974
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 775
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1038 AA; 113147 MW; 87B66B9970930DE0 CRC64;
MERARRLAYR GIVKRLVNEA KRHRNPETPH LVVPHAPARY VSSLSPFVST HRSPASFGRH
HSHQQTRPIS VEALQPGDTF PRRHNSATPD EQSHMAKFCG FDHIDSLVDA TVPKSIRLDS
MKFSKFDGGL TESQMIEHMV DLASKNKIFK SFIGMGYYNT YVPPVILRNI MENPAWYTQY
TPYQAEISQG RLESLLNFQT VITDLTGLPM SNASLLDEGT AAAEAMAMCN NIQKGKKKTF
LIASNCHPQT IDICKTRAGG FDLKVLSADL KDIDYSSGDV CGVLVQYPGT EGEVLDYAEF
VKTAHANGVK VVMATDLLAL TMLKPPGELG ADIVVGSAQR FGVPMGYGGP HAAFLATSQE
YKRMMPGRII GVSVDSSGKQ ALRMAMQTRE QHIRRDKATS NICTAQALLA NMAAMYAVYH
GPAGLKSIAQ RVHGLAGVFA LGLKKLGVAE VQELPFFDTV KIKCSDAHAV ADAAAKSEIN
LRVVDSNTIT ASFDETTTLD DVDKLFKVFA SGKPVPFTAE SLAPEVQNAI PSSLTRESPY
LTHPIFNMYH TEHELLRYIH KLQNKDLSLC HSMIPLGSCT MKLNATTEMM PVSWPSFTDI
HPFAPVEQAQ GYHEMFENLG DLLCTITGFD SFSLQPNAGA AGEYTGLMVI RAYHMSRGDH
HRNVCIIPVS AHGTNPASAA MTGMKIITVG TDAKGNINIE EVRKAAEANK DNLAALMVTY
PSTHGVYEEG IDEICNIIHE FGGQVYMDGA NMNAQVGLTS PGFIGADVCH LNLHKTFCIP
HGGGGPGMGP IGVKKHLAPF LPSHPVISTG GFPQPEKTEP LGTIAAAPWG SALILPISYT
YIAMMGSGGL TDASKIAILN ANYMAKRLEK HYPVLFRGAN GTVAHEFIID LRAFKNTAGI
EAEDVAKRLM DYGFHAPTMS WPVPGTLMIE PTESESKAEL DRFCDALISI REEIAQIEKG
NADVQNNVLK GAPHPQSVLM ADTWNKPYSR EYAAFPAPWL RSSKFWPITS RVDNVYGDRK
LVSTLLAEEE QVAAAVSA
//
