ID   GCSP_CUPPJ              Reviewed;         976 AA.
AC   Q46VZ5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=Reut_A3331;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000255|HAMAP-Rule:MF_00711}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
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DR   EMBL; CP000090; AAZ62689.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46VZ5; -.
DR   SMR; Q46VZ5; -.
DR   STRING; 264198.Reut_A3331; -.
DR   KEGG; reu:Reut_A3331; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_4; -.
DR   OrthoDB; 9801272at2; -.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..976
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227123"
FT   MOD_RES         722
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   976 AA;  105208 MW;  37C1F8DEB02584C3 CRC64;
     MNAPLPMTAT QGNRPTLAEL EARDAFAARH IGPDTPEQQH MLKVLGYDSR AALIDAVIPE
     AIRRRDGMPM GEFTEPLPEE AALAKLRKLA GKNKVLKSFI GQGYYNTLTP AVVLRNIFEN
     PAWYTAYTPY QPEISQGRLE AMLNFQQMVT DLTGLDIANA SMLDEGTAAA EAMTLLQRVN
     KHASNTFYVA DDVLPQTLEV VRTRAKPLGI EVKVGPAADA AAAHAFGVLL QYPGVNGDVT
     DYRAIADAVH AAGGLVVAAA DLLALTLITA PGEWGADVAV GNSQRFGVPL GFGGPHAGYM
     AVKDAFKRSM PGRLVGVTVD AQGNKAYRLA LQTREQHIRR EKATSNICTA QVLLAVMASM
     YAVYHGPQGL KRIAQRVHRL TATLAAGLQT LGFTRTNATF FDTLTFETGF NTDAIHAAAT
     ARGINLRHAG ATRIGVSLDE TATRDDVVAL WEIFSHGKPL PASLTFDAIE AAAEDAFPAN
     LARTSAYLTH PVFNTHHAEH EMLRYLRMLA DKDLALDRTM IPLGSCTMKL NATSEMIPVT
     WPEFSQIHPF APLDQTVGYR EMIDQLEAML CAATGYAAVS LQPNAGSQGE YAGLLIIHAY
     HASRGESHRD ICLIPSSAHG TNPASAQMAG MKVVVVACDE NGNVDLEDLA KKAELHSKNL
     AAIMITYPST HGVFEQGVQQ ICEIVHQHGG QVYVDGANMN AMVGTAAPGH FGGDVSHLNL
     HKTFCIPHGG GGPGVGPVAV GAHLADFLPN QDSVGYRRDD NGIGGVSAAP FGSASILPIS
     WMYIAMMGSA GLTAATENAI LTANYVAKRL SPHYPVLYTG QHGLVAHECI LDLRPLQKET
     GISNEDVAKR LMDYGFHAPT MSFPVPGTLM IEPTESEALH ELDRFIDAMI AIRKEIGRVE
     DGSFDRDDNP LKHAPHTAAV VTANEWTRKY TREEAAYPVA SLRTQKYWPP VGRADNVYGD
     RNLFCSCVPM SEYAQD
//