ID   GCSP_CUPMC              Reviewed;         974 AA.
AC   Q1LHM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, 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};
GN   OrderedLocusNames=Rmet_3482;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(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; CP000352; ABF10354.1; -; Genomic_DNA.
DR   RefSeq; WP_011517911.1; NC_007973.1.
DR   AlphaFoldDB; Q1LHM2; -.
DR   SMR; Q1LHM2; -.
DR   STRING; 266264.Rmet_3482; -.
DR   KEGG; rme:Rmet_3482; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   Proteomes; UP000002429; Chromosome.
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; Reference proteome.
FT   CHAIN           1..974
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045598"
FT   MOD_RES         720
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   974 AA;  104819 MW;  F79B97D16F9279DC CRC64;
     MNAPLPMNAA AQGARPTLAE LEARDAFAAR HIGPDSAEQQ HMLKVLGFES RAALIDAVVP
     AAIRRRDGMS LGEFTAPLTE EAALGRLRAL AGKNRVLKSF IGQGYYNTLT PGVILRNIFE
     NPAWYTAYTP YQPEISQGRL EAMLNFQQMI TDLTGLDIAN ASMLDEGTAA AEAMTLLQRV
     NKHASNTFYV AEDVLPQTLE VVRTRALPLG IEVKVGPAAD AAQAHAFGVL LQYPGVNGDV
     ADYRAIAEAV HASGGRVVAA ADLLALTLIA APGEWGADVT VGNSQRFGVP LGFGGPHAGY
     MAVKDEFKRS MPGRLVGVTI DAQGNKAYRL ALQTREQHIR REKATSNICT AQVLLAVMAS
     MYAVYHGPQG LKRIAQRVHR LTATLAAGLK TLGHTPLNAT FFDTLTLETG FNTDAFHASA
     TARGINLRHV DATRIGISFD ETASRDDVIA LWEIFAHGKA VPDFDTIEAS VQDGFPATLA
     RQSAYLTHPV FNTHHAEHEM LRYLRALADK DLALDRTMIP LGSCTMKLNA TSEMIPVTWP
     EFSNIHPFAP LDQTVGYREM IDQLEAMLCA ATGYAAVSLQ PNAGSQGEYA GLLIIHAYHA
     SRGESHRDIC LIPSSAHGTN PASAQMAGMK VVVVACDENG NVDLADLAKK AEQHSKNLAA
     IMITYPSTHG VFEQGVQQIC DIVHKHGGQV YVDGANMNAM VGVAAPGQFG GDVSHLNLHK
     TFCIPHGGGG PGVGPVAVGA HLADFLPNQD SVGYRRDENG IGGVSAAPFG SASILPISWM
     YIAMMGSAGL TAATENAILT ANYVARRLSP HFPVLYTGQH GLVAHECILD LRPLQKATGI
     SNEDVAKRLM DYGFHAPTMS FPVPGTLMIE PTESEALHEL DRFIDAMIAI RGEIARVEDG
     SFDREDNPLK HAPHTAAVVV SDKWNHKYTR EEAAYPVASL RTQKYWPPVG RADNVYGDRN
     LFCSCVPLSE YAED
//