ID   GCSP_RALSO              Reviewed;         982 AA.
AC   Q8XU98;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, 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=RSc3295;
GN   ORFNames=RS02524;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; 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; AL646052; CAD17083.1; -; Genomic_DNA.
DR   RefSeq; WP_011003179.1; NC_003295.1.
DR   AlphaFoldDB; Q8XU98; -.
DR   SMR; Q8XU98; -.
DR   STRING; 267608.RSc3295; -.
DR   PRIDE; Q8XU98; -.
DR   EnsemblBacteria; CAD17083; CAD17083; RSc3295.
DR   GeneID; 60502807; -.
DR   KEGG; rso:RSc3295; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001436; 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; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
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   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..982
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166930"
FT   MOD_RES         729
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   982 AA;  104704 MW;  F620E7238A14067A CRC64;
     MNAPHPASAA LTQTLAARPT LAELEARDAF AERHIGPSPD EQAAMLATLG YASRAALIDA
     VIPPAIRRQD GMPLGEFTQP LTEEAALAKL RGIAGQNRVV RSLIGQGYYG THTPGVILRN
     ILENPAWYTA YTPYQPEISQ GRLEAMLNFQ QMVMDLTAMD IANASMLDEA TAAAEAMTLL
     QRVGKHPSNV FFVADDVLPQ TLDVVRTRAE PIGVQVVTGP AADAAKHNAF GVLLQYPGTG
     GALLGGLSTY QALTDAVHAA GGLVVAAADL LALTLLAAPG EWGADVVIGN TQRFGVPFGF
     GGPHAGYMAV RDAFKRSMPG RLVGVTVDAQ GNPAYRLALQ TREQHIRREK ATSNICTAQV
     LLGVMASMYA VYHGPQGLKR IAQRVHRLTA TLAAGLRQIG YTLEAGAFFD TLTVATGPRT
     ANLHIAAQAH GFNLRQIDDG RLGVSLDETV TRAEVVALWE IFAHAAHAGA PDFDQVEAGI
     ADAFPASLAR QSAYLTHPVF NAHHSEHEML RYLRSLADKD LALDRTMIPL GSCTMKLNAT
     AEMLPVTWPE FANIHPFAPA DQTVGYREMI DQLEQMLCAA TGYAAVSLQP NAGSQGEYAG
     LLIIHAYHAS RGESHRDVCL IPSSAHGTNP ASAQMAGMKV VVVACDERGN VDLADLEKKA
     AEHSANLAAI MITYPSTHGV FEEGVKRVCE IVHSHGGQVY VDGANMNAMV GTAAPGHFGG
     DVSHLNLHKT FCIPHGGGGP GVGPVAVGAH LAPFLPGRAA SGEDASQNIG AVSAAPFGSA
     SILPISWMYI AMMGAAGLTA ATEAAILSAN YVARRLSPYY PVLYTGAHGL VAHECILDIR
     PLQKESGISN EDIAKRLMDF GFHAPTMSFP VPGTLMIEPT ESEPKVELDR FIDAMIAIRG
     EVDQVISGAF DREDNPLKHA PHTAQVVMAD DWSHRYTREQ AAYPVASLRT RKYWPPVGRA
     DNVYGDRNLF CACVPMSEYA QD