ID   GCSP_RALPJ              Reviewed;         979 AA.
AC   B2UG82;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=Rpic_3489;
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001068; ACD28609.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UG82; -.
DR   SMR; B2UG82; -.
DR   STRING; 402626.Rpic_3489; -.
DR   KEGG; rpi:Rpic_3489; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_4; -.
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..979
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132447"
FT   MOD_RES         726
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   979 AA;  104515 MW;  15C07551CAFF0841 CRC64;
     MNAPHPASSA LAAERPTLAD LEARDAFAHR HIGPSADEQT AMLGTLGYTS RAALIDAVIP
     PAIRRQDGMP LGEFTQPLTE EAALAKLRGI AGQNRVVKSL IGQGYYGTHT PGVILRNILE
     NPAWYTAYTP YQPEISQGRL EAMLNFQQMV IDLTAMDIAN ASMLDEATAA AEAMTLLQRI
     GKSKSTVFFV ADDVLPQTLE VVRTRAEPIG VQVVTGPAAD AAKHDAFGVL LQYPGANGAL
     LGDLATYQAL TDAVHAAGGL VVAAADLLAL TLLAAPGEWG ADVVIGNTQR FGVPFGFGGP
     HAGYMAVRDA FKRSMPGRLV GVTIDAQGNP AYRLALQTRE QHIRREKATS NICTAQVLLG
     VMASMYAVYH GPQGLKRIAQ RVHRLSATLA AGLRAIGYTL ESDAFFDTLT VVTGPRTANL
     HIAAQAHGIN LRQIDDARLG ISLDETVTRA DVVALWEVFA HAAHAAAPDF DQTEAGVADA
     YPASLVRQSA YLTHPVFNAH HSEHEMLRYL RSLADKDLAL DRTMIPLGSC TMKLNATAEM
     LPVTWPEFSN IHPFAPADQT VGYREMIDQL EQMLCAATGY AAVSLQPNAG SQGEYAGLLI
     IHAYHASRGE AHRNVCLIPS SAHGTNPASA QMAGMQVVVV ACDERGNVDL ADLEKKAAEH
     SKNLAAIMIT YPSTHGVFEE GVKRVCEIVH SHGGQVYVDG ANMNAMVGTA APGHFGGDVS
     HLNLHKTFCI PHGGGGPGVG PVAVGAHLAP FLPGRAASGE DASQNIGNVS ASAFGSASIL
     PISWMYIAMM GAAGLTAATE TAILSANYVA KRLAPYYPVL YTGAHGLVAH ECILDIRPLQ
     KESGISNEDI AKRLMDFGFH APTMSFPVPG TLMIEPTESE PKVELDRFID AMIAIRGEVD
     KVISGEFDRE DNPLKHAPHT AAVVMADDWS HKYTREQAAY PVASLRARKY WPPVGRADNV
     YGDRNLFCAC VPMSEYAQD
//