ID   GCSP_RHOP5              Reviewed;         961 AA.
AC   Q07R90;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=RPE_1595;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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=(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; CP000463; ABJ05544.1; -; Genomic_DNA.
DR   RefSeq; WP_011663030.1; NC_008435.1.
DR   AlphaFoldDB; Q07R90; -.
DR   SMR; Q07R90; -.
DR   STRING; 316055.RPE_1595; -.
DR   PRIDE; Q07R90; -.
DR   EnsemblBacteria; ABJ05544; ABJ05544; RPE_1595.
DR   KEGG; rpe:RPE_1595; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
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.
FT   CHAIN           1..961
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045601"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   961 AA;  103714 MW;  1DDFC24A10AD6A57 CRC64;
     MPVSRSPIED LANGFARRHI GPSPQEIAAM LRAVGAPSLD ALMGETLPAA IRQAKPLDLG
     PALSEPEALA HMAELAAKNQ VFTSLIGQGY YGTAMPTVIQ RNILENPAWY TAYTPYQPEI
     SQGRLEALFN FQTMICDLTG LDVANASLLD EGTAAAEAMA LAERAMPKKT KAFFVDRDTH
     PQTLAVLRTR AEPLGWQIIV GDPVSDLQKA DVFGALLQYP GSSGALRDPR PMIAALHAKG
     GLAVIAADLL ALTLLASPGD LGADIAIGSA QRFGVPMGYG GPHAGFMAVR DSLKRALPGR
     IVGQSIDSHG QPAYRLALQT REQHIRREKA TSNICTAQVL LAVLASMYAV YHGPEGLSAI
     ARSIHRKTAV LAAGLRKLGF TTRNEAFFDT ITVDVGDKQS EIIARARDEN INLRIGDGTL
     GLSLDETTTP KIVEAVWRAF GGALSYAEIE PAMRDALHPT LKRTSPFMTQ EVFHLYRSET
     ELLRYMRKLS DRDLALDRAM IPLGSCTMKL NATTEMMPLS LPGFAHLHPF APPEQALGYH
     ALFDKLETWL AEITGYDAVS LQPNSGAQGE YAGLLAIRGY YKSRGEPHRK ICLIPSSAHG
     TNPASAAMAG MEVVVVECND RGDVDVDDLR ARAELHSPNL AAVMITYPST HGVFEEHIRD
     ICDIVHAHGG QVYLDGANLN AQVGLARPGE YGADVSHINL HKTFAIPHGG GGPGMGPIGV
     KAHLAPFLPG HPCCDDTGPD GFSHGGGTVA AAPWGSASVL TISYVYILLM GGDGLKRATE
     VAILNANYVA AKLDPHFPVL YKNERGRVAH ECIVDPRALK NSSGVTVDDI AKRLIDYGFH
     APTMSFPVVG TLMIEPTESE SKAELDRFCD AMIAIRREIA EIETGRWKVE QSPLRFAPHT
     VHDLAEDHWH RPYSRAIGCF PAGTARHDKY WCPVGRIDNV YGDRNLVCSC PPIEDYALAA
     E