ID   GCSP_RHIE6              Reviewed;         954 AA.
AC   B3PP20;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=RHECIAT_CH0002352;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-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=(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; CP001074; ACE91306.1; -; Genomic_DNA.
DR   RefSeq; WP_012483955.1; NC_010994.1.
DR   AlphaFoldDB; B3PP20; -.
DR   SMR; B3PP20; -.
DR   EnsemblBacteria; ACE91306; ACE91306; RHECIAT_CH0002352.
DR   KEGG; rec:RHECIAT_CH0002352; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_5; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000008817; 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.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132448"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103943 MW;  EECDBC25C2126AA1 CRC64;
     MTTPTEFQFT DYQPYDFANR RHIGPSPAEM TDMLKVIGFN SLDGLIDATL PPTIRQKAPL
     VWGAPMTERE ALDKLRETAN KNKVLVSLIG QGYYGTITPP VIQRNILENP AWYTAYTPYQ
     PEISQGRLEA LLNYQTMVCD LTGLDVANAS LLDEATAAAE GMAMAERVSK SKAKAFFVDA
     DCHPQTIALI RTRAEPLGWS VIVGNPFTDL DPVDVFGAIF QYPGTHGHVH DFTGLIARLH
     QAGAISVVAA DILALTLLKS PGEMGADIAV GSSQRFGVPV GYGGPHAAYM AVKDAIKRSM
     PGRLVGVSVD ARGNRAYRLS LQTREQHIRR EKATSNICTA QVLLAVMASM YAVFHGPDGI
     KAIAQQVHQK AVLMAKGLEK LGYKVEPESF FDTITVDVGH MQGLILRAAV AEGVNLRKVG
     ETKIGMSLDE RTRPATLEAV WRAFGGNFTI ADFEPSYLLP KGLLRTTDYL AHPIFHMNRA
     ESEMTRYIRR LSDRDLALDR SMIPLGSCTM KLNATAEMLP ITWPEFSDIH PFVPADQALG
     YREMLDDLTE KLCAVTGYDA FSMQPNSGAQ GEYAGLLTIR NYHIANGEGH RDVCLIPTSA
     HGTNPASAQM VGMKVVVVKV RENGDIDLDD FRTKAEEHAA SLSCCMITYP STHGVFEETV
     KEICELVHKH GGQVYLDGAN MNAMVGLSRP GDIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKAHLAPHL PGHPETDGRP GAVSAAAFGS ASILPISWSY CLMMGGEGLT QATKVAILNA
     NYIAARLKGA YDVLYKSKTG RVAHECIIDT RPLVDSSGVT VDDVAKRLID CGFHAPTMSW
     PVSGTLMIEP TESETKAELD RFCEAMLAIR EEARAIEDGR MDKINNPLKN APHTVEDLVG
     EWDRPYSREQ ACFPPGAFRV DKYWSPVNRV DNVYGDRNLI CTCPPVESYA EAAE