ID   GCSP_RHILW              Reviewed;         954 AA.
AC   B5ZQP8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Rleg2_1891;
OS   Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2304;
RX   PubMed=21304679; DOI=10.4056/sigs.44642;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA   Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT   WSM2304, an effective microsymbiont of the South American clover Trifolium
RT   polymorphum.";
RL   Stand. Genomic Sci. 2:66-76(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=(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; CP001191; ACI55176.1; -; Genomic_DNA.
DR   RefSeq; WP_012557779.1; NC_011369.1.
DR   AlphaFoldDB; B5ZQP8; -.
DR   SMR; B5ZQP8; -.
DR   STRING; 395492.Rleg2_1891; -.
DR   EnsemblBacteria; ACI55176; ACI55176; Rleg2_1891.
DR   KEGG; rlt:Rleg2_1891; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000008330; 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_1000132449"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103878 MW;  657DB783103313E3 CRC64;
     MTTPTEFQFT DYQPYDFANR RHIGPSPAEM TDMLKVIGYN SLDGLIDGTL PPAIRQKAPL
     VWGAPMTERE ALDKLRETAN KNKVLVSLIG QGYHGTITPP VIQRNILENP AWYTAYTPYQ
     PEISQGRLEA LLNYQTMVCD LTGLDVANAS LLDEATAAAE GMAIAERVAK SKAKAFFVDA
     DCHPQTIALI RTRAEPLGWQ VIVGNPFTDL DPVDVFGAIF QYPGTHGHIN DFTGLIARLH
     QAGAISIVAA DILALTLLKS PGEMGADIAV GSSQRFGVPV GYGGPHAAYM AVKDAIKRSM
     PGRLVGVSVD ARGNRAYRLS LQTREQHIRR EKATSNICTA QVLLAVMASM YAVFHGPKGI
     KAIAQQVHQK AVLMAKGLEK LGYKVEPESF FDTITVDVGH MQGLILRAAV AEGVNLRKVG
     DTHIGMSLDE RTRPATLEAV WRAFGGNFKI ADFEPSYRLP KGLLRTSDYL THPIFHMNRA
     ESEMTRYIRR LSDRDLALDR SMIPLGSCTM KLNATAEMLP ITWPEFSDIH PFVPADQALG
     YREMIDDLIE KLCAVTGYDA FSMQPNSGAQ GEYAGLLTIR NFHIANGEGH RDVCLIPTSA
     HGTNPASAQM VGMKVVVVKV RENGDIDLDD FRAKAEEHAA NLSCCMITYP STHGVFEETV
     KEICDLVHAN GGQVYLDGAN MNAMVGLSRP GDIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKAHLAPHL PGHPETDGRP GAVSAAAFGS ASILPISWSY CLMMGGEGLT QATKVAILNA
     NYIATRLKGA YDVLYKSKTG RVAHECIIDT RPLVDSAGVT VDDVAKRLID CGFHAPTMSW
     PVAGTLMIEP TESETKAELD RFCEAMLAIR EEARAIEDGR MDKVNNPLKN APHTVEDLVG
     EWDRPYSREQ ACFPPGAFRV DKYWSPVNRV DNVYGDRNLI CTCPPVESYA EAAE