ID   GCSP_RHIME              Reviewed;         954 AA.
AC   Q92Q11;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=R01547;
GN   ORFNames=SMc02049;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591688; CAC46126.1; -; Genomic_DNA.
DR   RefSeq; NP_385653.1; NC_003047.1.
DR   RefSeq; WP_010969293.1; NC_003047.1.
DR   AlphaFoldDB; Q92Q11; -.
DR   SMR; Q92Q11; -.
DR   STRING; 266834.SMc02049; -.
DR   EnsemblBacteria; CAC46126; CAC46126; SMc02049.
DR   GeneID; 61603009; -.
DR   KEGG; sme:SMc02049; -.
DR   PATRIC; fig|266834.11.peg.2971; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_4_0_5; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001976; 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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166932"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104106 MW;  4E6FD4F3AD392C62 CRC64;
     MSMPKDFTFT DYKPYDFANR RHIGPSPAEM DEMLKVVGYP SLDALIDDTV PPSIRQRTPL
     AWGAPMTERE ALDKLRETAN RNRKLVSLIG QGYYGTITPP VIQRNILENP AWYTAYTPYQ
     PEISQGRLEA LLNYQTMVCD LTGLDVANAS LLDEATAAAE AMAIAERVAK SKAKAFFIDE
     NCHPQTIALL KTRAEPLGWQ IVLGDPFEDL DAAGVFGAIF QYPGTYGHVR DFSGLIAKLH
     GQGAIAAVAA DPLALALLKS PGEMGADIAI GSTQRFGVPV GYGGPHAAYM AVKDAYKRSM
     PGRLVGVSVD ARGNRAYRLS LQTREQHIRR EKATSNICTA QVLLAVMASM YAVFHGPDGI
     KAIAQSVHQK TVRLAMGLEK LGYTVEPDVF FDTITVEVGK LQGIILKAAV AEEVNLRKIG
     TTRIGISLDE RSRPVTLEAV WRAFGGDFKV EEFEPDYRLP QELLRTSAYL THPIFHMNRA
     ESEMTRYMRR LADRDLALDR AMIPLGSCTM KLNATAEMLP ITWPEFSEIH PFVPADQALG
     YQHLIEDLSQ KLCAITGYDA ISMQPNSGAQ GEYAGLLAIR AYHIANGNEH RDVCLIPTSA
     HGTNPASAQM AGMKVVVVKV SDAGEIDMDD FRAKAEQYAD TLSCCMITYP STHGVFEENV
     REVCEVVHKH GGQVYLDGAN MNAMVGLSRP GDIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKSHLAPFL PGHPQTDGHE GAVSAAPFGS ASILPISWSY CLMMGGEGLT QATKVAILNA
     NYVAARLKGA YDVLYKSAKG RVAHECIIDT RPLAESAGVT VDDVAKRLID CGFHAPTMSW
     PVAGTLMIEP TESETKAELD RFCDAMLAIR EEARAIEDGR MDKVNNPLKN APHTVEDLVG
     DWDRPYSREQ ACFPPGAFRV DKYWSPVNRV DNVYGDRNLV CTCPPIESYA EAAE