ID   GCSP_AGRRK              Reviewed;         954 AA.
AC   B9JFK7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Arad_2527;
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000628; ACM26697.1; -; Genomic_DNA.
DR   RefSeq; WP_012651540.1; NC_011985.1.
DR   AlphaFoldDB; B9JFK7; -.
DR   SMR; B9JFK7; -.
DR   STRING; 311403.Arad_2527; -.
DR   EnsemblBacteria; ACM26697; ACM26697; Arad_2527.
DR   KEGG; ara:Arad_2527; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001600; Chromosome 1.
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_1000147960"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104016 MW;  1913D9477596C5AB CRC64;
     MSTPTEFTFT DYQPYDFANR RHIGPSPSEM ADMLKVIGYS SLDKLIDATL PPSIRQKAPL
     VWGAPMTERE ALDKLRETAN KNKVLVSLIG QGYYGTITPP VIQRTILENP AWYTAYTPYQ
     PEISQGRLEA LLNYQTMICD LTGLDVANAS LLDEATAAAE GMAMAERVAK SKAKAFFVDA
     DCHPQTIALI KTRAEPLGWS VIVGNPFTDL DPVDVFGAIF QYPGTHGHIH DFTGLIARLH
     QTGAIAVVAA DPLALTLLKS PGEMGADIAI GCSQRFGVPV GYGGPHAAYM AVKDAYKRSM
     PGRLVGVSVD ARGNRAYRLS LQTREQHIRR EKATSNICTA QVLLAVMASM YAVFHGPQGL
     KAIAQQVHQK AVLMAKGLEK LGYTIEQETF FDTITVEVGH MQGLILRAAV AEGVNLRKVG
     ETKIGMSLDE RTRPATLEAV WRAFGGNFRL ADFEPGYRLP KTLLRTSEYL THPIFHMNRA
     ESEMTRYIRR LSDRDLALDR SMIPLGSCTM KLNATAEMLP ISWPEFSDIH PFVPTDQALG
     YREMIDDLTE KLCAVTGYDA FSMQPNSGAQ GEYAGLLTIR NYHIANGEGH RDICLIPTSA
     HGTNPASAQM AGMKVVVIKV SDDGDIDMAD FRAKAEQYAA NLSCCMITYP STHGVFEETV
     KEICDLVHKH GGQVYLDGAN MNAMVGLSRP GDIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKAHLAEHL PGHPETDGRP GAVSAAAFGS ASILPISWSY CLMMGGEGLT QATKVAILNA
     NYIAARLKGA YDVLYKSKTG RVAHECIIDT RPLVDSAGVT VDDVAKRLID CGFHAPTMSW
     PVAGTLMIEP TESETKAELD RFCAAMLAIR EEARAIEEGR MDKTDNPLKN APHTVEDLVG
     EWNRPYSREQ ACFPPGAFRV DKYWSPVNRV DNVYGDRNLV CSCPPVESYA EAAE