ID   GCSP_XANCP              Reviewed;         975 AA.
AC   Q8PBK7;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=XCC1112;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008922; AAM40411.1; -; Genomic_DNA.
DR   RefSeq; NP_636487.1; NC_003902.1.
DR   RefSeq; WP_011036312.1; NC_003902.1.
DR   AlphaFoldDB; Q8PBK7; -.
DR   SMR; Q8PBK7; -.
DR   STRING; 340.xcc-b100_3229; -.
DR   EnsemblBacteria; AAM40411; AAM40411; XCC1112.
DR   KEGG; xcc:XCC1112; -.
DR   PATRIC; fig|190485.4.peg.1188; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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..975
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166949"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   975 AA;  104719 MW;  7E55F8591F3654B2 CRC64;
     MSQTPSSLRD LEHHSAFVER HIGPNDAEIA QMLGVVGHDS LDAMTDAIVP SNIKSPAALA
     LPDAITEEEA LARIRAIASK NQVQRTFIGQ GYYGTHTPKV ILRNILENPA WYTAYTPYQA
     EISQGRMEAL INFQTMCADL TGMQIANASL LDEATAAAEA MTLAKRSAKS KSDTFFVHDA
     VHPQTQELLR TRAEPLGIVL RVGTPDEAMQ AECFGVLLQY PDSFGHIGDH AALADAVHAQ
     GGLVAVATDL LALTLIAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
     RLIGVSIDAA GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPEGLTR
     IARRTHRLAA ILAAALRSAG VTVGEHFFDT LHVKAIDADA IHAKAHAAGI NLRAIDSEAV
     GISLDETSTR ADVVALAQLF GAQADIDALD AATADALPQG MRRTSAFLQH PVFNTHHSEH
     ELLRYMRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFGAIHPL APPEQSAGYA
     QLIEELEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRNEAHRD ICLIPESAHG
     TNPASAQMCG MTVVVTKCDA NGNVDVDDIR AKAEKYSDRL AALMITYPST HGVFEEDVVA
     ICEAVHAHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
     KSHLAPFLPK TLPNAGIRAG ENQKAAIHGS GSNFGEGEVG MVSAASYGSA SILPISWMYV
     TMMGSAGLRK ATQVALLNAN YIAKRLSAHY KTLYTGRNGL VAHECILDVR PLEKTSGIGA
     EDIAKRLIDF GFHAPTLSFP VAGTLMVEPT ESESQHELDR FIDAMIQIRE EIRAIEDGRL
     DREDNPLKHA PHTATQVSAS EWTHAYPREL AAFPLPSLKQ QKYWPPVGRV DNVYGDKNVM
     CACIPVDAYK DDVVA