ID   GCSP_STRMK              Reviewed;         955 AA.
AC   B2FQE7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Smlt3579;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; AM743169; CAQ46996.1; -; Genomic_DNA.
DR   RefSeq; WP_005414179.1; NC_010943.1.
DR   AlphaFoldDB; B2FQE7; -.
DR   SMR; B2FQE7; -.
DR   EnsemblBacteria; CAQ46996; CAQ46996; Smlt3579.
DR   KEGG; sml:Smlt3579; -.
DR   PATRIC; fig|522373.3.peg.3361; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   Proteomes; UP000008840; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132460"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  102998 MW;  9AF7C403FAA3C8FC CRC64;
     MSQNTPSLRE LEHHNAFVER HIGPNDAEIA QMLDVVGHAS LDAMTDAIVP AKIKSPAPLA
     LPESMTEVQA LAKIRAIADK NTVLRSFIGQ GYYGTHTPNV ILRNILENPA WYTAYTPYQA
     EISQGRMEAL INFQTLCADL TGMEIANASL LDEATAAAEA MTLAKRSAKS KSDTFFVHDA
     VHPQTLELLR TRAEPMGIVL RVGTPAEALE AEAFGLLLQY PDTFGQVGDY KALVDAVHAR
     GGLVAVATDL LALTLLAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
     RLIGVSIDAQ GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPEGLTR
     IARRTHRLAS ILAAALRNAG VQVGGDFFDT LHVTGVHADE IHAKARAAGY NLRAIDSDSV
     GISLDETTTR ADIVAVAAVF GASLDVDALD ASTADALPAG LLRQSAFLTH PVFNTHHSEH
     ELLRYLRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFSQIHPL VPADQALGYK
     ELIDTLEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEGHRD ICLIPDSAHG
     TNPASAQMCG MKVVVTKTDA NGNVDVEDIR LNAEKYSDRL AAIMMTYPST HGVFEEEVVE
     ICEIIHKHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
     KEHLAPFLPG KLGDNGPVGM VSAASFGSAS ILPISWMYIA MMGREGLRKA TQVAQLNANY
     IAKRLAPHFK TLYTGRNGLV AHECILDVRP LEKTSGIGAE DVAKRLIDFG FHAPTLSFPV
     AGTLMVEPTE SESLHELDRF IDAMIQIREE ITAIEDGRLD REDNPLKNAP HTATAVTASE
     WTHAYPRELA AFPLASLKQS KYWPPVARVD NVYGDKNVMC ACIPVDAYKD DEVEA
//