ID   GCSP_STRM5              Reviewed;         955 AA.
AC   B4SS67;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Smal_3000;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF52699.1; -; Genomic_DNA.
DR   RefSeq; WP_012511825.1; NC_011071.1.
DR   AlphaFoldDB; B4SS67; -.
DR   SMR; B4SS67; -.
DR   STRING; 391008.Smal_3000; -.
DR   PRIDE; B4SS67; -.
DR   EnsemblBacteria; ACF52699; ACF52699; Smal_3000.
DR   KEGG; smt:Smal_3000; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   BioCyc; SMAL391008:SMAL_RS15260-MON; -.
DR   Proteomes; UP000001867; 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..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132459"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  103078 MW;  CA77D3E89617341C CRC64;
     MSQNTPSLRE LEHHSAFVER HIGPNDAEIA QMLGVIGHAS LDAMTDAIVP AKIKSPAPLA
     LPESITEVQA LAKIRAIADK NTVLRSFIGQ GYYGTHTPNV ILRNILENPA WYTAYTPYQA
     EISQGRMEAL INFQTLCADL TGMEIANASL LDEATAAAEA MTLAKRSAKS KSDTFFVHDA
     VHPQTLELLR TRAEPMGIVL RVGTPAEALE ADSFGLLLQY PDTFGQVGDY KALVDAVHAR
     GGLVAVATDL LALTLLAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
     RLIGVSIDAQ GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPEGLTR
     IARRTHRLAS ILAAALRKAG VQVGGDFFDT LHVTGVHAEE IHAKARAAGY NLRAIDSDSV
     GISLDETTTR ADIVAVASVF GASLDVDALD ASTADALPAG LLRQSEFLTH PVFNTHHSEH
     ELLRYLRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFSQIHPL VPADQALGYK
     ELIDSLEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEDHRD ICLIPDSAHG
     TNPASAQMCG MKVVVTKTDA NGNVDVEDIR LNAEKYSDRL AAIMMTYPST HGVFEEEVVE
     ICEIIHKHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
     KEHLAPFLPG KLGDHGPVGM VSAASFGSAS ILPISWMYIA MMGTEGLRKA TQVAQLNANY
     IAKRLAPHFK TLYTGRNGLV AHECILDVRP LEKTSGIGAE DVAKRLIDFG FHAPTLSFPV
     AGTLMVEPTE SESLHELDRF IDAMIQIREE ITAIEDGRLD REDNPLKNAP HTATAVTASE
     WTHAYPRELA AFPLPSLKLQ KYWPPVARVD NVYGDKNVMC ACIPVDAYKD DEVEA