ID   GCSP_PSEU5              Reviewed;         958 AA.
AC   A4VRT4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=PST_4062;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(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=(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; CP000304; ABP81685.1; -; Genomic_DNA.
DR   RefSeq; WP_011915065.1; NC_009434.1.
DR   AlphaFoldDB; A4VRT4; -.
DR   SMR; A4VRT4; -.
DR   STRING; 379731.PST_4062; -.
DR   EnsemblBacteria; ABP81685; ABP81685; PST_4062.
DR   KEGG; psa:PST_4062; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000233; 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; -; 1.
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..958
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045595"
FT   MOD_RES         707
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   958 AA;  103895 MW;  18A0427530F27288 CRC64;
     MPYMPSLSQL QQTDAFLRRH LGPDQGEQQA MLDALGLASR EQLIEQTVPP AIRLQGELNL
     PPALDEQAAL AKLKGYAEQN QLWTSLIGMG YHGTITPPVI LRNVLENPGW YTAYTPYQPE
     IAQGRLEALL NYQQMIIDLT GLDLANASLL DEATAAAEAM TLARRMAKSK SNRFFVDENC
     HPQTLSVVQT RAEAFGFELV VGTLDDLAGH EVFGALLQYP DTHGEIRDLR PAIEQLHAQQ
     ALACVAADLL SLLLLTPPGE LGADVVLGST QRFGVPMGYG GPHAAYFASR DEFKRGMPGR
     IIGVSKDARG NTALRMALQT REQHIRREKA NSNICTAQVL LANIAGFYAV YHGPQGLKRI
     AQRVHRLTAI LAAGLEQKGI VRLNRHFFDT LTLEVGGAQT AIIESAEAAQ INLRILGRGR
     LGVSLDETCD ERTVEQLLAI FLGADHGLDV AALDAGELAA GIPAGLQRDS GYLEHPVFNS
     HHSETEMLRY LKQLENKDLA LNQAMIPLGS CTMKLNATSE MIPITWAEFA NLHPFVPRGQ
     AQGYRLMIEE LEAWLCAITG FDAISMQPNS GAQGEYAGLV AIRKYHESRG EGQRDICLIP
     SSAHGTNPAS AQMVSMRVVI VECDKGGNVD LEDLKRKAAE AGDRLSCLMI TYPSTHGVYE
     ENVREICAAI HAQGGQVYMD GANLNAQVGL ARPADIGADV SHMNLHKTFC IPHGGGGPGM
     GPIGVKAHLA PFVANHPVVE LEGPQPGNGA VSAAPWGSAS ILPISWMYIA MMGPQLRDAT
     EVAILGANYL ANRLGGAFPV LYSGRNGRVA HECILDLRPL KAASGISEED VAKRLMDYGF
     HAPTMSFPVP GTLMIEPTES ESKAELDRFV EAMLSIRAEI AKVQDGEWPA DNNPLVRAPH
     TLADVIGEWD RPYSIAEAVT PSAHARAHKY WPAVNRVDNV YGDRNLFCAC VPVDAYRD