ID   GCSP_PSEFS              Reviewed;         946 AA.
AC   C3JYR1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, 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}; OrderedLocusNames=PFLU_4897;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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; AM181176; CAY51790.1; -; Genomic_DNA.
DR   RefSeq; WP_015885598.1; NC_012660.1.
DR   AlphaFoldDB; C3JYR1; -.
DR   SMR; C3JYR1; -.
DR   STRING; 294.SRM1_04328; -.
DR   PRIDE; C3JYR1; -.
DR   EnsemblBacteria; CAY51790; CAY51790; PFLU_4897.
DR   KEGG; pfs:PFLU_4897; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000002332; 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; Reference proteome.
FT   CHAIN           1..946
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000212656"
FT   MOD_RES         700
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   946 AA;  102240 MW;  CE2F89AF47C44C59 CRC64;
     MTVNLTTANE FIARHIGPRQ EDEQHMLASL GFDSLEALSA SVIPESIKGT SVLGLEDGLS
     EAEALAKIKA IAGQNQLFKT YIGQGYYNCH TPSPILRNLL ENPAWYTAYT PYQPEISQGR
     LEALLNFQTL ISDLTGLPIA NASLLDEATA AAEAMTFCKR LSKNKGSNAF FASIHSHPQT
     LDVLRTRAEP LGIDVVVGDE RELTDVSAFF GALLQYPASN GDVFDYRALT ERFHASNALV
     AVAADLLALT LLTPPGEFGA DVAIGSAQRF GVPLGFGGPH AAYFSTKDAF KRDMPGRLVG
     VSVDRFGKPA LRLAMQTREQ HIRREKATSN ICTAQVLLAN IASMYAVYHG PKGLTQIAQR
     IHQLTAILAK GLTALGQKVE QEHFFDTLTL NTGANTATLH DKARAQRINL RVVDAERLGV
     SVDETTTQAD IETLWAIFAD GKALPDFAAN VDSTLPAALL RQSPILSHPV FNRYHSETEL
     MRYLRKLADK DLALDRTMIP LGSCTMKLNA ASEMIPVTWA EFGALHPFAP AEQSAGYLQL
     TSDLEAMLCA ATGYDAISLQ PNAGSQGEYA GLLAIRAYHQ SRGEERRDIC LIPSSAHGTN
     PATANMAGMR VVVTACDARG NVDIEDLRAK AIEHRDHLAA LMITYPSTHG VFEEGIREIC
     GIIHDNGGQV YIDGANMNAM VGLCAPGKFG GDVSHLNLHK TFCIPHGGGG PGVGPIGVKS
     HLTPFLPGHA AMERKEGAVC AAPFGSASIL PITWMYISMM GGAGLKRASQ LAILNANYIS
     RRLEEHYPVL YTGSNGLVAH ECILDLRPLK DSSGISVDDV AKRLIDFGFH APTMSFPVAG
     TLMIEPTESE SKEELDRFCD AMIAIREEIR AVENGTLDKD DNPLKNAPHT AAELVGEWSH
     PYSREQAVYP VASLIEGKYW PPVGRVDNVF GDRNLVCACP SIESYA