ID   GCSP1_PSEPF             Reviewed;         950 AA.
AC   Q3K7X5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 1 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP1 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=Pfl01_4392;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
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=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; CP000094; ABA76129.1; -; Genomic_DNA.
DR   RefSeq; WP_011335631.1; NC_007492.2.
DR   AlphaFoldDB; Q3K7X5; -.
DR   SMR; Q3K7X5; -.
DR   KEGG; pfo:Pfl01_4392; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   Proteomes; UP000002704; 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; 1.
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.
FT   CHAIN           1..950
FT                   /note="Glycine dehydrogenase (decarboxylating) 1"
FT                   /id="PRO_0000227118"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   950 AA;  102581 MW;  C03E37A90AFB210C CRC64;
     MTQVNLGTAN EFIARHIGPR AGDEQAMLNS LGFDSLEALS ASVIPESIKG TSVLGLDDGL
     SEADALAMIK GIAGKNQLFK TYIGQGYYNC HTPSPILRNL LENPAWYTAY TPYQPEISQG
     RLEALLNFQT LISDLTGLPI ANASLLDEAT AAAEAMTFCK RLSKNKGSHQ FFASIHSHTQ
     TLDVLRTRAE PLGIDVVVGD ERELTDVTPF FGALLQYPAS NGDVFDYREL TERFHAANAL
     VAVAADLLAL TLLTPPGEFG ADVAIGSAQR FGVPLGFGGP HAAYFSTKDA FKRDMPGRLV
     GVSVDRFGKP ALRLAMQTRE QHIRREKATS NICTAQVLLA NIASMYAVYH GPKGLTQIAN
     RVHHLTAILA KGLSALGVTV EQTSFFDTLT LATGAQTAAL HDKARAQQIN LRVIDAQRLG
     LSVDETTTQA DIETLWGLFA DGKTLPDFAA LAAAAQSTIP ASLVRQSPIL SHPVFNRYHS
     ETELMRYLRK LADKDLALDR TMIPLGSCTM KLNAASEMIP VTWAEFGALH PFAPAEQSAG
     YQQLTDELEA MLCAATGYDS ISLQPNAGSQ GEYAGLLAIR AYHQSRGEDR RDICLIPSSA
     HGTNPATANM AGMRVVVTAC DARGNVDIED LRAKAIEHRE HLAALMITYP STHGVFEEGI
     REICGIIHDN GGQVYIDGAN MNAMVGLCAP GKFGGDVSHL NLHKTFCIPH GGGGPGVGPI
     GVKSHLTPFL PGHGHMERKE GAVCAAPFGS ASILPITWMY IRMMGGAGLK RASQLAILNA
     NYISRRLEEH YPVLYTGSNG LVAHECILDL RPLKDSSGIS VDDVAKRLID FGFHAPTMSF
     PVAGTLMIEP TESESKEELD RFCDAMIRIR EEIRAVENGT LDKDDNPLKN APHTAAELVG
     EWTHPYSREQ AVYPVASLIE GKYWPPVGRV DNVFGDRNLV CACPSIESYA
//