ID   GCSP2_PSEPF             Reviewed;         957 AA.
AC   Q3K4Z1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase 2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 2 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP2 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=Pfl01_5426;
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; ABA77163.1; -; Genomic_DNA.
DR   RefSeq; WP_011336463.1; NC_007492.2.
DR   AlphaFoldDB; Q3K4Z1; -.
DR   SMR; Q3K4Z1; -.
DR   KEGG; pfo:Pfl01_5426; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_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; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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..957
FT                   /note="Glycine dehydrogenase (decarboxylating) 2"
FT                   /id="PRO_0000227119"
FT   MOD_RES         707
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  104242 MW;  9F8868B26BEF8AC6 CRC64;
     MSQLPSLSQL RDPHAFLRRH LGPDAAEQQA MLDSLGLGSR VELIEQTVPP GIRLNRELDL
     PPALDEQAAL ARLRGYAEQN QVWTSLIGMG YHGTLTPTVI LRNVLENPGW YTAYTPYQPE
     IAQGRLEALL NFQQLTIDLT GLELANASLL DEATAAAEAM ALAKRVAKSK SNLFFVDENC
     HPQTISVVQT RAEGFGFELI VDAVDNLKQH QVFGALLQYP DTHGEIRDLR PLIDHLHAQQ
     ALACVAADLL SLLLLTPPGE LGADVVFGSS QRFGVPMGYG GPHAAVFASR EEYKRAIPGR
     IIGVSKDARG NVALRMALQT REQHIRREKA NSNICTAQVL LANIASFYAV YHGPEGLKRI
     AQRVHRLTCI LAAGLERHGI QRLNQHFFDT LTLDVGGAQT AIIESAQAAQ INLRILGRGQ
     LGLSLDEACD ENTVARLFDV LLGADHGLSI DDLDAETLAS GIPEMLQRST SYLRHPVFNA
     HHSETEMLRY LKQLENKDLA LNQSMIPLGS CTMKLNATSE MIPITWPQFA NLHPFVPREQ
     AVGYTLMIEE LERWLCAITG FDAICMQPNS GAQGEYAGLL AIRKYHESRQ QGGRDICLIP
     SSAHGTNPAS AQMAGMRVVI VECDDAGNVD LEDLKAKASE AGAKLSCLMA TYPSTHGVYE
     EGISEICEVI HKHGGQVYMD GANLNAQVGL ARPADIGADV SHMNLHKTFC IPHGGGGPGM
     GPIGVRAHLA PFVANHPVVP IDGPQPQNGA VSAAPWGSAS ILPISWMYIA MMGPQLADAS
     EVAILAANYL AQHLSGAFPV LYTGRNERVA HECILDLRPL KAATGISEED VAKRLMDYGF
     HAPTMSFPVP GTLMVEPTES ESKAELDRFI GAMLSIRAEI TEVQNGNWPA EDNPLKRAPH
     TMADITGVWE RPYSIEQGIT PDAHTKAHKY WPAVNRVDNV YGDRNLFCAC VPVDDYR
//