ID   GCSP2_PSEPK             Reviewed;         957 AA.
AC   Q88CI9;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 2;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P-protein 2;
DE   AltName: Full=Glycine decarboxylase 2;
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 2;
GN   Name=gcvP2; Synonyms=gcvP-2; OrderedLocusNames=PP_5192;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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 (By similarity). {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN70757.1; -; Genomic_DNA.
DR   RefSeq; NP_747293.1; NC_002947.4.
DR   RefSeq; WP_010955717.1; NC_002947.4.
DR   AlphaFoldDB; Q88CI9; -.
DR   SMR; Q88CI9; -.
DR   STRING; 160488.PP_5192; -.
DR   PRIDE; Q88CI9; -.
DR   EnsemblBacteria; AAN70757; AAN70757; PP_5192.
DR   KEGG; ppu:PP_5192; -.
DR   PATRIC; fig|160488.4.peg.5540; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; DEHCHPQ; -.
DR   PhylomeDB; Q88CI9; -.
DR   BioCyc; PPUT160488:G1G01-5538-MON; -.
DR   Proteomes; UP000000556; 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; IPR018247; EF_Hand_1_Ca_BS.
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..957
FT                   /note="Glycine dehydrogenase (decarboxylating) 2"
FT                   /id="PRO_0000166928"
FT   MOD_RES         707
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   957 AA;  104038 MW;  85277F8806A51C46 CRC64;
     MSQSPSLHQL QELNPFLRRH LGPDATEQQA MLNALGIASR NELIEQTVPP DIRLNRPLDL
     PAALDEQAAL AKLAGYAEQN QVWTSLIGMG YHGTITPTVI LRNVLENPGW YTAYTPYQPE
     IAQGRLEALL NFQQMVIDLT GLPLANASLL DEATAAAEAM ALAKRVARNK SNAFFADEHC
     HPQTLSVLKT RAEGFGFELI VDSVDNLAKH SVFGALLQYP DTHGEVRDLR PLIDQLHSQQ
     ALACVAADLL SLVVLAPPGE LGADVVLGST QRFGVPMGYG GPHAAYFACR DDYKRAMPGR
     IIGVSRDARG NTALRMALQT REQHIRREKA NSNICTAQVL LANIAGFYAV YHGPEGLQRI
     AQRVHRLTFI LAAGLEAKGI KRLNQHFFDT LTLNVGGAQA AIIESAEAAH INLRILGRGH
     LGVSLDETCT EQTVLRLLDI FLGVDHGLEI TALDQLALPE GIPASLVRRT PFLAHPVFNL
     HHSETEMLRY LKQLENKDLA LNQSMIPLGS CTMKLNATSE MIPITWPGFA QLHPFAPAAQ
     AAGYKAMIDE LESWLCAITG FDAICMQPNS GAQGEYAGLM AITRYHCSRH QPMRTLCLIP
     SSAHGTNPAS AQMAGMEVVI VDCDNDGNVD LADLKAKAHA AGERLSCLMI TYPSTHGVYE
     EGIREICDVV HQYGGQVYMD GANLNAQVGL ARPADIGADV SHMNLHKTFC IPHGGGGPGM
     GPIGIRAHLK PFVASHPVVP VPGLDPNNSA VSAAPWGSAS ILPISWMYIA MMGPQLADAS
     EVAILSANYL ASQLGAAFPV LYRGRNQRVA HECILDLRPL KALTGISEED VAKRLMDYGF
     HAPTMSFPVP GTLMVEPTES ESKAELDRFV EAMLAIRAEI DEVQQGNWPA ENNPLKHAPH
     TLADVLGVWD RPYSLEQAVA PSAHVRQHKY WPAVNRVDNV YGDRNLFCAC VPVEAYR