ID   GCSP1_PSEPK             Reviewed;         951 AA.
AC   Q88P65;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 1;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P-protein 1;
DE   AltName: Full=Glycine decarboxylase 1;
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 1;
GN   Name=gcvP1; Synonyms=gcvP-1; OrderedLocusNames=PP_0988;
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; AAN66613.1; -; Genomic_DNA.
DR   RefSeq; NP_743149.1; NC_002947.4.
DR   RefSeq; WP_003255089.1; NC_002947.4.
DR   AlphaFoldDB; Q88P65; -.
DR   SMR; Q88P65; -.
DR   STRING; 160488.PP_0988; -.
DR   PRIDE; Q88P65; -.
DR   EnsemblBacteria; AAN66613; AAN66613; PP_0988.
DR   KEGG; ppu:PP_0988; -.
DR   PATRIC; fig|160488.4.peg.1048; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   PhylomeDB; Q88P65; -.
DR   BioCyc; PPUT160488:G1G01-1061-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; 1.
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..951
FT                   /note="Glycine dehydrogenase (decarboxylating) 1"
FT                   /id="PRO_0000166927"
FT   MOD_RES         703
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   951 AA;  101992 MW;  EDDBDB715CDE148E CRC64;
     MTINLGTANE FIARHIGPRA ADEQAMLTAL GFDSLDAMTA AVIPDSIKGT SVLGSHDGQS
     EADALAALKA IAGKNQLFKS YIGQGYYNTH TPAPILRNLL ENPAWYTAYT PYQPEISQGR
     LEALLNFQTL ISDLTGLPIA NASLLDEATA AAEAMTFCKR LSKNKSSHAF FASVHCHPQT
     LDVLRTRAEP LGIEVVVGDE RELGDVSAFF GALLQYPASN GEVFDYREVV QRFHAANALV
     AVAADLLALT LLTPPGEFDA DVAIGSAQRF GVPLGFGGPH AAYFATRDAF KRDMPGRLVG
     VSIDRFGKTA LRLAMQTREQ HIRREKATSN ICTAQVLLAN IASMFAVYHG PAGLKRIAER
     THALTAILAA GLKALGVQVV GASAFDTLTL ATGTATASLH DKARAQGINL RQIDAAHVGL
     SLDETSTQAD VESLWQLLGG EQAQPDFTAL AASTGSLLPA ALLRQSAILE HPVFNRYHSE
     TELMRYLRRL ADKDLALDRS MIPLGSCTMK LNAASEMIPV TWAEFGNLHP FAPAEQSQGY
     LQMTTELEAM LCAATGYDAV SLQPNAGSQG EYAGLLAIRA YHRSRGEGHR DICLIPSSAH
     GTNPATAHMA GMRVVVTACD ARGNVDVEDL RAKAIEHRER LAAIMITYPS THGVFEEAIG
     EICAIIHDNG GQVYIDGANM NAMVGLCAPG KFGGDVSHLN LHKTFCIPHG GGGPGVGPIG
     VKSHLAPFLP GHAQLENTQG AVCAAPFGSA SILPITWMYI RMMGGAGLKR ASQMAILNAN
     YIARRLEEHY PVLYTGGNGL VAHECILDLR PLKDTSGISV DDVAKRLIDF GFHAPTMSFP
     VAGTLMIEPT ESESKEELDR FCNAMIQIRE EIRAVEDGSL DKDDNPLKNA PHTAAELVGE
     WTHGYSREQA VYPLASLVEG KYWPPVGRVD NVFGDRNLVC ACPSIESYQD A