ID   GCSP2_PSEF5             Reviewed;         957 AA.
AC   Q4K416;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   25-MAY-2022, entry version 95.
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}; OrderedLocusNames=PFL_5959;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY95149.2; -; Genomic_DNA.
DR   RefSeq; WP_011064133.1; NC_004129.6.
DR   AlphaFoldDB; Q4K416; -.
DR   SMR; Q4K416; -.
DR   STRING; 220664.PFL_5959; -.
DR   EnsemblBacteria; AAY95149; AAY95149; PFL_5959.
DR   KEGG; pfl:PFL_5959; -.
DR   PATRIC; fig|220664.5.peg.6076; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; DEHCHPQ; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000008540; 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; 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_0000227117"
FT   MOD_RES         707
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  103724 MW;  9C80D645FCCA4F57 CRC64;
     MSQLLSLSQL REPNAFLNRH LGPDAEEQQA MLASLGLGSR AELIEQTVPP GIRFNRALDL
     PPALDEAAAL ARLKGYAGQN QVWTSLIGMG YHATLTPTVI LRNVLENPGW YTAYTPYQPE
     IAQGRLEALL NFQQMTIDLT GLDLANASLL DEATAAAEAM ALAKRVSKSS SNLFFVDEHC
     HPQTVSVVRT RAEGFGFELV VGGVDELSGH QVFGALLQYP DTHGEIRDLR PLIDQLHAQQ
     ALACVAADLL SLLLLTPPGE LGADVVLGSS QRFGVPMGYG GPHAAFFACR DDYKRAMPGR
     IIGVSKDARG QVALRMALQT REQHIRREKA NSNICTAQVL LANIAGFYAV YHGPAGLKRI
     AQRVHRLTCI LAVGLERHGI ARVNRHFFDT LTLEVGGSQT AIIESARAQQ INLRILGRGR
     LGLSLDETCD ESTVTRLFDV FLGADHGLDV SNLDAEALES GIPDPLLRRT RYLTHPVFSA
     HHSETEMLRY LKQLENKDLA LNQSMIPLGS CTMKLNASSE MIPITWPEFA NLHPFAPREQ
     AAGYGLLIAE LERWLCAITG FDAICMQPNS GAQGEYAGLL AIRRYHESRR QGGRHVCLIP
     ASAHGTNPAS AQMAGMQVVI VECDEAGNVD LEDLKAKAQA AGERLSCLMA TYPSTHGVYE
     EGISQICEVI HSHGGQVYMD GANLNAQVGL ARPADIGADV SHMNLHKTFC IPHGGGGPGM
     GPIGVRAHLA PFVANHPVVP IDGPLPENGA VSAAPWGSAS ILPISWMYIA LMGPQLADAS
     EVAILAANYL AEQLSGAFPV LYSGRNGRVA HECILDLRPL KAQTGISEED VAKRLMDYGF
     HAPTMSFPVP GTLMVEPTES ESKAELDRFI EAMLSIRAEI AQVQEGNWPA EDNPLKGAPH
     TLADITGVWE RSYSIEQAVL PTAHTRAHKY WPAVNRVDNV YGDRNLFCAC VPLADYR