ID   GCSP_PSE14              Reviewed;         954 AA.
AC   Q48ME3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {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 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=PSPPH_1162;
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6;
RX   PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA   Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA   Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA   Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA   Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(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; CP000058; AAZ34685.1; -; Genomic_DNA.
DR   RefSeq; WP_011167929.1; NC_005773.3.
DR   AlphaFoldDB; Q48ME3; -.
DR   SMR; Q48ME3; -.
DR   STRING; 264730.PSPPH_1162; -.
DR   EnsemblBacteria; AAZ34685; AAZ34685; PSPPH_1162.
DR   KEGG; psp:PSPPH_1162; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000551; 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.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227120"
FT   MOD_RES         706
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103674 MW;  0797995B634B9355 CRC64;
     MTDRIELTTA NEFIARHIGP RAADEQAMLQ TLGFDSIEAL SESVIPESIK GTSVLNLPAG
     QSEADALASI KAIASKNQLF KTYIGQGYYN THTPAPILRN LLENPAWYTA YTPYQPEISQ
     GRLESLLNFQ TLISDLTGLP IANASLLDEA TAAAEAMTFC KRLSKNKGSQ QFFASSHCHP
     QTLDVLRTRA EPLGITVVVA DEAELGDVSD YFGALLQYPA SNGDVFDYRE LVERFHAANA
     LVAVAADLLA LTLLTPPGEF GADVAIGSAQ RFGVPLGFGG PHAAYFSTRD AFKRDMPGRL
     VGVSVDRHGK QALRLAMQTR EQHIRREKAT SNICTAQVLL ANIASMYAVY HGPRGLTQIA
     KRVHQLTAIL AEGLSTLGLK AEQAFFFDSL TLNTGSRTAA LHAAARARHI NLREIDDQHL
     GLSLDETTSQ SAVETLWEIF ASDGQNLPDF TALAASVPSR LPATLLRQSA ILSHPVFNRY
     HSETELMRYL RKLADKDLAL DRTMIPLGSC TMKLNAASEM IPVTWAEFGN LHPFAPAEQS
     TGYQQLTDEL EAMLCAATGY DAISLQPNAG SQGEYAGLLA IRAYHQSRGD EHRDICLIPS
     SAHGTNPATA NMAGMRVVVT ACDARGNVDI EDLRAKTVQH RDQLAAIMIT YPSTHGVFEE
     GIREICGIVH DNGGQVYIDG ANMNAMVGLC APGKFGGDVS HLNLHKTFCI PHGGGGPGVG
     PIGVKSHLAP FMPGHARMER KEGAVCAAPF GSASILPITW MYIRMMGGEG LKRASQLAIL
     NANYISRRLE EHYPVLYTGT NGLVAHECIL DLRPIKDSSG ISVDDVAKRL IDFGFHAPTM
     SFPVAGTLMI EPTESESREE LDRFCDAMIK IREEIRAVEN GTLDKDDNPL KNAPHTAAEI
     VGQWSHPYSR EQAVYPVDSL IENKYWPPVG RVDNVFGDRN LVCACPSIES YQEA