ID   GCSP_PSESM              Reviewed;         954 AA.
AC   Q887L5;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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};
GN   OrderedLocusNames=PSPTO_1276;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54801.1; -; Genomic_DNA.
DR   RefSeq; NP_791106.1; NC_004578.1.
DR   RefSeq; WP_005764078.1; NC_004578.1.
DR   AlphaFoldDB; Q887L5; -.
DR   SMR; Q887L5; -.
DR   STRING; 223283.PSPTO_1276; -.
DR   GeneID; 1182912; -.
DR   KEGG; pst:PSPTO_1276; -.
DR   PATRIC; fig|223283.9.peg.1298; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   PhylomeDB; Q887L5; -.
DR   Proteomes; UP000002515; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 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; Reference proteome.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166929"
FT   MOD_RES         706
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103604 MW;  503D639E9F6A16A0 CRC64;
     MTDRIELTTA NEFIARHIGP RAADELAMLH TLGFDSIEAL SDSVIPESIK GTSVLNLPAG
     QSEADALASI KAIASKNQLF KTYIGQGYYN THTPAPILRN LLENPAWYTA YTPYQPEISQ
     GRLESLLNFQ TLISDLTGLP IANASLLDEA TAAAEAMTFC KRLSKNKGSQ QFFASSHCHP
     QTLDVLRTRA EPLGITVVVA DETELGDVSD YFGALLQYPA SNGDVFDYRE LAERFHGANA
     LVAVAADLLA LTLLTPPGEF GADVAIGSAQ RFGVPLGFGG PHAAYFSTRD AFKRDMPGRL
     VGVSVDRHGK QALRLAMQTR EQHIRREKAT SNICTAQVLL ANIASMYAVY HGPRGLTQIA
     NRVHHLTAIL AEGLSQLGLN AEQAYFFDSL TLHTGGRTAA LHAAARARHI NLREIDDQRL
     GLSLDETTSQ SAVEVLWDIF ASTGQTLPDF TALAASVKSR LPAALLRQSA ILSHPVFNRY
     HSETELMRYL RKLADKDLAL DRTMIPLGSC TMKLNAASEM IPVTWAEFGN LHPFAPAEQS
     AGYQQLTDEL EAMLCAATGY DAISLQPNAG SQGEYAGLLA IRAYHQSRGD EHRDICLIPS
     SAHGTNPATA NMAGMRVVVT ACDARGNVDI EDLRAKALQH REQLAAIMIT YPSTHGVFEE
     GIREICGIVH DNGGQVYIDG ANMNAMVGLC APGKFGGDVS HLNLHKTFCI PHGGGGPGVG
     PIGVKSHLAP FMPGHARMQR KEGAVCAAPF GSASILPITW MYIRMMGGEG LKRASQLAIL
     NANYISRRLE EHYPVLYTGT NGLVAHECIL DLRPIKDSSG ISVDDVAKRL IDFGFHAPTM
     SFPVAGTLMI EPTESESREE LDRFCDAMIK IREEIRAVED GTLDKDDNPL KNAPHTAAEI
     VGQWSHPYSR EQAVYPVDSL IENKYWPPVG RVDNVFGDRN LVCACPSIES YQEA
//