ID   GCSP_PSEU2              Reviewed;         954 AA.
AC   Q4ZXH2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Psyr_1096;
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a;
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT   syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000075; AAY36150.1; -; Genomic_DNA.
DR   RefSeq; WP_011266822.1; NC_007005.1.
DR   RefSeq; YP_234188.1; NC_007005.1.
DR   AlphaFoldDB; Q4ZXH2; -.
DR   SMR; Q4ZXH2; -.
DR   STRING; 205918.Psyr_1096; -.
DR   PRIDE; Q4ZXH2; -.
DR   EnsemblBacteria; AAY36150; AAY36150; Psyr_1096.
DR   KEGG; psb:Psyr_1096; -.
DR   PATRIC; fig|205918.7.peg.1127; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000426; 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; -; 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.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227121"
FT   MOD_RES         706
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103677 MW;  4E1B3FA1A2B4FCD6 CRC64;
     MTDRIELTTA NEFIARHIGP RAADELAMLQ TLGFDSIEAL SESVIPESIK GTSVLNLPAG
     QSEADALASI KAIASKNQLF KTYIGQGYYN THTPAPILRN LLENPAWYTA YTPYQPEISQ
     GRLESLLNFQ TLISDLTGLP IANASLLDEA TAAAEAMTFC KRLSKNKASQ QFFASSHCHP
     QTLDVLRTRA EPLGITVVVA DEHELGDVSD YFGALLQYPA SNGDVFDYRE LVERFHAANA
     LVAVAADLLA LTLLTPPGEF GADVAIGSAQ RFGVPLGFGG PHAAYFSTRD AFKRDMPGRL
     VGVSVDRHGK QALRLAMQTR EQHIRREKAT SNICTAQVLL ANIASMYAVY HGPRGLTQIA
     NRVHQLTAIL AEGLSTLGLN AEQAFFFDSL TLHTGDRTAA LHAAARARHI NLREIDDQRL
     GLSLDETTSQ SAVETLWAIF ANDGQSLPDF AALADSVQSR LPAGLLRQSA ILSHPVFNRY
     HSETELMRYL RKLADKDLAL DRTMIPLGSC TMKLNAASEM IPVTWAEFGN LHPFAPAEQS
     AGYQQLTDEL EAMLCAATGY DAISLQPNAG SQGEYAGLLA IRAYHQSRGD EHRDICLIPS
     SAHGTNPATA NMAGMRVVVT ACDARGNVDI EDLRAKAVQH RDQLAAIMIT YPSTHGVFEE
     GIREICGIVH DNGGQVYIDG ANMNAMVGLC APGKFGGDVS HLNLHKTFCI PHGGGGPGVG
     PIGVKSHLAP FMPGHARMER KEGAVCAAPF GSASILPITW MYIRMMGGEG LKRASQLAIL
     NANYISRRLE EHYPVLYTGS NGLVAHECIL DLRPIKDSSG ISVDDVAKRL IDFGFHAPTM
     SFPVAGTLMI EPTESESREE LDRFCDAMIK IREEIRAVEN GTLDKDDNPL KNAPHTAAEI
     VGQWSHPYSR EQAVYPVDSL IENKYWPPVG RVDNVFGDRN LVCACPSIEN YQEA