ID   GCSP_SYNR3              Reviewed;         957 AA.
AC   A5GWN4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=SynRCC307_2390;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; CT978603; CAK29293.1; -; Genomic_DNA.
DR   RefSeq; WP_011936802.1; NC_009482.1.
DR   AlphaFoldDB; A5GWN4; -.
DR   SMR; A5GWN4; -.
DR   STRING; 316278.SynRCC307_2390; -.
DR   PRIDE; A5GWN4; -.
DR   EnsemblBacteria; CAK29293; CAK29293; SynRCC307_2390.
DR   KEGG; syr:SynRCC307_2390; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_3; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001115; 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..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045622"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  102294 MW;  E1DB8F28146EE3F4 CRC64;
     MSAGFVQRHL GPSPAEQAQM LQRLGCRDLE QLLQECVPAE ILIDADQARD ALPQECDERQ
     ALRELEQRAA ANTVLRNLIG LGYYDTATPA LIQRHVLENP AWYTAYTPYQ AEIAQGRLEA
     LLNFQTLISE LTGLPIANAS LLDEATAAAE AMTLAYGACR LKQARRFHVQ ADLFPQTLAV
     LQTRAEPLGI ELVVADPAAM DFGDDSFGLL LQLPTASGAC PDPTEVIARA KAADVLVIAA
     VDPLAQVLMP PVAQLGVQIA VGSAQRFGVP LGFGGPHAAF FATTEAYKRQ IPGRLVGMSR
     DAAGEPALRL ALQTREQHIR RDKATSNICT AQVLLAVMAG FYAVHHGPDG LTAIARRVQR
     LTAALAAGLQ QLGLDVAAAP AFDTLRLRLD QPNGWIERLE AAGFNLLPLP DGAGISLDEC
     SDEAEVQALL ECFAAGCGRT APAISELLAA TPQAKSVGEL PVRPAGWLPQ AVFQLYRSET
     ELLRYIQRLV SKDFSLVHGM IPLGSCTMKL NAAAELQPVS WAAFNRLHPF VPAAQRQGYD
     QLINELEAWL ATITGFAAVS LQPNAGSQGE YAGLLVIRAW HRQRGEGHRN ICLIPTSAHG
     TNPASAVMAG MQVVAVQCDE AGNIDQADLA AKAEQHADQL AALMVTYPST HGVFEQGISD
     ICALIHRHGG QVYLDGANLN AQVGVCQPGR FGADVCHLNL HKTFCIPHGG GGPGVGPIAV
     AAHLAPFLPG HPLVPCGGEQ AIGPVSAAPW GSASILPISW MYIRLMGGAG LRQATAVALL
     AANDLAERLE PHFPVLYRGA NGRVAHECIL DLRPLKRSAG LEVDDLAKRL MDYGFHAPTV
     SWPVAGTVMV EPTESESLLE LDRFVEAMMA IRAEAAAIEA GLCDRDDNPL RRAPHTLAAV
     TADVWERPYS REQAAYPVQG LRSNKLWPAV SRIDNAFGDR NLICTCPSVE ELARAAG