ID   GCSP_SYNS9              Reviewed;         958 AA.
AC   Q3AUM0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=Syncc9902_2188;
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=316279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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; CP000097; ABB27146.1; -; Genomic_DNA.
DR   RefSeq; WP_011360925.1; NC_007513.1.
DR   AlphaFoldDB; Q3AUM0; -.
DR   SMR; Q3AUM0; -.
DR   STRING; 316279.Syncc9902_2188; -.
DR   EnsemblBacteria; ABB27146; ABB27146; Syncc9902_2188.
DR   KEGG; sye:Syncc9902_2188; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_0_3; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000002712; 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..958
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045623"
FT   MOD_RES         705
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   958 AA;  102932 MW;  4509C36FE278452A CRC64;
     MTSPFLQRHL GPSETEQHQM LQTLGYQHLD DFIKDVVPDD ILDAAPPRNV LPAGCGEAEA
     LADLGTIAAK NLVQRSLIGL GYHGTATPAL IQRHVFENPA WYTAYTPYQA EIAQGRLEAL
     LNFQTLISEL TGLPIANASL LDEATAAAEA MGLSFGVCRR PEANRFLVDC HVLPQTWAVL
     QTRAEPLGIE LERVDPEQMA FDTRVFGVLL QLPGADGLLW DPTTLIERAH DAGALVTVAI
     DPLAQTLFAP VADFGADIAV GSAQRFGVPM GFGGPHAAFF ATREAYKRQI PGRLVGESKD
     AEGNPALRLA LQTREQHIRR DKATSNICTA QVLLAVIASF YAVHHGPDGL RAIAERLVGL
     RLQFEAGLRT LDVAVEEADR FDTVTVTTTH APAVHAAAAE AGFNLRVLPD GVPASQATGF
     GVSFDEFSDQ KEVAHLLEAV ARAVGKPVST APASAANTAL LSLPSRIRPW LTQPAFHRYR
     SETELMRYIQ RLVSRDLSLV HGMIPLGSCT MKLNAAAELL PVSWPEFARL HPFAPLDQAL
     GYRHLADDLE RWLAALTGFA AVSLQPNAGS QGEYAGLLVI RAWHRSRGDN HRDICLIPTS
     AHGTNPASAV MAGLKVVAVA CDAEGNIDQD DLAARATEYA DRLAALMVTY PSTHGVFETG
     IRHICEVVHR HGGQVYLDGA NLNAQVGLSR PGAFGADVCH LNLHKTFCIP HGGGGPGVGP
     IGVAAHLAPF LPGHPFENQT ASAIGPVSAA ALGSASILPI SWMYLRMMGA DALRQASAVA
     LLSANYLAHR LDDHFPVLFR GATGRVAHEC ILDLRPLKRD AGIDVDDIAK RLMDYGFHAP
     TVSWPVAGTV MVEPTESESL SELDRFADAL IAIRDEVRAI ETGAMDALNN PLKRAPHTMA
     AVMAEVWDRP YSRQQAAFPL PDQTQNKVWP AVARIDNAFG DRNLICTCPS VEAVAIAA