ID   GCSP_PARMW              Reviewed;         959 AA.
AC   Q7U3Q5;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=SYNW2374;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(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=(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; BX569695; CAE08889.1; -; Genomic_DNA.
DR   RefSeq; WP_011129227.1; NC_005070.1.
DR   AlphaFoldDB; Q7U3Q5; -.
DR   SMR; Q7U3Q5; -.
DR   STRING; 84588.SYNW2374; -.
DR   EnsemblBacteria; CAE08889; CAE08889; SYNW2374.
DR   KEGG; syw:SYNW2374; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_3; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001422; 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; 2.
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..959
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166941"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   959 AA;  102194 MW;  504C96688933F957 CRC64;
     MTSPFLQRHV GPSDSEQQQM LSALGYADMA AFLADVVPED ILDEFPPQGL LPPGCGEAEA
     LVHLREIAAA NNSRRSLIGL GYYGTSTPAL IQRHVFENPA WYTAYTPYQA EIAQGRLEAL
     LNFQTLISEL TGLPIANASL LDEATAAAEA MSLSYGICRR TEANRFLVDA NVLPQTWAVL
     QTRAEPLGID LERVTPEQAS FDASVFGVLL QLPGADGQIW DPTAVIARAH EAGALVTVAI
     DPLAQALIAP VASFGADIAV GSAQRFGVPM GFGGPHAAFF ATKDTYKRQI PGRLVGQSRD
     SAGNPALRLA LQTREQHIRR DKATSNICTA QVLLAVMASF YAVHHGPEGL MSIARRIVGQ
     RRQLERALQS LGFVVPDGER FDTVTVTSAL APAVHQAVGE AGFNLRVLPD GANPAESTGF
     GIALDECTTA DELSRLVAAL ATAAGQTSPS LPLAPVEELC GVPERVDPWL SQSVFHDHLS
     ETELMRYIQR LVSRDLSLVH GMIPLGSCTM KLNAAAELLP VSWPAFAGLH PFAPMAQAAG
     YQRLAEQLEA WLAALTGFAA VSLQPNAGSQ GEYAGLLVIR AWHRSRGDDH RDVCLIPTSA
     HGTNPASAVM AGLKVVAVAC DADGNIDQQD LAARAAEHAD RLAALMVTYP STHGVFETGI
     RGICELVHRH GGQVYLDGAN LNAQVGLCRP GAFGADVCHL NLHKTFCIPH GGGGPGVGPI
     GVADHLAPFL PGHPMQASPD QAIGPVSAAA LGSASILPIS WMYLRMMGAE ALRQATAVAL
     LSANYLALRL DPHYPVLFRG ATGRVAHECI LDLRPLKRDA GIDVDDIAKR LMDYGFHAPT
     VSWPVAGTVM VEPTESESLA ELDRFADAMI AIRNEIRDIE SGAMDASNNP LKQAPHTMAA
     VIAEDWDRPY SRQQAAFPLP DQQQNKVWPA VARIDNAYGD RNLICTCPSV EEIAVAVAA