ID   GCSP_STRGG              Reviewed;         961 AA.
AC   B1W4G3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=SGR_6151;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG22980.1; -; Genomic_DNA.
DR   RefSeq; WP_003970467.1; NC_010572.1.
DR   AlphaFoldDB; B1W4G3; -.
DR   SMR; B1W4G3; -.
DR   STRING; 455632.SGR_6151; -.
DR   EnsemblBacteria; BAG22980; BAG22980; SGR_6151.
DR   GeneID; 6209942; -.
DR   KEGG; sgr:SGR_6151; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_11; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
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..961
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132458"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   961 AA;  102006 MW;  819593B6B7225401 CRC64;
     MTPRRTPLSQ LEQGIPFEQR HIGPDAEAQA KMLAQVGYGS LDELTAAAVP DVIKSAEALN
     LPSARTEAEV LAELRSLADR NQVLAPMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
     EISQGRLEAL LNFQTMVAEL TGLPTSGASL LDEGTAAAEA MALSRRVGKV KKGVFLVDAD
     TLPQTVAVIE TRAEPTGVEV VVADLSDGIP AEIAERGVFG VLLQYPGASG AVRAIEPVIE
     QAHELGAIVT VAADLLALTL LTSPGALGAD IAVGTTQRFG VPMGFGGPHA GFMAVREKFA
     RSLPGRLVGV SVDADGNKAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
     DGLRTIARRT HRFAAILADG LRSAGVDVVH GAFFDTLTVR VPGKAAGIVA EARERGVNLR
     LVDADHVSIA CDETTTRSQI SAVWAAFGAE GDIEALDAAV ADALPEGLLR SDDILTHPVF
     HQHRSETAML RYLRKLADRD YALDRGMIPL GSCTMKLNAT AEMESITWPE FGALHPFAPA
     DQAQGFLTLI RELEERLAEV TGYDAVSIQP NAGSQGEFAG LLAVRAYHRA NGDDQRTVCL
     IPSSAHGTNA ASAVMAGMKV VVVKTADDGE VDIADLRAKI EQHRDELAVL MITYPSTHGV
     FEEHVAEICG EVHDAGGQVY VDGANLNALV GLAKPGKFGG DVSHLNLHKT FCIPHGGGGP
     GVGPVGVRAH LAPYLPNHPL QPAAGPETGV GPISAAPWGS AGILPISWAY VRLMGGEGLK
     RATQVAVLAA NYIAKRLEPH FPILYNGPAG LVAHECIVDL RPISKATGVS IDDVAKRLID
     YGFHSPTMSF PVAGTLMIEP TESEDLAELD RFCDTMIAIR AEIEKVASGE WSADDNPLSN
     APHTAAALGG DWEHGYSREE AVFPAGVSAA DKYWPPVRRI DGAFGDRNLV CSCPPLDAYD
     D