ID   GCSP_STRAW              Reviewed;         961 AA.
AC   Q827D7;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   27-MAR-2024, entry version 115.
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}; Synonyms=gcvB;
GN   OrderedLocusNames=SAV_6987;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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   -!- SEQUENCE CAUTION:
CC       Sequence=BAC74698.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000030; BAC74698.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_037646993.1; NZ_JZJK01000085.1.
DR   AlphaFoldDB; Q827D7; -.
DR   SMR; Q827D7; -.
DR   KEGG; sma:SAVERM_6987; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_11; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P: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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..961
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166938"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   961 AA;  102650 MW;  FC4CB0D2E06C32DD CRC64;
     MTAHRIPLSD LEQGIPFEQR HIGPDSEARA KMLAQVGYGS LDELTATAVP DVIKNAEALE
     LPGARTEAEV LAELRSLADR NQVLGSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
     EISQGRLEAL LNFQTVVAEL TGLPTSGASL LDEGTAAAEA MALSRRMGKN KKGLFLVDAD
     ALPQTIAVIE TRAEPTGVEV VVADLSEGIP AGIAEREING VLIQYPGASG AVRDIKPLVE
     QAHELGAVVT VAADLLALTL LTSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVREKFA
     RSLPGRLVGV SVDADGHKAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
     DGLRTIARRT HRYATILAEG LKAGGVEVVH GAYFDTLTAR VPGRAAEIVA AAREGGVNLH
     LVDADLVSIS CDETTTRAQL GAVWTAFGVE GDIEALDAAA EDTLPAALLR TDDYLTHPVF
     HQYRSETAML RYLRRLSDRD YALDRGMIPL GSCTMKLNAT TEMEPVTWPE FGQLHPFAPA
     EQAQGYLTLI RELEERLAEV TGYDKVSLQP NAGSQGELAG LLAVRGYHRA NGDEQRTVCL
     IPSSAHGTNA ASAVMAGMKV VVVKTADDGE IDVEDLRAKI EQYRDELSVL MITYPSTHGV
     FEEHVADICA QVHEAGGQVY VDGANLNALV GLAKPGHFGG DVSHLNLHKT FCIPHGGGGP
     GVGPVGVRAH LAPYLPNHPL QPEAGPATGV GPISAAPWGS AGILPISWSY VRLMGGEGLK
     RATQVAVLSA NYIAKRLEPH YPVLYTGPGG LVAHECIIDL RPLTKATGVS VDDIAKRLID
     YGFHAPTMSF PVAGTLMIEP TESEDLGELD RFCEAMIAIR AEVEKVGSGE WPAEDNPLRN
     APHTAAALGG EWEHAYSREE AVFPAGVSAA DKYWPPVRRI DQAFGDRNLV CSCPPLDAYD
     D
//