ID   GCSP_STRCO              Reviewed;         961 AA.
AC   Q9AK84;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 123.
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=SCO1378; ORFNames=SC10A9.20c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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}.
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DR   EMBL; AL939108; CAC32302.1; -; Genomic_DNA.
DR   RefSeq; NP_625662.1; NC_003888.3.
DR   RefSeq; WP_011027754.1; NZ_VNID01000006.1.
DR   AlphaFoldDB; Q9AK84; -.
DR   SMR; Q9AK84; -.
DR   STRING; 100226.gene:17758961; -.
DR   PaxDb; 100226-SCO1378; -.
DR   PATRIC; fig|100226.15.peg.1386; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_11; -.
DR   InParanoid; Q9AK84; -.
DR   OrthoDB; 9801272at2; -.
DR   PhylomeDB; Q9AK84; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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_0000166939"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   961 AA;  102809 MW;  7A9D905DD1E6D3D5 CRC64;
     MTAHRTPLSE LEQAMPFEQR HIGPDHEARA KMLAQVGYGS LDELTAAAVP DVIKNADRLD
     LPGARSEAEV LAELRSLADR NQVLDSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
     EISQGRLEAL LNFQTMVAEL TGLPTSGASL LDEGTAAAEA MALSRRMGKN KKGLFLVDAD
     ALPQTVAVIR TRAEPTGVEV VVADLSEGIP AEVAEREING VLLQYPGASG AVRDIKPVID
     RAHELGALVT VAADLLALTL LTSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVHEKFA
     RSLPGRLVGV SVDADGNKAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
     EGLRAIARRT HRYATITAAG LAAGGVEIVH GSYFDTVTAR VPGRAAGIVH AARENGINLR
     LVDADHVSFA CDETTTRAQV GGVWHAFGVE GDIESLDAEA GETLPEALLR TDDFLTHPVF
     HQHRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT TEMEPVTWPE FGALHPFAPA
     EQAQGYLTLI RELEERLAEV TGYDKVSLQP NAGSQGEFAG LLAVRGYHRA NGDEQRTVCL
     IPSSAHGTNA ASAVMAGMKV VVVKTAEDGE IDVEDLRAKI DKHRDELAVL MITYPSTHGV
     FEEHVADICA QVHDAGGQVY VDGANLNALV GLAKPGHFGG DVSHLNLHKT FCIPHGGGGP
     GVGPVGVRSH LAPYLPNHPL QPAAGPQTGV GPISAAPWGS AGILPISWSY VRLMGGEGLK
     RATQVAVLSA NYIAKRLEPH FPVLYNGPGG LVAHECIIDL RPLTKATGVS VDDVAKRLID
     YGFHAPTMSF PVAGTLMIEP TESEDLAELD RFCEAMIAIR AEIEKVGSGA WPADDNPLRG
     APHTADALGG EWDHAYTREE AVFPAGVSAA DKYWPPVRRI DQAYGDRNLV CSCPPLDAYE
     D
//