GCSP_STRCO
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 03-AUG-2022, 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}; OrderedLocusNames=SCO1378;
GN ORFNames=SC10A9.20c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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=(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; 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.SCO1378; -.
DR GeneID; 1096801; -.
DR KEGG; sco: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 OMA; CVPMSEY; -.
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:0044249; P:cellular 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; 3.40.640.10; -; 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..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
