GCSP_STRAW
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 03-AUG-2022, entry version 107.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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 / NRRL
RC 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 / NRRL
RC 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=(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}.
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 STRING; 227882.SAV_6987; -.
DR EnsemblBacteria; BAC74698; BAC74698; SAVERM_6987.
DR KEGG; sma:SAVERM_6987; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_11; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 70707at2; -.
DR Proteomes; UP000000428; 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; 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
