GCSPA_ENDTX
ID GCSPA_ENDTX Reviewed; 443 AA.
AC B1GYV7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; OrderedLocusNames=TGRD_717;
OS Endomicrobium trichonymphae.
OC Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC Endomicrobium.
OX NCBI_TaxID=1408204;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Complete genome of the uncultured termite group 1 bacteria in a single
RT host protist cell.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(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_00712}.
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_00712};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00712}.
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DR EMBL; AP009510; BAG14200.1; -; Genomic_DNA.
DR RefSeq; WP_015423721.1; NC_020419.1.
DR RefSeq; YP_001956661.1; NC_020419.1.
DR AlphaFoldDB; B1GYV7; -.
DR SMR; B1GYV7; -.
DR STRING; 471821.TGRD_717; -.
DR EnsemblBacteria; BAG14200; BAG14200; TGRD_717.
DR KEGG; rsd:TGRD_717; -.
DR PATRIC; fig|471821.5.peg.1223; -.
DR HOGENOM; CLU_004620_0_2_0; -.
DR OMA; MYDGASA; -.
DR OrthoDB; 870147at2; -.
DR Proteomes; UP000001691; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
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; PTHR42806; PTHR42806; 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Oxidoreductase.
FT CHAIN 1..443
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 1"
FT /id="PRO_1000147994"
SQ SEQUENCE 443 AA; 48595 MW; B78DAE46504BF191 CRC64;
MDYTPQNQKD KKKMLETIGI DDVSELFDTI PKDLRAKKLN ISGGKTEQEL LNYFSDIASE
NKVLISFRGA GIYDHYIPSL VGEVIGRSEF WTAYTPYQAE ASQGTLQSIF EYQSLICALT
GLDTSNASLY DGATATAEAV LLALRASGKN KILISQGLHP EYMQTVKTYL ENSKAEIVTL
NISENGVIEK DAVDASVDDD TAAVIIQSPN FFGVVEDMQA LSTVIKSRNS LFVAVLNPLS
LGVFMSPGEY KADIAVGEGQ VLGSAMRAGG ATFGFMAVKK ALEWKMPGRI AGQTTDKNGN
RGFVLTLQSR EQHIRREKAT SNICTSASLN ALAGCVFLSG WGNDGFKNLA EINISKARYA
FNKIKSLKGF KSKFENKVFF NEFVIETSKN IKKIQNILLK NGILGPLDLS CINENFKNCL
LFCVTEQRTK AEINRLTEIL AEA