ID   GCSPA_THEON             Reviewed;         446 AA.
AC   B6YT11;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=TON_0213;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(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; CP000855; ACJ15698.1; -; Genomic_DNA.
DR   RefSeq; WP_012571171.1; NC_011529.1.
DR   AlphaFoldDB; B6YT11; -.
DR   SMR; B6YT11; -.
DR   STRING; 523850.TON_0213; -.
DR   EnsemblBacteria; ACJ15698; ACJ15698; TON_0213.
DR   GeneID; 7017870; -.
DR   KEGG; ton:TON_0213; -.
DR   PATRIC; fig|523850.10.peg.215; -.
DR   eggNOG; arCOG00077; Archaea.
DR   HOGENOM; CLU_004620_0_2_2; -.
DR   OMA; MYDGASA; -.
DR   OrthoDB; 52784at2157; -.
DR   Proteomes; UP000002727; 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..446
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000132488"
SQ   SEQUENCE   446 AA;  49768 MW;  25C3EB745FFD0B80 CRC64;
     MGKHYLPNSA HKDEMLKKIG FNSIEDLFSD VPKGMVKEFN LPEGRSEYEV FLELNEVLSK
     NKTVLEMPSF LGAGTYFHYI PAHVKYLIER SEFLTAYTPY QPEISQGMLQ ALFEYQSLIA
     ELVGLPIVNS SMYDWGTAMA EAALMSARVT RKNKFVVPEH MSPEKKKVLH TYTAGPGLEI
     EYVNWNERGQ LDLEELKEKV EGAAGVYVEM PNFFGILEEE IRAIGEIAHD AGALFVVGVD
     PTILGIVEAP GELGADIVVG EAAYFGNPMN FGGPRAGIFA VRDDKKLIRQ MPGRIIGMTK
     DADGKRAFVM TLQTREQHIR RAKATSNICS NEALVAVAAA IHLASLGPRG LRELGEVILK
     NTAYLKKRLS EVAEIPFEGV NFKDVLVRFE KSYEEIHEVL LERNIHGGFY LKPHFPELGE
     SALFAATETT RKEWVDALIE ALREVA