ID   GCSPA_THEKO             Reviewed;         451 AA.
AC   Q5JGX5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=TK1380;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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; AP006878; BAD85569.1; -; Genomic_DNA.
DR   RefSeq; WP_011250331.1; NC_006624.1.
DR   AlphaFoldDB; Q5JGX5; -.
DR   SMR; Q5JGX5; -.
DR   STRING; 69014.TK1380; -.
DR   EnsemblBacteria; BAD85569; BAD85569; TK1380.
DR   GeneID; 3235784; -.
DR   KEGG; tko:TK1380; -.
DR   PATRIC; fig|69014.16.peg.1342; -.
DR   eggNOG; arCOG00077; Archaea.
DR   HOGENOM; CLU_004620_0_2_2; -.
DR   InParanoid; Q5JGX5; -.
DR   OMA; MYDGASA; -.
DR   OrthoDB; 52784at2157; -.
DR   PhylomeDB; Q5JGX5; -.
DR   Proteomes; UP000000536; 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; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_0000166987"
SQ   SEQUENCE   451 AA;  50014 MW;  9A29DDFFC0F7BE19 CRC64;
     MGKHYIPNSA HKDEMLKEIG FSSIEDLFSD VPKGMVKEFN LPEGKSEYEV FTELNETLSK
     NKTVLEMPSF LGAGTYFHYV PAHVKYLIER SEFLTAYTPY QPEISQGMLQ ALFEYQSLIA
     ELVGLPIVNS SMYDWGTAMA EAALMSARVT KRNKFVVPKH LSPEKKLVLK TYTAGPGLET
     VEVPWDERGQ MDIEKLKEAV EGAAGVYIEM PNFFGLLEEN IREIGEIAHD AGALFVVGVD
     PTILGIVEAP GELGADIVVG EAAYFGNPMN FGGPRAGIFA VRNDRKLIRQ MPGRIIGMTK
     DADGKRAFVM TLQTREQHIR RAKATSNICS NEALVAVAAA IHLATLGPKG VRELGEVILK
     NTAYLKKRLA EVGEIVFDGV NFKDVPVRFE VPYSVIHERL LERNIHGGYY IGKHFQELGE
     TALFAATETT RKEWVDGLVD ALREIIGEAE L