ID   GCSPB_PYRFU             Reviewed;         502 AA.
AC   Q8TZJ2;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713}; OrderedLocusNames=PF2000;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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_00713}.
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_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00713};
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_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR   EMBL; AE009950; AAL82124.1; -; Genomic_DNA.
DR   RefSeq; WP_011013144.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8TZJ2; -.
DR   SMR; Q8TZJ2; -.
DR   STRING; 186497.PF2000; -.
DR   PRIDE; Q8TZJ2; -.
DR   EnsemblBacteria; AAL82124; AAL82124; PF2000.
DR   GeneID; 41713824; -.
DR   KEGG; pfu:PF2000; -.
DR   PATRIC; fig|186497.12.peg.2076; -.
DR   eggNOG; arCOG00076; Archaea.
DR   HOGENOM; CLU_004620_5_0_2; -.
DR   OMA; MHINLHK; -.
DR   OrthoDB; 8883at2157; -.
DR   PhylomeDB; Q8TZJ2; -.
DR   Proteomes; UP000001013; 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   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00713; GcvPB; 1.
DR   InterPro; IPR023012; GcvPB.
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; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..502
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_0000167028"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   502 AA;  56113 MW;  70BE4DC35055A565 CRC64;
     MFRQAKWDEP LIFELSRPGR VGYTLPKPIE DIKVDIPEKL RRKSKLELPE LSEPEIVKHY
     TRLSEMNYGV DSGIYPLGSC TMKYNPKINE EIATHPKVAY IHPYQDERTV QGALAIMWEL
     EQWLKEITGM DRFTLQPAAG ANGEFTGVMI IRAYHLDNGE PQRNEMLVPD SAHGTNPASA
     AMAGFKVIEI PSNENGTIDL EALENAVSER TAGLMLTNPN TLGIFEDEIV EIAKIIHKAG
     GLLYYDGANL NGILGKIRPG DMGFDIVHLN LHKTFSTPHG GGGPGAGPVG VKEFLKDYLP
     VPLVSYDEKS GRYYLDYNVP KSIGKVKELY GNFAVLVRAL TYLKIMGRDG LREVSEIAVL
     NANYLTQKLK GTRGYSLPGK ELRKHEVVFS AEPMKKETGV KALDVAKRLL DFGMHAPTIY
     FPLIVHEALM IEPTETVSKE ELDAYVEALK RISEEAYTNP EIVKSAPHNT AVKRVDDVLA
     AKKPIVTWRM YKELKEKGEV DY