ID   GCSPB_PYRAB             Reviewed;         502 AA.
AC   Q9UXT1; G8ZKW0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=PYRAB17770;
GN   ORFNames=PAB1172;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50682.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71251.1; -; Genomic_DNA.
DR   PIR; D75030; D75030.
DR   RefSeq; WP_010868896.1; NC_000868.1.
DR   AlphaFoldDB; Q9UXT1; -.
DR   SMR; Q9UXT1; -.
DR   STRING; 272844.PAB1172; -.
DR   PRIDE; Q9UXT1; -.
DR   EnsemblBacteria; CAB50682; CAB50682; PAB1172.
DR   GeneID; 1496080; -.
DR   KEGG; pab:PAB1172; -.
DR   PATRIC; fig|272844.11.peg.1896; -.
DR   eggNOG; arCOG00076; Archaea.
DR   HOGENOM; CLU_004620_5_0_2; -.
DR   OMA; MHINLHK; -.
DR   OrthoDB; 8883at2157; -.
DR   PhylomeDB; Q9UXT1; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
FT   CHAIN           1..502
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_0000167027"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   502 AA;  56288 MW;  F8E8C9CFA27EBD3B CRC64;
     MYRQAKWDEP LIFELSRPGR VGYTLPKPIE DVDVEIPEKL KRKSPLNLPE VSEPEVVKHY
     TRLSEMNYGV DSGIYPLGSC TMKYNPKINE ELAGHPKVAY IHPYQDERTV QGALRIMWEL
     EQWLKEITGM DRFTLQPAAG ANGEFTGVMI IKAYHLDRGE TQRNEMLVPD SAHGTNPASA
     AMAGFKVIEI PSNENGTVDL EALENAVSER TAGLMLTNPN TLGIFEDEIE EIAKIVHKAG
     GLLYYDGANL NGILGKVRPG DMGFDIVHLN LHKTFSTPHG GGGPGAGPVG VKEFLKDYLP
     VPLVSYDEEN DRYYLDYDVP KSIGKVKELF GNFAVLVRAL TYLKVMGKDG LREVSEVAVL
     NANYLARKLK GTRGYELPHK ELRKHEVVFS AEPMKRETGV RTLDVAKRLL DFGMHAPTIY
     FPLIVHEALM IEPTETVSKE ELDAYVEAMK KISEEAYTNP EVVKSAPHNT AVRRVDDVLA
     SKKPIITWKM YKELKEKGEV DY