ID   GCSPB_SULIL             Reviewed;         509 AA.
AC   C3MPT6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=LS215_1391;
OS   Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=429572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.S.2.15 / Lassen #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001399; ACP35399.1; -; Genomic_DNA.
DR   RefSeq; WP_012711310.1; NC_012589.1.
DR   AlphaFoldDB; C3MPT6; -.
DR   SMR; C3MPT6; -.
DR   EnsemblBacteria; ACP35399; ACP35399; LS215_1391.
DR   GeneID; 7812565; -.
DR   GeneID; 7941037; -.
DR   KEGG; sis:LS215_1391; -.
DR   HOGENOM; CLU_004620_5_0_2; -.
DR   OMA; MHINLHK; -.
DR   OrthoDB; 8883at2157; -.
DR   Proteomes; UP000001747; 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..509
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_1000212675"
FT   MOD_RES         278
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   509 AA;  56584 MW;  2181A9B4FA39ABD2 CRC64;
     MVWRQAKWDE PLIFELNNSG ANRQGLLINK DDEIRSEIKE MKIPKNLLRE NGPNLPSLSE
     LEVVRHFIRL SQMNFGVDVG IMPLGSCTMK YNPKIEEKAT AITESHHPLE DEDHVQGILE
     MIYELQNWFS EITGMDECSL QVPAGSAGEF AGVLMIKKYH EDHNRNYKDT MLVADTAHGT
     NPASAAMAGY KVMYVKSNGE GLVDMDILRE IVNDKTAGFM LTNPNTLGLF EENILEISKI
     IHSANAILYY DGANLNGVLG IARPGDMGFD IVHLNLHKTF AVPHGGGGPG AGAICAKGEL
     VNYLPYPMVE KVNGKYRLSK IPKNSVGKIA TFYGNVGNLA RSFAYLLGLG PQGVQMVGKM
     STLATNYLIA KLRDIKELEL IAPNRHRKHE VVFSVKQLME NYGVSANDVA KALLDSGFYA
     PTIYFPPIIE EALMIEPTET ESKETLDMFA EALKKIVEDA KRNPEQLLKS PSNTSIARLD
     QAYANHPSTI TPTYRVLKLR RMGKINYLK