ID   GCSPA_DICTD             Reviewed;         453 AA.
AC   B8E2E7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Dtur_1517;
OS   Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=515635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6724 / Z-1310;
RX   PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA   Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT   "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT   6724 reveals a specialized carbohydrate fermentor.";
RL   Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK42791.1; -; Genomic_DNA.
DR   RefSeq; WP_012583867.1; NC_011661.1.
DR   RefSeq; YP_002353405.1; NC_011661.1.
DR   AlphaFoldDB; B8E2E7; -.
DR   SMR; B8E2E7; -.
DR   STRING; 515635.Dtur_1517; -.
DR   EnsemblBacteria; ACK42791; ACK42791; Dtur_1517.
DR   KEGG; dtu:Dtur_1517; -.
DR   PATRIC; fig|515635.4.peg.1566; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_0; -.
DR   InParanoid; B8E2E7; -.
DR   OMA; MYDGASA; -.
DR   OrthoDB; 870147at2; -.
DR   Proteomes; UP000007719; 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..453
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000147985"
SQ   SEQUENCE   453 AA;  50912 MW;  3E381E07BC2054D0 CRC64;
     MAYFPHTPQE IREMLNTIGV DSIEELFSEI PEEIRQKAKE NFKLSASPSE IDLLEEIKQI
     SKKNIGKDYI SFLGGGAYRH YIPSFVKLVS LFPTFYTSYT PYQPEISQGV LQSIFEYQSL
     ICDLTGMEVA NASLYEAGSG IAEAALMSVR ITGKKEVIVS SGLNPEYISV LKTYLQVQNI
     DLKILPLDEN GETDITALER TISPSTSGVI LQNPNFFGVI ETKLKEMETL IHKNNALFIL
     SIYPISLGIL KPPSEYNVDI VVGEGQSLGI PLGFGGPYLG ILATKKEFIR QIPGRIVGET
     IDLEGERGFV NTLQTREQHI RRAKATSNIC TNEALSAISA AVYMALLGKK GIKKIAEVCF
     SRAHYLKDRL QKKLGIDFIY PNSYFFNEFV IKTPENSKVF LKKLEERKIL GGIPLSKFYK
     EREKEILIAV TERNSIEEID YYVKSLKEVL KKD