GCSPA_THEMA
ID GCSPA_THEMA Reviewed; 437 AA.
AC Q9WY56;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=TM_0213;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(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_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; AE000512; AAD35305.1; -; Genomic_DNA.
DR PIR; G72403; G72403.
DR RefSeq; NP_228028.1; NC_000853.1.
DR RefSeq; WP_004082888.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WY56; -.
DR SMR; Q9WY56; -.
DR STRING; 243274.THEMA_03660; -.
DR EnsemblBacteria; AAD35305; AAD35305; TM_0213.
DR KEGG; tma:TM0213; -.
DR eggNOG; COG0403; Bacteria.
DR InParanoid; Q9WY56; -.
DR OMA; MYDGASA; -.
DR OrthoDB; 870147at2; -.
DR Proteomes; UP000008183; 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..437
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 1"
FT /id="PRO_0000166980"
SQ SEQUENCE 437 AA; 48942 MW; DDF0EDE9BB29BB1A CRC64;
MNYPYIPHTD EDVRAMLDFI GVSSIEELFS SIPVSARSSL NIPESRDEFS VFKQLKEISE
MNNSLEDYAV FLGAGVYKRY VPTVVYDLAM KPDFLTAYTP YQAEVSQGTL QALFEYQTMV
CELTGMEVAN ASMYDGATAL AEAALMSFRL TGKEKVVVAR SVHPEYRAVL RTYLEKRGFT
VVEAGYDETG RVLLEEVDEE TAAIAVQYPN FFGIIEDLDY VRSRSGNALL IVVVEPVSLA
LLEPPGSYGA DIVVGEGQSL GLPMWFGGYS LGIFATREEY VRQMPGRLIG QTVDQAGNTA
YTMILQTREQ HIRRARATSN ICSNHAHAAL IAAVYMSVMG PDGLKEVARR SYNAAHYLQE
RLEEIGFKLC FSGEFFNEFV FNVPEDYPDR WRKMMEKKIL GPLPLEEFYP ELGDTALACA
TEVISKEDIE KLLEAMK
