ID GCSPA_THEP1 Reviewed; 437 AA. AC A5IKK8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 89. 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}; GN OrderedLocusNames=Tpet_0711; OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 / OS RKU-1). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=390874; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.; RT "Complete sequence of Thermotoga petrophila RKU-1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. 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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]- CC L-lysyl-[glycine-cleavage complex H protein]; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000702; ABQ46731.1; -; Genomic_DNA. DR RefSeq; WP_011943315.1; NC_009486.1. DR AlphaFoldDB; A5IKK8; -. DR SMR; A5IKK8; -. DR STRING; 390874.Tpet_0711; -. DR KEGG; tpt:Tpet_0711; -. DR eggNOG; COG0403; Bacteria. DR HOGENOM; CLU_004620_0_2_0; -. DR Proteomes; UP000006558; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR HAMAP; MF_00712; GcvPA; 1. DR InterPro; IPR023010; GcvPA. DR InterPro; IPR049315; GDC-P_N. 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; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1. DR PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1. DR Pfam; PF02347; GDC-P; 1. DR PIRSF; PIRSF006815; GcvPA; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Oxidoreductase. FT CHAIN 1..437 FT /note="Probable glycine dehydrogenase (decarboxylating) FT subunit 1" FT /id="PRO_1000045684" SQ SEQUENCE 437 AA; 48830 MW; E3AEE3D2A5A638D6 CRC64; MNYPYIPHTD EDIRAMLEFI GVSSIEDLFS SIPVSARSSL NIPESRDEFS VFKRLKEISE VNASLEDYAV FLGAGVYKRY VPTVVYDLAM KPDFLTAYTP YQAEVSQGTL QALFEYQTMV CELTGMEVAN ASMYDGATAL AEAALMSFRL TGKEKVVVAR SVHPEYRAVL RTYLEKRGFT VVEAGYDETG RVLLEEVDEE TAAIAIQYPN FFGIIEDLDY VRSRSGNALL IVVVEPVSLA LLEPPGSYGA DIVVGEGQSL GLPMWFGGYS LGIFATKEKY VRQMPGRLIG QTVDQDGSVT YTMILQTREQ HIRRARATSN ICSNHAHAAL IAAVYMSVMG PDGLREVARR SYSAAHYLQE RLEDMGFKLC FSGEFFSEFV FNVPEDYPER WKWMMAKKIL GPLPLKGFYP ELGDTALACA TEVISKEDIE KLLEAMK //