ID GCSPA_STAS1 Reviewed; 450 AA. AC Q49XY0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 107. 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=SSP1219; OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM OS 20229 / NCIMB 8711 / NCTC 7292 / S-41). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=342451; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41; RX PubMed=16135568; DOI=10.1073/pnas.0502950102; RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.; RT "Whole genome sequence of Staphylococcus saprophyticus reveals the RT pathogenesis of uncomplicated urinary tract infection."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005). 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; AP008934; BAE18364.1; -; Genomic_DNA. DR RefSeq; WP_011303028.1; NZ_MTGA01000038.1. DR AlphaFoldDB; Q49XY0; -. DR SMR; Q49XY0; -. DR GeneID; 66867448; -. DR KEGG; ssp:SSP1219; -. DR eggNOG; COG0403; Bacteria. DR HOGENOM; CLU_004620_0_2_9; -. DR OrthoDB; 9771867at2; -. DR Proteomes; UP000006371; 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; Reference proteome. FT CHAIN 1..450 FT /note="Probable glycine dehydrogenase (decarboxylating) FT subunit 1" FT /id="PRO_0000166979" SQ SEQUENCE 450 AA; 49664 MW; 411CDBA9BB71F685 CRC64; MSHRYIPLTE QDKKEMLDTI GASSISELFG DVPKDILLNR ELAIPDGEAE TTLTKRLSRI ASKNVTKETH SSFLGAGVYD HYAPAVVDAM ISRSEFYTAY TPYQPEISQG ELQAIFEFQT LICELTDMDI ANSSMYDGIT SFAEACILAF NQTRKNKIVV SKGLHYQALQ VLKTYVKTRE EFEVVEVDLD GTITDLEKLE NAIDDDTAAV AVQYPNFYGS IEDLEKIHSF IEDKKALFIV YANPLALGLL TPPGSFGADI VVGDTQPFGI PAQFGGPHCG FFATTKKLMR KIPGRLVGQT EDGDGNRGFV LTLQAREQHI RRDKATSNIC SNQALNALAS SICMSALGKQ GIYDISVQNF ENANYAKAQF KEAGLEVSNG TSFNEFVVKF NKPVKDINDA LLQQDIIGGF DLSEVSKDYE NQMLVAVTEL RTKDEIDTFV KKAGELNGSK //