ID GCSPA_STAAM Reviewed; 448 AA. AC P64217; Q99TV8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 105. 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=SAV1536; OS Staphylococcus aureus (strain Mu50 / ATCC 700699). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=158878; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Mu50 / ATCC 700699; RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2; RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y., RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., RA Hiramatsu K.; RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus."; RL Lancet 357:1225-1240(2001). 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; BA000017; BAB57698.1; -; Genomic_DNA. DR RefSeq; WP_000019691.1; NC_002758.2. DR AlphaFoldDB; P64217; -. DR SMR; P64217; -. DR KEGG; sav:SAV1536; -. DR HOGENOM; CLU_004620_0_2_9; -. DR PhylomeDB; P64217; -. DR Proteomes; UP000002481; 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. DR World-2DPAGE; 0002:P64217; -. PE 3: Inferred from homology; KW Oxidoreductase. FT CHAIN 1..448 FT /note="Probable glycine dehydrogenase (decarboxylating) FT subunit 1" FT /id="PRO_0000166971" SQ SEQUENCE 448 AA; 49707 MW; 94EE79F2F967472F CRC64; MSHRYIPLTE KDKQEMLQTI GAKSIGELFG DVPSDILLNR DLNIAEGEAE TTLLRRLNRI ASKNITKETH TSFLGAGVYD HYAPSVVDAM ISRSEFYTAY TPYQPEISQG ELQAIFEFQT LICELTDMDV ANSSMYDGMT SFAEACILAF SQTKKNKIVV SKGLHYQALQ VLHTYAKTRK EFEVVEIDLD GTVTDLKKLE AAVDDETAAV AVQYPNFYGS IEDLEKIQSF IEDKKALFIV YANPLALGLL TPPGSFGADI VVGDTQPFGI PAQFGGPHCG YFATTKKLMR KVPGRLVGQT QDDEGNRGFV LTLQAREQHI RRDKATSNIC SNQALNALAS SIAMSALGKQ GIYDIAVQNI EHANYAKQQF IKKGFEVLDG TSFNEFVVKF DKPIQQVNEE LVKYNIIGGF DLGVVSDDFK NHMLIAVTEL RTKDEIDTFV EKAGELND //