ID GCSPA_SOLM1 Reviewed; 443 AA. AC C4XJB9; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 82. 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=DMR_31780; OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1) OS (Desulfovibrio magneticus). OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Solidesulfovibrio. OX NCBI_TaxID=573370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700980 / DSM 13731 / RS-1; RX PubMed=19675025; DOI=10.1101/gr.088906.108; RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N., RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H., RA Matsunaga T.; RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed RT common gene clusters in magnetotactic bacteria."; RL Genome Res. 19:1801-1808(2009). 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; AP010904; BAH76669.1; -; Genomic_DNA. DR RefSeq; WP_015861821.1; NC_012796.1. DR AlphaFoldDB; C4XJB9; -. DR SMR; C4XJB9; -. DR STRING; 573370.DMR_31780; -. DR KEGG; dma:DMR_31780; -. DR eggNOG; COG0403; Bacteria. DR HOGENOM; CLU_004620_0_2_7; -. DR OrthoDB; 9801272at2; -. DR Proteomes; UP000009071; 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..443 FT /note="Probable glycine dehydrogenase (decarboxylating) FT subunit 1" FT /id="PRO_1000212660" SQ SEQUENCE 443 AA; 47975 MW; 6AB5AD920094553E CRC64; MPYIPHTPAE IREMLDAVGA PDVDALFAEI PAALRPQSFD LAKGATEMAV RAAMEKLSAK NRTDLTSFLG GGFYDHYVPA ASDLLLSRGE FYTAYTPYQP EASQGTLQAI FEYQTAVCRL MDMECSNAGV YDGGTALYEA LMMAVRHTRR KKAVVSETVS PIYRIVLATY TKNLHLDLVV VPHKNGLDDF EALTAAVDGD TAAIVVQNPN FFGSVQDFTA LFDHAREKGA VSVISCYPVL QTVLKTPGAM GADIATAEGQ SLGLPLSFGG PYLGIMTCKK SLVRQMPGRI AGRTKDAAGR TGYVLTLQAR EQHIRRQKAT SNICSNQALC ALRALINLCL TGNEGLSRQA ARSIENANYA AWKLGAIPGV KLLNEAPFGN EFAAVFPVNA KQVARMLMDG GIVPGFPLGR YYQGLENALL ICCTEKHDRA DIDRLARRLE NAL //