ID GCSPA_SPHAL Reviewed; 452 AA. AC Q1GRZ2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 96. 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=Sala_1868; OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) OS (Sphingomonas alaskensis). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingopyxis. OX NCBI_TaxID=317655; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13593 / LMG 18877 / RB2256; RX PubMed=19805210; DOI=10.1073/pnas.0903507106; RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S., RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A., RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V., RA Robb F.T., Kjelleberg S., Cavicchioli R.; RT "The genomic basis of trophic strategy in marine bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(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; CP000356; ABF53580.1; -; Genomic_DNA. DR RefSeq; WP_011542158.1; NC_008048.1. DR AlphaFoldDB; Q1GRZ2; -. DR SMR; Q1GRZ2; -. DR STRING; 317655.Sala_1868; -. DR KEGG; sal:Sala_1868; -. DR eggNOG; COG0403; Bacteria. DR HOGENOM; CLU_004620_0_2_5; -. DR OrthoDB; 9801272at2; -. DR Proteomes; UP000006578; 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 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; 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..452 FT /note="Probable glycine dehydrogenase (decarboxylating) FT subunit 1" FT /id="PRO_1000045677" SQ SEQUENCE 452 AA; 48145 MW; 77E4241D35B4E318 CRC64; MRYLPLTPDD RAAMLGAIGA SSIDELFADV PAGARLDGPI AGLPMHASEL AVERHMGALA RRNRAAGDGP FFLGAGAYRH HVPASVDHLI QRGEFLTAYT PYQPEIAQGT LQMLFEFQSQ VARLFGTDVA NASMYDGSTA CWEAIVMARR ITRRSKALLS TGLHPHYRSV ARTMAKYTRD VLVDGDPRLE PGTDWAALAG RIDTETSCVV VQYPDILGRI DDMTTLAEAC QTAGALLIAV VTEPVALGLI KSPGEMGADI VVGEGQSLGV GLQFGGPYVG LFACKSKYVR QMPGRLCGET VDANGKRGFV LTLSTREQHI RREKATSNIC TNSGLCALAF SIHMTLLGEA GLRQLATINH GRAKAAATEL AKVPAVSVMN DSFFNEFTLL LPTAARPVVH RLAEQDILGG VSLGRLYPDT AALENGLVVA VTETVTEADI AAFAAALKEV LA //