ID GCSP1_PSEPF Reviewed; 950 AA. AC Q3K7X5; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Glycine dehydrogenase [decarboxylating] 1; DE EC=1.4.4.2; DE AltName: Full=Glycine decarboxylase 1; DE AltName: Full=Glycine cleavage system P-protein 1; GN Name=gcvP1; OrderedLocusNames=Pfl01_4392; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) 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 CC through its pyridoxal phosphate cofactor; CO(2) is released and CC the remaining methylamine moiety is then transferred to the CC lipoamide cofactor of the H protein (By similarity). CC -!- CATALYTIC ACTIVITY: Glycine + H-protein-lipoyllysine = H-protein- CC S-aminomethyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H (By similarity). CC -!- SIMILARITY: Belongs to the gcvP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000094; ABA76129.1; -; Genomic_DNA. DR RefSeq; YP_350120.1; -. DR GeneID; 3712835; -. DR GenomeReviews; CP000094_GR; Pfl01_4392. DR KEGG; pfo:Pfl01_4392; -. DR HOGENOM; Q3K7X5; -. DR OMA; Q3K7X5; PETIMIE. DR BioCyc; PFLU205922:PFL_4392-MON; -. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_00711; -; 1. DR InterPro; IPR003437; GDC-P. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR PANTHER; PTHR11773; GDC-P; 1. DR Pfam; PF02347; GDC-P; 1. DR TIGRFAMs; TIGR00461; gcvP; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Pyridoxal phosphate. FT CHAIN 1 950 Glycine dehydrogenase [decarboxylating] FT 1. FT /FTId=PRO_0000227118. FT MOD_RES 704 704 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 950 AA; 102581 MW; C03E37A90AFB210C CRC64; MTQVNLGTAN EFIARHIGPR AGDEQAMLNS LGFDSLEALS ASVIPESIKG TSVLGLDDGL SEADALAMIK GIAGKNQLFK TYIGQGYYNC HTPSPILRNL LENPAWYTAY TPYQPEISQG RLEALLNFQT LISDLTGLPI ANASLLDEAT AAAEAMTFCK RLSKNKGSHQ FFASIHSHTQ TLDVLRTRAE PLGIDVVVGD ERELTDVTPF FGALLQYPAS NGDVFDYREL TERFHAANAL VAVAADLLAL TLLTPPGEFG ADVAIGSAQR FGVPLGFGGP HAAYFSTKDA FKRDMPGRLV GVSVDRFGKP ALRLAMQTRE QHIRREKATS NICTAQVLLA NIASMYAVYH GPKGLTQIAN RVHHLTAILA KGLSALGVTV EQTSFFDTLT LATGAQTAAL HDKARAQQIN LRVIDAQRLG LSVDETTTQA DIETLWGLFA DGKTLPDFAA LAAAAQSTIP ASLVRQSPIL SHPVFNRYHS ETELMRYLRK LADKDLALDR TMIPLGSCTM KLNAASEMIP VTWAEFGALH PFAPAEQSAG YQQLTDELEA MLCAATGYDS ISLQPNAGSQ GEYAGLLAIR AYHQSRGEDR RDICLIPSSA HGTNPATANM AGMRVVVTAC DARGNVDIED LRAKAIEHRE HLAALMITYP STHGVFEEGI REICGIIHDN GGQVYIDGAN MNAMVGLCAP GKFGGDVSHL NLHKTFCIPH GGGGPGVGPI GVKSHLTPFL PGHGHMERKE GAVCAAPFGS ASILPITWMY IRMMGGAGLK RASQLAILNA NYISRRLEEH YPVLYTGSNG LVAHECILDL RPLKDSSGIS VDDVAKRLID FGFHAPTMSF PVAGTLMIEP TESESKEELD RFCDAMIRIR EEIRAVENGT LDKDDNPLKN APHTAAELVG EWTHPYSREQ AVYPVASLIE GKYWPPVGRV DNVFGDRNLV CACPSIESYA //