ID GCSPA_FRATF Reviewed; 455 AA. AC A7NAH8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 12. DE RecName: Full=Probable glycine dehydrogenase [decarboxylating] subunit 1; DE EC=1.4.4.2; DE AltName: Full=Glycine decarboxylase subunit 1; DE AltName: Full=Glycine cleavage system P-protein subunit 1; GN Name=gcvPA; OrderedLocusNames=FTA_0505; OS Francisella tularensis subsp. holarctica (strain FTA). OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales; OC Francisellaceae; Francisella. OX NCBI_TaxID=458234; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Godbole S., Zhou L., Bruce D., Crawford R., Detter C., Dempsey M.P., RA Lion C., Munk C., Noronha J., Scheuermann R.H., Brettin T.S.; RL Submitted (AUG-2007) 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 -!- SUBUNIT: The glycine cleavage system is composed of four proteins: CC P, T, L and H. In this organism, the P 'protein' is an heterodimer CC of two subunits (By similarity). CC -!- SIMILARITY: Belongs to the gcvP family. N-terminal subunit CC subfamily. 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; CP000803; ABU60981.1; -; Genomic_DNA. DR RefSeq; YP_001427937.1; -. DR GeneID; 5523214; -. DR GenomeReviews; CP000803_GR; FTA_0505. DR KEGG; fta:FTA_0505; -. DR OMA; A7NAH8; VANASMY. 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_00712; -; 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. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase. FT CHAIN 1 455 Probable glycine dehydrogenase FT [decarboxylating] subunit 1. FT /FTId=PRO_1000045650. SQ SEQUENCE 455 AA; 49639 MW; 02A749BC0A2E869C CRC64; MSFIPHKLEQ IKKMLDTIGA SSVDQLFDEI PRHLRADTLN IKDGINEIQL ANLMRKRANK NHHNINYIGA GAYSHHIPAA IWDIVARGEF YTAYTPYQAE ASQGGLQVIY EFQTMMAGLT GMDASNASMY DGATALAESV LMAIRSNKKA KSQKVLIAEA LHPTYLRVLE TITKHQGIEF DIVNLDSKNG KTDVTKLEDF ANTNYAAVVI QSPNFLGQLA DVDGITNWAH KHGALVIAVT NPMSLAILKS PAEWGDNGAD IVCGEGQPIG VPLASGGPYF GFMTCKMAHV RQMPGRIVGK TVDLDGNEGF CLTLQAREQH IRRAKATSNI CTNQGLMVTA ATIYMSLLGA EGLERVASIS HENTQTLATE LAKINGVSIR FNSAFFNEVV IDLPVNAETF VTEMEKEAID AGYFLGEYHS DLANSIMVCA TEIHTSEDIK EYIEATKKVL ARIGG //