ID GCSP2_PSEF5 Reviewed; 954 AA. AC Q4K416; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Glycine dehydrogenase [decarboxylating] 2; DE EC=1.4.4.2; DE AltName: Full=Glycine decarboxylase 2; DE AltName: Full=Glycine cleavage system P-protein 2; GN Name=gcvP2; OrderedLocusNames=PFL_5959; OS Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15980861; DOI=10.1038/nbt1110; RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A., RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J., RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., RA Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., RA Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., RA Pierson L.S. III, Thomashow L.S., Loper J.E.; RT "Complete genome sequence of the plant commensal Pseudomonas RT fluorescens Pf-5."; RL Nat. Biotechnol. 23:873-878(2005). 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; CP000076; AAY95149.1; -; Genomic_DNA. DR RefSeq; YP_263017.1; -. DR GeneID; 3480331; -. DR GenomeReviews; CP000076_GR; PFL_5959. DR KEGG; pfl:PFL_5959; -. DR NMPDR; fig|220664.3.peg.1152; -. DR HOGENOM; Q4K416; -. DR OMA; Q4K416; PAVNRVD. DR BioCyc; PFLU220664:PFL_5959-MON; -. DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:EC. DR GO; GO:0016829; F:lyase activity; IEA:InterPro. 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; IPR001597; ArAA_b-elim_lyase/Thr_aldolase. 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; 2. DR PANTHER; PTHR11773; GDC-P; 1. DR Pfam; PF01212; Beta_elim_lyase; 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 1 954 Glycine dehydrogenase [decarboxylating] FT 2. FT /FTId=PRO_0000227117. FT MOD_RES 704 704 N6-(pyridoxal phosphate)lysine (By FT similarity). SQ SEQUENCE 954 AA; 103396 MW; B5350A629DF79871 CRC64; MLSLSQLREP NAFLNRHLGP DAEEQQAMLA SLGLGSRAEL IEQTVPPGIR FNRALDLPPA LDEAAALARL KGYAGQNQVW TSLIGMGYHA TLTPTVILRN VLENPGWYTA YTPYQPEIAQ GRLEALLNFQ QMTIDLTGLD LANASLLDEA TAAAEAMALA KRVSKSSSNL FFVDEHCHPQ TVSVVRTRAE GFGFELVVGG VDELSGHQVF GALLQYPDTH GEIRDLRPLI DQLHAQQALA CVAADLLSLL LLTPPGELGA DVVLGSSQRF GVPMGYGGPH AAFFACRDDY KRAMPGRIIG VSKDARGQVA LRMALQTREQ HIRREKANSN ICTAQVLLAN IAGFYAVYHG PAGLKRIAQR VHRLTCILAV GLERHGIARV NRHFFDTLTL EVGGSQTAII ESARAQQINL RILGRGRLGL SLDETCDEST VTRLFDVFLG ADHGLDVSNL DAEALESGIP DPLLRRTRYL THPVFSAHHS ETEMLRYLKQ LENKDLALNQ SMIPLGSCTM KLNASSEMIP ITWPEFANLH PFAPREQAAG YGLLIAELER WLCAITGFDA ICMQPNSGAQ GEYAGLLAIR RYHESRRQGG RHVCLIPASA HGTNPASAQM AGMQVVIVEC DEAGNVDLED LKAKAQAAGE RLSCLMATYP STHGVYEEGI SQICEVIHSH GGQVYMDGAN LNAQVGLARP ADIGADVSHM NLHKTFCIPH GGGGPGMGPI GVRAHLAPFV ANHPVVPIDG PLPENGAVSA APWGSASILP ISWMYIALMG PQLADASEVA ILAANYLAEQ LSGAFPVLYS GRNGRVAHEC ILDLRPLKAQ TGISEEDVAK RLMDYGFHAP TMSFPVPGTL MVEPTESESK AELDRFIEAM LSIRAEIAQV QEGNWPAEDN PLKGAPHTLA DITGVWERSY SIEQAVLPTA HTRAHKYWPA VNRVDNVYGD RNLFCACVPL ADYR //