ID   F8FPU0_PAEMK            Unreviewed;       491 AA.
AC   F8FPU0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-APR-2013, entry version 13.
DE   RecName: Full=Probable glycine dehydrogenase [decarboxylating] subunit 2;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P-protein subunit 2;
DE   AltName: Full=Glycine decarboxylase subunit 2;
GN   Name=gcvPB; OrderedLocusNames=KNP414_07403;
OS   Paenibacillus mucilaginosus (strain KNP414).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1036673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNP414;
RA   Wang J., Hu S., Hu X., Zhang B., Dong D., Zhang S., Zhao K., Wu D.;
RT   "Complete genome sequence of Paenibacillus mucilaginosus KNP414.";
RL   Submitted (JUN-2011) 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. In this organism, the P 'protein' is a heterodimer
CC       of two subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit
CC       subfamily.
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DR   EMBL; CP002869; AEI45907.1; -; Genomic_DNA.
DR   RefSeq; YP_004645777.1; NC_015690.1.
DR   EnsemblBacteria; AEI45907; AEI45907; KNP414_07403.
DR   GeneID; 10860282; -.
DR   KEGG; pms:KNP414_07403; -.
DR   KO; K00283; -.
DR   BioCyc; PMUC1036673:GJD1-7403-MONOMER; -.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   HAMAP; MF_00713; GcvPB; 1; -.
DR   InterPro; IPR020580; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR023012; GDC_P_su2.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase; Pyridoxal phosphate.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   491 AA;  54086 MW;  7B846599A18317AF CRC64;
     MTEAFRVKDD QPLIFELSRP GRTAYSLPPC DVPETDPREL IPAELLREKP PALPEVYEVD
     VVRHYTALSR RNFGVDNGFY PLGSCTMKYN PKLHEDAARL DGFAKIHPYQ PEESIQGALE
     LLYRLQEDLA GLTGMDEVTL QPAAGAHGEW TGLMMIRAYH EARGEKRSKV LVPDSSHGTN
     PASATAAGFE TVTLPSGPDG LVDLERLREA AGPDTAALML TNPNTLGLFE SRITEIAAIV
     HEAGGLLYYD GANSNAIMGI TRPGDMGFDV VHLNLHKTMS TPHGGGGPGA GPVGVKKLLA
     PFLPKPVVAR RADGSYTLDG ERPDSIGRVK AFYGNFGILL RAYAYIRSYG PEGLRRVSEC
     AVLNANYMLR RLAGHYDVPY DRICKHEFVL SGRGLKKHGI RTLDVAKRLL DFGYHPPTIY
     FPLNVEECIM IEPTETESKE TLDGFIDTMI RIAEEAERDP DLLKNAPYTT PVRRLDETQA
     ARKPVLNCSC E
//