ID   GCSPA_FRAP2             Reviewed;         455 AA.
AC   B0TZJ6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 9.
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=Fphi_0338;
OS   Francisella philomiragia subsp. philomiragia (strain ATCC 25017).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=484022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Richardson P.;
RT   "Complete sequence of chromosome of Francisella philomiragia subsp.
RT   philomiragia ATCC 25017.";
RL   Submitted (DEC-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.
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DR   EMBL; CP000937; ABZ86555.1; -; Genomic_DNA.
DR   RefSeq; YP_001677056.1; -.
DR   GeneID; 5907508; -.
DR   GenomeReviews; CP000937_GR; Fphi_0338.
DR   KEGG; fph:Fphi_0338; -.
DR   OMA; B0TZJ6; 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_1000083221.
SQ   SEQUENCE   455 AA;  49664 MW;  DE1E0C9E5C1DD1FD CRC64;
     MSFIPHKPEQ IEKMLGTIGA SSIDQLFDEI PAHLRADTLK IKDGINEIQL ANQMRKRANR
     NHHNTNFIGA GAYSHHIPAA IWDIVARGEF YTAYTPYQAE ASQGGLQVIY EFQTMMAGLT
     GMDASNASMY DGATALAESV LMAIRSNKKA KSQKILIAEA LHPTYLRVLE TITKHQGIEF
     DIVNLDSKNG KTDITKLEDF ANTDYAAVVI QSPNFLGQLA DVDGITNWAH KHGALVIAVT
     NPMSLAILKS PAEWGENGAD IVCGEGQPMG VPLASGGPYF GFMTCKMAHV RQMPGRIVGR
     TVDLDGNEGF CLTLQAREQH IRRAKATSNI CTNQGLMVTA ATIYMSLLGA KGLERVASIS
     HENTTKLANE LSKLDGVNAR FNNVSFNEVV IDLPVNAEIF VTEMEKEGID AGYFLGEYHS
     DLDNSIMVCA TEIHTSEDIK EYIEATKKVL ARIGG
//