ID   GCSPA_MARMM             Reviewed;         447 AA.
AC   Q0AMJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Mmar10_2209;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) 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; CP000449; ABI66501.1; -; Genomic_DNA.
DR   RefSeq; YP_757439.1; -.
DR   GeneID; 4284978; -.
DR   GenomeReviews; CP000449_GR; Mmar10_2209.
DR   KEGG; mmr:Mmar10_2209; -.
DR   NMPDR; fig|394221.5.peg.2170; -.
DR   HOGENOM; Q0AMJ2; -.
DR   OMA; Q0AMJ2; 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    447       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045667.
SQ   SEQUENCE   447 AA;  48030 MW;  6C3833CB7510CA34 CRC64;
     MRYLPHTDTD RKAMLDAIGV ASIDDLFTDV PEAARLDGLI DLPTKQTELQ VERALAAMSS
     RNVAASHAPF FVGAGAYKHH VPATVDHLIQ RSEFLTAYTP YQPEISQGTL QTLFEFQTQV
     ALLTGMDVAN ASMYDGSTAC AEAVMMAARV TRRTKAVMAG SVHPHYVEAS QTLAKYSDVS
     ISVTDAAPAD LDAVIAEIDD TTACVVIQTP DIFGRLHDLR EVSRIAHEKG ALVIAVFTEA
     VSLGLVEAPG HMGADIAVGE GQSIGVGLNF GGPYVGLFAC KDDRRFIRQM PGRLAGETID
     ADGRRGYVLT LSTREQHIRR DKATSNICTN AGLCSLAWTI HMTLLGEKGL TQLARLNHET
     ACELADALSA VPGVELVNET FFNEFTILLP KNADQVVNDL ARFGVLGGVP ASRLYPGRFE
     NYLIIAATET NTPEDIAVFA KALAGVL
//