ID   GCSPA_BACA2             Reviewed;         448 AA.
AC   A7Z6M3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-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=RBAM_022880;
OS   Bacillus amyloliquefaciens (strain FZB42).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant
RT   growth-promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS74649.1; -; Genomic_DNA.
DR   RefSeq; YP_001421880.1; -.
DR   GeneID; 5461361; -.
DR   GenomeReviews; CP000560_GR; RBAM_022880.
DR   KEGG; bay:RBAM_022880; -.
DR   OMA; A7Z6M3; 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    448       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045637.
SQ   SEQUENCE   448 AA;  49172 MW;  7621707286981494 CRC64;
     MKHRYLPATE QDKKEMLKAI GAETIDELFA DIPENVRFQK DYQIKKAKSE TELTRELTKL
     AAKNKDAVTY ASFLGAGVYD HYQPVIVDHV ISRSEFYTAY TPYQPEISQG ELQAIFEFQT
     MICELTGMDI ANSSMYDGGT ALAEAAMLAS GHTKKKKIVI SAAVHPESRD VLKTYAKGQY
     IEVVEVPAKN GVTDLEALEH AVCDETAAVI VQYPNFFGQI EPLKDIEPLA HKGNSQLIVS
     SNPLALGILT PPGAYGADIV VGDAQPFGIP AAFGGPHCGY FAVTKKLMRK VPGRLVGQTE
     DENGRRGFVL TLQAREQHIR RDKATSNICS NQALNALAAS AAMTALGKNG VKDMARQNIL
     KADYARRQAE KAGLHVAFDG PIFNEFAVRL NLPVKEANRR LLQDGIIGGY DLGLAYPELN
     QHMLIAVTEL RTKEKIDSLI ARLGDQHE
//