ID   GCSPA_OCEIH             Reviewed;         449 AA.
AC   Q8CXE0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=OB1903;
OS   Oceanobacillus iheyensis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=182710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
RX   MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya
RT   Ridge and its unexpected adaptive capabilities to extreme
RT   environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13859.1; -; Genomic_DNA.
DR   RefSeq; NP_692824.1; -.
DR   GeneID; 1018395; -.
DR   GenomeReviews; BA000028_GR; OB1903.
DR   KEGG; oih:OB1903; -.
DR   NMPDR; fig|221109.1.peg.1903; -.
DR   HOGENOM; Q8CXE0; -.
DR   OMA; Q8CXE0; VANASMY.
DR   BioCyc; OIHE221109:OB1903-MON; -.
DR   BRENDA; 1.4.4.2; 278212.
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    449       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_0000166969.
SQ   SEQUENCE   449 AA;  49746 MW;  75554C029B2B1750 CRC64;
     MEFRYLPMTN QDKQEMLDAI GIKSTEELFS DIPEHVRFKG EMNLKAPISE YELTKELTEL
     ASRNIHTKEY TSFLGAGVYD HYIPSVVDHV ISRSEFYTAY TPYQPEISQG ELQAIFEFQT
     MISELTGLPV ANSSMYDGGT ALAEAVNLSA AHTKRKKVLV SKAVHPEYRA VIDSYTRGQS
     IDIVEIDTVN GVTDLAQLDQ AIDETIAGVV VQYPNFFGQL EPMKKIEQLL ENHQKTMLIV
     SSNPLALGYL TPPGEFGADI VTGDTQVFGI PAQFGGPHCG YFATSKKLMR KVPGRLVGET
     VDEEGTRGYV LTLQAREQHI RRDKATSNIC SNQALNALAS SVAMSSIGKH GLRKLASVNM
     QKARYARKKL LEAGVELAFD GSFFNEFVIK VPGSVSKINK QLLDKGIIAG YDLAKDDKSL
     EGYMLIAVTE VRTKQEIDQF VKELGDIHV
//