ID   GCSPA_GEOUR             Reviewed;         442 AA.
AC   A5GCZ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=Gura_0337;
OS   Geobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=351605;
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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Shelobolina E., Aklujkar M., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-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; CP000698; ABQ24553.1; -; Genomic_DNA.
DR   RefSeq; YP_001229126.1; -.
DR   GeneID; 5165879; -.
DR   GenomeReviews; CP000698_GR; Gura_0337.
DR   KEGG; gur:Gura_0337; -.
DR   NMPDR; fig|351605.3.peg.1036; -.
DR   OMA; A5GCZ8; 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    442       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000083222.
SQ   SEQUENCE   442 AA;  47142 MW;  7E815ADAE2A70EEF CRC64;
     MSYCPNTPED IREMLAAIGV ASVDALFAPI PAGLRARSFA LPDGTSEQEL LRQMKQLAGT
     DRPVTGFIGG GYYDHYIPAV VDHLSGRAEF YTAYTPYQPE CSQGTLQALF EYQTAICRLT
     GMEVSNASLY DGGTALAEAA MMALRVTGRN RLVIDGSVNP FSREIVRTYL TNLGVEIVEI
     PARDGLADRP ALTAALTDLT AAVILQNPNF FGSVEDLSDI ALTAHANGAL LIASVYPISL
     GLVKSPGAMG ADIVVGDGQS LGNPLSFGGP SFGFIATTKK YIRNLPGRII GETVDKSGRR
     GFVLTLQARE QHIKRHKATS NICSNQSLCA LRGMIFLASV GKEGLVDLAR LNRDKAEYAK
     GLLGSIKGVK LLNTAPTFNE FTIVLPKDAA EVAERLLGKG VAAGVPLGAY YHGMDNCLVV
     TVTEKRTRDE IDALAKELEG AL
//