ID   GCSPA_DESHY             Reviewed;         446 AA.
AC   Q24TH5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=DSY2878;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE84667.1; -; Genomic_DNA.
DR   RefSeq; YP_519111.1; -.
DR   GeneID; 3955264; -.
DR   GenomeReviews; AP008230_GR; DSY2878.
DR   KEGG; dsy:DSY2878; -.
DR   NMPDR; fig|138119.3.peg.3412; -.
DR   HOGENOM; Q24TH5; -.
DR   OMA; Q24TH5; VANASMY.
DR   BioCyc; DHAF138119:DSY2878-MON; -.
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    446       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045644.
SQ   SEQUENCE   446 AA;  49341 MW;  F98052E4B868FF36 CRC64;
     MNYVPNTVDQ QEQILTRIGV GSLEELFADI PESVRRQAQL KIREGLSELE LVKYMGRLAA
     ENKTVEEYTS YLGAGAYEHF IPSYVDQLLL RSEFYTAYTP YQPEISQGTL QAIYEFQTLV
     CELTGMDGAN ASMYDGASAL AEAALMSCDA TRRKKVLVPQ TIHPEYREVL RTYLLPRGVE
     ILEIPYQEGA VDSEALEKAL NTEVAAVLIQ SPNFFGMIEK AEEIGQMAHA KGGLLVMAVN
     PVSLGLLKSP GELGADIVVG EGQPFGNPLN FGGPYLGFLA CREKYVRRMP GRIVGATKDK
     NGKKGYVLTL QAREQHIRRE KAASNICSNE ALCALAFTIH LSGLGKRGLK EMARLNLQKA
     HYGAEEIGKL PGMSLAFQGP FFHEFVIKTE VSPRKINEAL LSHKIIGGLE LSRFYPELDQ
     HLLFCVTETK TKEDIDRLVA GMGEIK
//