ID   GCSPA_ERYLH             Reviewed;         453 AA.
AC   Q2N886;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=ELI_10065;
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=314225;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H.,
RA   Friedman R., Venter J.C.;
RL   Submitted (SEP-2005) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000157; ABC64105.1; -; Genomic_DNA.
DR   RefSeq; YP_458902.1; -.
DR   GeneID; 3870006; -.
DR   GenomeReviews; CP000157_GR; ELI_10065.
DR   KEGG; eli:ELI_10065; -.
DR   NMPDR; fig|314225.3.peg.1021; -.
DR   OMA; Q2N886; VANASMY.
DR   BioCyc; ELIT314225:ELI_10065-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    453       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045648.
SQ   SEQUENCE   453 AA;  48757 MW;  53AF83EEC23CEA0E CRC64;
     MRYLPLTDTD RSEMLSVVGA SSIDDLFVDV PKEARLDGPI RDLPMHASEM AVEKHMRARA
     AKNLVAGDVP FFLGAGAYRH HVPASVDHII QRGEFLTAYT PYQPEIAQGT LQMLFEFQTQ
     VAKLYGCEVA NASMYDGSTA CWEAISMASR VTKRNRAVLS GALHPHYSEV AKTMAKYLGL
     EIADAQPAIQ AAPDNAGLTS RIDENTSCVV VQYPDILGRI ADLTEIAEAA HAKGALLIVV
     NTEPVALGAI KSPGEMGADI VVGEGQSLGV GLQFGGPYLG LFAVRDKKHV RQMPGRLCGE
     TVDAEGKRGF VLTLSTREQH IRREKATSNI CTNSGLCALA FSVHMTLLGE VGLRRLAAEN
     HRLACLTADR LAKVPGVTVL NDTFFNEFTI QVGQDAREIV RTLADKGVLA GVSLGRLYPD
     VERLSDALIV ATTETTSEDD IEALGSALEE VLA
//