ID   GCSPA_NOVAD             Reviewed;         452 AA.
AC   Q2G781;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Saro_1852;
OS   Novosphingobium aromaticivorans (strain DSM 12444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-2006) 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; CP000248; ABD26292.1; -; Genomic_DNA.
DR   RefSeq; YP_497126.1; -.
DR   GeneID; 3918414; -.
DR   GenomeReviews; CP000248_GR; Saro_1852.
DR   KEGG; nar:Saro_1852; -.
DR   HOGENOM; Q2G781; -.
DR   OMA; Q2G781; VANASMY.
DR   BioCyc; NARO279238:SARO_1852-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    452       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045672.
SQ   SEQUENCE   452 AA;  47592 MW;  BCD17DC65E74DCFA CRC64;
     MRYLPLTDAD RSAMLSVVGA GSVDELFADV PAEARLSAPI AGLPNHASEM AVERHMARLS
     ANNVTAGSVP FFLGAGAYRH HVPATVDHMI QRGEFLTAYT PYQPEIAQGT LQVLFEFQTQ
     VARLFGTDVA NASLYDGSTA CWEAIAMAGR ITKRGKALLS GGLHPHYVET ARTMARFTGD
     VLDTSAPVLT AAPDDDALVA RIDGETSCVV VQYPDILGRI PDLAKIAAAA QAQGALLITV
     VTEPVALGVL QSPGSLGADI VVGEGQSLGV GLQFGGPYLG LFGCREKYLR QIPGRLCGET
     VDADGKRGFV LTLSTREQHI RREKATSNIC TNSGLCALAF SIHLTLLGGS GLADMARLSH
     LAARKTAAAL AQVSGIEVVN SHFFNEFTVA LPHDARQIVR DLADRHVLGG VSLGRLYPQE
     AALANGMVVA ATECTTDEDI AALVAALKEV LA
//