ID   GCSPA_NITEC             Reviewed;         451 AA.
AC   Q0AEP9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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=Neut_1953;
OS   Nitrosomonas eutropha (strain C91).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M.,
RA   Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium,
RT   Nitrosomonas eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI60183.1; -; Genomic_DNA.
DR   RefSeq; YP_748148.1; -.
DR   GeneID; 4273340; -.
DR   GenomeReviews; CP000450_GR; Neut_1953.
DR   KEGG; net:Neut_1953; -.
DR   NMPDR; fig|335283.3.peg.1076; -.
DR   OMA; Q0AEP9; 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    451       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045670.
SQ   SEQUENCE   451 AA;  49512 MW;  1C182493E485E078 CRC64;
     MPFIPHTEED VTEMLASIGA TSIDELFDEI PAELKNGKLT QVPTGMSEME ISRLMYERAQ
     KDGFYLSFIG AGAYEHHIPA AVWQITTRGE FYSSYTPYQA EASQGTLQLL YEYQTMMASL
     AGMDVSNASL YDGASALAEA ALMAVRQHKS SRRILVPQTV HPIYRSVVRT IVRNQAIEVV
     EVPYDPATGQ VSIDQLDQFA QEEFAALIIP QPNFFGVLEQ VDTLADWAHD KQSLAIAVVN
     PTALAMLKPP GEWGRQGADI AVGEGQPLGI PLSSGGPYFG FMACKQELVR QMPGRIIGRT
     TDLEGKEGFA LTLQAREQHI RRSKATSNIC TNQGLMVTAA TIYMSLLGPE GLYRVAAQSH
     ANTLALVEQL ETLPGVKKAF HSPFFHEAVL QLSVPADEVL NKLKAQGVLG GVLLENYYPD
     LKNTLLVCAT ETKIAEDLDK YTEMLRQILK A
//