ID   GCSPA_NITEU             Reviewed;         453 AA.
AC   Q82WQ4;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; OrderedLocusNames=NE0609;
OS   Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS   14298).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=228410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX   PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA   Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA   Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA   Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT   "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT   chemolithoautotroph Nitrosomonas europaea.";
RL   J. Bacteriol. 185:2759-2773(2003).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000255|HAMAP-Rule:MF_00712}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00712};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00712}.
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DR   EMBL; AL954747; CAD84520.1; -; Genomic_DNA.
DR   RefSeq; WP_011111235.1; NC_004757.1.
DR   AlphaFoldDB; Q82WQ4; -.
DR   SMR; Q82WQ4; -.
DR   STRING; 228410.NE0609; -.
DR   EnsemblBacteria; CAD84520; CAD84520; NE0609.
DR   KEGG; neu:NE0609; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_4; -.
DR   OMA; MYDGASA; -.
DR   OrthoDB; 870147at2; -.
DR   PhylomeDB; Q82WQ4; -.
DR   Proteomes; UP000001416; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42806; PTHR42806; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..453
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_0000166968"
SQ   SEQUENCE   453 AA;  49646 MW;  D790D6D788F9A469 CRC64;
     MPFIPHTEED VAEMLTSIGA RSIDELFDEI PAELKTGKLT QVPPGLSEME ISRLMYERAQ
     QDGFYLSFIG AGAYEHHIPA AVWQITTRGE FYSSYTPYQA EASQGTLQLL YEYQTMMASL
     AGMDVSNASL YDGASALAEA ALMAVRQHRT SRRILVPQTV HPVYRSVMRT IVRNQAIEVV
     EVPYDPATGQ VAIDKLDQFA QEEFAALIIP QPNFFGVLEQ VDALTDWAHD KQSLAVAVVN
     PTSLAMLKPP GEWGRRGADI AVGEGQPLGI PLSSGGPYFG FMTCKQELVR QMPGRIIGRT
     TDLEGKEGFA LTLQAREQHI RRSKATSNIC TNQGLMVTAA TIYMSLLGPE GLYRVAAHSH
     ANTVALVEQL EKLPGVKKAF HSPFFHEAAL QLSVPADKVL NRLKAQGVLG GVLLENHYPD
     LKNTLLVCAT ETKTAEDLDK YTEVLRQALA ASA