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GCSPA_LEGPH
ID   GCSPA_LEGPH             Reviewed;         456 AA.
AC   Q5ZZ95;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=lpg0116;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU26223.1; -; Genomic_DNA.
DR   RefSeq; WP_010945877.1; NC_002942.5.
DR   RefSeq; YP_094170.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZZ95; -.
DR   SMR; Q5ZZ95; -.
DR   STRING; 272624.lpg0116; -.
DR   PaxDb; Q5ZZ95; -.
DR   PRIDE; Q5ZZ95; -.
DR   EnsemblBacteria; AAU26223; AAU26223; lpg0116.
DR   GeneID; 66489321; -.
DR   KEGG; lpn:lpg0116; -.
DR   PATRIC; fig|272624.6.peg.122; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_6; -.
DR   OMA; MYDGASA; -.
DR   Proteomes; UP000000609; 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..456
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000045662"
SQ   SEQUENCE   456 AA;  49821 MW;  FEECB7D95E4E0959 CRC64;
     MPYIPHTPDD TKEMLEAIGA QDIQDLFDEI PASLQYAGFQ NIPAGINEME MLKEAQNQAQ
     KNRNGICFIG AGCYEHHIPA AVWDIASRGE FLTAYTPYQA EASQGTLQLL YEYQTMICEL
     TGMEVSNASM YDGATALAEA VLMAVRLNKH SKTNRVLIAG TVHPFYRETI ETIVRNQHIE
     VITLPFDEQQ GITNLGSLNQ YTGEDITALV IAQPNFFGCL EQVDKMTSWA HHNKTISVAC
     VNPTSLALLK PPGSWGEHGV DIVCGEGQPL GSPMASGGPY FGFLSTRMAH VRQMPGRIIG
     RTVDKDGKTG FSLTLQAREQ HIRRAKATSN ICTNQGLLVT AATIYMSLLG PEGLSQVATQ
     CHQNTHELIT ALTQIEGVEL AFKAPFFHEA LIKLNQPVQS VLQQLADAGI AGGYAPEQHY
     PQLANTLLVC ATEVRTAEDI AKYAKTLKTI MSKRGA
 
 
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