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