(data stored in ACNUC7421 zone)

SWISSPROT: GCSPA_LEGPC

ID   GCSPA_LEGPC             Reviewed;         456 AA.
AC   A5I9T5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 77.
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=LPC_0136;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-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 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=glycine + H(+) + N(6)-lipoyl-L-lysyl-[glycine-cleavage complex
CC         H protein] = (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}.
DR   EMBL; CP000675; ABQ54135.1; -; Genomic_DNA.
DR   RefSeq; WP_011945315.1; NC_009494.2.
DR   SMR; A5I9T5; -.
DR   EnsemblBacteria; ABQ54135; ABQ54135; LPC_0136.
DR   KEGG; lpc:LPC_0136; -.
DR   HOGENOM; HOG000132025; -.
DR   KO; K00282; -.
DR   OMA; MYDGASA; -.
DR   BioCyc; LPNE400673:LPC_RS00630-MONOMER; -.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; A5I9T5.
DR   SWISS-2DPAGE; A5I9T5.
KW   Oxidoreductase.
FT   CHAIN           1..456
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000045661"
SQ   SEQUENCE   456 AA;  49897 MW;  45C53A19F928E1F4 CRC64;
     MPYIPHTPND TKEMLEAIGA QDIQDLFDEI PASLQYAGFQ NIPAGINEME MLKEAQNQAQ
     KNRNGICFIG AGCYEHHIPA AVWDIASRGE FLTAYTPYQA EASQGTLQLL YEYQTMICEL
     TGMEVSNASM YDGATALAEA VLMAVRLNKH SKTNRVLIAG TVHPFYRETI ETIVRNQHIE
     VITLPFDEQQ GITDLGSLNQ YTGEDITALV IAQPNFFGCL EQVDKMTSWA HHNKTISVAC
     VNPTSLALLK PPGSWGEHGV DIVCGEGQPL GSPMASGGPY FGFLSTRMAH VRQMPGRIIG
     RTVDKDGKTG FSLTLQAREQ HIRRAKATSN ICTNQGLLVT AATIYMSLLG PEGLSQVATQ
     CHQNTHELIT ALTQIEGVEL AFKAPFFHEA LIKLNQPVQY VLQQLADAGI AGGYAPEQHY
     PQLANTLLVC ATEVRTAEDI AKYAKTLKTI MSKRGA
//

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