ID   GCSPB_LEGPC             Reviewed;         484 AA.
AC   A5I9T3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713};
GN   OrderedLocusNames=LPC_0134;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Pseudomonadota; 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_00713}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00713};
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_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR   EMBL; CP000675; ABQ54133.1; -; Genomic_DNA.
DR   RefSeq; WP_011945314.1; NZ_JAPMSS010000003.1.
DR   AlphaFoldDB; A5I9T3; -.
DR   SMR; A5I9T3; -.
DR   KEGG; lpc:LPC_0134; -.
DR   HOGENOM; CLU_004620_5_0_6; -.
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   Gene3D; 6.20.440.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00713; GcvPB; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR023012; GcvPB.
DR   InterPro; IPR049316; GDC-P_C.
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; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..484
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_1000045694"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   484 AA;  53367 MW;  0B910AE0900F9FF1 CRC64;
     MLIFELSKTG RQAKAQIPRA VGKNYSIPEE FQRKSPPRLP ACSELQVVRH FTCLSQKNFS
     IDTNFYPLGS CTMKYNPRGV HKAASLPGFI NRHPLAMDNE SQGFLETLYK LQNYISEITG
     MPGVSLTPMA GSQGEFAGVA MIKAYHQSRG DTARDEILIP DAAHGTNPAS AVMCGFKVVE
     IATAPDGDID LDELKRKVGP RTAGIMLTNP STLGLFMRQI KEIASLVHQA GGLLYYDGAN
     LNAILGKVRP GDMGFDVMHL NLHKTFATPH GGGGPGAGPV AVGKRLIPYM PLPVVKKTDS
     GYHWATRQDY PQSIGRLSCF MGNAGILLRA YFYMLVLGKE GLLRVSEFAT LNANYLLKEL
     TKVGYTAAYP DRRASHEFIL TLNSEKKNYD VTAMDFAKRL LDYGVHAPTT YFPLLVPECL
     LIEPPETESK EELDAFVAVM KTIREEASKQ PDILKTAPHT LPVKRLDDVK AARELDLNYF
     ATHE
//