ID A0A1R1RU57_9BACI Unreviewed; 484 AA.
AC A0A1R1RU57; A0A1R1QAL7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
GN Name=gcvPB {ECO:0000256|HAMAP-Rule:MF_00713};
GN ORFNames=BTA30_13535 {ECO:0000313|EMBL:OMI29540.1}, BW143_19565
GN {ECO:0000313|EMBL:OMH99884.1};
OS Bacillus swezeyi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1925020 {ECO:0000313|EMBL:OMI29540.1, ECO:0000313|Proteomes:UP000187536};
RN [1] {ECO:0000313|EMBL:OMI29540.1, ECO:0000313|Proteomes:UP000187536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41282 {ECO:0000313|EMBL:OMH99884.1,
RC ECO:0000313|Proteomes:UP000187367}, and NRRL B-41294
RC {ECO:0000313|EMBL:OMI29540.1, ECO:0000313|Proteomes:UP000187536};
RA Dunlap C.;
RT "Bacillus phylogenomics.";
RL Submitted (DEC-2016) 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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00713};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00713}.
CC -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00713}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMI29540.1}.
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DR EMBL; MTJL01000044; OMH99884.1; -; Genomic_DNA.
DR EMBL; MRBK01000014; OMI29540.1; -; Genomic_DNA.
DR RefSeq; WP_076761838.1; NZ_MTJL01000044.1.
DR AlphaFoldDB; A0A1R1RU57; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000187367; Unassembled WGS sequence.
DR Proteomes; UP000187536; Unassembled WGS sequence.
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 CDD; cd00613; GDC-P; 1.
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; IPR023012; GcvPB.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR049315; GDC-P_N.
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; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00713}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00713}.
FT DOMAIN 49..300
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 353..454
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ SEQUENCE 484 AA; 53977 MW; DA69ECCD0913475F CRC64;
MNNQDQSLIF EVSKDGRVGY SLPELDVPET DVSDLIAEAY IRDEPAELPE VSELDIMRHY
TALSRRNHGV DSGFYPLGSC TMKYNPKLNE KIARIPGFSS IHPLQDERTV QGALELLYDL
SKHLEEITGM DEVTLQPAAG AHGEWTGLMM IRAFHEANGD HKRTKVIVPD SAHGTNPASA
TVAGFETVTV KSNADGLVDL EDLKRVVDKE TAALMLTNPN TLGLFEENIL EMAEIVHQAG
GKLYYDGANL NAVLSKARPG DMGFDVVHLN LHKTFTGPHG GGGPGSGPVG VKKELIPYLP
KPVLVKKDGR YTFDNDRPQS IGRVKPYYGN FGINVRAYTY IRSMGPDGLK EVTENAVLNA
NYMMRKLAPY YDLPFDRHCK HEFVLSGRRQ KKLGVRTLDI AKRLLDFGFH PPTIYFPLNV
EECIMIEPTE TESKETLDAF IETMIQIARE AEENPEIVQE APHTTVVKRM DETKAARQPV
LRFE
//
