ID A0A060M3C9_9BACI Unreviewed; 494 AA.
AC A0A060M3C9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=BleG1_2472 {ECO:0000313|EMBL:AIC95048.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95048.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC95048.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC95048.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
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}.
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DR EMBL; CP003923; AIC95048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060M3C9; -.
DR STRING; 1246626.BleG1_2472; -.
DR KEGG; ble:BleG1_2472; -.
DR PATRIC; fig|1246626.3.peg.2470; -.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_5_0_9; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000027142; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027142}.
FT DOMAIN 30..299
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 355..458
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 275
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ SEQUENCE 494 AA; 55043 MW; D48143375E1E1482 CRC64;
MTVQNGGMAL IFEESKEGRL GHSLPELDII EEDIGSLIPE EFLREREPEL PQVSELQIMR
HYTALSRRNH GVDSGFYPLG SCTMKYNPKV NEDVARISGL SNVHPYQPAY QVQGSLKMLY
QLQTSLAEIT GMDEVTLQPA AGAHGEWTGL MMIRAYHEAN GDFKRTKVIV PDSAHGTNPA
SATVAGFDSV TVRTNEIGLV DLDHLREVVN EETAALMLTN PNTLGLFEAD IVEMASIIHE
AGGKLYYDGA NSNAILGITR PGDMGFDVVH LNLHKTFTGP HGGGGPGSGP VGVKKDLLPF
LPKPVLVKKA DQYEFDYQRP QSIGRVKPYY GNYGINLRAY TYIRTMGAEG LRLVSEYAVL
NANYMMRRLA PYYDLPYTQH CKHEFVLSGR RQKKLGVRTL DIAKRLLDFG YHPPTIYFPL
NVEECMMIEP TETESKETLD AFIDAMIQIA VEAEKTPEVV QEAPHHTVVS RLDETLAARK
PILKYERHGE TVHS
//
