ID I2HT29_9BACI Unreviewed; 448 AA.
AC I2HT29;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN ORFNames=MY7_2220 {ECO:0000313|EMBL:EIF13888.1};
OS Bacillus sp. 5B6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1127743 {ECO:0000313|EMBL:EIF13888.1, ECO:0000313|Proteomes:UP000005799};
RN [1] {ECO:0000313|EMBL:EIF13888.1, ECO:0000313|Proteomes:UP000005799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5B6 {ECO:0000313|EMBL:EIF13888.1,
RC ECO:0000313|Proteomes:UP000005799};
RX PubMed=22740678; DOI=10.1128/JB.00682-12;
RA Kim B.K., Chung J.H., Kim S.Y., Jeong H., Kang S.G., Kwon S.K., Lee C.H.,
RA Song J.Y., Yu D.S., Ryu C.M., Kim J.F.;
RT "Genome Sequence of the Leaf-Colonizing Bacterium Bacillus sp. Strain 5B6,
RT Isolated from a Cherry Tree.";
RL J. Bacteriol. 194:3758-3759(2012).
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_00712}.
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_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:0000256|HAMAP-Rule:MF_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00712}.
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:EIF13888.1}.
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DR EMBL; AJST01000001; EIF13888.1; -; Genomic_DNA.
DR RefSeq; WP_007612535.1; NZ_AJST01000001.1.
DR AlphaFoldDB; I2HT29; -.
DR PATRIC; fig|1127743.3.peg.2177; -.
DR Proteomes; UP000005799; 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 GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 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_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
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; PTHR42806; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 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_00712}.
FT DOMAIN 3..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 448 AA; 49203 MW; FBF4088F20D1AB4D CRC64;
MKHRYLPATE QDKKEMLKAI GAETIDELFA DIPENVRFQK DYRIKQAKSE TELTRELTKL
AAKNKDAVTY ASFLGAGVYD HYQPVIVDHV ISRSEFYTAY TPYQPEISQG ELQAIFEFQT
MICELTGMDI ANSSMYDGGT ALAEAAMLAS GHTKKKKIVI SAAVHPESRD VLKTYAKGQY
IEVVEVPAKN GVTDLEALEH AVCDETAAVI VQYPNFFGQI EPLKDIEPLA HKGNSQLIVS
SNPLALGILR PPGAYGADIV VGDAQPFGIP AVFGGPHCGY FAVTKKLMRK VPGRLVGQTE
DENGRRGFVL TLQAREQHIR RDKATSNICS NQALNALAAS VAMTALGKNG VKDMARQNIL
KADYARRQAE KAGLHVAFDG PIFNEFAVRL NLSVKEANRR LLQDGIIGGY DLGLAYPELN
QHMLIAVTEL RTKEEIDSLI AGLGDQHE
//
