ID A0A3M8CUC0_9BACL Unreviewed; 451 AA.
AC A0A3M8CUC0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EDM56_29790 {ECO:0000313|EMBL:RNB79228.1};
OS Brevibacillus fluminis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=511487 {ECO:0000313|EMBL:RNB79228.1, ECO:0000313|Proteomes:UP000271031};
RN [1] {ECO:0000313|EMBL:RNB79228.1, ECO:0000313|Proteomes:UP000271031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15716 {ECO:0000313|EMBL:RNB79228.1,
RC ECO:0000313|Proteomes:UP000271031};
RA Dunlap C.;
RT "Phylogenomics of Brevibacillus.";
RL Submitted (OCT-2018) 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_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:RNB79228.1}.
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DR EMBL; RHHQ01000029; RNB79228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8CUC0; -.
DR OrthoDB; 9771867at2; -.
DR Proteomes; UP000271031; 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}; Reference proteome {ECO:0000313|Proteomes:UP000271031}.
FT DOMAIN 3..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 451 AA; 48823 MW; 1DF662949A244B26 CRC64;
MKHRYLPQTD QDKRDMMETL GIESYEELFS DIPAEVRLNR GLNVSEALSE TELVAYFQGL
AKKNANFSTH ASFLGAGVYQ HYAPTVVNHM LLRGEFFTAY TPYQPEISQG ELQAIFEFQT
MVCELTGMEV ANSSMYDGAT SLAEAAMMAA GHTNKPRVVV SGAVHPESRE VLASYAKGQS
VELQETGYTA EGLTDLVQLE AAITEGTGAV IVQYPNFFGN VEDLKAIEQI VHSKGALLIV
SSNPVALGVL EAPGKLGADI VVGDMQPFGI PSSYGGPHCG YFATTSKLMR KMPGRIVGQT
KDEEGKRGFV LTLQAREQHI RREKATSNIC SNQALLALAA SITLSAIGKV GVQEMAMMNL
QKSHYAKQTL VNAKGVEAVF NAPFFNEFVI KLTKPVADVN KALLNAGIIG GYDLGKAYPE
LAGHMLVAVT ELRTKQEIDA FAQELEAILS A
//
