ID A0A2K2U113_9CLOT Unreviewed; 475 AA.
AC A0A2K2U113;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C0033_01410 {ECO:0000313|EMBL:PNV64006.1};
OS Clostridium sp. chh4-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2067550 {ECO:0000313|EMBL:PNV64006.1, ECO:0000313|Proteomes:UP000236356};
RN [1] {ECO:0000313|Proteomes:UP000236356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=chh4-2 {ECO:0000313|Proteomes:UP000236356};
RA Huang C.-H.;
RT "Clostridium sp. nov. strain chh-4-2., isolated from the gut of a healthy
RT Taiwan adult.";
RL Submitted (JAN-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_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:PNV64006.1}.
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DR EMBL; PKUU01000001; PNV64006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K2U113; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000236356; 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 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:UP000236356}.
FT DOMAIN 39..291
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 340..440
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ SEQUENCE 475 AA; 52409 MW; 389248DA8292CFAC CRC64;
MKLIFERSVE GRRCSILPEC DVPVVELGAA ARKQPLHLPE VSENDISRHY TELAKATHGV
NDGFYPLGSC TMKYNPKVNE ETASLKEFTQ IHPLQPEHTV QGCLKVLKTA ETVFCEITGM
DQMTFQPAAG AHGEFTGLLL IKAYHDKRKD LKRTKIIVPD SAHGTNPASA VMAGFEVVNI
PSQEDGCVDL EKLREAVGED TAGLMLTNPN TVGLFDKNIL EITRIIHEAG GLNYYDGANL
NAVMGVVRPG DMGFDVVHLN LHKTFSTPHG GGGPGSGPVG CKEFLAEFLP GLKVVEQDGY
HMEEYASSVG MVKSFYGNFL VVVKALTYAL MLGKDGIPDA CKNAVLNANY IRVKLSGKYH
MPYEETCMHE FVMSLEQEKH QIHVSAMDIA KALLDYGIHP PTMYFPLIVH EALMVEPTET
ESKEGLDELI GAFLDIYEKA ESDPEWIQGS PHTTRIKRLD EVAAARSPKL KYMFE
//
