ID A0A1H9S9E7_9BACI Unreviewed; 486 AA.
AC A0A1H9S9E7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05518872_102131 {ECO:0000313|EMBL:SER80799.1};
OS Psychrobacillus sp. OK032.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX NCBI_TaxID=1884358 {ECO:0000313|EMBL:SER80799.1, ECO:0000313|Proteomes:UP000199084};
RN [1] {ECO:0000313|EMBL:SER80799.1, ECO:0000313|Proteomes:UP000199084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK032 {ECO:0000313|EMBL:SER80799.1,
RC ECO:0000313|Proteomes:UP000199084};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOGY01000002; SER80799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9S9E7; -.
DR STRING; 1884358.SAMN05518872_102131; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000199084; 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 37..308
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 486 AA; 53947 MW; B88ED47F489C8FD4 CRC64;
MHKDNQPLIF ELTREGRVGY NLPELDVPEV DVASLLPQGM LRVEEAELPE VSELDIMRHY
TALSNRNHGV DTGFYPLGSC TMKYNPKVNE SVARFPGFAN IHPLQDESSV QGAMELMYDL
QEHLIEITGM DEVTLQPAAG AHGEWTALMM IRAFHEANGD SHRTKVIVPD SAHGTNPASA
TVAGFETITV KSDENGLVDL EDLRRVAGPD TAALMLTNPN TLGLFEESIL ELAEIIHGVG
GKLYYDGANL NAVMSKARPG DMGFDCVHLN LHKTFTGPHG GGGPGSGPVG VKADLIPFLP
SPVLVKEDDK YTFDYNRPQA IGRVKPFYGN FGINVRAYTY IRSMGPDGLK AVTEYAVLNA
NYMMRRLEEH FDLPYNRHCK HEFVLSGRRQ KKLGVRTLDM AKRLLDFGYH PPTIYFPLNV
EEGMMIEPTE TESKETLDAF CDALIQIAKE VQDNPEIVQN APHTTVINRL DETKAARKPV
LRYTKA
//
