ID A0A1T5J892_9BACT Unreviewed; 434 AA.
AC A0A1T5J892;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=SAMN06298214_0775 {ECO:0000313|EMBL:SKC47463.1};
OS Bacteroidales bacterium WCE2004.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1945890 {ECO:0000313|EMBL:SKC47463.1, ECO:0000313|Proteomes:UP000189975};
RN [1] {ECO:0000313|Proteomes:UP000189975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCE2004 {ECO:0000313|Proteomes:UP000189975};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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}.
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};
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DR EMBL; FUZR01000002; SKC47463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5J892; -.
DR STRING; 1945890.SAMN06298214_0775; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000189975; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000189975}.
FT DOMAIN 6..430
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 434 AA; 47763 MW; 43C541F5BF260BFD CRC64;
MGAFSYFPQT GEDIRVMLER IGVGSLDDLY ADVPADFIYK GEYDLPSAMS EQQVRDFFEG
LAAKNARLKV FVGQGAYDHY VPSVIPYITS RSEFLTAYTP YQCEISQGTL RYIFEWQSMI
CRLTGLDCAN ASMYDGPTAA AEAMRMCVAS TKKRNSVIVS ARLLPHVIDT VRTYAKYAGI
NVVVTDKVAE EVAEGVLDLA GVIVPSINRF GIIESHLGLA ELVHQAGALL VEYCDPSALA
VVKSPAEWGA DIAVGDGQSL GIPLCFGGPY VGFMACTAAL MRKLPGRIVG QTVDASGKRC
YVLTLQAREQ HIRREKATSN ICSNESLMAL WCTVYLSLMG PEGMRKLNAL CYEGAHYLHD
ALLATGKFEQ VFDGEFLKEF CLKPRCDVQK MQQALLDAGF FAGLQTEDGY VTFCVTEKHT
REELDRIVEI VKSI
//
