ID A0A1Y0GZ92_9BACT Unreviewed; 444 AA.
AC A0A1Y0GZ92;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=CCB80_08015 {ECO:0000313|EMBL:ARU41087.1};
OS Armatimonadetes bacterium Uphvl-Ar1.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=2004467 {ECO:0000313|EMBL:ARU41087.1, ECO:0000313|Proteomes:UP000196284};
RN [1] {ECO:0000313|EMBL:ARU41087.1, ECO:0000313|Proteomes:UP000196284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uphvl-Ar1 {ECO:0000313|EMBL:ARU41087.1,
RC ECO:0000313|Proteomes:UP000196284};
RA Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA Dittmann E.;
RT "Draft genome sequences of three Uncultured Armatimonadetes, binned from a
RT Microcystis sp. enrichment culture and from Microcystis bloom
RT metagenomes.";
RL Submitted (MAY-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, 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}.
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DR EMBL; CP021423; ARU41087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0GZ92; -.
DR OrthoDB; 9771867at2; -.
DR Proteomes; UP000196284; Chromosome.
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:UP000196284}.
FT DOMAIN 3..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 444 AA; 48418 MW; 7168458603A5624C CRC64;
MPYVPHTEKD VADMLATIGV KSIDDLFVEI PEELKLKEPL NIPSRLDEHA LLGRLQALSE
QNTDLTRVTC FLGAGIYDKF IPATVGAVIS RGEYLTAYTP YQPEASQGYL QTIYEFQSMI
AELYGMDLAN ASMYDGATSM AEAAIMATGI KKRTKVAASR AIHPHYRKVL GTYTWSMDIS
VDDLPDSNGA TQDYSKLTED HACLIVQYPN FYGIIEDLAE ARKAADRVGA ILIVVADPTA
CAILPPPGEF GADIVVGEGQ PLGIPMGFGG PLLGLFACKQ EFVRLIPGRI VGRTTDAQDR
SGYTMTLRTR EQDIRREKAT SNICTNEALM ALASTVYMSA LGKNGMEQVA HSTVRNTQYA
IEQLTQTGAK LRFPGKVFGE FVLELSKSAT SVRDGLLQRG ILAGLPLGDY DPTLENCLLV
AVTEIRTKAQ IDDFANKLRA ELSN
//
