ID A0A1V1PV66_9PROT Unreviewed; 446 AA.
AC A0A1V1PV66;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=U91I_03898 {ECO:0000313|EMBL:GAN00233.1};
OS alpha proteobacterium U9-1i.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1605283 {ECO:0000313|EMBL:GAN00233.1, ECO:0000313|Proteomes:UP000188260};
RN [1] {ECO:0000313|EMBL:GAN00233.1, ECO:0000313|Proteomes:UP000188260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U9-1i {ECO:0000313|EMBL:GAN00233.1,
RC ECO:0000313|Proteomes:UP000188260};
RA Okano K., Furuta S., Ichise S., Miyata N.;
RT "Whole-Genome Sequences of Two Manganese(II)-Oxidizing Bacteria, Bosea sp.
RT Strain BIWAKO-01 and Alphaproteobacterium Strain U9-1i.";
RL Genome Announc. 4:e01309-16(2016).
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|HAMAP-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; Evidence={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:GAN00233.1}.
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DR EMBL; BBSY01000004; GAN00233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1PV66; -.
DR STRING; 1605283.U91I_03898; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000188260; 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 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; 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:UP000188260}.
FT DOMAIN 1..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 446 AA; 47278 MW; 6DFACA05CB90348D CRC64;
MRYLPLTETD RKQMLALVGA KSIDELYADV PKGALLKTHV DLPKAQGELE VTRHLQRLAE
KNTPAGRTAF FLGAGAYRHH VPASVDHLIQ RSEFLTAYTP YQPEIAQGTL QALYEFQSQV
AMLLNMEVSN ASMYDGSTAC AEAAMMAARV TKRNRIVFSG GVHPHYVSTA RTACEALGLE
VVALPAAVDD EAAVTLALGA DVAAVIVQSP NVFGTITDLK PIADAAHGAG ALMVANFTEC
LAFGMIEPPG AMDADIVCGE GQSIGNALNF GGPYVGLFAV KEKYLRQMPG RVAGETLDAD
GKRGFVLTLS TREQHIRREK ATSNICTNSG LCQLAWTMHM TLLGEAGLSQ LAALNHEKAM
ALADALAGVK GVEVLTKRFF NEIALKLPKP AQGVVDALAA KGVIAGVAMS RLDPAAGMDD
VLITCATETN TDEDIAAFVK ALKAVL
//
