ID A0A088T212_9BACT Unreviewed; 481 AA.
AC A0A088T212;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ECO:0000313|EMBL:AIO18976.1};
GN ORFNames=KQ51_01099 {ECO:0000313|EMBL:AIO18976.1};
OS Candidatus Izimaplasma bacterium HR1.
OC Bacteria; Mycoplasmatota; Candidatus Izimaplasma.
OX NCBI_TaxID=1541959 {ECO:0000313|EMBL:AIO18976.1, ECO:0000313|Proteomes:UP000029408};
RN [1] {ECO:0000313|Proteomes:UP000029408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|Proteomes:UP000029408};
RA Skennerton C.T., Haroon M.F., Tyson G.W., Orphan V.J.;
RT "Phylogenomic Analysis of Candidatus Izimaplasma species: Representatives
RT from a Novel Mollicute Clade found in Ocean Sediments.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AIO18976.1, ECO:0000313|Proteomes:UP000029408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:AIO18976.1,
RC ECO:0000313|Proteomes:UP000029408};
RX PubMed=27058507; DOI=10.1038/ismej.2016.55;
RA Skennerton C.T., Haroon M.F., Briegel A., Shi J., Jensen G.J., Tyson G.W.,
RA Orphan V.J.;
RT "Phylogenomic analysis of Candidatus 'Izimaplasma' species: free-living
RT representatives from a Tenericutes clade found in methane seeps.";
RL ISME J. 10:2679-2692(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|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; CP009415; AIO18976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A088T212; -.
DR STRING; 1541959.KQ51_01099; -.
DR KEGG; mbj:KQ51_01099; -.
DR PATRIC; fig|1541959.3.peg.1053; -.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_5_0_14; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000029408; 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 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:UP000029408}.
FT DOMAIN 29..302
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 347..446
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ SEQUENCE 481 AA; 53615 MW; A2E69D2B1BB8EE67 CRC64;
MYYDNLIFEI SQKDRKGYSL PNYGIKQYGI PKELLRSEEA ILPEVSELEA VRHYTNVSFK
NFGVEKGFYP LGSCTMKYNP KINQDIASLP GFNLHPYQPL STIQGALEVY YETQRILSEL
SGLDTFTLNP YAGAHGELVG LMIMKRYHED RNDTKRNKII VPDSAHGTNP ASATVAGFDT
VEVKSNEDGT VNLEDLKSVL NDEIAGIMLT NPNTVGIFEK DIYEISELVH DAGGLLYYDG
ANLNPILGIA RPGDMGFDIM HINLHKTFST PHGGGGPGSG PVGVVDHLVK YLPKPVVKKG
KDGFYLEEDN ETTLGQISHF YGNFGVVIKA YTYLLSIGKE NFSNVGKLSV LNANYIKESL
RDLYLLPIKG VCKHEFVFDG LIDKSDHVTT LDIAKRLLDY DVHPPTIYFP LVVKEAIMIE
PTETESKVAV DNFIEVMRKV AIEAKENPDL VKGAPYNTVV KRLDEAQAAR KPIVKYRDLL
K
//
