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Database: UniProt
Entry: A0A2A1ZSE5_9BACT
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ID   A0A2A1ZSE5_9BACT        Unreviewed;       482 AA.
AC   A0A2A1ZSE5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=CI105_03065 {ECO:0000313|EMBL:PAT02336.1};
OS   Candidatus Izimaplasma bacterium ZiA1.
OC   Bacteria; Mycoplasmatota; Candidatus Izimaplasma.
OX   NCBI_TaxID=2024899 {ECO:0000313|EMBL:PAT02336.1, ECO:0000313|Proteomes:UP000217826};
RN   [1] {ECO:0000313|EMBL:PAT02336.1, ECO:0000313|Proteomes:UP000217826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZiA1 {ECO:0000313|EMBL:PAT02336.1,
RC   ECO:0000313|Proteomes:UP000217826};
RA   Kim S.-J., Rhee S.-K.;
RT   "Direct submision.";
RL   Submitted (AUG-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_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:ARBA00033655, 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}.
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:PAT02336.1}.
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DR   EMBL; NQYJ01000002; PAT02336.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A1ZSE5; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000217826; 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   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:UP000217826}.
FT   DOMAIN          42..303
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          348..447
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   482 AA;  53596 MW;  62191C4BCAF14669 CRC64;
     MYYDKLAFEI SKSGHTGYSL PKNVFKDYKI SESLLREEKI VLPELTEFEA VRHYTNVSFK
     NFGVEKGFYP LGSCTMKYNP KINEDIAALP GLSNVHPYQP TKTVQGLLEI YYNTQKILSE
     ISGLYEFTLN PYAGAHGELV GLMIMKKFHQ DNGDFKRTKV IVPESAHGTN PASATVAGFE
     SVEVKSNQDG TVNIESLKEV LGDDIAGIML TNPNTIGIFE KDILEIAKLV HEAGGLLYYD
     GANLNPLLGQ ARPGDMGFDI MHINIHKTFS TPHGGGGPGS GPVGVNKRLV HLLPSPVVKK
     VNDKFIIEDQ NDTAIGQVTH FYGNMAVIVK AYTYLLTVGK ENLGNIGRYS VLNANYIKES
     LKDLYLLPVD EVCKHEFVFD GLIDKSNHVT TLDIAKRMLD YDVHPPTVYF PLVFKESLMI
     EPPETESKET LDSFIDVMRK IALEAKTNPE LVKGAPYNTV VKRLDEAKAA RNPLVKYTDL
     IE
//
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