ID A0A2L0A9A2_9SPHN Unreviewed; 457 AA.
AC A0A2L0A9A2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C1T17_09895 {ECO:0000313|EMBL:AUW58369.1};
OS Sphingobium sp. SCG-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=2072936 {ECO:0000313|EMBL:AUW58369.1, ECO:0000313|Proteomes:UP000239825};
RN [1] {ECO:0000313|EMBL:AUW58369.1, ECO:0000313|Proteomes:UP000239825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCG-1 {ECO:0000313|EMBL:AUW58369.1,
RC ECO:0000313|Proteomes:UP000239825};
RA Tavormina P.L.;
RT "Members of Methylobacter and Sphingobium form part of a microbial response
RT to natural gas loading in southern Californian soils.";
RL Submitted (JAN-2018) 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; CP026372; AUW58369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0A9A2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000239825; 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:UP000239825}.
FT DOMAIN 1..446
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 457 AA; 48832 MW; 1B361DEA7950197C CRC64;
MRYLPLTDAD RSEMLSVIGA PSIDALFVDV PAEARLSAKI EGLPDHSSEM AVERHMGRLA
RQNVAAGDVP FFLGAGAYRH HVPASVDHLI QRGEFLTAYT PYQPEIAQGT LQVLFEFQTQ
VARLFGCDVA NASMYDGSTA CWEAIGMARR ITKRGKAILS SGLHPHYVSV AKTMAKFTGD
QLVYETPELD AETDALNLCS AIDEDTSCVV VQYPDILGRI SDLSALAAKA HEVGALLVAV
VTEPVALGAI TPPGDMGADI VVGEGQSIGV GLQFGGPYLG LFACKQKYLR QMPGRLCGET
VDAEGKRGFV LTLSTREQHI RREKATSNIC TNSGLCALAF SIHMTLLGER GLTELAALNH
ARAVQAAEAL EQVPGVRLMN NSFFNEFTIV LEKDAREVAR TLADRGILGG VSLGRLFPQA
EALSGGLVVA VTETTTEDDI EALCAALKDV LAMEVSA
//
