ID W9C0H3_9SPHN Unreviewed; 452 AA.
AC W9C0H3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=Q27BB25_02025 {ECO:0000313|EMBL:ESZ88909.1};
OS Blastomonas sp. CACIA14H2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Blastomonas.
OX NCBI_TaxID=1419876 {ECO:0000313|EMBL:ESZ88909.1, ECO:0000313|Proteomes:UP000019523};
RN [1] {ECO:0000313|EMBL:ESZ88909.1, ECO:0000313|Proteomes:UP000019523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIA14H2 {ECO:0000313|Proteomes:UP000019523};
RX PubMed=24435876;
RA Lima A.R., Siqueira A.S., Dos Santos B.G., da Silva F.D., Lima C.P.,
RA Cardoso J.F., Vianez-Junior J.L., Nunes M.R., Goncalves E.C.;
RT "Draft Genome Sequence of Blastomonas sp. Strain CACIA 14H2, a
RT Heterotrophic Bacterium Associated with Cyanobacteria.";
RL Genome Announc. 2:e01200-13(2014).
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}.
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:ESZ88909.1}.
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DR EMBL; AYSC01000002; ESZ88909.1; -; Genomic_DNA.
DR AlphaFoldDB; W9C0H3; -.
DR STRING; 1419876.Q27BB25_02025; -.
DR PATRIC; fig|1419876.3.peg.402; -.
DR Proteomes; UP000019523; 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 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}.
FT DOMAIN 1..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 452 AA; 48223 MW; 1989F3786E1DF79A CRC64;
MRYLPLTTQD RSSMLATIGA AAIDDLFVDI PEEARLTGPI HGLPMHAPEM AVERHMKALA
SQNLVAGDVP FFMGAGAYRH HVPASVDHLI QRGEFLTAYT PYQPEIAQGT LQMLFEFQTQ
VARLLGCDVA NASMYDGSTA CWEAIGMARR ITKRATALLS SGLHPHYVGV AKTMARFTGD
ALVHQAPSLT PETDIAGLIG QIDKNTSCVV VQYPDILGRV DDLSALAQAA QAAGALLIAV
VTEPVALGAL RSPGEMGADI VVGEGQSLGV GLQFGGPYVG LFGCKQKYVR QMPGRLCGET
VDAEGKRGFV LTLSTREQHI RREKATSNIC TNSGLCALAF SIHMTLLGEK GLRGLAEVNH
AMAVTAAERL EKIAGVKLLN SSFFNEFTLV LPKDARSIVR ALADRKILGG VSLGRLYPEE
ADLANGLVVA VTETATLDDI EAFATNLEEL LA
//
