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Database: UniProt
Entry: A0A0S8EPQ3_9GAMM
LinkDB: A0A0S8EPQ3_9GAMM
Original site: A0A0S8EPQ3_9GAMM 
ID   A0A0S8EPQ3_9GAMM        Unreviewed;       465 AA.
AC   A0A0S8EPQ3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AMS22_12445 {ECO:0000313|EMBL:KPK50222.1};
OS   Thiotrichales bacterium SG8_50.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales.
OX   NCBI_TaxID=1703416 {ECO:0000313|EMBL:KPK50222.1, ECO:0000313|Proteomes:UP000051903};
RN   [1] {ECO:0000313|EMBL:KPK50222.1, ECO:0000313|Proteomes:UP000051903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_50 {ECO:0000313|EMBL:KPK50222.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:ARBA00033655, 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:KPK50222.1}.
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DR   EMBL; LJTW01000188; KPK50222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8EPQ3; -.
DR   PATRIC; fig|1703416.3.peg.1129; -.
DR   Proteomes; UP000051903; 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          3..440
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   465 AA;  50296 MW;  3477781C7F9EEA72 CRC64;
     MPFIPHTESD IRAMLKSIGA KSIDDLFDEI PKELRAGKLT QVPEGLSEMQ VTRLMQERAQ
     QDGHYLNFIG AGAYEHHIPA AVWEIVTRGE FYSAYTPYQA EASQGTLQLL YEYQTMMASL
     TGMDISNASL YDGASGLAEA VLMAVRAHKK ARKILMPRTV HPIYRSVVGA IVANQNIEIV
     EVPFDTVGGY VAPDSLSAFA GGEYAALVIP QPNFFGVLEE VDALTDWAHA NNMLAIALVN
     PTSLAILKAP GEWGSKGADI AVGEGQPLGA PLSSGGPYFG FMACKEPLVR QMPGRIIGRT
     VDKDGKSGFT LTLQAREQHI RRSKATSNIC TNQGLIVTAA TIYMSLLGPE GLERVAAACH
     ANTLATIEKL TAIKGVTRVF SRPVFHEAVL RLDMPVADAL RALEPQGILG GFDLADHYPE
     LGQALLICAT ETRSPADIDQ YAFHLERVVS KRRLDPPCAV KANPV
//
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