ID A0A1H8IU07_9BACI Unreviewed; 448 AA.
AC A0A1H8IU07;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04488134_101730 {ECO:0000313|EMBL:SEN72113.1};
OS Amphibacillus marinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=872970 {ECO:0000313|EMBL:SEN72113.1, ECO:0000313|Proteomes:UP000199300};
RN [1] {ECO:0000313|EMBL:SEN72113.1, ECO:0000313|Proteomes:UP000199300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10434 {ECO:0000313|EMBL:SEN72113.1,
RC ECO:0000313|Proteomes:UP000199300};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FODJ01000001; SEN72113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8IU07; -.
DR STRING; 872970.SAMN04488134_101730; -.
DR OrthoDB; 9771867at2; -.
DR Proteomes; UP000199300; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199300}.
FT DOMAIN 6..444
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 448 AA; 48849 MW; 6097F9D527F0410A CRC64;
MTARFRYLPD TIEDQQAMLD FLKMDSLDDL YADLPKSIRL TEPLTIPAAL PESLLVKKMH
QLAGRNINAN QYSYFLGAGT YDHFIPSVVN HVISRSEFYT AYTPYQPEIS QGELQAIFEF
QTMVCELTGM DVANSSMYDG FTAVAEAAAL AVTSTKRPKV IVAETVHPET RAILATNAEG
LEYTVNTAER TGDITSLTCL AEQTDEQTAA IIVQYPNFLG SIEDLAEIKK IAQDNGALFI
VSANPLALAV LQAPGKLGAD IVVGDMQPLG IPMSFGGPHC GYFAATKKLM RKIPGRIVGQ
SNDADGKRGF TLALQAREQH IRRERASSNI CSNQALNALA SAVCMSALGK KGIQQMAKLN
IEKADYLANQ LREKGFPIHN QSAFFNEFVV ELPVSTKDAN QALFEAGFIG GFDLSGIYSL
DTHMLIAVTE QRTKEEIDQF VAVLGALS
//
