ID A1APD7_PELPD Unreviewed; 448 AA.
AC A1APD7;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 18-JUN-2025, entry version 110.
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 OrderedLocusNames=Ppro_1592 {ECO:0000313|EMBL:ABK99207.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia;
OC Desulfuromonadales; Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99207.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK99207.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026, 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; CP000482; ABK99207.1; -; Genomic_DNA.
DR RefSeq; WP_011735497.1; NC_008609.1.
DR AlphaFoldDB; A1APD7; -.
DR STRING; 338966.Ppro_1592; -.
DR KEGG; ppd:Ppro_1592; -.
DR eggNOG; COG0403; Bacteria.
DR HOGENOM; CLU_004620_0_2_7; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000006732; 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 NCBIfam; NF001696; PRK00451.1; 1.
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:UP000006732}.
FT DOMAIN 5..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 448 AA; 48459 MW; F4C25E45B9498703 CRC64;
MDDSHYCPHT PEERGEMLDL IGVASVDDLF ASIPEELRAR TFNIPPGMSE FEALARMREL
AAENGQGIVP FIGGGYFDHL VPSVVSHLAG RSEFYTAYTP YQPECSQGTL QALFEYQTAI
CRLTDLDVSN ASLYDGATAC AEAAMMALRV TGRRRIVVDG CVNPFSRQVL KTYLGNLDVE
VLEIEPLDGL LNRGELETVL DDGVAGLLVQ NPTFFGTVDD YSSLADLLHA RGALLISSVY
PVSLGLLKTP GEMGVDIAVG DGQSLGNPLS FGGPSFGFMA ARKALVRNMP GRMVGETVDG
QGRRGYVLTL QAREQHIKRH RATSNICSNQ SLCALRGLIF LSSLGRDGLT ELARLNRDKS
EYAKARLEEI PGVSVLRSAP TFNEFTVSLP APAGIAVAAL LGQGVAAGVP LSTYYRDSER
LMVVTVTEKR SRREIDHLAR QLEVALCG
//
