ID W0B5C8_9GAMM Unreviewed; 456 AA.
AC W0B5C8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=gcsA {ECO:0000313|EMBL:AHE65728.1};
GN Synonyms=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN ORFNames=Loa_00137 {ECO:0000313|EMBL:AHE65728.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE65728.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE65728.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
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; CP004006; AHE65728.1; -; Genomic_DNA.
DR RefSeq; WP_025384710.1; NZ_CP004006.1.
DR AlphaFoldDB; W0B5C8; -.
DR STRING; 1268635.Loa_00137; -.
DR KEGG; lok:Loa_00137; -.
DR PATRIC; fig|1268635.3.peg.142; -.
DR eggNOG; COG0403; Bacteria.
DR HOGENOM; CLU_004620_0_2_6; -.
DR Proteomes; UP000018838; 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:UP000018838}.
FT DOMAIN 3..445
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 456 AA; 50076 MW; 06E66F14E980351E CRC64;
MPYIPHTAED VAAMLASINV ADVQALFDEI PHSMLHDELK NIPSGISEMA MLREAQQLAA
KNHNAICFIG AGCYDHHIPA AVWDIASRGE FLTAYTPYQA EASQGTLQLL YEYQTMIAEL
TGMDVANASL YDGATALAEA MLMAIRINRH SKSNRILVAG TVHPFYRETI ETIARNQHIE
LITLPFDKEL GITSLATLEK YRGEDVAALV IAQPNFFGCL EEVDDLCNWA QANNTISIAC
VNPISLGLLK PPGLWGEQGA DIVCGEGQPL GAPMASGGPY FGFFSTRHQY VRQMPGRLIG
RTLDKDGKTG YTLTLQAREQ HIRRGKATSN ICTNQGLLVT AATLHMSLLG AQGLMQTARL
CHHNTQMLVN ALTQIEGVKT VFKTPYFHEA LLKLNRPVNK ILHLLREKGI AGGYPVESHY
PQQANTLLVC ATETRTEENI AHYAQTLKTI LAEINE
//