GCSPA_DESPS
ID GCSPA_DESPS Reviewed; 450 AA.
AC Q6ARJ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; OrderedLocusNames=DP0299;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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:0000255|HAMAP-Rule:MF_00712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(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; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00712}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR522870; CAG35028.1; -; Genomic_DNA.
DR RefSeq; WP_011187544.1; NC_006138.1.
DR AlphaFoldDB; Q6ARJ7; -.
DR SMR; Q6ARJ7; -.
DR STRING; 177439.DP0299; -.
DR EnsemblBacteria; CAG35028; CAG35028; DP0299.
DR KEGG; dps:DP0299; -.
DR eggNOG; COG0403; Bacteria.
DR HOGENOM; CLU_004620_0_2_7; -.
DR OMA; MYDGASA; -.
DR OrthoDB; 870147at2; -.
DR Proteomes; UP000000602; 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
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; PTHR42806; 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..450
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 1"
FT /id="PRO_1000045645"
SQ SEQUENCE 450 AA; 49373 MW; 7F0BCA16A29959B1 CRC64;
MRYLPHTEEE IQEMLEVVGK ESLDDLFSSV PAECRYQGDI PIPAALTEWQ LKDHFAALMS
KNRVNQEHKV LIGAGSYDHY VPEILPSLMS RSEFLTAYTP YQPEVAQGTL QGIFEYQTLT
ARLLGTDAVN ASMYDGASAL AESALMSFRI ARKKKTVALS AAIHPHYREV VATYLQATDF
TIIELPVDAE GRTDLSSLAG IEGLASVAIQ SPNFFGVVED LQGCGEKIHD VDALFISCFS
EALAYGLLKS PGECGADIIC GEGQSFGLGR SYGGPGVGMM GCRDKLVRNM PGRIVGQTLD
TKGKRGFVLT LATREQHIRR EKATSNICSN QGICAMTAGM YMATLGGTGI RQLARLNYDK
AAYLRSELIK LGAKPLFDAP VFNEFALRFP FDFERVREAL KEESVVAGLS LEAYYPDLQG
AYLFCATETL KKEDIDRIVS SIKKHALQEV