GCSP_PSET1
ID GCSP_PSET1 Reviewed; 963 AA.
AC Q3IFW1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=PSHAa2473;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
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_00711}.
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_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC Rule:MF_00711}.
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DR EMBL; CR954246; CAI87521.1; -; Genomic_DNA.
DR RefSeq; WP_011329121.1; NC_007481.1.
DR AlphaFoldDB; Q3IFW1; -.
DR SMR; Q3IFW1; -.
DR STRING; 326442.PSHAa2473; -.
DR PRIDE; Q3IFW1; -.
DR EnsemblBacteria; CAI87521; CAI87521; PSHAa2473.
DR KEGG; pha:PSHAa2473; -.
DR PATRIC; fig|326442.8.peg.2383; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_6; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 70707at2; -.
DR BioCyc; PHAL326442:PSHA_RS12175-MON; -.
DR Proteomes; UP000006843; Chromosome I.
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 CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR003437; GcvP.
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; PTHR11773; PTHR11773; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..963
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000227115"
FT MOD_RES 710
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 963 AA; 104691 MW; C732B6F522FF4035 CRC64;
MSNAKSLEQL EQTQDFIRRH IGPSPAQVSD MLSALEVSSV EELIGQTVPA GIRLEQPLTV
GESRTEVETL SYLKSVASKN KVFKSYIGQG YHPTHVPHVI LRNVLENPGW YTAYTPYQPE
IAQGRLESLL NFQTMTLDLT GLDLASASLL DESTAAAEAM GLAKRVSKAK KANAFFIADD
VHTQTIDVVS TRAEQFGFEI IVGKAADAVN HEIFGALFQY PSTTGEVVDI TDLIAGVQSK
KAIACVAADI MSLLLLKAPG KLGADVVLGS AQRFGVPMGY GGPHAAFFAT RDAYKRSLPG
RIIGVSKDRL GNDALRMAMQ TREQHIRRDK ANSNICTAQV LLANMAAFYA VYHGPQGLKT
IAQRIHRFAD ILAAGLQAKG VSLKHNTWFD TLTVVSDSKA DVIARALASG VNFATNRDGE
YSIALSETTT RADVAQLFDI VLGEGHGLSV DAIAADIENN GSTSIPASLE RDDEVLTHPN
FNSYHSETEM LRYIKRLENK DLALNHSMIS LGSCTMKLNA TAEMIPITWP EFSNLHPFCP
LDQAQGYQIM MGELHDWLVN ITGYDAVSLQ PNSGAQGEYA GLIAIRKYHE SRGDAHRNVC
LIPSSAHGTN PASAQMASMK IVVVDCDKNG NVDMADLKAK AEAVAENLSC IMITYPSTHG
VYEETIREIC DVIHQHGGQV YMDGANMNAQ VGVTSPGFIG SDVSHLNLHK TFCIPHGGGG
PGVGPIGVKS HLAPFMPNHS IINVPGTNEG NGAVSAAPYG SASILPISWA YITMMGSEGL
KQATEMAIVN ANYLTHELSK HFPILYRGRN NRVAHECIVD LRPLKELSGI TEMDVAKRLQ
DYGFHSPTMS FPVAGTLMIE PTESESKVEI DRFIEAMVSI KSEIDKVISG EWSIENNPLV
FAPHTQGDVL GNEWDRAYDR FYAAFPVPSV AKNKFWPTVT RIDDVYGDRN LVCACPPVET
YRD