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   27-MAR-2024, entry version 101.
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};
GN   OrderedLocusNames=PSHAa2473;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Pseudomonadota; 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=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; 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   AlphaFoldDB; Q3IFW1; -.
DR   SMR; Q3IFW1; -.
DR   STRING; 326442.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   BioCyc; PHAL326442:PSHA_RS12175-MONOMER; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
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; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
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
//