GCSP_PSESM
ID GCSP_PSESM Reviewed; 954 AA.
AC Q887L5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=PSPTO_1276;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54801.1; -; Genomic_DNA.
DR RefSeq; NP_791106.1; NC_004578.1.
DR RefSeq; WP_005764078.1; NC_004578.1.
DR AlphaFoldDB; Q887L5; -.
DR SMR; Q887L5; -.
DR STRING; 223283.PSPTO_1276; -.
DR EnsemblBacteria; AAO54801; AAO54801; PSPTO_1276.
DR GeneID; 1182912; -.
DR KEGG; pst:PSPTO_1276; -.
DR PATRIC; fig|223283.9.peg.1298; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 70707at2; -.
DR PhylomeDB; Q887L5; -.
DR Proteomes; UP000002515; 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 CDD; cd00613; GDC-P; 1.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
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..954
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166929"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 954 AA; 103604 MW; 503D639E9F6A16A0 CRC64;
MTDRIELTTA NEFIARHIGP RAADELAMLH TLGFDSIEAL SDSVIPESIK GTSVLNLPAG
QSEADALASI KAIASKNQLF KTYIGQGYYN THTPAPILRN LLENPAWYTA YTPYQPEISQ
GRLESLLNFQ TLISDLTGLP IANASLLDEA TAAAEAMTFC KRLSKNKGSQ QFFASSHCHP
QTLDVLRTRA EPLGITVVVA DETELGDVSD YFGALLQYPA SNGDVFDYRE LAERFHGANA
LVAVAADLLA LTLLTPPGEF GADVAIGSAQ RFGVPLGFGG PHAAYFSTRD AFKRDMPGRL
VGVSVDRHGK QALRLAMQTR EQHIRREKAT SNICTAQVLL ANIASMYAVY HGPRGLTQIA
NRVHHLTAIL AEGLSQLGLN AEQAYFFDSL TLHTGGRTAA LHAAARARHI NLREIDDQRL
GLSLDETTSQ SAVEVLWDIF ASTGQTLPDF TALAASVKSR LPAALLRQSA ILSHPVFNRY
HSETELMRYL RKLADKDLAL DRTMIPLGSC TMKLNAASEM IPVTWAEFGN LHPFAPAEQS
AGYQQLTDEL EAMLCAATGY DAISLQPNAG SQGEYAGLLA IRAYHQSRGD EHRDICLIPS
SAHGTNPATA NMAGMRVVVT ACDARGNVDI EDLRAKALQH REQLAAIMIT YPSTHGVFEE
GIREICGIVH DNGGQVYIDG ANMNAMVGLC APGKFGGDVS HLNLHKTFCI PHGGGGPGVG
PIGVKSHLAP FMPGHARMQR KEGAVCAAPF GSASILPITW MYIRMMGGEG LKRASQLAIL
NANYISRRLE EHYPVLYTGT NGLVAHECIL DLRPIKDSSG ISVDDVAKRL IDFGFHAPTM
SFPVAGTLMI EPTESESREE LDRFCDAMIK IREEIRAVED GTLDKDDNPL KNAPHTAAEI
VGQWSHPYSR EQAVYPVDSL IENKYWPPVG RVDNVFGDRN LVCACPSIES YQEA
