GCSP_ECO57
ID GCSP_ECO57 Reviewed; 957 AA.
AC Q8XD33;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
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=Z4240, ECs3774;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG58030.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37197.1; -; Genomic_DNA.
DR PIR; B85946; B85946.
DR PIR; F91100; F91100.
DR RefSeq; NP_311801.1; NC_002695.1.
DR RefSeq; WP_000195009.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XD33; -.
DR SMR; Q8XD33; -.
DR STRING; 155864.EDL933_4105; -.
DR EnsemblBacteria; AAG58030; AAG58030; Z4240.
DR EnsemblBacteria; BAB37197; BAB37197; ECs_3774.
DR GeneID; 916407; -.
DR KEGG; ece:Z4240; -.
DR KEGG; ecs:ECs_3774; -.
DR PATRIC; fig|386585.9.peg.3939; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 1.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..957
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166915"
FT MOD_RES 708
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 957 AA; 104347 MW; 026A17DFFA1C150D CRC64;
MTQTLSQLEN SGAFIERHIG PDAAQQQEML NAVGAQSLNA LTGQIVPKDI QLATPPQVGA
PATEYAALAE LKAIASRNKR FTSYIGMGYT AVQLPPVILR NMLENPGWYT AYTPYQPEVS
QGRLEALLNF QQVTLDLTGL DMASASLLDE ATAAAEAMAM AKRVSKLKNA NRFFVASDVH
PQTLDVVRTR AETFGFEVIV DDAQKVLDHQ DIFGVLLQQV GTTGEIHDYT ALISELKSRK
IVVSVAADIM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAK DEYKRSMPGR
IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPIGLKRI
ANRIHRLTDI LAAGLQQKGL KLRHAHYFDT LCVEVADKAG VLARAEAAEI NLRSDILNAV
GITLDETTTR ENVMQLFSVL LGDNHGLDID TLDKDVAHDS RSIQPAMLRD DEILTHPVFN
RYHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPPE
QAEGYQQMIA QLADWLVKLT GYDAVCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI
PASAHGTNPA SAHMAGMQVV VVACDKNGNI DLTDLRAKAE QAGDNLSCIM VTYPSTHGVY
EETIREVCEV VHQFGGQVYL DGANMNAQVG ITSPGFIGAD VSHLNLHKTF CIPHGGGGPG
MGPIGVKAHL APFVPGHSVV QIEGMLTRQG AVSAAPFGSA SILPISWMYI RMMGAEGLKK
ASQVAILNAN YIASRLQDAF PVLYTGRDGR VAHECILDIR PLKEETGISE LDIAKRLIDY
GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRA EIDQVKAGVW PLEDNPLVNA
PHIQSELVAE WAHPYSREVA VFPAGVADKY WPTVKRLDDV YGDRNLFCSC VPISEYQ
