GCSP_SHIFL
ID GCSP_SHIFL Reviewed; 957 AA.
AC Q83QA2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 120.
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=SF2889, S3088;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN44373.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18195.1; -; Genomic_DNA.
DR RefSeq; NP_708666.1; NC_004337.2.
DR RefSeq; WP_000195082.1; NZ_WPGW01000018.1.
DR AlphaFoldDB; Q83QA2; -.
DR SMR; Q83QA2; -.
DR STRING; 198214.SF2889; -.
DR EnsemblBacteria; AAN44373; AAN44373; SF2889.
DR EnsemblBacteria; AAP18195; AAP18195; S3088.
DR GeneID; 1025878; -.
DR KEGG; sfl:SF2889; -.
DR KEGG; sfx:S3088; -.
DR PATRIC; fig|198214.7.peg.3438; -.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000166937"
FT MOD_RES 708
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 957 AA; 104366 MW; A2C869BD5FD383D4 CRC64;
MTQTLSQLEN SGAFIERHIG PDAAQQQEML NAVGAQSLNA LTGQIVPKDI QLATPPQVGA
PATEYAALAE LKAIASRNKR FTSYIGMGYT AVQLPPVILR NMLENPGWYT AYTPYQPEVS
QGRLEALLNF QQVTLDLTGL DMASASLLDE ATAAAEAMAM AKRVSKLKNA NRFFVASNVH
PQTLDVVRTR AETFGFEVIV DDAQKVLDHQ DVFGVLLQQV GTTGEIHDYT ALISELKSRK
IVVSVAADIM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAK DEYKRSMPGR
IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPVGLKRI
ANRIHRLTDI LAAGLQQKGL KLRHAHYFDT LCVEVADKAG VLTRAEAAEI NLRSDILNAV
GITLDETTTR ENVMQLFSVL LGDNHGLEID TLDKDVAHDS RSIQPAMLRD DEILTHPVFN
RYHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWTEF 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
