SGBH_ECOLI
ID SGBH_ECOLI Reviewed; 220 AA.
AC P37678; Q2M7P4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=3-keto-L-gulonate-6-phosphate decarboxylase SgbH;
DE Short=KGPDC;
DE EC=4.1.1.85 {ECO:0000269|PubMed:11741871};
DE AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase;
GN Name=sgbH; Synonyms=yiaQ; OrderedLocusNames=b3581, JW3553;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP DISCUSSION OF SEQUENCE.
RA Reizer J., Charbit A., Reizer A., Saier M.H. Jr.;
RT "Novel phosphotransferases system genes revealed by bacterial genome
RT analysis: operons encoding homologues of sugar-specific permease domains of
RT the phosphotransferase system and pentose catabolic enzymes.";
RL Genome Sci. Technol. 1:53-75(1996).
RN [5]
RP DISCUSSION OF SEQUENCE.
RX PubMed=9274005; DOI=10.1099/00221287-143-8-2519;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "Is the ribulose monophosphate pathway widely distributed in bacteria?";
RL Microbiology 143:2519-2520(1997).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002;
RA Yew W.S., Gerlt J.A.;
RT "Utilization of L-ascorbate by Escherichia coli K-12: assignments of
RT functions to products of the yjf-sga and yia-sgb operons.";
RL J. Bacteriol. 184:302-306(2002).
CC -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into
CC L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L-
CC gulonate. {ECO:0000269|PubMed:11741871}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-
CC phosphate; Xref=Rhea:RHEA:14353, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57829, ChEBI:CHEBI:58774; EC=4.1.1.85;
CC Evidence={ECO:0000269|PubMed:11741871};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14354;
CC Evidence={ECO:0000269|PubMed:11741871};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P37678; Q93K97: nudF; NbExp=2; IntAct=EBI-555448, EBI-562814;
CC -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
CC {ECO:0000305}.
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DR EMBL; U00039; AAB18558.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76605.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77712.1; -; Genomic_DNA.
DR PIR; S47802; S47802.
DR RefSeq; NP_418038.1; NC_000913.3.
DR RefSeq; WP_000089481.1; NZ_SSZK01000041.1.
DR AlphaFoldDB; P37678; -.
DR SMR; P37678; -.
DR BioGRID; 4259346; 191.
DR DIP; DIP-10873N; -.
DR IntAct; P37678; 3.
DR STRING; 511145.b3581; -.
DR jPOST; P37678; -.
DR PaxDb; P37678; -.
DR PRIDE; P37678; -.
DR EnsemblBacteria; AAC76605; AAC76605; b3581.
DR EnsemblBacteria; BAE77712; BAE77712; BAE77712.
DR GeneID; 948098; -.
DR KEGG; ecj:JW3553; -.
DR KEGG; eco:b3581; -.
DR PATRIC; fig|511145.12.peg.3696; -.
DR EchoBASE; EB2193; -.
DR eggNOG; COG0269; Bacteria.
DR HOGENOM; CLU_081825_0_0_6; -.
DR InParanoid; P37678; -.
DR OMA; WMTVICA; -.
DR PhylomeDB; P37678; -.
DR BioCyc; EcoCyc:EG12285-MON; -.
DR BioCyc; MetaCyc:EG12285-MON; -.
DR PRO; PR:P37678; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEP:EcoCyc.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IBA:GO_Central.
DR CDD; cd04726; KGPDC_HPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041710; HPS/KGPDC.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..220
FT /note="3-keto-L-gulonate-6-phosphate decarboxylase SgbH"
FT /id="PRO_0000212105"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 64
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 67
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 220 AA; 23445 MW; 89465A10F6AECD87 CRC64;
MSRPLLQLAL DHSSLEAAQR DVTLLKDSVD IVEAGTILCL NEGLGAVKAL REQCPDKIIV
ADWKVADAGE TLAQQAFGAG ANWMTIICAA PLATVEKGHA MAQRCGGEIQ IELFGNWTLD
DARDWHRIGV RQAIYHRGRD AQASGQQWGE ADLARMKALS DIGLELSITG GITPADLPLF
KDIRVKAFIA GRALAGAANP AQVAGDFHAQ IDAIWGGARA
