ID SGBH_HAEIN Reviewed; 225 AA.
AC P44988;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Probable 3-keto-L-gulonate-6-phosphate decarboxylase;
DE Short=KGPDC;
DE EC=4.1.1.85;
DE AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase;
GN Name=sgbH; OrderedLocusNames=HI_1024;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
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).
CC -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into
CC L-xylulose-5-P. {ECO:0000250}.
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 -!- 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 -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22684.1; -; Genomic_DNA.
DR PIR; F64164; F64164.
DR RefSeq; NP_439184.1; NC_000907.1.
DR AlphaFoldDB; P44988; -.
DR SMR; P44988; -.
DR STRING; 71421.HI_1024; -.
DR EnsemblBacteria; AAC22684; AAC22684; HI_1024.
DR KEGG; hin:HI_1024; -.
DR PATRIC; fig|71421.8.peg.1068; -.
DR eggNOG; COG0269; Bacteria.
DR HOGENOM; CLU_081825_0_0_6; -.
DR OrthoDB; 43475at2; -.
DR PhylomeDB; P44988; -.
DR BioCyc; HINF71421:G1GJ1-1064-MONOMER; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IBA:GO_Central.
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:0019854; P:L-ascorbic acid catabolic process; IBA:GO_Central.
DR CDD; cd04726; KGPDC_HPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041710; HPS/KGPDC.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR35039; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR PANTHER; PTHR35039:SF3; 3-KETO-L-GULONATE-6-PHOSPHATE DECARBOXYLASE SGBH-RELATED; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..225
FT /note="Probable 3-keto-L-gulonate-6-phosphate
FT decarboxylase"
FT /id="PRO_0000212106"
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 202
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 225 AA; 24867 MW; 3829D48797FA710C CRC64;
MGKPLLQIAL DAQYLETALV DVKQIEHNID IIEVGTILAC SEGMRAVRIL RALYPNQILV
CDLKTTDAGA TLAKMAFEAG ADWLTVSAAA HPATKAACQK VAEEFNKIQP NLGVPKEIQI
ELYGNWNFDE VKNWLQLGIK QAIYHRSRDA ELSGLSWSNQ DIENIEKLDS LGIELSITGG
ITPDDLHLFK NTKNLKAFIA GRALVGKSGR EIAEQLKQKI GQFWI
//
