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SGBH_HAEIN
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   03-AUG-2022, entry version 108.
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; Proteobacteria; 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   RefSeq; WP_005693359.1; 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   OMA; WMTVICA; -.
DR   PhylomeDB; P44988; -.
DR   BioCyc; HINF71421:G1GJ1-1064-MON; -.
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; -; 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   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
 
 
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