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IOLE_BACAH
ID   IOLE_BACAH              Reviewed;         298 AA.
AC   A0REB7;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Inosose dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
DE            EC=4.2.1.44 {ECO:0000255|HAMAP-Rule:MF_01672};
DE   AltName: Full=2-keto-myo-inositol dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
DE            Short=2KMI dehydratase {ECO:0000255|HAMAP-Rule:MF_01672};
GN   Name=iolE {ECO:0000255|HAMAP-Rule:MF_01672}; OrderedLocusNames=BALH_2261;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Al Hakam;
RX   PubMed=17337577; DOI=10.1128/jb.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA   McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
CC   -!- FUNCTION: Catalyzes the dehydration of inosose (2-keto-myo-inositol,
CC       2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)-
CC       trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol).
CC       {ECO:0000255|HAMAP-Rule:MF_01672}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=scyllo-inosose = 3D-3,5/4-trihydroxycyclohexane-1,2-dione +
CC         H2O; Xref=Rhea:RHEA:14065, ChEBI:CHEBI:15377, ChEBI:CHEBI:17811,
CC         ChEBI:CHEBI:28446; EC=4.2.1.44; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01672};
CC   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01672};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol degradation into acetyl-CoA;
CC       acetyl-CoA from myo-inositol: step 2/7. {ECO:0000255|HAMAP-
CC       Rule:MF_01672}.
CC   -!- SIMILARITY: Belongs to the IolE/MocC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01672}.
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DR   EMBL; CP000485; ABK85560.1; -; Genomic_DNA.
DR   RefSeq; WP_000471988.1; NC_008600.1.
DR   AlphaFoldDB; A0REB7; -.
DR   SMR; A0REB7; -.
DR   EnsemblBacteria; ABK85560; ABK85560; BALH_2261.
DR   KEGG; btl:BALH_2261; -.
DR   HOGENOM; CLU_059523_0_0_9; -.
DR   OMA; VHCKDIR; -.
DR   UniPathway; UPA00076; UER00144.
DR   Proteomes; UP000000761; Chromosome.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050114; F:myo-inosose-2 dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01672; IolE; 1.
DR   InterPro; IPR023952; IolE.
DR   InterPro; IPR030823; IolE/MocC.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR04379; myo_inos_iolE; 1.
PE   3: Inferred from homology;
KW   Cobalt; Lyase; Manganese.
FT   CHAIN           1..298
FT                   /note="Inosose dehydratase"
FT                   /id="PRO_0000352359"
SQ   SEQUENCE   298 AA;  33639 MW;  0236087B12403135 CRC64;
     MFKENTIKLG IAPIAWTNDD MPELGAENTF EQCISEMALA GFNGSEVGNK YPRNTVVLKK
     SLELRNLEIA SAWFSTFLTT KPLEETVEEF IKHRDFLHDM GAKVIVVSEQ GHSIQGLMDV
     PLFKNKPVFT EEEWNKLADG LHHLGKLAQE KGLHIVYHHH MGTGVQTTAE IEKLMDITDS
     ALVSLLFDTG HLVFSGEEPL YILKKYLPRI KHVHLKDIRQ EVVDIVKENE LSFLQAVKNG
     AFTVPGDGVI EFDEVFTILA NSDYQGWFVV EAEQDPALAN PFEYALKARE FIREKAGL
 
 
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