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IOLE_ALKHC
ID   IOLE_ALKHC              Reviewed;         303 AA.
AC   Q9KAH0;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=BH2317;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06036.1; -; Genomic_DNA.
DR   PIR; E83939; E83939.
DR   RefSeq; WP_010898473.1; NC_002570.2.
DR   AlphaFoldDB; Q9KAH0; -.
DR   SMR; Q9KAH0; -.
DR   STRING; 272558.10174937; -.
DR   EnsemblBacteria; BAB06036; BAB06036; BAB06036.
DR   KEGG; bha:BH2317; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_059523_0_0_9; -.
DR   OMA; YDSRPEL; -.
DR   OrthoDB; 1194699at2; -.
DR   UniPathway; UPA00076; UER00144.
DR   Proteomes; UP000001258; 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; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Inosose dehydratase"
FT                   /id="PRO_0000352357"
SQ   SEQUENCE   303 AA;  34421 MW;  2A1DBE7AB9B8BE9F CRC64;
     MADQKILWGI APIGWRNDDI PEIGAGNTLS HLLSDIVVAR FQGTEVGGFF PDAKTLNKEL
     ELRNLKIAGQ WFSSYLIRDP FESVSKEFHA HCAYLEEVGA SVAVVSEQTY SIQQSEQNIF
     TEKPMFTDSE WLTLCEGLNE LGKIAQQYGL TLVYHHHMGT GVQTLAEVDR LMENTDPTLV
     SLLYDTGHIY VSDNDYMLLL TKHLDRIKHV HFKDVRSDIL AKCQEQGQSF LQSFLAGMFT
     VPGDGCIDFT KVYDVLLTHD YRGWIVVEAE QDPAKAHPLE YALKARQYID EKLLTTDEMK
     ERI
 
 
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