ID K2AEF6_9BACT Unreviewed; 338 AA.
AC K2AEF6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=mannonate dehydratase {ECO:0000256|ARBA:ARBA00012927};
DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927};
DE Flags: Fragment;
GN ORFNames=ACD_54C01000G0001 {ECO:0000313|EMBL:EKD60006.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD60006.1};
RN [1] {ECO:0000313|EMBL:EKD60006.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate.
CC {ECO:0000256|ARBA:ARBA00002713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O;
CC Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767,
CC ChEBI:CHEBI:57990; EC=4.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001794};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|ARBA:ARBA00004892}.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC {ECO:0000256|ARBA:ARBA00007389}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD60006.1}.
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DR EMBL; AMFJ01023769; EKD60006.1; -; Genomic_DNA.
DR AlphaFoldDB; K2AEF6; -.
DR UniPathway; UPA00246; -.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR HAMAP; MF_00106; UxuA; 1.
DR InterPro; IPR004628; Man_deHydtase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR NCBIfam; TIGR00695; uxuA; 1.
DR PANTHER; PTHR30387; MANNONATE DEHYDRATASE; 1.
DR PANTHER; PTHR30387:SF2; MANNONATE DEHYDRATASE; 1.
DR Pfam; PF03786; UxuA; 1.
DR PIRSF; PIRSF016049; Man_dehyd; 1.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211}.
FT NON_TER 338
FT /evidence="ECO:0000313|EMBL:EKD60006.1"
SQ SEQUENCE 338 AA; 37325 MW; 850E9A8B2FE99BF2 CRC64;
MEFMEECFRW YGPDDPVPLA HIRQAGATGI VSALHRIYDG SAWPDAAIAD HKAGIEAAGL
SWSVVESIPV HASIKIGTPL RDRYIGWYKD TLRALARQGI ATICYNFMPV VDWTRTELKH
PMPNGALALR FDAVDFAAYD LCVLRRPGAE ADYTPDRLAE AEARFASLTP EAMERIERNL
IAGLPATEVR YDRAGFQRAL SEYDGISADD LHENLAYFLR QIVPVADELG LRLCIHPDDP
AFSLFGLPRI VSTAADVRRI LAAQDVQANG LTFCTGSYGT RADNDLVAMI HEFGPRIHFA
HLRNVTREPD GSFHEADHLG GSSDMPAVIL ALLAEQAR
//
