UXUA_ENTFA
ID UXUA_ENTFA Reviewed; 357 AA.
AC Q82ZC9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Mannonate dehydratase {ECO:0000255|HAMAP-Rule:MF_00106};
DE EC=4.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00106};
DE AltName: Full=D-mannonate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00106};
GN Name=uxuA {ECO:0000255|HAMAP-Rule:MF_00106}; OrderedLocusNames=EF_3135;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000255|HAMAP-
CC Rule:MF_00106}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00106};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00106};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00106}.
CC -!- SIMILARITY: Belongs to the mannonate dehydratase family.
CC {ECO:0000255|HAMAP-Rule:MF_00106}.
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DR EMBL; AE016830; AAO82813.1; -; Genomic_DNA.
DR RefSeq; NP_816743.1; NC_004668.1.
DR RefSeq; WP_002388613.1; NZ_KE136524.1.
DR PDB; 1TZ9; X-ray; 2.90 A; A/B=1-357.
DR PDBsum; 1TZ9; -.
DR AlphaFoldDB; Q82ZC9; -.
DR SMR; Q82ZC9; -.
DR STRING; 226185.EF_3135; -.
DR EnsemblBacteria; AAO82813; AAO82813; EF_3135.
DR GeneID; 60892381; -.
DR KEGG; efa:EF3135; -.
DR PATRIC; fig|226185.45.peg.439; -.
DR eggNOG; COG1312; Bacteria.
DR HOGENOM; CLU_058621_1_0_9; -.
DR OMA; RFVWEDF; -.
DR UniPathway; UPA00246; -.
DR EvolutionaryTrace; Q82ZC9; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR HAMAP; MF_00106; UxuA; 1.
DR InterPro; IPR004628; Man_deHydtase.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR PANTHER; PTHR30387; PTHR30387; 1.
DR Pfam; PF03786; UxuA; 1.
DR PIRSF; PIRSF016049; Man_dehyd; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00695; uxuA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Lyase; Manganese; Reference proteome.
FT CHAIN 1..357
FT /note="Mannonate dehydratase"
FT /id="PRO_0000170673"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 44..56
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 80..96
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 179..200
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1TZ9"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:1TZ9"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:1TZ9"
SQ SEQUENCE 357 AA; 40282 MW; 4CA7E9E55D33A061 CRC64;
MKWGFRWYGA AGDAIPLKHI RQIPGITGVV GTLLNKLPGD VWTVAEIQAL KQSVEQEGLA
LLGIESVAIH DAIKAGTDQR DHYIDNYRQT LRNLGKCGIS LVCYSFKPIF GWAKTDLAYE
NEDGSLSLLF DQAVVENMQP EDMYQLIHSQ SKGFRLPGWE EERLQQFQEL KAMYAGVTEE
DLVENLRYFL ERVIPVCEEE NIKMGIHPDD PPWEIFGLPR ITKNLADLKR ILSLVDSPAN
GITFCTGSLG ADPTNDLPTM IREIGHRINF VHFRNVKYLG EHRFEETAHP SVAGSLDMAE
LMQALVDVGY EGVIRPDHGR AIWDEKAMPG YGLYDRAMGL TYIQGLYEAT KAKQNRK
