ID UXUA_HAEI8 Reviewed; 394 AA. AC Q4QPI9; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 10-JUN-2026, entry version 99. 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}; GN OrderedLocusNames=NTHI0065; OS Haemophilus influenzae (strain 86-028NP). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=281310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=86-028NP; RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005; RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., RA Munson R.S. Jr.; RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus RT influenzae: comparative study with H. influenzae serotype d, strain KW20."; RL J. Bacteriol. 187:4627-4636(2005). 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00106}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000057; AAX87058.1; -; Genomic_DNA. DR RefSeq; WP_011271799.1; NC_007146.2. DR AlphaFoldDB; Q4QPI9; -. DR SMR; Q4QPI9; -. DR GeneID; 93218931; -. DR KEGG; hit:NTHI0065; -. DR HOGENOM; CLU_058621_2_0_6; -. DR UniPathway; UPA00246; -. DR GO; GO:0008198; F:ferrous iron binding; IEA:TreeGrafter. DR GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter. DR GO; GO:0008927; F:mannonate dehydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042840; P:D-glucuronate catabolic process; IEA:TreeGrafter. DR FunFam; 3.20.20.150:FF:000004; Mannonate dehydratase; 1. DR FunFam; 3.20.20.150:FF:000005; Mannonate dehydratase; 1. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 2. DR HAMAP; MF_00106; UxuA; 1. DR InterPro; IPR004628; Man_deHydtase. DR InterPro; IPR036237; Xyl_isomerase-like_sf. DR NCBIfam; NF003027; PRK03906.1; 1. 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; Lyase; Manganese. FT CHAIN 1..394 FT /note="Mannonate dehydratase" FT /id="PRO_0000231053" SQ SEQUENCE 394 AA; 45307 MW; 944B1515B026BF41 CRC64; MEQAWRWYGP KDPVSLSDIR QAGATGIVTA LHHIPNGEVW SIEEIKKRKT EIENAGLSWS VVESVPVHEE IKTQTGNYQK WINNYKQTLR NLAQCGIDTV CYNFMPVLDW TRTDLAYELP DGSKALRFDH IAFAAFELHI LKRPDAEKAY NQEEQVAART YYDKMSEQDI TQLTRNIIAG LPGAEEGYTL DEFQTQLDRY KDISPEKFRT HLAYFLNEIV PVAQEVGIKM AIHPDDPPRP ILGLPRIVST IEDMQWFVET QPLPANGFTM CTGSYGVRSD NDLVKMTEQF ADRIYFAHLR STQREDNPLT FHEAAHLEGD VDMFNVVKAL LNEEYRRLNQ GETRLIPMRP DHGHQMLDDL RKKTNPGYSA IGRLKGLAEF RGLEMALKKV YFNK //