ID A8AMU9_CITK8 Unreviewed; 354 AA. AC A8AMU9; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 28-JAN-2026, entry version 98. DE RecName: Full=Mannonate dehydratase {ECO:0000256|ARBA:ARBA00016339, ECO:0000256|HAMAP-Rule:MF_00106}; DE EC=4.2.1.8 {ECO:0000256|ARBA:ARBA00012927, ECO:0000256|HAMAP-Rule:MF_00106}; DE AltName: Full=D-mannonate hydro-lyase {ECO:0000256|ARBA:ARBA00033474, ECO:0000256|HAMAP-Rule:MF_00106}; GN Name=uxuA {ECO:0000256|HAMAP-Rule:MF_00106}; GN OrderedLocusNames=CKO_03736 {ECO:0000313|EMBL:ABV14812.1}; OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Citrobacter. OX NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV14812.1, ECO:0000313|Proteomes:UP000008148}; RN [1] {ECO:0000313|EMBL:ABV14812.1, ECO:0000313|Proteomes:UP000008148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696 RC {ECO:0000313|Proteomes:UP000008148}; RG The Citrobacter koseri Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the dehydration of D-mannonate. CC {ECO:0000256|ARBA:ARBA00002713, ECO:0000256|HAMAP-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; CC Evidence={ECO:0000256|ARBA:ARBA00001794, ECO:0000256|HAMAP- CC Rule:MF_00106}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00106}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00106}; CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. {ECO:0000256|ARBA:ARBA00004892, ECO:0000256|HAMAP- CC Rule:MF_00106}. CC -!- SIMILARITY: Belongs to the mannonate dehydratase family. CC {ECO:0000256|ARBA:ARBA00007389, ECO:0000256|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; CP000822; ABV14812.1; -; Genomic_DNA. DR RefSeq; WP_012134508.1; NC_009792.1. DR AlphaFoldDB; A8AMU9; -. DR STRING; 290338.CKO_03736; -. DR GeneID; 45137432; -. DR KEGG; cko:CKO_03736; -. DR HOGENOM; CLU_058621_1_0_6; -. DR OrthoDB; 9780250at2; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000008148; Chromosome. 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 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; NF003027; PRK03906.1; 2. 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, ECO:0000256|HAMAP-Rule:MF_00106}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00106}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00106}; KW Reference proteome {ECO:0000313|Proteomes:UP000008148}. SQ SEQUENCE 354 AA; 40398 MW; 0A29AE8808202405 CRC64; MQMTMRWFGP QEDKIPLEYI RQVPGVEGVV GALYDVAPGE VWPVEKIKAL VEQAHAAGLK MEVIESVNIH DDIKIGTPER DRYIENYKQT IRNLAGFGIK VICYNFMPVF DWMKTDMNYV LPDGSLTMAF EKHGIDKTLE EVVKEVLDNS NGFALPGWEP ERLAKVQELF ARYSGVDDDK LRENLFYFLR EIIPVCEEVG VKMAIHPDDP PYSIFGLPRV VKNHADLAMI CDAVDSPANG ITLCTGSIAE DPENNVYEIL AEFTRRKRLH FAHVRNIKLI KDKDFYESAH PSQYGSLDMY RVMQALHDNG FDGYIRPDHG RFIWGETGRP GYGLYDRALG VTYLSGLWEA LEKK //