ID UXAC_PECCP Reviewed; 469 AA. AC C6DKE7; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=Uronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675}; DE EC=5.3.1.12 {ECO:0000255|HAMAP-Rule:MF_00675}; DE AltName: Full=Glucuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675}; DE AltName: Full=Uronic isomerase {ECO:0000255|HAMAP-Rule:MF_00675}; GN Name=uxaC {ECO:0000255|HAMAP-Rule:MF_00675}; GN OrderedLocusNames=PC1_0529; OS Pectobacterium carotovorum subsp. carotovorum (strain PC1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=561230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucuronate = D-fructuronate; Xref=Rhea:RHEA:13049, CC ChEBI:CHEBI:58720, ChEBI:CHEBI:59863; EC=5.3.1.12; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00675}; CC -!- CATALYTIC ACTIVITY: CC Reaction=aldehydo-D-galacturonate = keto-D-tagaturonate; CC Xref=Rhea:RHEA:27702, ChEBI:CHEBI:12952, ChEBI:CHEBI:17886; CC EC=5.3.1.12; Evidence={ECO:0000255|HAMAP-Rule:MF_00675}; CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00675}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Uronate isomerase family. {ECO:0000255|HAMAP-Rule:MF_00675}. 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; CP001657; ACT11584.1; -; Genomic_DNA. DR RefSeq; WP_012773236.1; NC_012917.1. DR AlphaFoldDB; C6DKE7; -. DR SMR; C6DKE7; -. DR STRING; 561230.PC1_0529; -. DR GeneID; 67795636; -. DR KEGG; pct:PC1_0529; -. DR eggNOG; COG1904; Bacteria. DR HOGENOM; CLU_044465_1_0_6; -. DR OrthoDB; 9766564at2; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000002736; Chromosome. DR GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 1.10.2020.10; uronate isomerase, domain 2, chain A; 1. DR HAMAP; MF_00675; UxaC; 1. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR003766; Uronate_isomerase. DR PANTHER; PTHR30068; URONATE ISOMERASE; 1. DR PANTHER; PTHR30068:SF4; URONATE ISOMERASE; 1. DR Pfam; PF02614; UxaC; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. PE 3: Inferred from homology; KW Isomerase. FT CHAIN 1..469 FT /note="Uronate isomerase" FT /id="PRO_1000212519" SQ SEQUENCE 469 AA; 54004 MW; BB3210BF70DDCD97 CRC64; MPQFLSEDFL LDSEFARRLY HEYAVDQPIF DYHCHLPPEQ IAENYRFKNL YDIWLKGDHY KWRAMRTNGV PERLCTGDAS DWEKFEAWAA TVPHTIGNPL YHWTHLELRR PFGVTGTLLS PSTAKDIWDR CNAMLERDDF TARGIMQQMN VKMVGTTDDP IDDLRHHKTV AQDSSFSIKV LPSWRPDKAF NIELATFNDY MAKLGEVSDT DIRRFSDLQA ALTKRLDHFA AHGCKVSDHA LDVVMFAEAD DATLDSILAR RLSGETLSEH EVAQFKTGVL VWLGAEYARR GWVQQYHIGA LRNNNLRQFK LLGPDVGFDS INDRPLAQEL SRLLSKQNEE NLLPKTILYC LNPRDNEVLG TMIGNFQGEG MPGKMQFGSG WWFNDQKDGM QRQMTQLAQL GLLSRFVGML TDSRSFLSYT RHEYFRRILC QMIGRWVEDG EAPADLPLLG EMVKNISFDN AKNYFAIEL //