ID UXAC_XANAC Reviewed; 472 AA. AC Q8PET9; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 99. 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}; Synonyms=hrmI; GN OrderedLocusNames=XAC4251; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). 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; AE008923; AAM39086.1; -; Genomic_DNA. DR RefSeq; WP_005916173.1; NC_003919.1. DR AlphaFoldDB; Q8PET9; -. DR SMR; Q8PET9; -. DR GeneID; 66913231; -. DR KEGG; xac:XAC4251; -. DR eggNOG; COG1904; Bacteria. DR HOGENOM; CLU_044465_0_0_6; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000000576; 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..472 FT /note="Uronate isomerase" FT /id="PRO_0000172794" SQ SEQUENCE 472 AA; 52896 MW; 8F59D75349D217CC CRC64; MRSSVLSLHP DRLLPADPGT RAIARRLYAQ VATLPIISPH GHTDPAWFAT NAPFANATEL LLVPDHYVFR MLYSQGIDLD ALGIPRADGT RATVDPRAAW RVFAEHYTLL RGTPSALWLN HVFHDVFDLR IRLDAGTADH YYDHITAALQ TPAFLPRALF ERFNIEVIAT TESPLDRLQH HAAIAASGWQ GRVVTAYRPD PVVDPEHEQF AGALQQFGAL TGEDVLTWDG YLRAHRQRRA FFAAHGATST DHGHPSAATA DLSPAEAQRL FDTVVRGAAT PEQAELFRAQ VLTEMAAMSL DDGLVMQLHP GCFRNHNRQL FEQYGRDKGA DIPMRTDYVH ALKPLLDRHG NDPRLRLIVF TLDETSYSRE LAPLAGHYPS LLLGPAWWFH DAPEGMWRFR EQTLASAGFY NTVGFNDDTR AFLSIPARHD VARRVDSAFL AKLVAEHRLE EDEATEVAID LAYRLPKQAY KL //