ID C1F2M5_ACIC5 Unreviewed; 463 AA. AC C1F2M5; DT 26-MAY-2009, integrated into UniProtKB/TrEMBL. DT 26-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 73. DE RecName: Full=Uronate isomerase {ECO:0000256|ARBA:ARBA00020555, ECO:0000256|HAMAP-Rule:MF_00675}; DE EC=5.3.1.12 {ECO:0000256|ARBA:ARBA00012546, ECO:0000256|HAMAP-Rule:MF_00675}; DE AltName: Full=Glucuronate isomerase {ECO:0000256|HAMAP-Rule:MF_00675}; DE AltName: Full=Uronic isomerase {ECO:0000256|HAMAP-Rule:MF_00675}; GN Name=uxaC {ECO:0000256|HAMAP-Rule:MF_00675, GN ECO:0000313|EMBL:ACO31794.1}; GN OrderedLocusNames=ACP_2685 {ECO:0000313|EMBL:ACO31794.1}; OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM OS 7670 / NBRC 15755 / NCIMB 13165 / 161). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Acidobacterium. OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO31794.1, ECO:0000313|Proteomes:UP000002207}; RN [1] {ECO:0000313|EMBL:ACO31794.1, ECO:0000313|Proteomes:UP000002207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / RC NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207}; RX PubMed=19201974; DOI=10.1128/AEM.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). 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:0000256|ARBA:ARBA00001165, ECO:0000256|HAMAP- CC 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 Evidence={ECO:0000256|HAMAP-Rule:MF_00675}; CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate CC interconversion. {ECO:0000256|ARBA:ARBA00004892, ECO:0000256|HAMAP- CC Rule:MF_00675}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Uronate isomerase family. {ECO:0000256|ARBA:ARBA00008397, CC ECO:0000256|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; CP001472; ACO31794.1; -; Genomic_DNA. DR RefSeq; WP_015897749.1; NC_012483.1. DR AlphaFoldDB; C1F2M5; -. DR STRING; 240015.ACP_2685; -. DR KEGG; aca:ACP_2685; -. DR eggNOG; COG1904; Bacteria. DR HOGENOM; CLU_044465_0_0_0; -. DR InParanoid; C1F2M5; -. DR OrthoDB; 9766564at2; -. DR UniPathway; UPA00246; -. DR Proteomes; UP000002207; 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 {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00675}; KW Reference proteome {ECO:0000313|Proteomes:UP000002207}. SQ SEQUENCE 463 AA; 52627 MW; 58A556B193228BEF CRC64; MLMHEDRLFP ADPTTRRIAR SLYEQVRSLP IVSPHGHTQA AWFAHNEPFP DPAKLFVQPD HYIYRMLYSQ GVTLEDLEIG VEQIQNPRKV WRIFASHYYL FRGTPTRLWL DFAFETLFGL TESLSAKTSD LYFDTISEKL QTPEFRPRAL YERFHLEVLA TTDSPLDSLA DHQIIRDSGW PARILATFRP DSVVDPDFTG FADNIATLGA QTGEDTAHWS GYLKALRQAR ARFRSLGATA TDHGHPTAQT ANLSEPEAAQ LFITVLSGNA TAAQRELFRA QMLTEMARMS VEDGLVMQIH PGSARNHNRK LYERYGRDVG ADIPMPTNYV DALRPMLDLV GNERGLTIIL FTLDETAYSR ELAPLAGHYP CLRLGPPWWF HDSPEGMMRF REQVTETAGF YNTVGFNDDT RAFLSIPARH DVARRIDCAF LARLVAEHRL SEEEAAEVAH DLAYKLVKAA YRL //