ID   F6BKC2_THEXL            Unreviewed;       466 AA.
AC   F6BKC2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   OrderedLocusNames=Thexy_2056 {ECO:0000313|EMBL:AEF18069.1};
OS   Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 / LX-11).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=858215 {ECO:0000313|EMBL:AEF18069.1, ECO:0000313|Proteomes:UP000007239};
RN   [1] {ECO:0000313|Proteomes:UP000007239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Hemme C., Woyke T.;
RT   "Complete sequence of Thermoanaerobacterium xylanolyticum LX-11.";
RL   Submitted (MAY-2011) 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: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}.
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DR   EMBL; CP002739; AEF18069.1; -; Genomic_DNA.
DR   RefSeq; WP_013788799.1; NC_015555.1.
DR   AlphaFoldDB; F6BKC2; -.
DR   STRING; 858215.Thexy_2056; -.
DR   KEGG; txy:Thexy_2056; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000007239; 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}.
SQ   SEQUENCE   466 AA;  54111 MW;  8971B4794731613E CRC64;
     MKNFMDDDFL LNNEVAVKLF HDYASKMPIF DFHCHLNPKD IYEDKKFKNI TEVWLYGDHY
     KWRLMRSNGV DEKYITGDAD DYSKFLEFAK TMPMAIGNPV FHWTHLELQR YFGVNELLNE
     KTAPMIWEKV NSVLESSEFS VRNIIKKSNV KILCTTDDPT DSLEYHKLLM DDESFGVKVL
     PAFRPDKGIN IERDDFRDWV KKLGEVSGKT IEDYEDYLDA LNSRIEYFDS LGCRLSDHAL
     DFVAYEESTK SKVNEIFKKA LEGEELSKFE IDQYKTSVLQ FLARKYKEFG WAMQLHIAAL
     RNTNTRMFRK LGPDTGYDAI NDVDIAQKVA KLLDSLDLTG SLPKTILYTL NPKDNYVLAT
     IMGCFQGEGI PGKMQFGSAW WFNDNIDGMR EQMRTLANVG LLSKFVGMVT DSRSFLSYPR
     HEYFRRILCN LIGEWVDRGE VPYDIDLLGK IVQDISYNNA VNYFGV
//