ID   UXAC_CLOAB              Reviewed;         467 AA.
AC   Q97L70;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 89.
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}; OrderedLocusNames=CA_C0692;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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}.
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DR   EMBL; AE001437; AAK78669.1; -; Genomic_DNA.
DR   PIR; B96985; B96985.
DR   RefSeq; NP_347329.1; NC_003030.1.
DR   RefSeq; WP_010964011.1; NC_003030.1.
DR   AlphaFoldDB; Q97L70; -.
DR   SMR; Q97L70; -.
DR   STRING; 272562.CA_C0692; -.
DR   EnsemblBacteria; AAK78669; AAK78669; CA_C0692.
DR   GeneID; 44997203; -.
DR   KEGG; cac:CA_C0692; -.
DR   PATRIC; fig|272562.8.peg.895; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_9; -.
DR   OMA; IWHQCNE; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006064; P:glucuronate catabolic process; IEA:InterPro.
DR   HAMAP; MF_00675; UxaC; 1.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR003766; Uronate_isomerase.
DR   Pfam; PF02614; UxaC; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..467
FT                   /note="Uronate isomerase"
FT                   /id="PRO_0000172767"
SQ   SEQUENCE   467 AA;  53720 MW;  51B6813E793CAA61 CRC64;
     MKNFMDEKFM LSTKVAEDLY NDFAKDMPII DYHCHISPQE ICENKSFKNI TEVWLYGDHY
     KWRLMRSSGV DEKYITGDSS DYEKFLAYVK AIETAIGNPL YHWSHLELQR YFGVYEVISE
     KNAPVIWEKA NKVLNDGLTV REIIKKSNVK AICTTDDPID SLEYHLKLKE DTSFNVKVLP
     AFRPDKALGI NKDGYTDWVS KLAKVSKKNI NSYDMFLEAL NDRIEFFHSV GGRVSDHALD
     YVPYLEASKE EVNTIFAKAL KGEKVSFEEE TKFRTFTMKF LGKKYASLGW AMELHMNAKR
     DNNTRMYNKL GPDTGFDSVN DNGVAGPLSR FLDSLEKEGS LPKTIIYSLN PNDNFVIGTL
     LGCFQGTEAF GKIQFGAAWW FNDHRDGMVE QMETLANLGA FSTFIGMLTD SRSFLSYTRH
     EYFRRILCDL IGKWVENGEV PNDMELLGRI TKNICFNNAN NYFEMGL