ID   A9BHG9_PETMO            Unreviewed;       455 AA.
AC   A9BHG9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=Pmob_0854 {ECO:0000313|EMBL:ABX31578.1};
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Petrotoga.
OX   NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31578.1, ECO:0000313|Proteomes:UP000000789};
RN   [1] {ECO:0000313|EMBL:ABX31578.1, ECO:0000313|Proteomes:UP000000789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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; CP000879; ABX31578.1; -; Genomic_DNA.
DR   RefSeq; WP_012208681.1; NC_010003.1.
DR   AlphaFoldDB; A9BHG9; -.
DR   STRING; 403833.Pmob_0854; -.
DR   KEGG; pmo:Pmob_0854; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_1_0_0; -.
DR   OrthoDB; 9766564at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000789; 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   455 AA;  53021 MW;  3FB211BD7284A557 CRC64;
     MSFLDENYLL QNNTSKMLYN SIKDFPILDA HNHGDVKEIV ENKGWDDIWQ VEGATDHYVW
     ESMRKRGVPE EKITGNASNK EKWMALAKVF PGFVGNPTYE WIHLDLKRRF KIEDTISKYT
     AEKIWQDTSL LLKSESMKPQ RLLKEMNVEV MCTTNDPTED LSFHEKAKDI EGIKILPTWR
     PDKAMNIEKE NWKDFVEKLG EITKENVERF EGFLNALYKT HKKFEKLGGV SSDHGILEPI
     SYPVERERVK EVYEKALSKK ELTKQEISDF KSFMFYEFGT MNAESNWVMQ LHIGAIRDYR
     DKLYNTLGPD TGGDISTSKI DLANGLRYFL NQFDEKLKVV LYCLDPSLFP TVATIARAFP
     NVSLGAPWWF NDSPFGMEIY LKYIATVDLL SDLAGWVTDS RKLISYGSRT EMFRRELSNV
     VGEMVEKGQI PIREAFDLVR DISYFRPKRL FFEKI
//