UXAC_ALKCK
ID UXAC_ALKCK Reviewed; 472 AA.
AC Q5WJC1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=ABC0995;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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: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; AP006627; BAD63534.1; -; Genomic_DNA.
DR RefSeq; WP_011245850.1; NC_006582.1.
DR AlphaFoldDB; Q5WJC1; -.
DR SMR; Q5WJC1; -.
DR STRING; 66692.ABC0995; -.
DR PRIDE; Q5WJC1; -.
DR EnsemblBacteria; BAD63534; BAD63534; ABC0995.
DR KEGG; bcl:ABC0995; -.
DR eggNOG; COG1904; Bacteria.
DR HOGENOM; CLU_044465_1_0_9; -.
DR OMA; TDHGHPT; -.
DR OrthoDB; 167900at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000001168; 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..472
FT /note="Uronate isomerase"
FT /id="PRO_0000172760"
SQ SEQUENCE 472 AA; 53983 MW; 8274B351590594E7 CRC64;
MISTGKAFIH ENFMLQNKTA ETLYHTYAKT LPIIDYHCHV PPQEIAENRQ FNNISEIWLH
GDHYKWRAMR AVGVEETFIT GDGDDKEKFL KWAETVPYTM GNPLYHWTHL ELKRYFGIDE
LLSSETAEAI WSATKEQLAA PERSVQGIIK ESNVKVICTT DDPSDHLEAH QQIRKEGACQ
AAVYPAFRPD KALVASAPSF VPYLETLGAA AEVDISSLRS LLEALEKRAT FFAEEGCVLS
DHGLRTLPFV DTTEKEAEAA FQKALNQETL TPQEEEKYQT YVLLFLARLY NKLGWTMQFH
LGALRNNNSR MVEQVGPDSG FDSMADDRFA ESLNRFLNEL ERTNELPKTI LYTLNPIFNE
VIATTIGNFQ GGGIPGKIQF GSGWWFNDTK DGMEKQMTDL ANNGLLSLFV GMLTDSRSFL
SYTRHEYFRR ILCNRIGEWV ERGEWPADEK WLGKVVEDIS YYNAKRYFAF PK