ID   UXAC_SPHAL              Reviewed;         470 AA.
AC   Q1GNM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=Sala_3046;
OS   Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS   (Sphingomonas alaskensis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=317655;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13593 / LMG 18877 / RB2256;
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(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: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; CP000356; ABF54750.1; -; Genomic_DNA.
DR   RefSeq; WP_011543313.1; NC_008048.1.
DR   AlphaFoldDB; Q1GNM2; -.
DR   SMR; Q1GNM2; -.
DR   STRING; 317655.Sala_3046; -.
DR   PRIDE; Q1GNM2; -.
DR   EnsemblBacteria; ABF54750; ABF54750; Sala_3046.
DR   KEGG; sal:Sala_3046; -.
DR   eggNOG; COG1904; Bacteria.
DR   HOGENOM; CLU_044465_0_0_5; -.
DR   OMA; TDHGHPT; -.
DR   OrthoDB; 167900at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000006578; 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..470
FT                   /note="Uronate isomerase"
FT                   /id="PRO_1000044777"
SQ   SEQUENCE   470 AA;  52409 MW;  93040A502BA83DDB CRC64;
     MPRPLYLSPD RLFPSDPAQR DIARRLYKAV AGLPIVSPHG HTDPAWFAGD APFGNAAELL
     LHPDHYVFRM LYSQGVSLDA LGIGNADADP RESWRLFAEN YHLFRATPSR MWMDWVFAEV
     FGFDVQLSAE TSDLYYDRIT EALAIDAFRP RALFDRFGIE VIATTESPLD SLDHHAVIRA
     ANASGEWGGR VITAYRPDPV VDPEFEGFRD NLARFSNLSG EDAFSYSGYL AAHRKRRAFF
     ASMGATSTDH GHPSAATADL SETQAEALFA RVTGEDMSAA DAELFRAHML TVMAGMSLDD
     GLVMQIHPGA FRNHNPWLFA NHGRDKGADI PTATDYVHAL RPLLGRYGNE ADLTIILFTL
     DETSYARELA PLAGHYPALK LGPAWWFHDS PEGMRRFRSQ MTETAGFYNT VGFNDDTRAF
     LSIPARHDVA RRIDCGFLAQ LVSEHRLEEW EAAELAADLS YNLAKASYKL