UXAC_XANAC
ID UXAC_XANAC Reviewed; 472 AA.
AC Q8PET9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
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}; Synonyms=hrmI;
GN OrderedLocusNames=XAC4251;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008923; AAM39086.1; -; Genomic_DNA.
DR RefSeq; WP_005916173.1; NC_003919.1.
DR AlphaFoldDB; Q8PET9; -.
DR SMR; Q8PET9; -.
DR STRING; 190486.XAC4251; -.
DR EnsemblBacteria; AAM39086; AAM39086; XAC4251.
DR GeneID; 66913231; -.
DR KEGG; xac:XAC4251; -.
DR eggNOG; COG1904; Bacteria.
DR HOGENOM; CLU_044465_0_0_6; -.
DR OMA; TDHGHPT; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000576; 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.
FT CHAIN 1..472
FT /note="Uronate isomerase"
FT /id="PRO_0000172794"
SQ SEQUENCE 472 AA; 52896 MW; 8F59D75349D217CC CRC64;
MRSSVLSLHP DRLLPADPGT RAIARRLYAQ VATLPIISPH GHTDPAWFAT NAPFANATEL
LLVPDHYVFR MLYSQGIDLD ALGIPRADGT RATVDPRAAW RVFAEHYTLL RGTPSALWLN
HVFHDVFDLR IRLDAGTADH YYDHITAALQ TPAFLPRALF ERFNIEVIAT TESPLDRLQH
HAAIAASGWQ GRVVTAYRPD PVVDPEHEQF AGALQQFGAL TGEDVLTWDG YLRAHRQRRA
FFAAHGATST DHGHPSAATA DLSPAEAQRL FDTVVRGAAT PEQAELFRAQ VLTEMAAMSL
DDGLVMQLHP GCFRNHNRQL FEQYGRDKGA DIPMRTDYVH ALKPLLDRHG NDPRLRLIVF
TLDETSYSRE LAPLAGHYPS LLLGPAWWFH DAPEGMWRFR EQTLASAGFY NTVGFNDDTR
AFLSIPARHD VARRVDSAFL AKLVAEHRLE EDEATEVAID LAYRLPKQAY KL