UXAC_VIBPA
ID UXAC_VIBPA Reviewed; 470 AA.
AC Q87FH3;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=VPA1706;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000032; BAC63049.1; -; Genomic_DNA.
DR RefSeq; NP_801216.1; NC_004605.1.
DR RefSeq; WP_005477444.1; NC_004605.1.
DR AlphaFoldDB; Q87FH3; -.
DR SMR; Q87FH3; -.
DR STRING; 223926.28810108; -.
DR EnsemblBacteria; BAC63049; BAC63049; BAC63049.
DR GeneID; 1192402; -.
DR KEGG; vpa:VPA1706; -.
DR PATRIC; fig|223926.6.peg.4622; -.
DR eggNOG; COG1904; Bacteria.
DR HOGENOM; CLU_044465_1_0_6; -.
DR OMA; IWHQCNE; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000002493; Chromosome 2.
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_0000172791"
SQ SEQUENCE 470 AA; 53987 MW; 61A064C622AC735E CRC64;
MKNFLCEDFL LSNETARRLY HEHAFHQPIY DYHCHLNPAE VTQNRQFDNL GQIWLEGDHY
KWRGMRSAGI EERLITGDAS DYDKYMAWAK TVPQTLGNPL YHWTHLELRR PFGITNTLFS
PDTADQIWHQ CNELLATPEF TARGIMQQMN VVMAGTTDDP IDSLEHHKAI AEDDTFNVKV
LPSWRPDKAF KIELDLFADY MHKLGEVADI DIRRFDDLLS ALDKRLAHFD SHGCRAADHG
IEIVRYAPIP SEADLDALLA RRLSGEVLSE LECAQFSTAV QVWLGKRYAQ LGWVMQLHIG
AQRNNSTRMF QLLGADAGFD SIGDRPFAFE LAHLLDEMDQ TNELPRTILY CLNPRDNEMM
ATMIGNFQGG GIAGKVQFGS GWWFNDQKDG MQRQMEQLSQ LGLLSQFVGM LTDSRSFLSY
TRHEYFRRIL CDMVGRWAEN GEVPNDLSLL GPMVEDICFG NAKRYFEERA