UXAC_SALTY
ID UXAC_SALTY Reviewed; 470 AA.
AC Q8ZM23;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=STM3137;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22011.1; -; Genomic_DNA.
DR RefSeq; NP_462052.1; NC_003197.2.
DR RefSeq; WP_000190182.1; NC_003197.2.
DR PDB; 3IAC; X-ray; 2.22 A; A/B/C=1-470.
DR PDBsum; 3IAC; -.
DR AlphaFoldDB; Q8ZM23; -.
DR SMR; Q8ZM23; -.
DR STRING; 99287.STM3137; -.
DR PaxDb; Q8ZM23; -.
DR EnsemblBacteria; AAL22011; AAL22011; STM3137.
DR GeneID; 1254660; -.
DR KEGG; stm:STM3137; -.
DR PATRIC; fig|99287.12.peg.3325; -.
DR HOGENOM; CLU_044465_1_0_6; -.
DR OMA; IWHQCNE; -.
DR PhylomeDB; Q8ZM23; -.
DR BioCyc; SENT99287:STM3137-MON; -.
DR UniPathway; UPA00246; -.
DR EvolutionaryTrace; Q8ZM23; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0008880; F:glucuronate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..470
FT /note="Uronate isomerase"
FT /id="PRO_0000172785"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:3IAC"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:3IAC"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 253..264
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 271..292
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:3IAC"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3IAC"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3IAC"
FT TURN 418..421
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 422..440
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 448..459
FT /evidence="ECO:0007829|PDB:3IAC"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:3IAC"
SQ SEQUENCE 470 AA; 53610 MW; 78D5EE0CB2B11218 CRC64;
MATFMTEDFL LKNDIARTLY HKYAAPMPIY DFHCHLSPQE IADDRRFDNL GQIWLEGDHY
KWRALRSAGV DESLITGKET SDYEKYMAWA NTVPKTLGNP LYHWTHLELR RPFGITGTLF
GPDTAESIWT QCNEKLATPA FSARGIMQQM NVRMVGTTDD PIDSLEYHRQ IAADDSIDIE
VAPSWRPDKV FKIELDGFVD YLRKLEAAAD VSITRFDDLR QALTRRLDHF AACGCRASDH
GIETLRFAPV PDDAQLDAIL GKRLAGETLS ELEIAQFTTA VLVWLGRQYA ARGWVMQLHI
GAIRNNNTRM FRLLGPDTGF DSIGDNNISW ALSRLLDSMD VTNELPKTIL YCLNPRDNEV
LATMIGNFQG PGIAGKVQFG SGWWFNDQKD GMLRQLEQLS QMGLLSQFVG MLTDSRSFLS
YTRHEYFRRI LCNLLGQWAQ DGEIPDDEAM LSRMVQDICF NNAQRYFTIK
