UXAC_THEMA
ID UXAC_THEMA Reviewed; 451 AA.
AC Q9WXR9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Uronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675, ECO:0000303|PubMed:12945057};
DE EC=5.3.1.12 {ECO:0000255|HAMAP-Rule:MF_00675, ECO:0000269|PubMed:22925190};
DE AltName: Full=D-GalA/D-TagA isomerase {ECO:0000303|PubMed:22925190};
DE AltName: Full=D-GlcA/D-FruA isomerase {ECO:0000303|PubMed:22925190};
DE AltName: Full=Glucuronate isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
DE AltName: Full=Hexuronate isomerase {ECO:0000303|PubMed:22925190};
DE AltName: Full=Uronic isomerase {ECO:0000255|HAMAP-Rule:MF_00675};
GN Name=uxaC {ECO:0000303|PubMed:22925190}; OrderedLocusNames=TM_0064;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22925190; DOI=10.1111/j.1462-2920.2012.02856.x;
RA Rodionova I.A., Scott D.A., Grishin N.V., Osterman A.L., Rodionov D.A.;
RT "Tagaturonate-fructuronate epimerase UxaE, a novel enzyme in the hexuronate
RT catabolic network in Thermotoga maritima.";
RL Environ. Microbiol. 14:2920-2934(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), AND SUBUNIT.
RX PubMed=12945057; DOI=10.1002/prot.10462;
RA Schwarzenbacher R., Canaves J.M., Brinen L.S., Dai X., Deacon A.M.,
RA Elsliger M.-A., Eshaghi S., Floyd R., Godzik A., Grittini C.,
RA Grzechnik S.K., Guda C., Jaroszewski L., Karlak C., Klock H.E., Koesema E.,
RA Kovarik J.S., Kreusch A., Kuhn P., Lesley S.A., McMullan D.,
RA McPhillips T.M., Miller M.A., Miller M.D., Morse A., Moy K., Ouyang J.,
RA Robb A., Rodrigues K., Selby T.L., Spraggon G., Stevens R.C.,
RA van den Bedem H., Velasquez J., Vincent J., Wang X., West B., Wolf G.,
RA Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of uronate isomerase (TM0064) from Thermotoga maritima
RT at 2.85 A resolution.";
RL Proteins 53:142-145(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 ECO:0000269|PubMed:22925190};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-galacturonate = keto-D-tagaturonate;
CC Xref=Rhea:RHEA:27702, ChEBI:CHEBI:12952, ChEBI:CHEBI:17886;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00675,
CC ECO:0000269|PubMed:22925190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for D-galacturonate {ECO:0000269|PubMed:22925190};
CC KM=2.6 mM for D-glucuronate {ECO:0000269|PubMed:22925190};
CC Note=kcat is 3.8 sec(-1) with D-galacturonate as substrate. kcat is
CC 0.35 sec(-1) with D-glucuronate as substrate.
CC {ECO:0000269|PubMed:22925190};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00675}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12945057}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Uronate isomerase family. {ECO:0000255|HAMAP-Rule:MF_00675,
CC ECO:0000305}.
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DR EMBL; AE000512; AAD35158.1; -; Genomic_DNA.
DR PIR; D72422; D72422.
DR RefSeq; NP_227880.1; NC_000853.1.
DR RefSeq; WP_004082556.1; NZ_CP011107.1.
DR PDB; 1J5S; X-ray; 2.85 A; A/B/C=1-451.
DR PDBsum; 1J5S; -.
DR AlphaFoldDB; Q9WXR9; -.
DR SMR; Q9WXR9; -.
DR STRING; 243274.THEMA_04485; -.
DR PRIDE; Q9WXR9; -.
DR EnsemblBacteria; AAD35158; AAD35158; TM_0064.
DR KEGG; tma:TM0064; -.
DR eggNOG; COG1904; Bacteria.
DR InParanoid; Q9WXR9; -.
DR OMA; TDHGHPT; -.
DR OrthoDB; 167900at2; -.
DR BioCyc; MetaCyc:MON-17959; -.
DR UniPathway; UPA00246; -.
DR EvolutionaryTrace; Q9WXR9; -.
DR Proteomes; UP000008183; 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..451
FT /note="Uronate isomerase"
FT /id="PRO_0000172789"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 12..21
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:1J5S"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:1J5S"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:1J5S"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 262..283
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:1J5S"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:1J5S"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 372..383
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 403..424
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:1J5S"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:1J5S"
SQ SEQUENCE 451 AA; 52306 MW; FC0B3221F740B927 CRC64;
MFLGEDYLLT NRAAVRLFNE VKDLPIVDPH NHLDAKDIVE NKPWNDIWEV EGATDHYVWE
LMRRCGVSEE YITGSRSNKE KWLALAKVFP RFVGNPTYEW IHLDLWRRFN IKKVISEETA
EEIWEETKKK LPEMTPQKLL RDMKVEILCT TDDPVSTLEH HRKAKEAVEG VTILPTWRPD
RAMNVDKEGW REYVEKMGER YGEDTSTLDG FLNALWKSHE HFKEHGCVAS DHALLEPSVY
YVDENRARAV HEKAFSGEKL TQDEINDYKA FMMVQFGKMN QETNWVTQLH IGALRDYRDS
LFKTLGPDSG GDISTNFLRI AEGLRYFLNE FDGKLKIVLY VLDPTHLPTI STIARAFPNV
YVGAPWWFND SPFGMEMHLK YLASVDLLYN LAGMVTDSRK LLSFGSRTEM FRRVLSNVVG
EMVEKGQIPI KEARELVKHV SYDGPKALFF G
