UXAE_THEMA
ID UXAE_THEMA Reviewed; 481 AA.
AC Q9WYS1; G4FE30; R4NYH0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tagaturonate/fructuronate epimerase {ECO:0000303|PubMed:22925190};
DE Short=D-TagA/D-FruA epimerase {ECO:0000303|PubMed:22925190};
DE EC=5.1.2.7 {ECO:0000269|PubMed:22925190};
GN Name=uxaE {ECO:0000303|PubMed:22925190};
GN OrderedLocusNames=TM_0440 {ECO:0000312|EMBL:AAD35525.1};
GN ORFNames=Tmari_0437 {ECO:0000312|EMBL:AGL49362.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND ACTIVE SITE.
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).
CC -!- FUNCTION: Catalyzes the epimerization of D-tagaturonate (D-TagA) to D-
CC fructuronate (D-FruA). {ECO:0000255|HAMAP-Rule:MF_02243,
CC ECO:0000269|PubMed:22925190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=keto-D-tagaturonate = keto-D-fructuronate;
CC Xref=Rhea:RHEA:51656, ChEBI:CHEBI:17886, ChEBI:CHEBI:59881;
CC EC=5.1.2.7; Evidence={ECO:0000255|HAMAP-Rule:MF_02243,
CC ECO:0000269|PubMed:22925190};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02243,
CC ECO:0000305|PubMed:22925190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.68 mM for D-fructuronate {ECO:0000269|PubMed:22925190};
CC Note=kcat is 6.5 sec(-1) with D-fructuronate as substrate.
CC {ECO:0000269|PubMed:22925190};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:22925190};
CC -!- SIMILARITY: Belongs to the UxaE family. {ECO:0000255|HAMAP-
CC Rule:MF_02243, ECO:0000305}.
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DR EMBL; AE000512; AAD35525.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49362.1; -; Genomic_DNA.
DR PIR; C72377; C72377.
DR RefSeq; NP_228250.1; NC_000853.1.
DR RefSeq; WP_004081526.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYS1; -.
DR SMR; Q9WYS1; -.
DR STRING; 243274.THEMA_02525; -.
DR EnsemblBacteria; AAD35525; AAD35525; TM_0440.
DR EnsemblBacteria; AGL49362; AGL49362; Tmari_0437.
DR KEGG; tma:TM0440; -.
DR KEGG; tmm:Tmari_0437; -.
DR KEGG; tmw:THMA_0446; -.
DR PATRIC; fig|243274.17.peg.438; -.
DR eggNOG; ENOG502Z82R; Bacteria.
DR InParanoid; Q9WYS1; -.
DR OMA; TIAPKFT; -.
DR OrthoDB; 647950at2; -.
DR BioCyc; MetaCyc:MON-17952; -.
DR BRENDA; 5.1.2.7; 6331.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016856; F:racemase and epimerase activity, acting on hydroxy acids and derivatives; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02243; UxaE; 1.
DR InterPro; IPR032586; UxaE.
DR Pfam; PF16257; UxaE; 1.
PE 1: Evidence at protein level;
KW Isomerase; Metal-binding; Reference proteome.
FT CHAIN 1..481
FT /note="Tagaturonate/fructuronate epimerase"
FT /id="PRO_0000449571"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02243,
FT ECO:0000305|PubMed:22925190"
FT ACT_SITE 266
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02243,
FT ECO:0000305|PubMed:22925190"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02243,
FT ECO:0000305|PubMed:22925190"
FT BINDING 308
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02243,
FT ECO:0000305|PubMed:22925190"
FT BINDING 341
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02243,
FT ECO:0000305|PubMed:22925190"
SQ SEQUENCE 481 AA; 55626 MW; FDA35A5CEF6EDC27 CRC64;
MVLKVFKDHF GRGYEVYEKS YREKDSLSFF LTKEEEGKIL VVAGEKAPEG LSFFKKQRAE
GVSFFFCERN HENLEVLRKY FPDLKPVRAG LRASFGTGDR LGITTPAHVR ALKDSGLFPI
FAQQSVRENE RTGRTWRDVL DDATWGVFQE GYSEGFGADA DHVKRPEDLV SAAREGFTMF
TIDPSDHVRN LSKLTEKERN EKFEEILRKE RIDRIYLGKK YSVLGEKIEF DEKNLRDAAL
VYYDAIAHVD MMYQILKDET PDFDFEVSVD ETETPTSPLF HIFVVEELRR RGVEFTNLAL
RFIGEWEKGI DYKGDLAQFE REIKMHAEIA RMFEGYKISL HSGSDKFSVY PAFASATGGL
FHVKTAGTSY LEAVKVISMV NPELFREIYR CTLDHFEEDR KSYHISADLS KVPEVEKVKD
EDLPGLFEDI NVRQLIHVTY GSVLKDASLK ERLFKTLEQN EELFYETVAK HIKRHVDLLE
G
