UXUB_THEMA
ID UXUB_THEMA Reviewed; 539 AA.
AC Q9WXS3; G4FGY3; R4NP83;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=D-mannonate oxidoreductase {ECO:0000305};
DE EC=1.1.1.57 {ECO:0000269|PubMed:22925190};
DE AltName: Full=Fructuronate reductase {ECO:0000305};
DE AltName: Full=Mannonate dehydrogenase {ECO:0000303|PubMed:22925190};
GN Name=uxuB {ECO:0000303|PubMed:22925190};
GN OrderedLocusNames=TM_0068 {ECO:0000312|EMBL:AAD35162.1};
GN ORFNames=Tmari_0065 {ECO:0000312|EMBL:AGL48991.1};
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, 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).
CC -!- FUNCTION: Catalyzes the reduction of D-fructuronate (D-FruA) to D-
CC mannonate (D-ManA). {ECO:0000269|PubMed:22925190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannonate + NAD(+) = H(+) + keto-D-fructuronate + NADH;
CC Xref=Rhea:RHEA:15729, ChEBI:CHEBI:15378, ChEBI:CHEBI:17767,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:59881; EC=1.1.1.57;
CC Evidence={ECO:0000269|PubMed:22925190};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.63 mM for D-mannonate {ECO:0000269|PubMed:22925190};
CC Note=kcat is 4.2 sec(-1) with D-mannonate as substrate.
CC {ECO:0000269|PubMed:22925190};
CC -!- PATHWAY: Carbohydrate metabolism. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxuB
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD35162.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL48991.1; -; Genomic_DNA.
DR PIR; H72422; H72422.
DR RefSeq; NP_227884.1; NC_000853.1.
DR RefSeq; WP_004082564.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WXS3; -.
DR SMR; Q9WXS3; -.
DR STRING; 243274.THEMA_04465; -.
DR EnsemblBacteria; AAD35162; AAD35162; TM_0068.
DR EnsemblBacteria; AGL48991; AGL48991; Tmari_0065.
DR KEGG; tma:TM0068; -.
DR KEGG; tmm:Tmari_0065; -.
DR KEGG; tmw:THMA_0064; -.
DR PATRIC; fig|243274.17.peg.67; -.
DR eggNOG; COG0246; Bacteria.
DR InParanoid; Q9WXS3; -.
DR OMA; YKPYDNL; -.
DR OrthoDB; 1442117at2; -.
DR BioCyc; MetaCyc:MON-17954; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0008866; F:fructuronate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..539
FT /note="D-mannonate oxidoreductase"
FT /id="PRO_0000449570"
FT BINDING 39..50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 539 AA; 61432 MW; 47EF19B7F733CAF0 CRC64;
MRLNRETIKD RAAWEKIGVR PPYFDLDEVE KNTKEQPKWV HFGGGNIFRG FVAAVLQNLL
EEGKEDTGIN VIELFDYEVI DKVYKPYDNL SIAVTIKPDG DFEKRIIASV MEALKGDPSH
PDWERAKEIF RNPSLQLASL TITEKGYNIE DQAGNLFPQV MEDMKNGPVS PQTSMGKVAA
LLYERFKAGR LPIALLSLDN FSRNGEKLYS SVKRISEEWV KSGLVEKDFI DYLEKDVAFP
WSMIDKIVPG PSEFIKEHLE KLGIEGMEIF VTSKRTHIAP FVNMEWAQYL VIEDSFPNGR
PKLEGADRNV FLTDRETVEK AERMKVTTCL NPLHTALAIF GCLLGYKKIA DEMKDPLLKK
LVEGVGEEGI KVVVDPGIIN PREFLNEVIN IRLPNPYLPD TPQRIATDTS QKMPIRFGET
IKAYHERPDL DPRNLKYIPL VIAGWCRYLM GIDDEGREMQ LSPDPLLENL RSYVSKIKFG
DPESTDDHLK PILSSQQLFR VNLYEVGLGE KIEELFKKMI TGPRAVRKTL EEVVGREDG
