UXAB_ECOL5
ID UXAB_ECOL5 Reviewed; 483 AA.
AC Q0THR7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Altronate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00670};
DE EC=1.1.1.58 {ECO:0000255|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate reductase {ECO:0000255|HAMAP-Rule:MF_00670};
GN Name=uxaB {ECO:0000255|HAMAP-Rule:MF_00670}; OrderedLocusNames=ECP_1505;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-altronate + NAD(+) = H(+) + keto-D-tagaturonate + NADH;
CC Xref=Rhea:RHEA:17813, ChEBI:CHEBI:15378, ChEBI:CHEBI:17360,
CC ChEBI:CHEBI:17886, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.58;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00670};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000255|HAMAP-Rule:MF_00670}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00670}.
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DR EMBL; CP000247; ABG69512.1; -; Genomic_DNA.
DR RefSeq; WP_000854642.1; NC_008253.1.
DR AlphaFoldDB; Q0THR7; -.
DR SMR; Q0THR7; -.
DR STRING; 362663.ECP_1505; -.
DR EnsemblBacteria; ABG69512; ABG69512; ECP_1505.
DR KEGG; ecp:ECP_1505; -.
DR HOGENOM; CLU_027324_1_0_6; -.
DR OMA; VVIVRPI; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000009182; Chromosome.
DR GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1040.10; -; 1.
DR HAMAP; MF_00670; Altron_oxidoreduct; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023668; Altronate_OxRdtase.
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 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..483
FT /note="Altronate oxidoreductase"
FT /id="PRO_1000044703"
FT BINDING 18..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ SEQUENCE 483 AA; 54860 MW; 19A2AD0049367426 CRC64;
MKTLNRRDFP GAQYPERIIQ FGEGNFLRAF VDWQIDLLNE HTDLNSGVVV VRPIETSFPP
SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYS EYDEFLKLAH NPEMRFVFSN
TTEAGISYHA GDKFDDAPAV SYPAKLTRLL FERFSHFNGA LDKGWIIIPC ELIDYNGDAL
RELVLRYAQE WALPEAFIQW LDQANSFCST LVDRIVTGYP RDEVAKLEEE LGYHDGFLDT
AEYFYLFVIQ GPKSLATELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG
LDTVGEAMND AEICAFVEKA IYEEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA
LNGMTKFRTR ILPQLLAGQK ANGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER
YQQLWSQYRD RVIGTQELVA IVLAEKDHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR
PLC