ID   UXAB_CROS8              Reviewed;         483 AA.
AC   A7MPR2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
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};
GN   OrderedLocusNames=ESA_01824;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU77078.1; -; Genomic_DNA.
DR   RefSeq; WP_012124768.1; NC_009778.1.
DR   AlphaFoldDB; A7MPR2; -.
DR   SMR; A7MPR2; -.
DR   KEGG; esa:ESA_01824; -.
DR   PATRIC; fig|290339.8.peg.1626; -.
DR   HOGENOM; CLU_027324_1_0_6; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   PANTHER; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..483
FT                   /note="Altronate oxidoreductase"
FT                   /id="PRO_1000044705"
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;  54430 MW;  290D81D64C61243C CRC64;
     MKTLNRRDFP GALWPERIIQ FGEGNFLRAF IDWQVDLLNE HTDLNAGVVV VRPIASDFPP
     SLSTQDGLYT TIIRGLNEKG EAVSESRLIR SVNREISVYA QYDEFLKLAH NPDIRFVFSN
     TTEAGISYHA GDQFDDAPAV SYPAKLTRLL FERFSHFDGA QDKGWVIIPC ELIDYNGEAL
     RELVLRYAHE WALPAAFTTW LESANSFCST LVDRIVTGYP RDEVAQLEES LGYHDAFLDT
     AEHFYLFVIQ GPQWLARELR LDKLPLNVLI VDDIKPYKAR KVAILNGAHT ALVPVAFLAG
     LNTVGEAMND AQICAFVERA IHDEIIPVLD LPRNELESFA DAVVSRFRNP YIKHQLLSIA
     LNGMTKFRTR ILPQLLAGQA QMGTLPPRLT FALAALIAFY RGERNGEGYP LQDDAHWLAR
     FEQLWTQRGD NTITLRELVD AVLSDCEHWE QDLTAVPGLA AQVTRDLDAI LNQGMRHAVA
     PLC
//