ID   UXAB_PECCP              Reviewed;         488 AA.
AC   C6DKE8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=PC1_0530;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT11585.1; -; Genomic_DNA.
DR   RefSeq; WP_012773237.1; NC_012917.1.
DR   AlphaFoldDB; C6DKE8; -.
DR   SMR; C6DKE8; -.
DR   STRING; 561230.PC1_0530; -.
DR   EnsemblBacteria; ACT11585; ACT11585; PC1_0530.
DR   KEGG; pct:PC1_0530; -.
DR   eggNOG; COG0246; Bacteria.
DR   HOGENOM; CLU_027324_1_0_6; -.
DR   OMA; VVIVRPI; -.
DR   OrthoDB; 1442117at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000002736; 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..488
FT                   /note="Altronate oxidoreductase"
FT                   /id="PRO_1000212506"
FT   BINDING         18..29
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ   SEQUENCE   488 AA;  55573 MW;  678B2D8CF35009A3 CRC64;
     MQTLNRRNFP GRQHPDRVIQ FGEGNFLRAF VDWQLDLLNE HTDLDAGIVI VRPIDSDFPP
     ALDTQDGLYT TIIRGLNEQG EAVREPRLIR SVNREINVYR QFDEYLALAH DPNIRFVFSN
     TTEAGISYHA DDSLSDAPPV SFPAKLTRLL YERFCHFDGA ADKGWVLLPC ELIDYNGVAL
     KELVLRYAAQ WKLTPTFTAW LNDHNTFCST LVDRIVTGYP RAEVEALQQE MGYQDTFWDT
     AEHFYLFVIQ GPQWLAEELR LNKLDLNVRI VDDIKPYKER KVAILNGAHT ALVPVAFLAG
     LDTVGESMDD ALIGKFVEKT IAEEIVPVLD LPHDELTSFA QAVLSRFRNP FIQHQLLSIS
     LNGMTKFRTR ILPQLLTYRE RHGELPARLT FALAALIAFY RGERSGEGDT LQTYPLQDDA
     HWLERYSTLW AGVKENTVSL AELVNVVLRD ADHWEQDLTQ VPGLAAQVTE QLQTIVERGM
     RAAVEGYC