UXAB_CLOAB
ID UXAB_CLOAB Reviewed; 482 AA.
AC Q97L67;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=CA_C0695;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78672.1; -; Genomic_DNA.
DR PIR; E96985; E96985.
DR RefSeq; NP_347332.1; NC_003030.1.
DR RefSeq; WP_010964014.1; NC_003030.1.
DR AlphaFoldDB; Q97L67; -.
DR SMR; Q97L67; -.
DR STRING; 272562.CA_C0695; -.
DR EnsemblBacteria; AAK78672; AAK78672; CA_C0695.
DR GeneID; 44997206; -.
DR KEGG; cac:CA_C0695; -.
DR PATRIC; fig|272562.8.peg.898; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_1_0_9; -.
DR OMA; VVIVRPI; -.
DR OrthoDB; 1442117at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000814; 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; IPR000669; Mannitol_DH.
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 PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..482
FT /note="Altronate oxidoreductase"
FT /id="PRO_0000170741"
FT BINDING 18..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ SEQUENCE 482 AA; 55250 MW; A569F3B18D0919CA CRC64;
MKLNRSNFSE FKKYPEKILQ FGEGNFLRAF VDWQVDRMNK AADFNAGVVI VQPLEQGLVD
MLNEQDGLYT LYLQGLKEGK AVKEHSVIDC VTRGLNPYTQ YEEYLKLAEN PEMEIVISNT
TEAGIAFDEN DKLGRTCQNS YPGKLTAFLY RRFKTFNGDK SKGMLIIPCE LIDRNGEKLK
ATILKFAELW NLEKEFADWI EEANTFCCTL VDRIVPGYPR DTIEEVHAEL GYEDSLVDVG
EQFHLWVIEG PEWIKDILPF EKAGVNIQVV KDVTPYRTRK VRILNGAHTA LVPVAYLYGL
DTVGHSVEDK VIGKYLTELV YDEIIPTLDL PEEELKYFAG AVLERFLNPF VNHYLMSIAL
NSMPKFETRD LPSLLEYKKR KGQLPKKLVF SLAALIEFYK GKRGDEDIKL ADGEDILELY
KDLWSKFDGT DACYRNIVET VLGYEKNWKM NLNELEGLTD AVTENLIKID KLGMKEAVKS
VM