ID C6PWS8_9CLOT Unreviewed; 482 AA.
AC C6PWS8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Altronate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00670};
DE EC=1.1.1.58 {ECO:0000256|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00670};
DE AltName: Full=Tagaturonate reductase {ECO:0000256|HAMAP-Rule:MF_00670};
GN Name=uxaB {ECO:0000256|HAMAP-Rule:MF_00670};
GN ORFNames=CcarbDRAFT_3245 {ECO:0000313|EMBL:EET86303.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET86303.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET86303.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET86303.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-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:0000256|HAMAP-Rule:MF_00670};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000292};
CC -!- PATHWAY: Carbohydrate metabolism; pentose and glucuronate
CC interconversion. {ECO:0000256|HAMAP-Rule:MF_00670}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00670}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EET86303.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACVI01000058; EET86303.1; -; Genomic_DNA.
DR RefSeq; WP_007062130.1; NZ_GG770688.1.
DR AlphaFoldDB; C6PWS8; -.
DR STRING; 536227.Ccar_14410; -.
DR KEGG; cck:Ccar_14410; -.
DR PATRIC; fig|536227.13.peg.3019; -.
DR eggNOG; COG0246; Bacteria.
DR OrthoDB; 9768714at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000004198; Unassembled WGS sequence.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:RHEA.
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; IPR000669; Mannitol_DH.
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 PRINTS; PR00084; MTLDHDRGNASE.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00670};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00670};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198}.
FT DOMAIN 17..171
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 203..454
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
FT BINDING 18..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00670"
SQ SEQUENCE 482 AA; 55572 MW; A59257072BDADA46 CRC64;
MKLNKEIYKE YKKYPEKVLQ FGEGNFLRAF VDWQVDKMNR EADFNGSVVV IPPTKNGKVD
KLNEQDGLFN LYLQGIKEGK AVKEHFVINS ISRGINCYEQ YDEYLKVAEQ PEIRFIFSNT
TEAGITFDEN DKLEDKPQNS YPGKLTAFLY HRFKAFKGEK DKGVIVIPCE LIDRNGEKLK
SIILKYAELW QLEEQFSSWL NEANTFCCSL VDRIVPGYPK DTIEEVTKEL GYEDSLVDVS
EQFHLWVIEG PEWIKNEFPA DKAGLNVKFV EDMTPYRTRK VRILNGAHTS LVPVAYLYGL
ETVGQAVEHE VIGRYVNKTV YDEIIPTLDL PEEELKYFAG AVLERFANPF VKHYLMSIAL
NSMSKFETRD LPSLIEYVNR KGKLPKKLCF SLAALIEFYK GKRGEENIEL ADNEDILNLY
KSLWENYDGT EAGLKNIVST VLSYEKNWKM NLNAIEGLTD TVTNYLSKIE KLGIKEAIKE
VM
//
