ID I8XGG0_9BACE Unreviewed; 479 AA.
AC I8XGG0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=HMPREF1068_02529 {ECO:0000313|EMBL:EIY49970.1};
OS Bacteroides nordii CL02T12C05.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997884 {ECO:0000313|EMBL:EIY49970.1, ECO:0000313|Proteomes:UP000003089};
RN [1] {ECO:0000313|EMBL:EIY49970.1, ECO:0000313|Proteomes:UP000003089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C05 {ECO:0000313|EMBL:EIY49970.1,
RC ECO:0000313|Proteomes:UP000003089};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides nordii CL02T12C05.";
RL Submitted (FEB-2012) 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 -!- 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:EIY49970.1}.
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DR EMBL; AGXS01000016; EIY49970.1; -; Genomic_DNA.
DR RefSeq; WP_002560250.1; NZ_JH724314.1.
DR AlphaFoldDB; I8XGG0; -.
DR STRING; 997884.HMPREF1068_02529; -.
DR GeneID; 69502215; -.
DR PATRIC; fig|997884.3.peg.2600; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_1_0_10; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000003089; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00670};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00670};
KW Reference proteome {ECO:0000313|Proteomes:UP000003089}.
FT DOMAIN 17..171
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 205..452
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 479 AA; 53957 MW; D2CFB8B77F721F3F CRC64;
MKALNKETAL KVQRPERIIQ FGEGNFLRAF VDWIIYNMNE KADFNSSVVV VQPIDKGMVD
MLNAQDDLYH VNLQGLDKGE VVNSLTMIDV ISRALNPYTQ NAEFMKLAEQ PEMRFVISNT
TEAGIAFDPS CKLDDAPATS YPGKLTQLLY HRFKTFNGDK SKGLIIFPCE LIFLNGHKLK
ETIYQYIELW NLGEEFKTWF EEACGVYATL VDRIVPGFPR KDIAAIKEKL QYDDNLVVQA
EIFHLWVIEA PQEIAKEFPA DKAGLNVLFV PSEAPYHERK VTLLNGPHTV LSPVAYLSGV
NIVREACEHE VVGKYIHKVM FDELMETLNL PKDELEKFAH DVLERFNNPF VDHAVTSIML
NSFPKYQTRD LPGLKTYLER KGELPKGLVL GLAAIITYYK GGVRADGAEI IPNDAPEIMN
LLKELWATGC TQKVAEGVLG AEFIWGENLN NIPGLAEAVK ANLDSIQEKG MLETVKSIL
//
