UXAB_ALKHC
ID UXAB_ALKHC Reviewed; 512 AA.
AC Q9KFI7;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=BH0492;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB04211.1; -; Genomic_DNA.
DR PIR; D83711; D83711.
DR RefSeq; WP_010896670.1; NC_002570.2.
DR AlphaFoldDB; Q9KFI7; -.
DR SMR; Q9KFI7; -.
DR STRING; 272558.10173105; -.
DR DNASU; 892054; -.
DR EnsemblBacteria; BAB04211; BAB04211; BAB04211.
DR KEGG; bha:BH0492; -.
DR eggNOG; COG0246; Bacteria.
DR HOGENOM; CLU_027324_1_0_9; -.
DR OMA; VVIVRPI; -.
DR OrthoDB; 1442117at2; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000001258; 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; Reference proteome.
FT CHAIN 1..512
FT /note="Altronate oxidoreductase"
FT /id="PRO_0000170738"
FT BINDING 26..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ SEQUENCE 512 AA; 58450 MW; D27D7862C2913A05 CRC64;
MEKLSHGLVT SRNMIRYKSS QLPERVLQFG EGNFLRGFID WMIQQMNKQN VFNGRVVAIQ
PTPHGKVVPK LQEQDSLYTV WLRGIADGET VDHHEVITSI SRGLNPYTNW QDVLEVAASP
DISVVFSNTT EAGLTYLEEG YDKEKAPLSF PGKLAACLWH RYETLGWGEG SGLVIIPCEL
VEQNGKVLKE LVCRYAKAWN FPQEFFTWLE RENEFCHTLV DRIVPGFPSD TADECFERLG
YEDILLTVAE PYHLFIIEGS ERVRKLLPFN EAGLHVRWNH LEKHRNMKVR VLNGTHTFMF
ALSYLSGVDT VGEAMADEQL CSFIRKGLFE EIIPCVDAPE QEVTAFAETV LERFENPFLQ
HRLTDIGLNA VNKFRTRLMP TFNDYVAQTG EAPTYLLFSL AALINYYRGV EEDGPFLIGR
RREDSYLIRD DLEVIEAFKV GWQQVNTGKL SLAQLCEDLL SKRELWGVDL SMERKVVDKV
AESLQIIVEK GMRQAISGVL NQIGGNNHVH KQ