UXAB_SHIF8
ID UXAB_SHIF8 Reviewed; 483 AA.
AC Q0T4K8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SFV_1580;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF03757.1; -; Genomic_DNA.
DR RefSeq; WP_000854635.1; NC_008258.1.
DR AlphaFoldDB; Q0T4K8; -.
DR SMR; Q0T4K8; -.
DR EnsemblBacteria; ABF03757; ABF03757; SFV_1580.
DR KEGG; sfv:SFV_1580; -.
DR HOGENOM; CLU_027324_1_0_6; -.
DR OMA; VVIVRPI; -.
DR BioCyc; SFLE373384:SFV_RS08855-MON; -.
DR UniPathway; UPA00246; -.
DR Proteomes; UP000000659; 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..483
FT /note="Altronate oxidoreductase"
FT /id="PRO_1000044707"
FT BINDING 18..29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00670"
SQ SEQUENCE 483 AA; 54856 MW; AFA4677CE3B5CC10 CRC64;
MKTLNRRDFP GAQYPERIIQ FGEGNFLRAF VDWQIDLLNE HTDLNSGVVV VRPIETSFPP
SLSTQDGLYT TIIRGLNEKG EAVSDARLIR SVNREISVYS EYDEFLKLAH NPEMRFVFSN
TTEAGISYHA GDKFDDAPAV SYPAKLTRLL FERFSHFNGA LDKGWIIIPC ELIDYNGDAL
RELVLRYAQE WALPEAFIQW LDQANSFCST LVDRIVTGYP RDEVAKLEEE LGYHDGFLDT
AEHFYLFVIQ GPKSLATELR LDKYPLNVLI VDDIKPYKER KVAILNGAHT ALVPVAFQAG
LDTVGEAMND AEICAFVEKA IYEEIIPVLD LPRDELESFA SAVTGRFRNP YIKHQLLSIA
LNGMTKFRTR ILPQLLAGQK ANGTLPARLT FALAALIAFY RGERNGETYP VQDDAHWLER
YQQLWSQHRD RVIGTQELVA IVLAEKYHWE QDLTQVPGLV EQVANDLDAI LEKGMREAVR
PLC