ID Q5WIW3_SHOC1 Unreviewed; 493 AA. AC Q5WIW3; DT 23-NOV-2004, integrated into UniProtKB/TrEMBL. DT 23-NOV-2004, sequence version 1. DT 02-SEP-2026, entry version 108. DE SubName: Full=Altronate oxidoreductase {ECO:0000313|EMBL:BAD63692.1}; DE EC=1.1.1.58 {ECO:0000313|EMBL:BAD63692.1}; GN OrderedLocusNames=ABC1154 {ECO:0000313|EMBL:BAD63692.1}; OS Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Shouchella. OX NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD63692.1, ECO:0000313|Proteomes:UP000001168}; RN [1] {ECO:0000313|EMBL:BAD63692.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63692.1, RC ECO:0000313|Proteomes:UP000001168}; RA Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.; RT "Molecular cloning and nucleotide sequence of the gene for an alkaline RT protease from the alkalophilic Bacillus sp. KSM-K16."; RL J. Ferment. Bioeng. 78:105-108(1994). RN [2] {ECO:0000313|EMBL:BAD63692.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63692.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=7632397; DOI=10.1007/s002530050437; RA Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K., RA Kawai S., Ito S.; RT "Purification and properties of an alkaline protease from alkalophilic RT Bacillus sp. KSM-K16."; RL Appl. Microbiol. Biotechnol. 43:473-481(1995). RN [3] {ECO:0000313|EMBL:BAD63692.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63692.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=9278275; DOI=10.1093/protein/10.6.627; RA Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.; RT "High-resolution crystal structure of M-protease: phylogeny aided analysis RT of the high-alkaline adaptation mechanism."; RL Protein Eng. 10:627-634(1997). RN [4] {ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168}; RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM- RT K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAD63692.1, ECO:0000313|Proteomes:UP000001168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD63692.1, RC ECO:0000313|Proteomes:UP000001168}; RX PubMed=17429572; DOI=10.1007/s00792-007-0074-1; RA Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K., RA Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.; RT "Intragenomic diversity of the V1 regions of 16S rRNA genes in high- RT alkaline protease-producing Bacillus clausii spp."; RL Extremophiles 11:597-603(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate CC + NADH + H(+); 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:ARBA00048615}; 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; AP006627; BAD63692.1; -; Genomic_DNA. DR RefSeq; WP_011246007.1; NC_006582.1. DR AlphaFoldDB; Q5WIW3; -. DR STRING; 66692.ABC1154; -. DR PaxDb; 66692-ABC1154; -. DR KEGG; bcl:ABC1154; -. DR eggNOG; COG0246; Bacteria. DR HOGENOM; CLU_027324_1_0_9; -. DR Proteomes; UP000001168; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0009026; F:tagaturonate reductase activity; IEA:UniProtKB-EC. DR GO; GO:0019592; P:mannitol catabolic process; IEA:TreeGrafter. DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR013118; Mannitol_DH_C. DR InterPro; IPR013131; Mannitol_DH_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; NF002969; PRK03643.1; 1. 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 4: Predicted; KW NAD {ECO:0000256|ARBA:ARBA00023027}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:BAD63692.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001168}. FT DOMAIN 24..266 FT /note="Mannitol dehydrogenase N-terminal" FT /evidence="ECO:0000259|Pfam:PF01232" FT DOMAIN 284..476 FT /note="Mannitol dehydrogenase C-terminal" FT /evidence="ECO:0000259|Pfam:PF08125" SQ SEQUENCE 493 AA; 55810 MW; C8C97CEF46117F4B CRC64; MDRIETKQLT KKLVGQETPA GKETIVQIGE GNFMRGFIDW MVDQLHQQRL YDGRVAAIQP TPHGKIVPVL QAQDGLYTVI LRGKLDGKVI DEAEVVQSIA RGINPYNDWE EVKKLARSPD VKWLFSNTTE AGLVYQQERY EKDKAPLSFP GKVTAFLYER FLAFAGALEA GITLVPCELI EDNGAVLKDI VETIAEDWEL PIEFGQWLRK ANVFCNTLVD RIVTGFPHGE EETWANRLGY EDRLLTVAEP YHLFVIEPER PLDERLPFEQ AGLNVKWEPV ALHRELKVRL LNGLHTMMFA LSFLAGEDTV KGALHSPRLR RFIERGLEQE LIPVVNAPEE EKQAYAASVI ERFENPFLAH KLTDIGLNAI YKFKTRLLPA LEAHEQQDNE PSQLLASLAA LLVYMKPQER DGAFLKGNWQ GRTYQIRENE TALALLEATW CQYDAGEATL AETISTLLQA DGLWGRDLSR YSEKVADCAY GLLNGDLFKM IEG //