GenomeNet

Database: UniProt
Entry: A0A1H0RNU3_9BACI
LinkDB: A0A1H0RNU3_9BACI
Original site: A0A1H0RNU3_9BACI 
ID   A0A1H0RNU3_9BACI        Unreviewed;       489 AA.
AC   A0A1H0RNU3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=SAMN05216565_102291 {ECO:0000313|EMBL:SDP30648.1};
OS   Litchfieldia salsa.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Litchfieldia.
OX   NCBI_TaxID=930152 {ECO:0000313|EMBL:SDP30648.1, ECO:0000313|Proteomes:UP000199159};
RN   [1] {ECO:0000313|Proteomes:UP000199159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M10078 {ECO:0000313|Proteomes:UP000199159};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
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; FNJU01000002; SDP30648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0RNU3; -.
DR   STRING; 930152.SAMN05216565_102291; -.
DR   OrthoDB; 9768714at2; -.
DR   UniPathway; UPA00246; -.
DR   Proteomes; UP000199159; 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:UP000199159}.
FT   DOMAIN          18..172
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         19..30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00670"
SQ   SEQUENCE   489 AA;  56317 MW;  6B36D79BA6E08F3A CRC64;
     MEKLNRNTWK ESKKYPVKVL QFGEGNFLRA FVNWQIDKMN KETDFNGGVV VAQPIEFGLI
     DKLNEQEGLY TLFLQGIKNE EAVREHSVID CINYGINPYA NYDQLLEVTE NPELRFIISN
     TTEAGITFEE NDRLSDSPQK SFPGKLTALL YHRFNTFAGA EDKGFVILPC ELIDRNGEKL
     KEIVLKYIEL WNLELGFKEW VLQSNTFCCT LVDRIVTGYP RDTIDEITTE LGYKDELVVV
     GEQFHLWVIE GPQWISDEFP TNQAGLNVKV VNDMTPYRTR KVRILNGAHT AMTPVCYLYG
     LDTVGDSMKD EVTRDFIERL IFDEIIPTLD LPEEELKSFA SAVLERFMNP YVNHYLLSIA
     LNSMSKFKTR DLPTLIEYHG RTGELPRRLV FSLSALIALY KGKRDSEEIN LQDDDHVMEL
     YSSLWKDYDG SEDRIREIVT TVLAYEKNWE LDLTIIPGLT DMVTEFLVKI ERSGMKVAIK
     DVTKISLGN
//
DBGET integrated database retrieval system