ID F7NJ99_9FIRM Unreviewed; 509 AA.
AC F7NJ99;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Altronate oxidoreductase {ECO:0000313|EMBL:EGO63847.1};
DE EC=1.1.1.58 {ECO:0000313|EMBL:EGO63847.1};
GN ORFNames=ALO_10774 {ECO:0000313|EMBL:EGO63847.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO63847.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO63847.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO63847.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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 -!- 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:EGO63847.1}.
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; AFGF01000085; EGO63847.1; -; Genomic_DNA.
DR RefSeq; WP_004095391.1; NZ_AFGF01000085.1.
DR AlphaFoldDB; F7NJ99; -.
DR STRING; 1009370.ALO_10774; -.
DR eggNOG; COG0246; Bacteria.
DR OrthoDB; 9768714at2; -.
DR Proteomes; UP000003240; 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-EC.
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 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:0000313|EMBL:EGO63847.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT DOMAIN 30..184
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 217..479
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 509 AA; 57078 MW; FE52C7236C0D6C35 CRC64;
MEKLSASFLR SYQPASGLAV GKATEHLPER VLQFGEGNFL RAFVDSMIHQ LNQHNLFNGR
VVVVQPIAEG LAGQLNEQNG LYTLLLRGLQ GGKITEHKEI IAAVSRGLNP YTQWEEVLQC
AENPSTEFIV SNTTEAGIVF DPADKFTHTP PVSFPGKLTA YLYRRYTHFQ GDPAKGLIML
PCELIDRNGD NLKSAVLRLA AAWNRPAAFS QWVENCNTFA NTLVDRVVTG YPRDEAQELQ
RQFGYIDELM DTGEIFHLWV IEGPQALSER LPFHKIGLDV IWTNDMTPYR TRKVRILNGA
HTSSVPAAFL YGLETVQEMM EHPVTGKFIR QIMQDEILPS LEFSGLDKKM LNEFSASVVE
RFENPFIKHY LLSILLNSSS KFKARVLPSI LEYAKIKGTL PKRLVFSLSA LLFVYKDGVI
DGTSMKARRP AGEFIMKDDL PVLQFMAERW SAFDGSSAGA AKLAKEILAN EAIWGENLNR
IAGLTEMTGH YLHLLNTRGM QKTIAGLIR
//
