ID A0A1M5U5L5_9FIRM Unreviewed; 451 AA.
AC A0A1M5U5L5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Tagaturonate reductase {ECO:0000313|EMBL:SHH58307.1};
GN ORFNames=SAMN02745245_01662 {ECO:0000313|EMBL:SHH58307.1};
OS Anaerosphaera aminiphila DSM 21120.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerosphaera.
OX NCBI_TaxID=1120995 {ECO:0000313|EMBL:SHH58307.1, ECO:0000313|Proteomes:UP000184032};
RN [1] {ECO:0000313|EMBL:SHH58307.1, ECO:0000313|Proteomes:UP000184032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21120 {ECO:0000313|EMBL:SHH58307.1,
RC ECO:0000313|Proteomes:UP000184032};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FQXI01000014; SHH58307.1; -; Genomic_DNA.
DR RefSeq; WP_073185299.1; NZ_FQXI01000014.1.
DR AlphaFoldDB; A0A1M5U5L5; -.
DR STRING; 1120995.SAMN02745245_01662; -.
DR OrthoDB; 9768714at2; -.
DR Proteomes; UP000184032; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000184032}.
FT DOMAIN 8..158
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 191..391
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
SQ SEQUENCE 451 AA; 52289 MW; 688741A110CF7A48 CRC64;
MENKELKRVI QFGEGNFLRG FVDDFLYELK EKNLFNGDVV VVQPIKQGMC DVLEKQDCNY
NLYLRGIENG QVVNEHKFID IISHCINPYI SFEEYLDLAN DKNFRFIVSN TTESGIVVNE
DDKFEDKPAS SFPGKLTQLL YKRYENNLPG FIVLSCELID NNGLELKKCV NKYIELWELE
EGFKRWIDTE NDFCSTLVDR IVTGYPKDEA ELKKLEAEIG YKDLCLDTAE IFHQWVIEGN
YESELPLQEA GFNVIWTDDV SPYKKRKVRI LNGAHTSMVL GARLYGLSTV RECLEDETIN
KFLRKCIFKE IIPAIGGSDE DLKFGNAVIE RFSNPFIEHQ LLSIALNSVS KFDVRVLPTI
LEYREKFGYY PAGLSFSMAA LIKFYKTNEA NDSEEVMKFM AENSVEDILK NRDLWHSDLI
ELIPIVQKYY DMINENGIEK AFEYVIEEEV I
//