ID A0A179SV57_9BACI Unreviewed; 378 AA.
AC A0A179SV57;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Mannitol-1-phosphate 5-dehydrogenase {ECO:0000256|ARBA:ARBA00016219, ECO:0000256|HAMAP-Rule:MF_00196};
DE EC=1.1.1.17 {ECO:0000256|ARBA:ARBA00012939, ECO:0000256|HAMAP-Rule:MF_00196};
GN Name=mtlD {ECO:0000256|HAMAP-Rule:MF_00196};
GN ORFNames=A6K24_24755 {ECO:0000313|EMBL:OAS84739.1};
OS Metabacillus litoralis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Metabacillus.
OX NCBI_TaxID=152268 {ECO:0000313|EMBL:OAS84739.1, ECO:0000313|Proteomes:UP000078534};
RN [1] {ECO:0000313|Proteomes:UP000078534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C44 {ECO:0000313|Proteomes:UP000078534};
RA Lyu Z., Lyu W.;
RL Submitted (APR-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, ECO:0000256|HAMAP-
CC Rule:MF_00196};
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_00196}.
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:OAS84739.1}.
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DR EMBL; LWSG01000024; OAS84739.1; -; Genomic_DNA.
DR RefSeq; WP_066335613.1; NZ_LWSG01000024.1.
DR AlphaFoldDB; A0A179SV57; -.
DR STRING; 152268.A6K24_24755; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000078534; Unassembled WGS sequence.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR InterPro; IPR000669; Mannitol_DH.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR023027; Mannitol_DH_CS.
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.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00196};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00196};
KW Reference proteome {ECO:0000313|Proteomes:UP000078534}.
FT DOMAIN 1..124
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 149..372
FT /note="Mannitol dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08125"
FT BINDING 3..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00196"
SQ SEQUENCE 378 AA; 41525 MW; EE715EE1C7F7D906 CRC64;
MKATHFGAGN IGRGFIGLLL HQSGYEVEFV DVNETVIDEI NKEKAYRVIL ANEEKQAFQV
KGVSGINSGQ APEAVIQAIS TANLVTTAVG PHILKFVAPL IAEGLKKRMQ ANSQPVNIIA
CENMVGGSSE LKKHVLEKLT ADEAAWVQEH VGFPNSAVDR IVPNQHNEKL LDVLVEPFHE
WVIDSTELKG TKPDIKEALF VENLQAYIER KLFTVNTGHA ATAYLGNLAG HTTIADTISD
EKIKQAVLGT LEETGKVLIA KYAFQADEHQ KYIEKIIGRF ANPNIIDDVQ RVGRAPLRKL
GAKDRLVAPA LEYMNEFDQV PEHLVNVIVA ALKFVSEEDQ ESLTLKEKVQ EKGVGPAFSE
ITGLTLDHPL VEKVVALY
//
