ID U1LA39_9MICO Unreviewed; 377 AA.
AC U1LA39;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=L332_05370 {ECO:0000313|EMBL:ERG63898.1};
OS Agrococcus pavilionensis RW1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agrococcus.
OX NCBI_TaxID=1330458 {ECO:0000313|EMBL:ERG63898.1, ECO:0000313|Proteomes:UP000016462};
RN [1] {ECO:0000313|EMBL:ERG63898.1, ECO:0000313|Proteomes:UP000016462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW1 {ECO:0000313|EMBL:ERG63898.1,
RC ECO:0000313|Proteomes:UP000016462};
RX PubMed=23814108;
RA White R.A.III., Grassa C.J., Suttle C.A.;
RT "First draft genome sequence from a member of the genus agrococcus,
RT isolated from modern microbialites.";
RL Genome Announc. 1:e00391-13(2013).
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; Evidence={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:ERG63898.1}.
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DR EMBL; ASHR01000028; ERG63898.1; -; Genomic_DNA.
DR RefSeq; WP_021010863.1; NZ_ASHR01000028.1.
DR AlphaFoldDB; U1LA39; -.
DR OrthoDB; 271711at2; -.
DR Proteomes; UP000016462; 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; 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_00196};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00196};
KW Reference proteome {ECO:0000313|Proteomes:UP000016462}.
FT DOMAIN 1..120
FT /note="Mannitol dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01232"
FT DOMAIN 144..362
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 377 AA; 40217 MW; E4C864D86E687E41 CRC64;
MRAVHFGAGN IGRGFVGLIL HRAGFEVTFV DVNAELIGML QSADAYRVRE VGPEARIHTV
TGFSGIDSSA DPEAAARAVA EADVVTCAVG PSAMRFIAPA IRAGLEQREG APVVVMACEN
AIGASDTLRE HVLDGAPELA DRAVFANTAV DRIIPPQDPH GLDVVVEDFF EWSIDRAAFE
RGGIAAPEIG DAHFVDDLGP YIERKLFTVN TGHATTAYAG WVAGAGTIAA ALELPEIRAA
VEAALTDTSR LLVAKHGFDE AEHAAYVARA IARFENPALP DTCERIGRQP LRKLSRHERF
VEPAAQLVDR GESADALVAA FGTALRFDAP GDEQALELQE LLRSLDPAAF VARVTGLEAE
HPLTARLVEV VREARAR
//
