ID A0A348AKM3_9FIRM Unreviewed; 338 AA.
AC A0A348AKM3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
DE EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
GN Name=rfbB {ECO:0000313|EMBL:BBB91621.1};
GN ORFNames=MAMMFC1_02305 {ECO:0000313|EMBL:BBB91621.1};
OS Methylomusa anaerophila.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Methylomusa.
OX NCBI_TaxID=1930071 {ECO:0000313|EMBL:BBB91621.1, ECO:0000313|Proteomes:UP000276437};
RN [1] {ECO:0000313|EMBL:BBB91621.1, ECO:0000313|Proteomes:UP000276437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMFC1 {ECO:0000313|EMBL:BBB91621.1,
RC ECO:0000313|Proteomes:UP000276437};
RX PubMed=29458677; DOI=10.1099/ijsem.0.002635;
RA Amano N., Yamamuro A., Miyahara M., Kouzuma A., Abe T., Watanabe K.;
RT "Methylomusa anaerophila gen. nov., sp. nov., an anaerobic methanol-
RT utilizing bacterium isolated from a microbial fuel cell.";
RL Int. J. Syst. Evol. Microbiol. 68:1118-1122(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:57649; EC=4.2.1.46;
CC Evidence={ECO:0000256|ARBA:ARBA00001539,
CC ECO:0000256|RuleBase:RU004473};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911,
CC ECO:0000256|RuleBase:RU004473};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily.
CC {ECO:0000256|ARBA:ARBA00008178, ECO:0000256|RuleBase:RU004473}.
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DR EMBL; AP018449; BBB91621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348AKM3; -.
DR KEGG; mana:MAMMFC1_02305; -.
DR OrthoDB; 9766450at2; -.
DR Proteomes; UP000276437; Chromosome.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01181; dTDP_gluc_dehyt; 1.
DR PANTHER; PTHR43000:SF7; DTDP-D-GLUCOSE 4,6-DEHYDRATASE; 1.
DR PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU004473, ECO:0000313|EMBL:BBB91621.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000276437}.
FT DOMAIN 6..307
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 338 AA; 38537 MW; 620455AD6961B7E5 CRC64;
MTTNVLVTGG AGFIGSNFVR HMLNKYPEYK IINVDMLTYA GNLANLRDIE TDADYIFHKA
DIADHAAMDA FFADYSFEYV VNFAAESHVD RSIEEPEKFI RTNIMGTQVL LDQAKKYGVK
KYLQVSTDEV YGALGAEGLF TEETPIAPNS PYSASKAGAD LMVRAYYETF GLPVNITRCS
NNYGPYHFPE KLIPLMVTNA LENKELPVYG DGLHVRDWLH VSDHCQAIDQ VLHRGSVGEV
YNIGGNNEKT NIEIVRNILA ALGKPDTLIR YVKDRPGHDR RYGIDATKIK RELGWKPLYT
FEQGLIETVA WYQEHADWWR AIKSGEYREY YKKMYAKR
//
