ID A0A419SHF5_9BACL Unreviewed; 337 AA.
AC A0A419SHF5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 10.
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 ORFNames=BEP19_12900 {ECO:0000313|EMBL:RKD23241.1};
OS Ammoniphilus oxalaticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Ammoniphilus.
OX NCBI_TaxID=66863 {ECO:0000313|EMBL:RKD23241.1, ECO:0000313|Proteomes:UP000284219};
RN [1] {ECO:0000313|EMBL:RKD23241.1, ECO:0000313|Proteomes:UP000284219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAOx-1 {ECO:0000313|EMBL:RKD23241.1,
RC ECO:0000313|Proteomes:UP000284219};
RA Poppleton D.I., Gribaldo S.;
RT "Novel Firmicute Genomes.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:RKD23241.1}.
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DR EMBL; MCHY01000009; RKD23241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419SHF5; -.
DR OrthoDB; 9811743at2; -.
DR Proteomes; UP000284219; Unassembled WGS sequence.
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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000284219}.
FT DOMAIN 5..308
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 337 AA; 38959 MW; 4B5A2E6E026F09DC CRC64;
MKKVLVTGGA GFIGGNFVRY MADKYSDYQI YNLDLLTYAG DLTKHRDIEN KANYHFIKAD
IANRDEIKPL FEKERFDYVI HFAAESHVDR SITDPEIFIR TNVLGTQVLL DAAREFAVTK
FVHVSTDEVY GELDFDPNTF FTEDTPLQPN SPYSASKASS DFLVRSYYET YGLPMNITRC
SNNYGPYHFP EKLIPLTISR VLNDQKVPVY GDGKNIRDWL HVIDHCAAID LVMHKAPSGE
VYNIGGHNER TNLEVVKTII HALGKSEDLI EFVEDRLGHD KRYAIDPTKL EQLGWKPTYT
FETGIAQTIQ WYLDNKEWWE QIISGEYQKY FEKQYAM
//
