ID D9TDA3_MICAI Unreviewed; 333 AA. AC D9TDA3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00016977, ECO:0000256|RuleBase:RU004473}; DE EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473}; GN OrderedLocusNames=Micau_1179 {ECO:0000313|EMBL:ADL44741.1}; OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Micromonospora. OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL44741.1, ECO:0000313|Proteomes:UP000001908}; RN [1] {ECO:0000313|EMBL:ADL44741.1, ECO:0000313|Proteomes:UP000001908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442 RC {ECO:0000313|Proteomes:UP000001908}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora aurantiaca ATCC 27029."; RL Submitted (AUG-2010) 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP002162; ADL44741.1; -; Genomic_DNA. DR RefSeq; WP_013284380.1; NC_014391.1. DR AlphaFoldDB; D9TDA3; -. DR STRING; 644283.Micau_1179; -. DR KEGG; mau:Micau_1179; -. DR eggNOG; COG1088; Bacteria. DR HOGENOM; CLU_007383_1_14_11; -. DR OrthoDB; 9801785at2; -. DR Proteomes; UP000001908; Chromosome. DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 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 InterPro; IPR020904; Sc_DH/Rdtase_CS. 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. DR PROSITE; PS00061; ADH_SHORT; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|RuleBase:RU004473}; NAD {ECO:0000256|ARBA:ARBA00023027}; KW Reference proteome {ECO:0000313|Proteomes:UP000001908}. FT DOMAIN 4..313 FT /note="NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF16363" SQ SEQUENCE 333 AA; 36152 MW; 039A398F58F958AE CRC64; MRILVTGGAG FIGSEYVRML LGVPGGDASG VPVEDPAALT VLDKLTYSGN LANLAPVRDD PRLRFVRGDI CDPALVDEVV PGHDVIVHFA AESHVDRSIT GAAPFVTTNV LGTQTLLDAA LRHGISRFVH VSTDEVYGSI DSGSWTEDWP LAPNSPYSAS KAGSDLLALS YHRTHGLDVV VTRCSNNYGP YQFPEKVVPL FVTNLLDGGT VPLYGDGGNV RDWLHVHDHC RGVAMVQEKG RAGEVYHIGG GTELTNRQLT ERLLATCGAG WDRVVPVTDR KGHDRRYSLD IGKISSELGY APSIDLDRGL AETVRWYRDN RAWWEPLKTA GPE //