ID D6A3M1_STRV1 Unreviewed; 353 AA.
AC D6A3M1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ORFNames=SSFG_04776 {ECO:0000313|EMBL:EFE69534.2};
OS Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS 9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE69534.2, ECO:0000313|Proteomes:UP000003824};
RN [1] {ECO:0000313|Proteomes:UP000003824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; DS999641; EFE69534.2; -; Genomic_DNA.
DR AlphaFoldDB; D6A3M1; -.
DR eggNOG; COG1088; Bacteria.
DR Proteomes; UP000003824; 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}.
FT DOMAIN 30..332
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 38873 MW; AF13661ACFF82B99 CRC64;
MTAPSSPARP TQASPARPAQ ASPARPTRIL VTGGAGFIGS HYVRTLLGPQ GPGDVAITVL
DKLTYAGNPA NLDEVRAHPG FAFVQGDICD PELVGKLMAE HDQVVHFAAE SHVDRSIDGG
AEFVRTNVVG THTLIDAAHR AGIETFVHIS TDEVYGSIDE GSWPETHPLQ PNSPYSSAKA
SSDLIALSYH RTHGLDVRVT RCSNNYGHHH FPEKVIPLFV TNLLDGKKVP LYGDGGNVRD
WLHIDDHVQG IELVRTKGRA GEVYNIGGGT ELSNRELTEL LLEACGADWE TSVEYVEDRK
GHDRRYSVDC TKISEELGYA PRKDFREGLA ETVQWYRDNR DWWEPLKERA ALR
//
