ID A0A0C2Q3H5_9CYAN Unreviewed; 360 AA.
AC A0A0C2Q3H5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 08-NOV-2023, entry version 36.
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=SD81_02775 {ECO:0000313|EMBL:KIJ78339.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ78339.1};
RN [1] {ECO:0000313|EMBL:KIJ78339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ78339.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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:KIJ78339.1}.
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DR EMBL; JXCB01000004; KIJ78339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2Q3H5; -.
DR OrthoDB; 9811743at2; -.
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; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR43000:SF47; DTDP-GLUCOSE 4,6-DEHYDRATASE 2; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Capsid protein {ECO:0000313|EMBL:KIJ78339.1};
KW Lyase {ECO:0000256|RuleBase:RU004473}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Virion {ECO:0000313|EMBL:KIJ78339.1}.
FT DOMAIN 5..321
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 360 AA; 41084 MW; B102B567E0ACCBAA CRC64;
MQKILVTGGT GFIGSNFILK ARKEQWANII NLDKLTYASN PQTLAQLQDD SGYHFVRGDI
GDLELLRNLL EQYQPDAIIN FAAESHVDRS ILSPQDFIQT NVLGTFQLLE ASRAYWEKLS
LQKREQFRFL HVSTDEVYGT LSPTDPAFRE DTPYAPNSPY AASKAGSDHF VRAYYHTYGL
PTLTTNCSNN YGPRQFPEKL IPLIILNALN GKPLPIYGDG QNVRDWLYVV DHCEAIYLVL
KHSRVGETYN IGGNNEQTNL SVVEKICVIL DELAPKPDFR HSSLMTFVKD RPGHDRRYAI
DCSKISRDLG WQPKEDFDSG LLKTIHWYLS NPTWVEQVQS GVYQTWIMQN YGDREVVPSR
//
