ID A0A239CTM5_9BURK Unreviewed; 351 AA.
AC A0A239CTM5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN06265795_101644 {ECO:0000313|EMBL:SNS23460.1};
OS Noviherbaspirillum humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1688639 {ECO:0000313|EMBL:SNS23460.1, ECO:0000313|Proteomes:UP000198284};
RN [1] {ECO:0000313|EMBL:SNS23460.1, ECO:0000313|Proteomes:UP000198284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U15 {ECO:0000313|EMBL:SNS23460.1,
RC ECO:0000313|Proteomes:UP000198284};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOT01000001; SNS23460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239CTM5; -.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000198284; Unassembled WGS sequence.
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; 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.
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:UP000198284}.
FT DOMAIN 3..323
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 39269 MW; D4B1EBF24908A475 CRC64;
MILVTGGAGF IGSNFVLDWL TQSGEPVVNL DKLTYAGNLE NLASLKGDAR HVFVQGDIGD
QTLVAGLLEK HKPRAVLHFA AESHVDRSIH GPDAFIQTNV VGTFQLLEAV RAYWASLEEP
EKSAFRFLHV STDEVYGSLG KEDPPFAETN RYEPNSPYSA SKAASDHLVR AYHHTYGLPV
LTTNCSNNYG PYHFPEKLIP LIIVNALAGK PLPVYGDGQQ IRDWLYVGDH CSAIRRVLEA
GRLGETYNVG GWNEQANLDV VKIVCGILDE LQPRADGKRY AEQITFVKDR PGHDRRYAID
ARKLERELGW KPAETFETGI RKTVKWYLAN GDWVRNVQSG AYREWISRNY G
//
