ID A0A087DEF1_9BIFI Unreviewed; 344 AA.
AC A0A087DEF1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BISA_1725 {ECO:0000313|EMBL:KFI93901.1};
OS Bifidobacterium saguini DSM 23967.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437607 {ECO:0000313|EMBL:KFI93901.1, ECO:0000313|Proteomes:UP000029066};
RN [1] {ECO:0000313|EMBL:KFI93901.1, ECO:0000313|Proteomes:UP000029066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23967 {ECO:0000313|EMBL:KFI93901.1,
RC ECO:0000313|Proteomes:UP000029066};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI93901.1}.
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DR EMBL; JGZN01000004; KFI93901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087DEF1; -.
DR STRING; 1437607.BISA_1725; -.
DR Proteomes; UP000029066; 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, ECO:0000313|EMBL:KFI93901.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 16..316
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 344 AA; 39104 MW; 8EFDEB93B70DC680 CRC64;
MICRMADEVF IPKNIIVTGG CGFIGSNFVH YVYNNHPDVH VTVLDALTYA GNLENIKGIL
GDRVEFVHGN ICDAELLDRI VPGHDAIVHY AAESHNDNSI ANPEPFLKTN VEGTFRLLEA
CRKYDVRYHH VSTDEVYGDL ALDDPAKFTE ETPYHPSSPY SSTKASSDLL VRAWHRTFGI
RATISNCSNN YGPYQHVEKF IPRQITNILE GLKPKLYGNG LNVRDWIHTD DHSTGVWTIL
TRGRIGETYL IGANGERNNI TVLRDILTVM GKDPDDFDWV KDRPGHDRRY AIDSTKLQTE
LGWKPTHTDF QKGLEQTIQW YTDNRAWWEP SKAATEAKYK QQGQ
//
