ID A0A0M1N2F2_9BACL Unreviewed; 340 AA.
AC A0A0M1N2F2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=AM231_27380 {ECO:0000313|EMBL:KOR76337.1};
OS Paenibacillus solani.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR76337.1, ECO:0000313|Proteomes:UP000036932};
RN [1] {ECO:0000313|Proteomes:UP000036932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-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:KOR76337.1}.
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DR EMBL; LIUT01000008; KOR76337.1; -; Genomic_DNA.
DR RefSeq; WP_054405452.1; NZ_LIUT01000008.1.
DR AlphaFoldDB; A0A0M1N2F2; -.
DR PATRIC; fig|1705565.3.peg.1705; -.
DR OrthoDB; 9811743at2; -.
DR Proteomes; UP000036932; 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 Capsid protein {ECO:0000313|EMBL:KOR76337.1};
KW Lyase {ECO:0000256|RuleBase:RU004473}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000036932};
KW Virion {ECO:0000313|EMBL:KOR76337.1}.
FT DOMAIN 4..305
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 340 AA; 38197 MW; C403BEE0B285B473 CRC64;
MKLLVTGGAG FIGSNFILYI MQQYPDYQIV NMDSLTYAGN LENLKSVEGN PNYTFVQADI
ADKQAVDAIF QQGVDVVVNF AAESHVDRSI LEPEIFVNTN VLGTQVLLDA SKNYGVTKFV
QVSTDEVYGT LGETGLFSET TLLAPNSPYS ASKAGGDLLV RAYHETFGLP VNITRCSNNY
GPYQFPEKLI PLIISRALND ESLPIYGDGL NIRDWLYVED HCSAIDLVIH QGKIGEVYNI
GGNNERTNLH IVTTILEELG KPESLITFVA DRPGHDRRYG IDPSKITNEL GWKPRHNFET
GIKETIRWYL NHKDWWTRIQ SGAYREYMTQ QYGKRLGEPE
//
