ID A0A0K9GWL5_9BACI Unreviewed; 334 AA.
AC A0A0K9GWL5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=AC625_17120 {ECO:0000313|EMBL:KMY51035.1};
OS Peribacillus loiseleuriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1679170 {ECO:0000313|EMBL:KMY51035.1, ECO:0000313|Proteomes:UP000037146};
RN [1] {ECO:0000313|Proteomes:UP000037146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27997 {ECO:0000313|Proteomes:UP000037146};
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 (JUL-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:KMY51035.1}.
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DR EMBL; LFZW01000001; KMY51035.1; -; Genomic_DNA.
DR RefSeq; WP_049682387.1; NZ_LFZW01000001.1.
DR AlphaFoldDB; A0A0K9GWL5; -.
DR STRING; 1679170.AC625_17120; -.
DR PATRIC; fig|1679170.3.peg.3895; -.
DR OrthoDB; 9811743at2; -.
DR Proteomes; UP000037146; 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:KMY51035.1};
KW Lyase {ECO:0000256|RuleBase:RU004473}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000037146};
KW Virion {ECO:0000313|EMBL:KMY51035.1}.
FT DOMAIN 6..309
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 334 AA; 38289 MW; 91A5693C80B3BB67 CRC64;
MKKKILVTGG AGFIGGNFVR FMVNKHSDYE IYNLDLLTYA GDLTKHRDIE SESNYHFVKA
DISDRESISA LFEKEQFDYV VHFAAESHVD RSITNPEIFV VTNVLGTQVL LDAAKTNNIT
KFVHVSTDEV YGELDFDPST FFTEETPLQP NSPYSASKAS SDLLVRAYAE TFNLPVNITR
CSNNYGPYHF PEKLIPLTIS RVVNDQKVPV YGDGENIRDW LHVLDHCAAI DLVLHEGING
EVYNVGGHNE RTNLEVVKTI INTLDKSENL IEFVEDRLGH DKRYAIDPTK LEQLGWKPIY
TFETGIAQTI QWYLDNKEWW ERIISGEYQE YFEK
//
