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Database: UniProt
Entry: A0A267MK23_9CLOT
LinkDB: A0A267MK23_9CLOT
Original site: A0A267MK23_9CLOT 
ID   A0A267MK23_9CLOT        Unreviewed;       325 AA.
AC   A0A267MK23;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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   Name=rfbB {ECO:0000313|EMBL:PAB59143.1};
GN   ORFNames=CCE28_11535 {ECO:0000313|EMBL:PAB59143.1};
OS   Anaeromicrobium sediminis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Anaeromicrobium.
OX   NCBI_TaxID=1478221 {ECO:0000313|EMBL:PAB59143.1, ECO:0000313|Proteomes:UP000216024};
RN   [1] {ECO:0000313|EMBL:PAB59143.1, ECO:0000313|Proteomes:UP000216024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY2726D {ECO:0000313|EMBL:PAB59143.1,
RC   ECO:0000313|Proteomes:UP000216024};
RA   Zeng X.;
RT   "Draft genome sequence of anaerobic fermentative bacterium Anaeromicrobium
RT   sediminis DY2726D isolated from West Pacific Ocean sediments.";
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}.
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:PAB59143.1}.
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DR   EMBL; NIBG01000009; PAB59143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A267MK23; -.
DR   OrthoDB; 9811743at2; -.
DR   Proteomes; UP000216024; 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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216024}.
FT   DOMAIN          5..306
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   325 AA;  37533 MW;  4D3C50028C7E3B4F CRC64;
     MKTLLVTGGA GFIGSNFIRY MIDKYKNYKI INLDLLTYAG NLENLKDIEH NPNYEFIKGD
     ISDKKLVDKI VSKKVDYIIN FAAASHVDRS IEDPEVFIRT NIMGTQVLLD AAKKYNIEKY
     VQISTDEVYG SLGKEGLFIE ETPIAPNSPY AASKAAADLL VRAYYKTYKL AVNITRCSNN
     YGPYQFPEKL IPLMIANAYE NRELPVYGDG LQIRDWLHVK DHCRAIDLVL HKGKIGEVYN
     VGGNNEKANI YIVKFILEKL KKSETLIRYV EDRLGHDRRY AIDSSKIQNE LGWKPKYDFE
     RGIEETINWY LDNKNWWKKL ISRSF
//
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