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Database: UniProt
Entry: B6GCA7_9ACTN
LinkDB: B6GCA7_9ACTN
Original site: B6GCA7_9ACTN 
ID   B6GCA7_9ACTN            Unreviewed;       344 AA.
AC   B6GCA7;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-NOV-2023, entry version 58.
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   Name=rfbB {ECO:0000313|EMBL:EEA90075.1};
GN   ORFNames=COLSTE_01730 {ECO:0000313|EMBL:EEA90075.1};
OS   Collinsella stercoris DSM 13279.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90075.1, ECO:0000313|Proteomes:UP000003560};
RN   [1] {ECO:0000313|EMBL:EEA90075.1, ECO:0000313|Proteomes:UP000003560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90075.1,
RC   ECO:0000313|Proteomes:UP000003560};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEA90075.1, ECO:0000313|Proteomes:UP000003560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90075.1,
RC   ECO:0000313|Proteomes:UP000003560};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) 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:EEA90075.1}.
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DR   EMBL; ABXJ01000096; EEA90075.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6GCA7; -.
DR   STRING; 445975.COLSTE_01730; -.
DR   eggNOG; COG1088; Bacteria.
DR   HOGENOM; CLU_007383_1_14_11; -.
DR   Proteomes; UP000003560; 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:EEA90075.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003560}.
FT   DOMAIN          16..316
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   344 AA;  38861 MW;  1611727937678786 CRC64;
     MGEAMSNDIF EPRRIIVTGG CGFIGSNFVH HVVREHPGVR VTVLDKLTYA GNPENIAGLP
     SDRVELVVGD ICDAALVDRL VSETDAVVHY AAESHNDNSI ADPSPFLETN VRGTYTLIEA
     CRKYGVRYHH VSTDEVYGDL ALDDPARFTE ETPYRPSSPY SSTKAASDML VRAWARTFGL
     KATISNCSNN YGPYQHVEKF IPRQVTNLID GARPRLYGDG RNVRDWIHTE DHSSAVWAIL
     TRGRVGETYL VGADGERDNI TVLREILRAF GRPEDDFDWV RDRPGHDRRY AIDATKLRRE
     LGWEPAHTDF AAGLAETIRW YRDNEPWWRP AKEATEARYR AQGQ
//
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