RMLB_ACTS5
ID RMLB_ACTS5 Reviewed; 320 AA.
AC Q9ZAE8; G8SLW2;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000303|PubMed:10196166};
DE EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN Name=acbB {ECO:0000303|PubMed:10196166}; OrderedLocusNames=ACPL_3681;
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Actinoplanes; unclassified Actinoplanes.
OX NCBI_TaxID=134676;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RX PubMed=10196166; DOI=10.1074/jbc.274.16.10889;
RA Stratmann A., Mahmud T., Lee S., Distler J., Floss H.G., Piepersberg W.;
RT "The AcbC protein from Actinoplanes species is a C7-cyclitol synthase
RT related to 3-dehydroquinate synthases and is involved in the biosynthesis
RT of the alpha-glucosidase inhibitor acarbose.";
RL J. Biol. Chem. 274:10889-10896(1999).
RN [2]
RP SEQUENCE REVISION.
RA Wehmeier U.F.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably involved in the biosynthesis of the acarviose moiety
CC of the alpha-glucosidase inhibitor acarbose (PubMed:10196166).
CC Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-
CC xylo-4-hexulose via a three-step process involving oxidation,
CC dehydration and reduction (By similarity).
CC {ECO:0000250|UniProtKB:P27830, ECO:0000269|PubMed:10196166}.
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:0000250|UniProtKB:P27830};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P27830};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P27830};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27830}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; Y18523; CAA77209.2; -; Genomic_DNA.
DR EMBL; CP003170; AEV84576.1; -; Genomic_DNA.
DR RefSeq; WP_014690648.1; NZ_LT827010.1.
DR AlphaFoldDB; Q9ZAE8; -.
DR SMR; Q9ZAE8; -.
DR STRING; 134676.ACPL_3681; -.
DR EnsemblBacteria; AEV84576; AEV84576; ACPL_3681.
DR KEGG; ase:ACPL_3681; -.
DR PATRIC; fig|134676.3.peg.3597; -.
DR eggNOG; COG1088; Bacteria.
DR HOGENOM; CLU_007383_1_14_11; -.
DR OMA; LDNKQWW; -.
DR OrthoDB; 707977at2; -.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 3: Inferred from homology;
KW Lyase; NAD; Reference proteome.
FT CHAIN 1..320
FT /note="dTDP-glucose 4,6-dehydratase"
FT /id="PRO_0000183249"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 38..41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 64..65
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 84..88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 152..156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P27830"
FT BINDING 191..192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
FT BINDING 274..278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26391"
SQ SEQUENCE 320 AA; 34671 MW; 233B8552C4B6283B CRC64;
MKILVTGGAG FIGSHFVTSL ISGDIATPQP VTQVTVVDKL GYGGNLRNLA EASADPRFSF
VRGDICDEGL IEGLMARHDT VAHFAAETHV DRSVVASGPF VASNLVGTQV LLDAALRHHI
GRFLHVSTDE VYGSIDTGSW AEGHPLAPNS PYAASKAGSD LLALAYHQTH GMDVVVTRCS
NNYGPRQFPE KMIPLFVTRL LDGLDVPVYG DGRNIRDWLH VSDHCRGLAL ALGAGRAGEV
YHIGGGWEAT NLELTEILLE ACGAPASRIS FVTDRKGHDR RYSLDYSKIA GELGYRPRVD
FTDGIAETVA WYRANRSWWT