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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
 
 
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