GRA26_STRVN
ID GRA26_STRVN Reviewed; 342 AA.
AC Q9ZA33;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-reductase {ECO:0000303|Ref.4};
DE EC=1.1.1.384 {ECO:0000269|Ref.4};
DE AltName: Full=Gra-orf26 protein {ECO:0000303|Ref.4};
DE AltName: Full=dTDP-3,4-diketo-2,6-dideoxyglucose 3-ketoreductase {ECO:0000305};
GN Name=gra-orf26 {ECO:0000312|EMBL:CAA09647.1};
OS Streptomyces violaceoruber.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1935;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tu22 {ECO:0000312|EMBL:CAA09647.1};
RX PubMed=2583128; DOI=10.1002/j.1460-2075.1989.tb08413.x;
RA Sherman D.H., Malpartida F., Bibb M.J., Kieser H.M., Bibb M.J.,
RA Hopwood D.A.;
RT "Structure and deduced function of the granaticin-producing polyketide
RT synthase gene cluster of Streptomyces violaceoruber Tu22.";
RL EMBO J. 8:2717-2725(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tu22 {ECO:0000312|EMBL:CAA09647.1};
RX PubMed=7476861; DOI=10.1007/bf02423457;
RA Bechthold A., Sohng J.K., Smith T.M., Chu X., Floss H.G.;
RT "Identification of Streptomyces violaceoruber Tu22 genes involved in the
RT biosynthesis of granaticin.";
RL Mol. Gen. Genet. 248:610-620(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=Tu22 {ECO:0000312|EMBL:CAA09647.1};
RX PubMed=9831526; DOI=10.1016/s1074-5521(98)90292-7;
RA Ichinose K., Bedford D.J., Tornus D., Bechthold A., Bibb M.J., Revill W.P.,
RA Floss H.G., Hopwood D.A.;
RT "The granaticin biosynthetic gene cluster of Streptomyces violaceoruber
RT Tu22: sequence analysis and expression in a heterologous host.";
RL Chem. Biol. 5:647-659(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=Tu22;
RA Draeger G., Park S.-H.H., Floss H.G.;
RT "Mechanism of the 2-deoxygenation step in the biosynthesis of the
RT deoxyhexose moieties of the antibiotics granaticin and oleandomycin.";
RL J. Am. Chem. Soc. 121:2611-2612(1999).
CC -!- FUNCTION: Involved in the biosynthesis of the 2,6-deoxysugar, dTDP-L-
CC rhodinose, attached to the benzoisochromane quinone chromophore to
CC produce the aglycone antibiotics granaticin and granaticin B. Catalyzes
CC the reduction of the C-3 keto moiety of dTDP-3,4-diketo-2,6-dideoxy-
CC alpha-D-glucose to yield dTDP-4-keto-2,6-dideoxy-alpha-D-glucose. NADPH
CC is the better reductant, however NADH can also be used.
CC {ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-
CC 3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH;
CC Xref=Rhea:RHEA:44624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:84537, ChEBI:CHEBI:84540;
CC EC=1.1.1.384; Evidence={ECO:0000269|Ref.4};
CC -!- PATHWAY: Antibiotic biosynthesis; granaticin biosynthesis.
CC {ECO:0000305|PubMed:9831526, ECO:0000305|Ref.4}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. {ECO:0000305}.
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DR EMBL; AJ011500; CAA09647.1; -; Genomic_DNA.
DR PIR; T46531; T46531.
DR AlphaFoldDB; Q9ZA33; -.
DR SMR; Q9ZA33; -.
DR UniPathway; UPA00175; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..342
FT /note="dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose 3-
FT reductase"
FT /id="PRO_5004337355"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 19..25
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 44..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 184
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B3TMR8"
SQ SEQUENCE 342 AA; 36109 MW; 54E5D05EB3269440 CRC64;
MNAGHTETVR ALRIGVAGCA DIALRRMLPA FAASPHTEPT AVASRSSEKA RAAAETFGCA
AVEGYDALLE RRDVDAVYIP LPVALHAPWT ERALRAGKHV LAEKPLTARA ADTARLLDLA
RERGLVLAEN YLFVHHSAYT AVRDLVDAGA IGDVRALSAS FTIPPRSADD IRYRADLDGG
ALLDIGVYPL RLASLLLGSE LRVRGAVLRH DTVRGVDLGG SALLGDPGTG VSAQLVFGME
HAYTAGWRLL GSEGSLTLDR AYSPPAGHRP VLRIERPDGT EERILPAHDQ ATAAVAAFAE
AVRRAGQGAG QDKGRSSGDA AAVLRQAELV DAVRQAAHLV KI
