GERKI_STRSQ
ID GERKI_STRSQ Reviewed; 326 AA.
AC Q331Q7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=dTDP-4-dehydro-6-deoxy-D-allose reductase {ECO:0000305|PubMed:17053005};
DE EC=1.1.1.364 {ECO:0000269|PubMed:17053005};
DE AltName: Full=dTDP-4-dehydro-6-deoxy-alpha-D-gulose 4-ketoreductase {ECO:0000305};
DE AltName: Full=dTDP-4-keto-6-deoxy-D-hexose reductase GerKI {ECO:0000303|PubMed:17053005};
DE AltName: Full=dTDP-4-keto-6-deoxyallose reductase {ECO:0000303|PubMed:17053005};
GN Name=gerKI; Synonyms=gerK1;
OS Streptomyces sp.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KCTC 0041BP / GERI-155;
RA Jaishy B.P., Lim S.K., Yoo I.D., Yoo J.C., Sohng J.K., Nam D.H.;
RT "Cloning and characterization of a gene cluster for the production of the
RT polyketide macrolide antibiotic dihydrochalcomycin in Streptomyces sp. KCTC
RT 0041BP.";
RL J. Microbiol. Biotechnol. 16:764-770(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=KCTC 0041BP / GERI-155;
RX PubMed=17053005; DOI=10.1093/glycob/cwl060;
RA Thuy T.T., Liou K., Oh T.J., Kim D.H., Nam D.H., Yoo J.C., Sohng J.K.;
RT "Biosynthesis of dTDP-6-deoxy-beta-D-allose, biochemical characterization
RT of dTDP-4-keto-6-deoxyglucose reductase (GerKI) from Streptomyces sp. KCTC
RT 0041BP.";
RL Glycobiology 17:119-126(2007).
CC -!- FUNCTION: Catalyzes the stereospecific reduction of the C-4 keto group
CC of dTDP-4-dehydro-6-deoxy-D-allose, leading to dTDP-6-deoxy-D-allose,
CC an intermediate in the biosynthesis of the mycinose moiety of
CC dihydrochalcomycin (GERI-155) antibiotic. Cannot directly reduce dTDP-
CC 4-dehydro-6-deoxyglucose, and thus acts after the epimerization step
CC catalyzed by GerF. {ECO:0000269|PubMed:17053005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-6-deoxy-alpha-D-allose + NAD(+) = dTDP-4-dehydro-6-deoxy-
CC alpha-D-allose + H(+) + NADH; Xref=Rhea:RHEA:36679,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:74143, ChEBI:CHEBI:76253; EC=1.1.1.364;
CC Evidence={ECO:0000269|PubMed:17053005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-6-deoxy-alpha-D-allose + NADP(+) = dTDP-4-dehydro-6-
CC deoxy-alpha-D-allose + H(+) + NADPH; Xref=Rhea:RHEA:39883,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:74143, ChEBI:CHEBI:76253; EC=1.1.1.364;
CC Evidence={ECO:0000269|PubMed:17053005};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
CC -!- CAUTION: Although PubMed:17053005 refers to the biosynthesis of dTDP-6-
CC deoxy-beta-D-allose, it seems it is the alpha anomer which is produced
CC by GerKI and involved in dihydrochalcomycin biosynthesis, as shown by
CC the NMR analysis of this compound made in the same article.
CC {ECO:0000305}.
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DR EMBL; AY118081; ABB52541.1; -; Genomic_DNA.
DR AlphaFoldDB; Q331Q7; -.
DR SMR; Q331Q7; -.
DR KEGG; ag:ABB52541; -.
DR BioCyc; MetaCyc:MON-18348; -.
DR BRENDA; 1.1.1.364; 1284.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Carbohydrate metabolism; NAD; Oxidoreductase.
FT CHAIN 1..326
FT /note="dTDP-4-dehydro-6-deoxy-D-allose reductase"
FT /id="PRO_0000419114"
FT ACT_SITE 160
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 15..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 187..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 36261 MW; A064C144941BED78 CRC64;
MTADRWAGRT VLVTGALGFI GSHFVRQLDA RGAEVLALYR TERPEIQAEL AALNRVRLVR
TELRDESDVR GAFKYLAPSI DTVVHCAAMD GNAQFKLERS AEILDSNQRT ISNLLNCVRD
FGVGEVVVMS SSELYSASPT VAAREEDDFR RSMRYTDNGY VLSKTYGEIL ARLHREQFGT
NVFLVRPGNV YGPGDGFDCS RGRVIPSMLA KADAGEEIEI WGDGSQTRSF VHVADLVRAS
LRLLETGKYP EMNVAGAEQV SILELAGMVM AVLGRPERIR LDPSRPVGAP SRLLDLSRMS
EVIDFDPQPL RAGLEETARW YRLHKR
