GRA27_STRVN
ID GRA27_STRVN Reviewed; 443 AA.
AC Q9ZA32;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase {ECO:0000303|Ref.4};
DE EC=4.2.1.159 {ECO:0000269|Ref.4};
DE AltName: Full=2,3-dehydratase {ECO:0000303|Ref.4};
DE AltName: Full=Gra-orf27 protein {ECO:0000303|Ref.4};
GN Name=gra-orf27 {ECO:0000312|EMBL:CAA09648.1};
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:CAA09648.1};
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:CAA09648.1};
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].
RC STRAIN=Tu22 {ECO:0000312|EMBL:CAA09648.1};
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, AND PATHWAY.
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 removal of the hydroxyl group at position C-2 of the hexose ring of
CC dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose, and the oxidation of the
CC hydroxyl group at position C-3 to form a carbonyl functionality. The
CC product of the reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose,
CC is a highly unstable diketosugar, which spontaneously forms dTDP-3,4-
CC didehydro-2,6-dideoxy-alpha-D-glucose. {ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3,4-didehydro-
CC 2,6-dideoxy-alpha-D-glucose + H2O; Xref=Rhea:RHEA:47972,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57649, ChEBI:CHEBI:84540;
CC EC=4.2.1.159; Evidence={ECO:0000269|Ref.4};
CC -!- PATHWAY: Antibiotic biosynthesis; granaticin biosynthesis.
CC {ECO:0000305|Ref.4}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O52793}.
CC -!- MISCELLANEOUS: Two binding sites (pockets A and B) for the dTDP-sugar
CC ligands have been identified in each subunit. It seems that pocket A
CC represents the active site and pocket B is a vestige of the gene
CC duplication event. {ECO:0000250|UniProtKB:O52793}.
CC -!- SIMILARITY: Belongs to the hexose 2,3-dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AJ011500; CAA09648.1; -; Genomic_DNA.
DR PIR; T46532; T46532.
DR AlphaFoldDB; Q9ZA32; -.
DR SMR; Q9ZA32; -.
DR UniPathway; UPA00175; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.79.40; -; 2.
DR InterPro; IPR005212; EvaA-like.
DR InterPro; IPR038153; EvaA-like_sf.
DR Pfam; PF03559; Hexose_dehydrat; 2.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Lyase.
FT CHAIN 1..443
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-
FT dehydratase"
FT /id="PRO_0000444210"
FT REGION 118..122
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 1; pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 341..343
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 2; pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 346..347
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 2; pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT REGION 377..380
FT /note="dTDP-4-dehydro-6-deoxy-alpha-D-glucose 1; pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 35
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="1"
FT /note="from pocket A"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 157
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="2"
FT /note="from pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 260
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="2"
FT /note="from pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
FT BINDING 325
FT /ligand="dTDP-4-dehydro-6-deoxy-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57649"
FT /ligand_label="2"
FT /note="from pocket B"
FT /evidence="ECO:0000250|UniProtKB:O52793"
SQ SEQUENCE 443 AA; 49703 MW; 7A94BF8F45FEDBDA CRC64;
MRITDTAGFH AWFAERGAAH RYRITRTPLH DLEGWYTDPA SGDVRHRSGR FFSIEGLRYG
RQEPDGPAWT QPIIRQPETG VLGVLIKWFD GVPHLLMQAK MEPGNINTLQ VSPTVQATFS
NYTRVHHGSP VRYIDHFLTP GAGDRVHYDA LQSEQGSWFL GKRNRNIVVE TTGEIPVHED
FCWVPRPVMA ELLRVDNLVN MDSRTVLAGL PDDPGEGSVP RRAVEKPLHD TAALLHWFTG
AKVRHRPERT TIPLSRVGGW RRDDDRGEIV HETGRYFRII GVDVEADSRE VTSWSQPMLA
PVGRGVVAFV SKEIHGERHL LVQARAEAGT FDAVELGPTV QCNPGNLPDG APRPPYLDTV
LTARPEQVLF DTVHSEEGGR FYHAENRYLV LDGDDVPVDV PEDYTWMTVR QLTRAGRIGN
LVDVEARTLL ACVRTLPDHG ASR
