DDGS_TRIV2
ID DDGS_TRIV2 Reviewed; 410 AA.
AC Q3M6C3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Demethyl-4-deoxygadusol synthase {ECO:0000305};
DE Short=DDGS {ECO:0000303|PubMed:22741921};
DE EC=4.2.3.154 {ECO:0000269|PubMed:22741921};
GN OrderedLocusNames=Ava_3858 {ECO:0000312|EMBL:ABA23463.1};
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22741921; DOI=10.1021/ja3041866;
RA Asamizu S., Xie P., Brumsted C.J., Flatt P.M., Mahmud T.;
RT "Evolutionary divergence of sedoheptulose 7-phosphate cyclases leads to
RT several distinct cyclic products.";
RL J. Am. Chem. Soc. 134:12219-12229(2012).
RN [3] {ECO:0007744|PDB:5TPR}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC,
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLU-254; ALA-268 AND THR-347.
RX PubMed=28182402; DOI=10.1021/acschembio.7b00066;
RA Osborn A.R., Kean K.M., Alseud K.M., Almabruk K.H., Asamizu S., Lee J.A.,
RA Karplus P.A., Mahmud T.;
RT "Evolution and distribution of C7-cyclitol synthases in prokaryotes and
RT eukaryotes.";
RL ACS Chem. Biol. 12:979-988(2017).
CC -!- FUNCTION: Catalyzes the conversion of sedoheptulose 7-phosphate to
CC demethyl-4-deoxygadusol (DDG) (PubMed:22741921). Involved in the
CC synthesis of the mycosporine-like amino acid shinorine, a natural
CC sunscreen compound that protects the cell against UV radiation (By
CC similarity). {ECO:0000250|UniProtKB:B2J6X9,
CC ECO:0000269|PubMed:22741921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 7-phosphate = (R)-demethyl-4-deoxygadusol +
CC H(+) + H2O + phosphate; Xref=Rhea:RHEA:49560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:132139; EC=4.2.3.154;
CC Evidence={ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:22741921, ECO:0000269|PubMed:28182402};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:22741921};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:28182402};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.6 uM for sedoheptulose 7-phosphate
CC {ECO:0000269|PubMed:22741921};
CC Note=kcat is 3.2 min(-1). {ECO:0000269|PubMed:22741921};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28182402}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DDGS
CC family. {ECO:0000305}.
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DR EMBL; CP000117; ABA23463.1; -; Genomic_DNA.
DR PDB; 5TPR; X-ray; 1.70 A; A/B=1-410.
DR PDBsum; 5TPR; -.
DR AlphaFoldDB; Q3M6C3; -.
DR SMR; Q3M6C3; -.
DR STRING; 240292.Ava_3858; -.
DR DNASU; 3678498; -.
DR EnsemblBacteria; ABA23463; ABA23463; Ava_3858.
DR KEGG; ava:Ava_3858; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_3; -.
DR OMA; HAVNIDM; -.
DR BRENDA; 4.2.3.154; 322.
DR Proteomes; UP000002533; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd08199; EEVS; 1.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR035872; EEVS-like.
DR Pfam; PF01761; DHQ_synthase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalt; Lyase; Metal-binding; NAD; Nucleotide-binding; Zinc.
FT CHAIN 1..410
FT /note="Demethyl-4-deoxygadusol synthase"
FT /id="PRO_0000441281"
FT BINDING 56..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 87..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 119..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 143..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 183..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:28182402"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28182402,
FT ECO:0007744|PDB:5TPR"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28182402,
FT ECO:0007744|PDB:5TPR"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28182402,
FT ECO:0007744|PDB:5TPR"
FT MUTAGEN 254
FT /note="E->L: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28182402"
FT MUTAGEN 268
FT /note="A->D: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28182402"
FT MUTAGEN 347
FT /note="T->H: No change in activity."
FT /evidence="ECO:0000269|PubMed:28182402"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 12..29
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:5TPR"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:5TPR"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:5TPR"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 233..254
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 287..304
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 334..347
FT /evidence="ECO:0007829|PDB:5TPR"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:5TPR"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 371..385
FT /evidence="ECO:0007829|PDB:5TPR"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:5TPR"
SQ SEQUENCE 410 AA; 46172 MW; 38765FE96EDD2174 CRC64;
MSIVQAKFEA KETSFHVEGY EKIEYDLVYV DGIFEIQNSA LADVYQGFGR CLAIVDANVS
RLYGNQIQAY FQYYGIELRL FPITITEPDK TIQTFERVID VFADFKLVRK EPVLVVGGGL
ITDVVGFACS TYRRSSNYIR IPTTLIGLID ASVAIKVAVN HRKLKNRLGA YHASRKVFLD
FSLLRTLPTD QVRNGMAELV KIAVVAHQEV FELLEKYGEE LLRTHFGNID ATPEIKEIAH
RLTYKAIHKM LELEVPNLHE LDLDRVIAYG HTWSPTLELA PRLPMFHGHA VNVDMAFSAT
IAARRGYITI AERDRILGLM SRVGLSLDHP MLDIDILWRG TESITLTRDG LLRAAMPKPI
GDCVFVNDLT REELAAALAD HKELCTSYPR GGEGVDVYPV YQKELIGSVK
