DDGS_NOSP7
ID DDGS_NOSP7 Reviewed; 410 AA.
AC B2J6X9;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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:20813918, ECO:0000269|PubMed:22741921};
GN OrderedLocusNames=Npun_R5600 {ECO:0000312|EMBL:ACC83905.1};
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 29133 / PCC 73102;
RX PubMed=20813918; DOI=10.1126/science.1193637;
RA Balskus E.P., Walsh C.T.;
RT "The genetic and molecular basis for sunscreen biosynthesis in
RT cyanobacteria.";
RL Science 329:1653-1656(2010).
RN [3]
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).
CC -!- FUNCTION: Catalyzes the conversion of sedoheptulose 7-phosphate to
CC demethyl-4-deoxygadusol (DDG) (PubMed:20813918, PubMed:22741921).
CC Involved in the synthesis of the mycosporine-like amino acid shinorine,
CC a natural sunscreen compound that protects the cell against UV
CC radiation (PubMed:20813918). {ECO:0000269|PubMed:20813918,
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:20813918, ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:20813918, ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:20813918, ECO:0000269|PubMed:22741921};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q3M6C3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.9 uM for sedoheptulose 7-phosphate
CC {ECO:0000269|PubMed:20813918};
CC KM=65.1 uM for sedoheptulose 7-phosphate
CC {ECO:0000269|PubMed:22741921};
CC Note=kcat is 5.0 min(-1). {ECO:0000269|PubMed:22741921};
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. DDGS
CC family. {ECO:0000305}.
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DR EMBL; CP001037; ACC83905.1; -; Genomic_DNA.
DR RefSeq; WP_012411849.1; NC_010628.1.
DR AlphaFoldDB; B2J6X9; -.
DR SMR; B2J6X9; -.
DR STRING; 63737.Npun_R5600; -.
DR EnsemblBacteria; ACC83905; ACC83905; Npun_R5600.
DR KEGG; npu:Npun_R5600; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_3; -.
DR OMA; HAVNIDM; -.
DR OrthoDB; 1677032at2; -.
DR PhylomeDB; B2J6X9; -.
DR BioCyc; MetaCyc:MON-19680; -.
DR Proteomes; UP000001191; 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 Cobalt; Lyase; Metal-binding; NAD; Nucleotide-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..410
FT /note="Demethyl-4-deoxygadusol synthase"
FT /id="PRO_0000441282"
FT BINDING 56..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 87..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 119..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 143..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 183..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
SQ SEQUENCE 410 AA; 45646 MW; F0C21D669DE8C8B5 CRC64;
MSNVQASFEA TEAEFRVEGY EKIEFSLVYV NGAFDISNRE IADSYEKFGR CLTVIDANVN
RLYGKQIKSY FRHYGIDLTV VPIVITEPTK TLATFEKIVD AFSDFGLIRK EPVLVVGGGL
TTDVAGFACA AYRRKSNYIR VPTTLIGLID AGVAIKVAVN HRKLKNRLGA YHAPLKVILD
FSFLQTLPTA QVRNGMAELV KIAVVANSEV FELLYEYGEE LLSTHFGYVN GTKELKAIAH
KLNYEAIKTM LELETPNLHE LDLDRVIAYG HTWSPTLELA PMIPLFHGHA VNIDMALSAT
IAARRGYITS GERDRILSLM SRIGLSIDHP LLDGDLLWYA TQSISLTRDG KQRAAMPKPI
GECFFVNDFT REELDAALAE HKRLCATYPR GGDGIDAYIE TQEESKLLGV
