ID L8DMF2_9NOCA Unreviewed; 403 AA.
AC L8DMF2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000256|ARBA:ARBA00024092};
DE EC=4.2.3.152 {ECO:0000256|ARBA:ARBA00024060};
GN ORFNames=RHODMAR_4539 {ECO:0000313|EMBL:CCQ17926.1};
OS Rhodococcus sp. AW25M09.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1268303 {ECO:0000313|EMBL:CCQ17926.1, ECO:0000313|Proteomes:UP000011207};
RN [1] {ECO:0000313|EMBL:CCQ17926.1, ECO:0000313|Proteomes:UP000011207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AW25M09 {ECO:0000313|EMBL:CCQ17926.1,
RC ECO:0000313|Proteomes:UP000011207};
RA Hjerde E., Pierechod M.M., Williamson A.K., Bjerga G., Willassen N.P.,
RA Smalaas A.O., Altermark B.;
RT "Draft genome sequence of Rhodococcus sp. AW25M09. An Actinomycete isolated
RT from Atlantic Hagfish caught in Hadselfjorden, North- Norway.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 7-phosphate = 2-epi-5-epi-valiolone +
CC phosphate; Xref=Rhea:RHEA:44184, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57483, ChEBI:CHEBI:84187; EC=4.2.3.152;
CC Evidence={ECO:0000256|ARBA:ARBA00023993};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCQ17926.1}.
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DR EMBL; CAPS01000123; CCQ17926.1; -; Genomic_DNA.
DR RefSeq; WP_008719709.1; NZ_CAPS01000123.1.
DR AlphaFoldDB; L8DMF2; -.
DR STRING; 1268303.RHODMAR_4539; -.
DR eggNOG; COG0337; Bacteria.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000011207; Unassembled WGS sequence.
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 Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR035872; EEVS-like.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 83..339
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 403 AA; 44471 MW; 87EE51391E1DECD6 CRC64;
MSNLQAQVVA GDRSFRVEGY ERIEYDLLYV DGVFEPENTE LADSYRPYGR ALMVVDESVH
QIYGDRIKAY FDHHDLALTV VPVQIRETAK SLETFERIVG EFDAFGLVRT EPVLVVGGGL
TTDVAGFACA SYRRNTPYIR IPTTLIGLID ASVSIKVAVN YGKHKNRLGA YHASQKVLLD
FSFLGTLPED QVRNGMAELI KISVVGNLEI FELLEQYGPE LLRTRFGHLD GTPELRSVAD
RLTYSAIATM LELEAPNLHE IDLDRVIAFG HTWSPTLELT PPAPFFHGHA INIDMALSTT
VAEQRGHLST ADRDRVLGVM SSIGLALDSP YLTPELLSEA TASILKTRDG ILRAAVPDPI
GTCRFLNDLD VGELADVLTL HKKICLDFPR AGEGLDMFTA PTP
//
