ID I4BCH0_MYCCN Unreviewed; 405 AA.
AC I4BCH0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000256|ARBA:ARBA00024092};
DE EC=4.2.3.152 {ECO:0000256|ARBA:ARBA00024060};
DE Flags: Precursor;
GN OrderedLocusNames=Mycch_0151 {ECO:0000313|EMBL:AFM14977.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM14977.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM14977.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM14977.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-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};
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DR EMBL; CP003053; AFM14977.1; -; Genomic_DNA.
DR RefSeq; WP_014813469.1; NC_018027.1.
DR AlphaFoldDB; I4BCH0; -.
DR STRING; 710421.Mycch_0151; -.
DR KEGG; mcb:Mycch_0151; -.
DR PATRIC; fig|710421.3.peg.143; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_11; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000006057; 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 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, ECO:0000313|EMBL:AFM14977.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057}.
FT DOMAIN 84..338
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 405 AA; 44496 MW; BFFF62C6496C3253 CRC64;
MSQLTARVTA GDRNFHVEGY ERIEYDLTYV DGVFDIDNTE LADAYRPYGR ALMVVDEVVY
DLYRDSVDAY FAHHGIDLSV IGVHIHETAK SLETFERIVT AFDDFGLVRT EPVLVVGGGL
TTDVAGFACA GYRRNTPYIR IPTTLIGLID ASVSIKVAVN HGKHKNRLGA YHASQQVFLD
FSFLKTLPED QIRNGMAELI KISVVGNAEI FDMLERFGPE LLSTRFGHLG GSERLRAAAH
RLTYEAIATM LELEAPNLHE IDLDRVIAFG HTWSPTLELT PPTPFFHGHA ISIDMALSVT
LAERRGLLTA GGRDRVLAAM SALGLALDSE YLTPELLTHA TAAILRTRDG LLRAAVPDPI
GTCRFLNDVT VDELADTLTL HKKLCAEYDR GGDGIDAFTA EAVHG
//
