ID A0A177YGV5_9NOCA Unreviewed; 403 AA.
AC A0A177YGV5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=A3K89_04845 {ECO:0000313|EMBL:OAK54671.1};
OS Rhodococcus kyotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK54671.1, ECO:0000313|Proteomes:UP000077519};
RN [1] {ECO:0000313|EMBL:OAK54671.1, ECO:0000313|Proteomes:UP000077519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB10 {ECO:0000313|EMBL:OAK54671.1,
RC ECO:0000313|Proteomes:UP000077519};
RA Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT "Genome sequence of Rhodococcus kyotonensis KB10.";
RL Submitted (MAR-2016) 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:OAK54671.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LVHI01000012; OAK54671.1; -; Genomic_DNA.
DR RefSeq; WP_068425280.1; NZ_LVHI01000012.1.
DR AlphaFoldDB; A0A177YGV5; -.
DR Proteomes; UP000077519; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077519}.
FT DOMAIN 83..339
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 403 AA; 44214 MW; D73DDDD579057844 CRC64;
MSNMQAQVTA TDRAFHVEGY ERIEYDLLYV DGVFDVANPE LAESYRQYGR CLMVVDETVH
ALYGDRARAY FDHYEIALTV VPVTIAETAK SLETFERIVG EFDAFGLVRT EPVLVVGGGL
TTDVAGFACA SYRRNTPYIR IPTTLIGLID ASVSIKVAVN YGKHKNRLGA YHASQKVLLD
FSFLATLPED QIRNGMAELI KISVVGNSAI FDMLDQHGAE LLSTKFGHSG GTPELRAVAD
RLTYQAIETM LELEAPNLHE IELDRVIAFG HTWSPTLELT PPAPFFHGHA INIDMALSTT
VAEQRGLIST SERDRILGVM SRLGLALDSD HLTPELLADA TASILRTRDG ILRAAVPDPI
GSCRFLNDLT TEELSDALAL HKKICLEFDR GGAGIDMFTG AHT
//
