ID U0EA39_9NOCA Unreviewed; 411 AA.
AC U0EA39;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=N806_02285 {ECO:0000313|EMBL:ERB50021.1};
OS Rhodococcus sp. P27.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1384060 {ECO:0000313|EMBL:ERB50021.1, ECO:0000313|Proteomes:UP000016008};
RN [1] {ECO:0000313|EMBL:ERB50021.1, ECO:0000313|Proteomes:UP000016008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P27 {ECO:0000313|EMBL:ERB50021.1,
RC ECO:0000313|Proteomes:UP000016008};
RX PubMed=24072865;
RA Gouvea Taketani R., Domingues Zucchi T., Soares de Melo I., Mendes R.;
RT "Whole-Genome Shotgun Sequencing of Rhodococcus erythropolis Strain P27, a
RT Highly Radiation-Resistant Actinomycete from Antarctica.";
RL Genome Announc. 1:e00763-13(2013).
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:ERB50021.1}.
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DR EMBL; AVCO01000054; ERB50021.1; -; Genomic_DNA.
DR AlphaFoldDB; U0EA39; -.
DR PATRIC; fig|1384060.5.peg.6123; -.
DR Proteomes; UP000016008; 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 94..346
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 411 AA; 44974 MW; 0DFA893DDF2A42E5 CRC64;
MRSAASFKLG LSHSAATDST WKVEAVKQVE YHVIAARNLF AKDSTRLLDG CSAASLHRGD
RRLIIIDANV DRIHGDRIRG YFEHHGIRAS FVPMRADETV KEWGSAVRVV DAMNGFGIDR
RREPVIAIGG GVLLDIVGFA ASVYRRGTPY IRVPTTLIGL VDAGVGVKTG VNYGMGKNRL
GTYAPALATF VDRAFLRTLD NRHLSNGLAE ILKMALIKSL DLFELLEIFG ERLIDDRFQG
SSDELDTAAT QVIAESIHLM LEELQPNLWE SCLERCVDYG HTFSPTLEME ALPELLHGEA
VAVDMALTSA LGYLRGSISE AELDRVLTVM RRLGLPTWND VLSTPGVLGA ALADTVRHRD
GRQRLPLPVG IGGHHFVNDV TIDGINSASA LLNRKSDELR VRETSVTKVA S
//
