EVS_ACTMD
ID EVS_ACTMD Reviewed; 382 AA.
AC C6WFL3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=2-epi-valiolone synthase {ECO:0000303|PubMed:22741921};
DE Short=EVS {ECO:0000303|PubMed:22741921};
DE EC=4.2.3.155 {ECO:0000269|PubMed:22741921};
DE AltName: Full=Sedoheptulose 7-phosphate cyclase {ECO:0000303|PubMed:22741921};
GN OrderedLocusNames=Amir_2000 {ECO:0000312|EMBL:ACU35948.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Actinosynnema.
OX NCBI_TaxID=446462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL
RC B-12336 / IMRU 3971 / 101;
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL
RC B-12336 / IMRU 3971 / 101;
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 2-
CC epi-valiolone, which may serve as an alternative precursor for
CC aminocyclitol biosynthesis. {ECO:0000269|PubMed:22741921}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 7-phosphate = 2-epi-valiolone + phosphate;
CC Xref=Rhea:RHEA:49564, ChEBI:CHEBI:43474, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:131717; EC=4.2.3.155;
CC Evidence={ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:22741921};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:22741921};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22741921};
CC Note=Binds 1 divalent metal cation per subunit. Co(2+) is the preferred
CC cofactor. {ECO:0000269|PubMed:22741921};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=59.9 uM for sedoheptulose 7-phosphate
CC {ECO:0000269|PubMed:22741921};
CC Note=kcat is 2.0 min(-1). {ECO:0000269|PubMed:22741921};
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EVS
CC family. {ECO:0000305}.
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DR EMBL; CP001630; ACU35948.1; -; Genomic_DNA.
DR RefSeq; WP_015800837.1; NC_013093.1.
DR AlphaFoldDB; C6WFL3; -.
DR SMR; C6WFL3; -.
DR STRING; 446462.Amir_2000; -.
DR EnsemblBacteria; ACU35948; ACU35948; Amir_2000.
DR KEGG; ami:Amir_2000; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_2_11; -.
DR OMA; IKMAVCF; -.
DR OrthoDB; 1677032at2; -.
DR BioCyc; MetaCyc:MON-19685; -.
DR BRENDA; 4.2.3.155; 14507.
DR Proteomes; UP000002213; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR InterPro; IPR016037; DHQ_synth_AroB.
DR InterPro; IPR030963; DHQ_synth_fam.
DR InterPro; IPR030960; DHQS/DOIS.
DR Pfam; PF01761; DHQ_synthase; 1.
DR PIRSF; PIRSF001455; DHQ_synth; 1.
DR TIGRFAMs; TIGR01357; aroB; 1.
PE 1: Evidence at protein level;
KW Cobalt; Lyase; Metal-binding; NAD; Nucleotide-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..382
FT /note="2-epi-valiolone synthase"
FT /id="PRO_0000441283"
FT BINDING 92..95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 124..128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 148..149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 188..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q3M6C3"
SQ SEQUENCE 382 AA; 41009 MW; 2516C51670C278A8 CRC64;
MDSPAGYRIH DNIPLPGNLD QVDVHVTRDD DYRIHVLPDV DRAVDALLTE LDGRRAVVIT
DDVVADLHEG RVSAELAARG QLIGRTAIRA GEKSKSLTTA FELIDWLAEV NLARRDVVIA
LGGGVVVDTV GFVASAYMRG VPYVNMPTTL LAQVDAGIGG KVAVDHSEAK NLVGAFYQPK
AVISCLEHLR TLDTRQIRSG LAEVVKKAVI ASPELFDYIE ANADDLLACA SPAIDVLVHA
AGAIKTKLVG RDPYEIDLRR PLNFGHTTGH AVETVTNYGP VLHGEAVAFG MVVAVDVARA
RGLVVPEVAD RVTALIRRLG LPVALEELGA VPRVDDVVAA LLKIRQIRDG SLRFVLPVEL
GATVIAEDVT EEEVRAALVR LR
