ACBC_ACTS5
ID ACBC_ACTS5 Reviewed; 398 AA.
AC Q9ZAE9; G8SLW1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=2-epi-5-epi-valiolone synthase {ECO:0000305};
DE Short=EEVS {ECO:0000305};
DE EC=4.2.3.152 {ECO:0000269|PubMed:10196166};
DE AltName: Full=C7-cyclitol synthase {ECO:0000303|PubMed:10196166};
DE AltName: Full=Sedoheptulose 7-phosphate cyclase {ECO:0000303|PubMed:10196166};
GN Name=acbC {ECO:0000303|PubMed:10196166}; OrderedLocusNames=ACPL_3680;
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Actinoplanes; unclassified Actinoplanes.
OX NCBI_TaxID=134676;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RX PubMed=10196166; DOI=10.1074/jbc.274.16.10889;
RA Stratmann A., Mahmud T., Lee S., Distler J., Floss H.G., Piepersberg W.;
RT "The AcbC protein from Actinoplanes species is a C7-cyclitol synthase
RT related to 3-dehydroquinate synthases and is involved in the biosynthesis
RT of the alpha-glucosidase inhibitor acarbose.";
RL J. Biol. Chem. 274:10889-10896(1999).
RN [2]
RP SEQUENCE REVISION.
RA Wehmeier U.F.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the cyclization of D-sedoheptulose 7-phosphate to
CC 2-epi-5-epi-valiolone. Does not use ido-heptulose 7-phosphate and 3-
CC deoxy-arabino-heptulosonate 7-phosphate. Involved in the biosynthesis
CC of the acarviose moiety of the alpha-glucosidase inhibitor acarbose.
CC {ECO:0000269|PubMed:10196166}.
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:0000269|PubMed:10196166};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:10196166};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:10196166};
CC Note=Divalent metal cation such as Co(2+).
CC {ECO:0000269|PubMed:10196166};
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily. EEVS
CC family. {ECO:0000305}.
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DR EMBL; Y18523; CAA77208.2; -; Genomic_DNA.
DR EMBL; CP003170; AEV84575.1; -; Genomic_DNA.
DR RefSeq; WP_014690647.1; NZ_LT827010.1.
DR AlphaFoldDB; Q9ZAE9; -.
DR SMR; Q9ZAE9; -.
DR STRING; 134676.ACPL_3680; -.
DR EnsemblBacteria; AEV84575; AEV84575; ACPL_3680.
DR KEGG; ase:ACPL_3680; -.
DR PATRIC; fig|134676.3.peg.3596; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_11; -.
DR OMA; INRAGIH; -.
DR OrthoDB; 1677032at2; -.
DR BRENDA; 4.2.3.152; 144.
DR Proteomes; UP000005440; 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 InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR035872; EEVS-like.
DR Pfam; PF01761; DHQ_synthase; 1.
PE 1: Evidence at protein level;
KW Cobalt; Lyase; Metal-binding; NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..398
FT /note="2-epi-5-epi-valiolone synthase"
FT /id="PRO_0000140826"
FT ACT_SITE 163
FT /evidence="ECO:0000250|UniProtKB:Q9S5E2"
FT BINDING 62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 93..96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 126..130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 150..151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 190..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 205
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 276
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT BINDING 292
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:H2K887"
FT CONFLICT 377..398
FT /note="AELQAAALMQHRLAEDALLLRA -> GRAAGRPR (in Ref. 1;
FT CAA77208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43747 MW; 5A276A973F7FBD17 CRC64;
MSGVETVGVH ADAHRDSWQV RAQKQITYEV RFRDDVFGLD STDLLEAGAD GAGSRRRFVV
VDSAVDALYG SRIREYFTHH GIDHSILVMR VGETVKDFDT AGRIVAAMDA FGLARRREPM
IVVGGGVLMD VAGLVASLYR RGTPFLRVPT TLVGLIDAGV GAKTGVNFNG HKNRLGTYAP
ADLTLLDRRF LATLDRRHLS NGLAEMLKIA LIKDAELFQL LERHGRVLIE ERFQGRTGTG
DRAAVRALRA ATHGMLEELG PNLWESRLER SVDYGHTFSP TIEMRALPAL LHGEAVCVDM
ALTTVLAYRR GLLDVAQRDR IFAVMTALGL PTWHPLLTPE VLEAALQDTV RHRDGWQRLP
LPVGIGGVTF VNDVTAAELQ AAALMQHRLA EDALLLRA
