ID   ACBO_ACTS5              Reviewed;         270 AA.
AC   Q8RMD1;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=2-epi-5-epi-valiolone 7-phosphate 2-epimerase {ECO:0000303|PubMed:12681481};
DE            EC=5.1.3.35 {ECO:0000269|PubMed:12681481};
GN   Name=acbO; OrderedLocusNames=ACPL_3679;
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].
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RX   PubMed=12681481; DOI=10.1016/s0014-5793(03)00221-7;
RA   Zhang C.S., Podeschwa M., Altenbach H.J., Piepersberg W., Wehmeier U.F.;
RT   "The acarbose-biosynthetic enzyme AcbO from Actinoplanes sp. SE 50/110 is a
RT   2-epi-5-epi-valiolone-7-phosphate 2-epimerase.";
RL   FEBS Lett. 540:47-52(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RA   Wehmeier U.F.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: Involved in the biosynthesis of the alpha-glucosidase
CC       inhibitor acarbose. Catalyzes the 2-epimerisation of 2-epi-5-
CC       epivaliolone 7-phosphate to yield 5-epi-valiolone 7-phosphate.
CC       {ECO:0000269|PubMed:12681481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-epi-5-epi-valiolone 7-phosphate = 5-epi-valiolone 7-
CC         phosphate; Xref=Rhea:RHEA:46932, ChEBI:CHEBI:84362,
CC         ChEBI:CHEBI:87125; EC=5.1.3.35;
CC         Evidence={ECO:0000269|PubMed:12681481};
CC   -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR   EMBL; Y18523; CAD29485.2; -; Genomic_DNA.
DR   EMBL; CP003170; AEV84574.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RMD1; -.
DR   SMR; Q8RMD1; -.
DR   STRING; 134676.ACPL_3679; -.
DR   EnsemblBacteria; AEV84574; AEV84574; ACPL_3679.
DR   KEGG; ase:ACPL_3679; -.
DR   PATRIC; fig|134676.3.peg.3595; -.
DR   eggNOG; COG1082; Bacteria.
DR   HOGENOM; CLU_1064864_0_0_11; -.
DR   OMA; IGACDWS; -.
DR   BRENDA; 5.1.3.35; 144.
DR   Proteomes; UP000005440; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..270
FT                   /note="2-epi-5-epi-valiolone 7-phosphate 2-epimerase"
FT                   /id="PRO_0000435305"
FT   ACT_SITE        143
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT   ACT_SITE        236
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WYP7"
SQ   SEQUENCE   270 AA;  28458 MW;  EB8CD131D4B9F476 CRC64;
     MTCRVGLTEW RLAPSGAAAI RLAAAVGADG IQLDFGGPGR GVLVDGPGRA GQLRAVADEA
     GVDLLALAGN LLNDIGLTSQ PAVVQPVLAR LADTATELGV PLLIVPSFRR SAITDAMSFT
     RTAAALRWAV SLAEARGIVL ASENVLPPAR ARQLVEEVGS PAFRLLLDTF NPVRYGLDPA
     WLATELRPWW ADQIHLKDGP PDTGPSPLLG AGQGGVRRTL TALRGSPAPV RALVLENDYR
     DGHGARLRAD LEWARRAAVN ARESEKGKLT