ACBM_ACTS5
ID ACBM_ACTS5 Reviewed; 359 AA.
AC Q8RIS8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=2-epi-5-epi-valiolone 7-kinase {ECO:0000305};
DE EC=2.7.1.188 {ECO:0000269|PubMed:11937512};
GN Name=acbM {ECO:0000303|PubMed:11937512};
GN OrderedLocusNames=ACPL_3676 {ECO:0000312|EMBL:AEV84571.1};
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, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110;
RX PubMed=11937512; DOI=10.1074/jbc.m202375200;
RA Zhang C.S., Stratmann A., Block O., Bruckner R., Podeschwa M.,
RA Altenbach H.J., Wehmeier U.F., Piepersberg W.;
RT "Biosynthesis of the C(7)-cyclitol moiety of acarbose in Actinoplanes
RT species SE50/110. 7-O-phosphorylation of the initial cyclitol precursor
RT leads to proposal of a new biosynthetic pathway.";
RL J. Biol. Chem. 277:22853-22862(2002).
RN [2]
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 conversion of 2-epi-5-epi-valiolone to 2-epi-5-
CC epi-valiolone 7-phosphate. Involved in the biosynthesis of the
CC acarviose moiety of the alpha-glucosidase inhibitor acarbose.
CC {ECO:0000269|PubMed:11937512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-epi-5-epi-valiolone + ATP = 2-epi-5-epi-valiolone 7-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:44364, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:84187, ChEBI:CHEBI:84362,
CC ChEBI:CHEBI:456216; EC=2.7.1.188;
CC Evidence={ECO:0000269|PubMed:11937512};
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; Y18523; CAD29482.2; -; Genomic_DNA.
DR EMBL; CP003170; AEV84571.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RIS8; -.
DR SMR; Q8RIS8; -.
DR STRING; 134676.ACPL_3676; -.
DR EnsemblBacteria; AEV84571; AEV84571; ACPL_3676.
DR KEGG; ase:ACPL_3676; -.
DR PATRIC; fig|134676.3.peg.3592; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_075306_0_0_11; -.
DR OMA; GLMCECG; -.
DR BRENDA; 2.7.1.188; 144.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW Kinase; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="2-epi-5-epi-valiolone 7-kinase"
FT /id="PRO_0000435391"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 36943 MW; 32708FB0692EA1F0 CRC64;
MKRPPHHPVT VADVGGTHLR WARWSPDGGL GEVHTTPSPG HARRPGAGAA DLQAELIREL
ASRVEPGARA GVSLGAAMDH HSGTAYASAP LWGPQVSPFD VPAALRAARP DVHWTVVNDV
TAGLLHLAEM VRDAGVRKAC LVTISTGIAC RTMDLRTGGI PVDAAGLQGE IGHLPATVLA
DGVPVVTRCD CGEPGHVAAS SSGPGIRRVA AVLARRDPAT WAGSGPTTRM MAGSGFEDAF
RAALDDGDPV AADLLTAVTA PIADLLRTAL CLDPELDLIA LTGGVAHGLE PHYSAAVHDH
LRRRGLYLTS EREPDWLTGR IRVVPPATAD PLVGAGLAAL AAGPVPAYSG GGREALVGR
