ACBK_ACTS5
ID ACBK_ACTS5 Reviewed; 299 AA.
AC Q8RMD4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Acarbose 7(IV)-phosphotransferase {ECO:0000305};
DE EC=2.7.1.187 {ECO:0000269|PubMed:11937512};
DE AltName: Full=Acarbose 7-kinase {ECO:0000303|PubMed:11937512};
GN Name=acbK {ECO:0000303|PubMed:11937512};
GN OrderedLocusNames=ACPL_3675 {ECO:0000312|EMBL:AEV84570.1};
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 phosphorylation of the alpha-glucosidase
CC inhibitor acarbose. Phosphorylation of acarbose could be a resistance-
CC like self-protection mechanism. {ECO:0000269|PubMed:11937512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acarbose + ATP = acarbose 7(IV)-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:45124, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:84363, ChEBI:CHEBI:84975, ChEBI:CHEBI:456216;
CC EC=2.7.1.187; Evidence={ECO:0000269|PubMed:11937512};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; Y18523; CAD29481.2; -; Genomic_DNA.
DR EMBL; CP003170; AEV84570.1; -; Genomic_DNA.
DR RefSeq; WP_014690642.1; NZ_LT827010.1.
DR PDB; 6WB7; X-ray; 2.44 A; A/B/C/D=1-299.
DR PDBsum; 6WB7; -.
DR AlphaFoldDB; Q8RMD4; -.
DR SMR; Q8RMD4; -.
DR STRING; 134676.ACPL_3675; -.
DR EnsemblBacteria; AEV84570; AEV84570; ACPL_3675.
DR KEGG; ase:ACPL_3675; -.
DR PATRIC; fig|134676.3.peg.3591; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_12_0_11; -.
DR OMA; NPYHEPF; -.
DR OrthoDB; 1604782at2; -.
DR BRENDA; 2.7.1.187; 144.
DR Proteomes; UP000005440; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Kinase; Reference proteome; Transferase.
FT CHAIN 1..299
FT /note="Acarbose 7(IV)-phosphotransferase"
FT /id="PRO_0000435390"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6WB7"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6WB7"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:6WB7"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6WB7"
SQ SEQUENCE 299 AA; 31480 MW; ABAEF0E4CA66F0A8 CRC64;
MSEHTDVLVL GGAGVDTIAY VPELPLPFQD SYVVAAIEPR AGQTGDNVAL GLHTLGLRTM
HVDVLGDDPE GDLVRAFHTR HGLPFAALPT AAGTKRAVNL VGPDGRRLSL WDGSREAEED
RYPAALIAAH TAHARHVHVC ITPPGQHVFG QLNDLPVTVS TDLHNWDGAY EGFEVYAFNA
DLVFLSATAL TDVAATMRRV IDRGRARLVV ATDGAHGGSV LVRGETEVRR YAAVAPEAPV
VDSNGAGDAF VSGFLFGHLA GEPLETCLRY GAIAGAYACT IPATRAGAID RAALLRPAA
