ACMA_GORST
ID ACMA_GORST Reviewed; 533 AA.
AC A1IHE6; A0A3G5BIW4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Acetone monooxygenase (methyl acetate-forming) {ECO:0000305};
DE Short=ACMO {ECO:0000303|PubMed:30392152};
DE EC=1.14.13.226 {ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:30392152};
DE AltName: Full=NADPH-dependent acetone monooxygenase {ECO:0000303|PubMed:17071761};
GN Name=acmA {ECO:0000303|PubMed:17071761};
OS Gordonia sp. (strain TY-5).
OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX NCBI_TaxID=235467;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP INDUCTION.
RC STRAIN=TY-5;
RX PubMed=17071761; DOI=10.1128/jb.01054-06;
RA Kotani T., Yurimoto H., Kato N., Sakai Y.;
RT "Novel acetone metabolism in a propane-utilizing bacterium, Gordonia sp.
RT strain TY-5.";
RL J. Bacteriol. 189:886-893(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-325.
RC STRAIN=TY-5;
RX PubMed=30392152; DOI=10.1186/s13568-018-0709-x;
RA Fordwour O.B., Luka G., Hoorfar M., Wolthers K.R.;
RT "Kinetic characterization of acetone monooxygenase from Gordonia sp. strain
RT TY-5.";
RL AMB Express 8:181-181(2018).
CC -!- FUNCTION: Plays an important role in the metabolism of acetone derived
CC from propane oxidation (PubMed:17071761). Catalyzes the oxidation of
CC acetone to methyl acetate (PubMed:17071761, PubMed:30392152). Exhibits
CC high catalytic efficiency towards various linear and cyclic ketones,
CC such as butanone, 2-pentanone, 2-heptanone, 2-octanone, 2-nonanone, 2-
CC decanone, cyclobutanone, cyclopentanone and cyclohexanone
CC (PubMed:17071761, PubMed:30392152). Elicits the highest catalytic
CC efficiency towards butanone and cyclobutanone (PubMed:30392152). Is
CC highly specific for NADPH and cannot use NADH (PubMed:17071761,
CC PubMed:30392152). {ECO:0000269|PubMed:17071761,
CC ECO:0000269|PubMed:30392152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetone + H(+) + NADPH + O2 = H2O + methyl acetate + NADP(+);
CC Xref=Rhea:RHEA:49988, ChEBI:CHEBI:15347, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:77700; EC=1.14.13.226;
CC Evidence={ECO:0000269|PubMed:17071761, ECO:0000269|PubMed:30392152};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49989;
CC Evidence={ECO:0000269|PubMed:17071761};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:30392152, ECO:0000305|PubMed:17071761};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:H3JQW0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 uM for NADPH {ECO:0000269|PubMed:30392152};
CC KM=170 uM for acetone {ECO:0000269|PubMed:30392152};
CC KM=0.34 uM for butanone {ECO:0000269|PubMed:30392152};
CC KM=0.37 uM for 2-pentanone {ECO:0000269|PubMed:30392152};
CC KM=1.5 uM for 2-heptanone {ECO:0000269|PubMed:30392152};
CC KM=4.4 uM for 3-methylbutanone {ECO:0000269|PubMed:30392152};
CC KM=1500 uM for 2,4-dimethyl-3-pentanone
CC {ECO:0000269|PubMed:30392152};
CC KM=1.5 uM for cyclobutanone {ECO:0000269|PubMed:30392152};
CC KM=120 uM for cyclopentanone {ECO:0000269|PubMed:30392152};
CC KM=2400 uM for cyclohexanone {ECO:0000269|PubMed:30392152};
CC KM=6.7 uM for bicyclo[3.2.0]hept-2-en-6-one
CC {ECO:0000269|PubMed:30392152};
CC KM=8.9 uM for phenylacetone {ECO:0000269|PubMed:30392152};
CC Note=kcat is 2.0 sec(-1) with NADPH as substrate. kcat is 1.4 sec(-1)
CC with acetone as substrate. kcat is 2.1 sec(-1) with butanone as
CC substrate. kcat is 1.9 sec(-1) with 2-pentanone as substrate. kcat is
CC 3.9 sec(-1) with 2-heptanone as substrate. kcat is 2.2 sec(-1) with
CC 3-methylbutanone as substrate. kcat is 1.5 sec(-1) with 2,4-dimethyl-
CC 3-pentanone as substrate. kcat is 2.0 sec(-1) with cyclobutanone as
CC substrate. kcat is 4.3 sec(-1) with cyclopentanone as substrate. kcat
CC is 3.6 sec(-1) with cyclohexanone as substrate. kcat is 1.5 sec(-1)
CC with bicyclo[3.2.0]hept-2-en-6-one as substrate. kcat is 1.0 sec(-1)
CC with phenylacetone as substrate. {ECO:0000269|PubMed:30392152};
CC pH dependence:
CC Optimum pH is 8.0-8.5 (PubMed:17071761). Optimum pH is 7.0-8.0
CC (PubMed:30392152). {ECO:0000269|PubMed:17071761,
CC ECO:0000269|PubMed:30392152};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:17071761};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17071761}.
CC -!- INDUCTION: Induced by propane, 2-propanol and acetone.
CC {ECO:0000269|PubMed:17071761}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB252677; BAF43791.1; -; Genomic_DNA.
DR EMBL; MH880286; AYV99719.1; -; mRNA.
DR SMR; A1IHE6; -.
DR BioCyc; MetaCyc:MON-19814; -.
DR BRENDA; 1.14.13.226; 14626.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17071761"
FT CHAIN 2..533
FT /note="Acetone monooxygenase (methyl acetate-forming)"
FT /id="PRO_0000453642"
FT BINDING 43..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 53..55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 55..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 183..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 206..207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT BINDING 492
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:H3JQW0"
FT MUTAGEN 325
FT /note="H->K: 6-fold decrease in Km for NADPH."
FT /evidence="ECO:0000269|PubMed:30392152"
FT CONFLICT 23..25
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 533 AA; 59679 MW; 489EADB71A511A3F CRC64;
MSTTTLDAAV IGTGVAGLYE LHMLREQGLE VRAYDKASGV GGTWYWNRYP GARFDSEAYI
YQYLFDEDLY KGWSWSQRFP GQEEIERWLN YVADSLDLRR DISLETEITS AVFDEDRNRW
TLTTADGDTI DAQFLITCCG MLSAPMKDLF PGQSDFGGQL VHTARWPKEG IDFAGKRVGV
IGNGATGIQV IQSIAADVDE LKVFIRTPQY ALPMKNPSYG PDEVAWYKSR FGELKDTLPH
TFTGFEYDFT DAWEDLTPEQ RRARLEDDYE NGSLKLWLAS FAEIFSDEQV SEEVSEFVRE
KMRARLVDPE LCDLLIPSDY GFGTHRVPLE TNYLEVYHRD NVTAVLVRDN PITRIRENGI
ELADGTVHEL DVIIMATGFD AGTGALTRID IRGRDGRTLA DDWSRDIRTT MGLMVHGYPN
MLTTAVPLAP SAALCNMTTC LQQQTEWISE AIRHLRATGK TVIEPTAEGE EAWVAHHDEL
ADANLISKTN SWYVGSNVPG KPRRVLSYVG GVGAYRDATL EAAAAGYKGF ALS
