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Aklanonic acid methyl ester cyclase AcmA (AAME cyclase) (EC 5.5.1.23) (Methyl aklanonate cyclase)

 DNRD_STRGJ              Reviewed;         144 AA.
O52646;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
20-DEC-2017, entry version 67.
RecName: Full=Aklanonic acid methyl ester cyclase AcmA;
Short=AAME cyclase;
EC=5.5.1.23;
AltName: Full=Methyl aklanonate cyclase;
Name=acma; Synonyms=aknH;
Streptomyces galilaeus.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=33899;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBSTRATE
SPECIFICITY.
STRAIN=ATCC 31615;
PubMed=10658662;
Kantola J., Kunnari T., Hautala A., Hakala J., Ylihonko K.,
Mantsala P.;
"Elucidation of anthracyclinone biosynthesis by stepwise cloning of
genes for anthracyclines from three different Streptomyces spp.";
Microbiology 146:155-163(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC31615;
PubMed=12137949; DOI=10.1016/S0378-1119(02)00699-6;
Raty K., Kantola J., Hautala A., Hakala J., Ylihonko K., Mantsala P.;
"Cloning and characterization of Streptomyces galilaeus aclacinomycins
polyketide synthase (PKS) cluster.";
Gene 293:115-122(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=3AR-33;
PubMed=12399480; DOI=10.1128/JB.184.22.6115-6122.2002;
Chung J., Fujii I., Tsukamoto N., Sankawa U., Ebizuka Y.;
"Expression, purification, and characterization of AknX anthrone
oxygenase, which is involved in aklavinone biosynthesis in
Streptomyces galilaeus.";
J. Bacteriol. 184:6115-6122(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC31615;
Niemi J.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[5]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-144 IN COMPLEX WITH
SUBSTRATE ANALOGS, FUNCTION, MUTAGENESIS OF TYR-15; ASN-51; GLN-105;
HIS-107 AND ASP-121, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
SPECIFICITY, REACTION MECHANISM, AND SUBUNIT.
PubMed=16414075; DOI=10.1016/j.jmb.2005.12.064;
Kallio P., Sultana A., Niemi J., Mantsala P., Schneider G.;
"Crystal structure of the polyketide cyclase AknH with bound substrate
and product analogue: implications for catalytic mechanism and product
stereoselectivity.";
J. Mol. Biol. 357:210-220(2006).
-!- FUNCTION: Involved in the biosynthesis of aklavinone which is an
important precursor common to the formation of the clinically
significant anthracyclines such as carminomycin, daunorubicin
(daunomycin), rhodomycin, aclacinomycin T (aklavin) and
aclacinomycin A (aclarubicin). These compounds are aromatic
polyketide antibiotics that exhibit high cytotoxicity and are
widely applied in the chemotherapy of a variety of cancers.
Catalyzes the cyclization of aklanonic acid methyl ester to yield
aklaviketone. It is also able to use nogalonic acid methyl ester
as substrate, but produces exclusively auraviketone with C9-R
stereochemistry. {ECO:0000269|PubMed:10658662,
ECO:0000269|PubMed:16414075}.
-!- CATALYTIC ACTIVITY: Aklaviketone = methyl aklanonate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2 uM for nogalonic acid methyl ester
{ECO:0000269|PubMed:16414075};
Note=kcat is 1 sec(-1) for cyclization with nogalonic acid
methyl ester.;
pH dependence:
Optimum pH is 7.2. {ECO:0000269|PubMed:16414075};
-!- PATHWAY: Antibiotic biosynthesis; daunorubicin biosynthesis.
-!- PATHWAY: Antibiotic biosynthesis; carminomycin biosynthesis.
-!- PATHWAY: Antibiotic biosynthesis; rhodomycin biosynthesis.
-!- PATHWAY: Antibiotic biosynthesis; aclacinomycin biosynthesis.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16414075}.
-!- SIMILARITY: Belongs to the polyketide cyclase DnrD family.
{ECO:0000305}.
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EMBL; AF043550; AAB99853.1; -; Genomic_DNA.
EMBL; AF257324; AAF70112.1; -; Genomic_DNA.
EMBL; AB008466; BAB72051.1; -; Genomic_DNA.
PDB; 2F98; X-ray; 2.10 A; A/B/C/D=2-144.
PDB; 2F99; X-ray; 1.90 A; A/B/C/D=2-144.
PDBsum; 2F98; -.
PDBsum; 2F99; -.
ProteinModelPortal; O52646; -.
SMR; O52646; -.
DrugBank; DB04624; DERIVATIVE OF AKLANONIC ACID METHYL ESTER (AAME).
KEGG; ag:AAF70112; -.
KO; K15943; -.
BioCyc; MetaCyc:MONOMER-18179; -.
UniPathway; UPA00054; -.
UniPathway; UPA01040; -.
UniPathway; UPA01042; -.
UniPathway; UPA01043; -.
EvolutionaryTrace; O52646; -.
GO; GO:0016872; F:intramolecular lyase activity; IDA:UniProtKB.
GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
GO; GO:1901771; P:daunorubicin biosynthetic process; IDA:UniProtKB.
GO; GO:0044598; P:doxorubicin metabolic process; IDA:UniProtKB.
InterPro; IPR009959; Cyclase_SnoaL-like.
InterPro; IPR032710; NTF2-like_dom_sf.
PANTHER; PTHR38436; PTHR38436; 1.
Pfam; PF07366; SnoaL; 1.
SUPFAM; SSF54427; SSF54427; 1.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; Isomerase.
CHAIN 1 144 Aklanonic acid methyl ester cyclase AcmA.
/FTId=PRO_0000425673.
BINDING 51 51 Substrate.
BINDING 105 105 Substrate.
MUTAGEN 15 15 Y->F: Retains 45% of cyclase activity
with a partial loss in stereoselectivity
of the final product (20% of C9-S and 80%
of C9-R isomers). Retains 20% of cyclase
activity with a total loss in
stereoselectivity of the final product
(racemic mixture of both stereoisomers);
when associated with L-51.
{ECO:0000269|PubMed:16414075}.
MUTAGEN 51 51 N->L: Retains 20% of cyclase activity
with a total loss in stereoselectivity of
the final product (racemic mixture of
both stereoisomers); when associated with
F-15. {ECO:0000269|PubMed:16414075}.
MUTAGEN 105 105 Q->A: Retains significant cyclase
activity (100% of C9-R isomer).
{ECO:0000269|PubMed:16414075}.
MUTAGEN 107 107 H->A: Retains significant cyclase
activity (100% of C9-R isomer).
{ECO:0000269|PubMed:16414075}.
MUTAGEN 121 121 D->A: Loss of cyclase activity.
{ECO:0000269|PubMed:16414075}.
HELIX 3 17 {ECO:0000244|PDB:2F99}.
HELIX 23 25 {ECO:0000244|PDB:2F99}.
STRAND 27 32 {ECO:0000244|PDB:2F99}.
HELIX 34 36 {ECO:0000244|PDB:2F99}.
TURN 37 39 {ECO:0000244|PDB:2F99}.
HELIX 44 59 {ECO:0000244|PDB:2F99}.
STRAND 64 73 {ECO:0000244|PDB:2F99}.
STRAND 76 86 {ECO:0000244|PDB:2F99}.
STRAND 100 112 {ECO:0000244|PDB:2F99}.
STRAND 115 123 {ECO:0000244|PDB:2F99}.
HELIX 125 131 {ECO:0000244|PDB:2F99}.
SEQUENCE 144 AA; 16731 MW; 30083BDD35E808C0 CRC64;
MSEQIAAVRR MVEAYNTGKT DDVADYIHPE YMNPGTLEFT SLRGPELFAI NVAWVKKTFS
EEARLEEVGI EERADWVRAR LVLYGRHVGE MVGMAPTGRL FSGEQIHLLH FVDGKIHHHR
DWPDYQGTYR QLGEPWPETE HRRP


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