SNOAB_STRNO
ID SNOAB_STRNO Reviewed; 118 AA.
AC O54259; Q54493;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Deoxynogalonate monooxygenase {ECO:0000303|PubMed:19255477};
DE EC=1.13.12.22 {ECO:0000305|PubMed:19255477, ECO:0000305|PubMed:20052967};
DE AltName: Full=12-deoxy-nogalonic acid oxygenase {ECO:0000303|PubMed:19255477};
DE AltName: Full=Cofactor-independent monooxygenase SnoaB {ECO:0000303|PubMed:20052967};
GN Name=snoaB {ECO:0000303|PubMed:19255477};
OS Streptomyces nogalater.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=38314;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 27451 / DSM 40546 / JCM 4553 / NBRC 13445 / NCIMB 9489 / VKM
RC Ac-1290;
RX PubMed=8760909; DOI=10.1099/13500872-142-8-1965;
RA Ylihonko K., Hakala J., Kunnari T., Mantsala P.;
RT "Production of hybrid anthracycline antibiotics by heterologous expression
RT of Streptomyces nogalater nogalamycin biosynthesis genes.";
RL Microbiology 142:1965-1972(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 27451 / DSM 40546 / JCM 4553 / NBRC 13445 / NCIMB 9489 / VKM
RC Ac-1290;
RX PubMed=8668120; DOI=10.1007/bf02172908;
RA Ylihonko K., Tuikkanen J., Jussila S., Cong L., Mantsala P.;
RT "A gene cluster involved in nogalamycin biosynthesis from Streptomyces
RT nogalater: sequence analysis and complementation of early-block mutations
RT in the anthracycline pathway.";
RL Mol. Gen. Genet. 251:113-120(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27451 / DSM 40546 / JCM 4553 / NBRC 13445 / NCIMB 9489 / VKM
RC Ac-1290;
RX PubMed=9349712; DOI=10.1007/s004380050562;
RA Torkkell S., Ylihonko K., Hakala J., Skurnik M., Mantsala P.;
RT "Characterization of Streptomyces nogalater genes encoding enzymes involved
RT in glycosylation steps in nogalamycin biosynthesis.";
RL Mol. Gen. Genet. 256:203-209(1997).
RN [4]
RP CRYSTALLIZATION, FUNCTION, MUTAGENESIS OF PHE-29; PHE-40 AND LEU-89,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=19255477; DOI=10.1107/s1744309109001389;
RA Koskiniemi H., Grocholski T., Schneider G., Niemi J.;
RT "Expression, purification and crystallization of the cofactor-independent
RT monooxygenase SnoaB from the nogalamycin biosynthetic pathway.";
RL Acta Crystallogr. F 65:256-259(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-63,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP ASN-18; HIS-49; ASN-63; TRP-67 AND ARG-90, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=20052967; DOI=10.1021/bi901985b;
RA Grocholski T., Koskiniemi H., Lindqvist Y., Mantsala P., Niemi J.,
RA Schneider G.;
RT "Crystal structure of the cofactor-independent monooxygenase SnoaB from
RT Streptomyces nogalater: implications for the reaction mechanism.";
RL Biochemistry 49:934-944(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the anthracycline (aromatic
CC polyketide) antibiotic nogalamycin (PubMed:8760909, PubMed:8668120).
CC Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to
CC yield nogalonic acid (PubMed:19255477, PubMed:20052967).
CC {ECO:0000269|PubMed:8668120, ECO:0000269|PubMed:8760909,
CC ECO:0000305|PubMed:19255477, ECO:0000305|PubMed:20052967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=deoxynogalonate + O2 = H(+) + H2O + nogalonate;
CC Xref=Rhea:RHEA:45056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:84897, ChEBI:CHEBI:84900;
CC EC=1.13.12.22; Evidence={ECO:0000305|PubMed:19255477,
CC ECO:0000305|PubMed:20052967};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=140 uM for dithranol {ECO:0000269|PubMed:20052967};
CC Vmax=6.3 umol/min/mg enzyme with dithranol as substrate
CC {ECO:0000269|PubMed:20052967};
CC Note=kcat is 1.5 sec(-1) for monooxygenase activity with dithranol as
CC substrate. {ECO:0000269|PubMed:20052967};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:8760909}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19255477,
CC ECO:0000269|PubMed:20052967}.
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DR EMBL; AJ224512; CAA12015.1; -; Genomic_DNA.
DR PIR; T46674; T46674.
DR PDB; 3KG0; X-ray; 1.70 A; A/B/C=1-118.
DR PDB; 3KG1; X-ray; 2.50 A; A/B/C=1-118.
DR PDB; 3KNG; X-ray; 1.90 A; A/B=2-118.
DR PDBsum; 3KG0; -.
DR PDBsum; 3KG1; -.
DR PDBsum; 3KNG; -.
DR AlphaFoldDB; O54259; -.
DR SMR; O54259; -.
DR KEGG; ag:CAA12015; -.
DR BRENDA; 1.13.12.22; 13766.
DR EvolutionaryTrace; O54259; -.
DR GO; GO:0016703; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases); IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS51725; ABM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Oxidoreductase.
FT CHAIN 1..118
FT /note="Deoxynogalonate monooxygenase"
FT /id="PRO_0000435850"
FT DOMAIN 14..100
FT /note="ABM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01062"
FT SITE 18
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:20052967"
FT SITE 63
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:20052967"
FT SITE 67
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:20052967"
FT MUTAGEN 18
FT /note="N->A: Loss of monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:20052967"
FT MUTAGEN 29
FT /note="F->M: Oxygenase activity comparable to the wild-
FT type; when associated with M-40 and M-89."
FT /evidence="ECO:0000269|PubMed:19255477"
FT MUTAGEN 40
FT /note="F->M: Oxygenase activity comparable to the wild-
FT type; when associated with M-29 and M-89."
FT /evidence="ECO:0000269|PubMed:19255477"
FT MUTAGEN 49
FT /note="H->A: Moderate decrease of catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20052967"
FT MUTAGEN 63
FT /note="N->A: Loss of monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:20052967"
FT MUTAGEN 67
FT /note="W->F: Loss of monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:20052967"
FT MUTAGEN 89
FT /note="L->M: Oxygenase activity comparable to the wild-
FT type; when associated with M-29 and M-40."
FT /evidence="ECO:0000269|PubMed:19255477"
FT MUTAGEN 90
FT /note="R->Q: Moderate decrease of catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20052967"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:3KG0"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:3KG0"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:3KG0"
FT STRAND 58..69
FT /evidence="ECO:0007829|PDB:3KG0"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:3KG0"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3KG0"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:3KG0"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3KG0"
SQ SEQUENCE 118 AA; 13039 MW; 8AC690B7B6EBE390 CRC64;
MPTRVNDGVD ADEVTFVNRF TVHGGPAEFE SVFARTAAFF ARQPGFVRHT LLRERDKDNS
YVNIAVWTDH DAFRRALAQP GFLPHATALR ALSTSEHGLF TARQTLPEGG DTTGSGHR
