ADAB_ASPNG
ID ADAB_ASPNG Reviewed; 317 AA.
AC G3KLH5;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Lactamase-like protein adaB {ECO:0000303|PubMed:21866960};
DE EC=3.1.-.- {ECO:0000269|PubMed:21866960};
DE AltName: Full=2-acetyl-2-decarboxamidoanthrotainin biosynthesis cluster protein B {ECO:0000303|PubMed:21866960};
GN Name=adaB {ECO:0000303|PubMed:21866960};
GN ORFNames=ATCC64974_92710, CAN33_24695;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 1015 / NV DSM 2061;
RX PubMed=21866960; DOI=10.1021/ja206906d;
RA Li Y., Chooi Y.H., Sheng Y., Valentine J.S., Tang Y.;
RT "Comparative characterization of fungal anthracenone and naphthacenedione
RT biosynthetic pathways reveals an alpha-hydroxylation-dependent Claisen-like
RT cyclization catalyzed by a dimanganese thioesterase.";
RL J. Am. Chem. Soc. 133:15773-15785(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_311;
RA Kerrigan L., Tallon L., Sadzewicz L., Sengamalay N., Ott S., Godinez A.,
RA Nagaraj S., Vavikolanu K., Nadendla S., George J., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64974 / FGSC A733 / N402;
RX PubMed=30319579; DOI=10.3389/fmicb.2018.02269;
RA Laothanachareon T., Tamayo-Ramos J.A., Nijsse B., Schaap P.J.;
RT "Forward genetics by genome sequencing uncovers the central role of the
RT Aspergillus niger goxB locus in hydrogen peroxide induced glucose oxidase
RT expression.";
RL Front. Microbiol. 9:2269-2269(2018).
CC -!- FUNCTION: Lactamase-like protein; part of the gene cluster that
CC mediates the biosynthesis of the linear tetracyclic TAN-1612
CC neuropeptide Y receptor antagonist (PubMed:21866960). The decaketide
CC backbone of TAN-1612 is synthesized by the non-reducing polyketide
CC synthase adaA via condensation of one acetyl-CoA starter unit with 9
CC malonyl-CoA units. The FAD-dependent monooxygenase adaC then performs
CC hydroxylation at C2 while the polaketide chain is still attached to the
CC NRPKS adaA (PubMed:21866960). The alpha-hydroxylation step at C2
CC appears to be crucial for the following C18-C1 Claisen cyclization and
CC release of the C9-hydroxyl version of TAN-1612 from the NRPKS adaA, two
CC steps performed by the lactamase-like protein adaB (PubMed:21866960).
CC Finally, the O-methyltransferase adaD performs the C9 O-methylation to
CC complete the biosynthesis of TAN-1612 (PubMed:21866960).
CC {ECO:0000269|PubMed:21866960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(2,4-dioxopentyl)-2,3,6,8,9-pentahydroxy-1-oxo-1,2,3,4-
CC tetrahydroanthracene-2-carboxyl-[ACP] = 2-acetyl-3,4a,8,10,11,12a-
CC hexahydroxy-1,4,4a,5,12,12a-hexahydrotetracene-1,12-dione + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:64096, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:16520, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:146218,
CC ChEBI:CHEBI:149688; Evidence={ECO:0000269|PubMed:21866960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64097;
CC Evidence={ECO:0000269|PubMed:21866960};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q988B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q988B9};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:21866960}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; JN257714; AEN83888.1; -; Genomic_DNA.
DR EMBL; NKJJ01000002; OWW37979.1; -; Genomic_DNA.
DR EMBL; OGUI01000016; SPB51661.1; -; Genomic_DNA.
DR AlphaFoldDB; G3KLH5; -.
DR SMR; G3KLH5; -.
DR STRING; 5061.CADANGAP00008888; -.
DR VEuPathDB; FungiDB:An11g07320; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1095189; -.
DR VEuPathDB; FungiDB:ATCC64974_92710; -.
DR VEuPathDB; FungiDB:M747DRAFT_334471; -.
DR eggNOG; KOG0813; Eukaryota.
DR OrthoDB; 576967at2759; -.
DR Proteomes; UP000236662; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..317
FT /note="Lactamase-like protein adaB"
FT /id="PRO_0000446351"
FT ACT_SITE 101
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ SEQUENCE 317 AA; 35195 MW; 04C16EB02BD5431E CRC64;
MAFRIPFAQS FWQEYLSGQE ANLPRLPEVE QVTETVMRIL GGNPGRMQLQ GTNTYLVGTG
KFRILIDTGQ GEASWIEALT KQLEANGLEI SHVLLTHWHG DHTGGVPDLI TYNPELSSRV
YKNTPDLGQQ AIHDGQKFHV EGATIRAVFT PGHAFDHMCF LLEEENALFT GDNVLGHGYS
VVEDLGTYMT SLTRMADLNC ALGYPAHGTR IEDLPAKMKE YIQHKESRMR QVLAALERSR
ARMTATGGGR RAGALTFPEL INSMYGGIPD EIEQALTPFL SQVLWKLAED RKVGFEGEPS
QRRWFAVGPP AATAVRL
