STBB_STABI
ID STBB_STABI Reviewed; 1057 AA.
AC A0A193PS46;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Adenylate-forming reductase stbB {ECO:0000303|PubMed:26972702};
DE EC=1.2.1.- {ECO:0000269|PubMed:26972702};
DE AltName: Full=Ilicicolin B biosynthesis cluster protein stbB {ECO:0000303|PubMed:26972702};
DE AltName: Full=LL-Z1272-beta biosynthesis cluster protein stbB {ECO:0000303|PubMed:26972702};
DE AltName: Full=Nonribosomal peptide synthase-like protein stbB {ECO:0000303|PubMed:26972702};
DE Short=NRPS-like protein stbB {ECO:0000303|PubMed:26972702};
GN Name=stbB {ECO:0000303|PubMed:26972702};
OS Stachybotrys bisbyi (Hyalostachybotrys bisbyi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=80385;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DOMAIN, FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=PYH05-7;
RX PubMed=26972702; DOI=10.1002/cbic.201600087;
RA Li C., Matsuda Y., Gao H., Hu D., Yao X.S., Abe I.;
RT "Biosynthesis of LL-Z1272beta: discovery of a new member of NRPS-like
RT enzymes for aryl-aldehyde formation.";
RL ChemBioChem 17:904-907(2016).
CC -!- FUNCTION: Nonribosomal peptide synthase-like protein; part of the
CC cluster that mediates the biosynthesis of LL-Z1272-beta, also known as
CC ilicicolin B, a prenylated aryl-aldehyde produced by several fungi and
CC that serves as a key pathway intermediate for many fungal
CC meroterpenoids (PubMed:26972702). The first step in the pathway is
CC performed by the non-reducing polyketide synthase stbA that produces
CC orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units
CC (PubMed:26972702). The prenyltransferase stbC then prenylates orsenilic
CC acid into grifolic acid (PubMed:26972702). Finally, grifolic acid is
CC reduced to ilicicolin B by the NRPS-like protein stbB
CC (PubMed:26972702). {ECO:0000269|PubMed:26972702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + ATP + ilicicolinate B = A + AMP + diphosphate +
CC ilicicolin B; Xref=Rhea:RHEA:63080, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:146152, ChEBI:CHEBI:146153, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:26972702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63081;
CC Evidence={ECO:0000269|PubMed:26972702};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:26972702}.
CC -!- DOMAIN: Contains three distinct domains: an adenylation (A) domain that
CC activates the substrate amino acid which is subsequently covalently
CC linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine
CC prosthetic group of the second domain, the peptidyl carrier protein
CC (PCP) domain, as well as a reductase (R) release domain.
CC {ECO:0000305|PubMed:26972702}.
CC -!- SIMILARITY: Belongs to the adenylate-forming reductase family.
CC {ECO:0000305}.
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DR EMBL; LC125467; BAV19380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A193PS46; -.
DR SMR; A0A193PS46; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; NADP; Nucleotide-binding; Oxidoreductase; Phosphopantetheine;
KW Phosphoprotein.
FT CHAIN 1..1057
FT /note="Adenylate-forming reductase stbB"
FT /id="PRO_0000450380"
FT DOMAIN 564..651
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:26972702"
FT REGION 21..378
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26972702"
FT REGION 693..1025
FT /note="Reductase (R) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:26972702"
FT BINDING 251
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 344..345
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 349
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 423..426
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 700..703
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 783..785
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 858
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT BINDING 862
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q6RKB1"
FT MOD_RES 600
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1057 AA; 113347 MW; F25A725F500DA07C CRC64;
MGSLGSSQLK PFNKAPIDFV STKRQPGAVC SLPELVDYNA QHNASHNFCI QGKPGGEFDT
FTHADFKVAA ANCAKWLKAN LPLGASQAPN AITKNAPVAL FMESDFGLVV HEFALLSLGI
PPLVLSVRLP PNAIMHLLKS TGATSFIVSQ KLSGPAKPAL AALAANGIAT AVGNPYTSFL
EPGVDVASKG TFEVPENPDD ITLLLHSSGT TGLPKPIPIS HRMLMFAVST AKFDTEDEAQ
GLNVSSLPLF HGFGLVAPGI SMTVGKTTVY PASDGIPNIV SIIDLIKRTN ARSLMTVPFL
LDDVINNEEG LRVLAGLDFV GTGGAALGPG VGDKLAAAGI KLLNFYGTTE SGPLSLVFVP
KDNYNWKFFR LRTDMNFEIA NLEPKDGVKR YRLTIRAFGE GEDQEIADQL IRNDEYPETD
FAAVGRDDDV IVLATGEKAS PQILENMLTE APMVKAAIAF GENQFNLGVI VEPKEPLAEG
GEAAFKELIW PIIVAAGQKM DAHSVIPSQE AVIVVPNGVR VPRTDKGSIA RKEVYALFAD
AMKDVYEKLA RAVGGADLKP LDLETLEEDI KALIIEHSGL KVPAEGLSAE ESLFDFGLDS
LQALKLRRVL AAAANKSEAM KDVNVDKVIP PEFVYLNPSV AQMAAAIKNP SAGSAAPTVD
ANAYKGVEKF AEQYALPGAS AEEKAPSVRE RAIVVVTGSS GSLGSHVVAT LARDPKVMRV
VVMVRQGSKP FDREPWTSRG INLKEDEFAK IVPLPVDPTA ENLGVDPMMY GMLQNNLTHI
VHAAWPMNYL TTLPSFQYQF EYLSGLLKLA TSGNTANKRR FIFVSSIAAV ARLSLSNSGA
MISETPVEPV DAACGIGYAD GKLVCEKILE KAAVSHAGQL EIAYVRCGQM TGSRATGAWN
ADEQIPMIFR TAKNLGVLPR IPGTLSWIPV DDAAQYIMDL SFFEGALPIA SHLENPVRQS
WADLMDGAGK FLGIQKSVSW PEWLELAGAA EDGPQDKYPV KKLFAFFKFS FGPMASGAVI
LGTDVARAHS ATIKNMGALD ASTIMKYFLH WQKINYL
