LPSB_EPIFI
ID LPSB_EPIFI Reviewed; 1351 AA.
AC A2TBU4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=D-lysergyl-peptide-synthetase subunit 2 {ECO:0000303|PubMed:17308187};
DE Short=LPS2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:17308187};
DE AltName: Full=Ergot alkaloid synthesis protein B {ECO:0000303|PubMed:17308187};
DE AltName: Full=Nonribosomal peptide synthetase lpsB {ECO:0000303|PubMed:17308187};
GN Name=lpsB {ECO:0000303|PubMed:17308187};
OS Epichloe festucae var. lolii (Neotyphodium lolii) (Acremonium lolii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=73839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Lp19;
RX PubMed=17308187; DOI=10.1128/aem.00257-07;
RA Fleetwood D.J., Scott B., Lane G.A., Tanaka A., Johnson R.D.;
RT "A complex ergovaline gene cluster in epichloe endophytes of grasses.";
RL Appl. Environ. Microbiol. 73:2571-2579(2007).
RN [2]
RP FUNCTION.
RX PubMed=11592979; DOI=10.1073/pnas.221198698;
RA Panaccione D.G., Johnson R.D., Wang J., Young C.A., Damrongkool P.,
RA Scott B., Schardl C.L.;
RT "Elimination of ergovaline from a grass-Neotyphodium endophyte symbiosis by
RT genetic modification of the endophyte.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12820-12825(2001).
CC -!- FUNCTION: D-lysergyl-peptide-synthetase subunit 2; part of the gene
CC cluster that mediates the biosynthesis of fungal ergot alkaloid
CC ergovaline, the predominant ergopeptine product in E.festucae var.
CC lolii (PubMed:17308187). DmaW catalyzes the first step of ergot
CC alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP)
CC and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity).
CC The second step is catalyzed by the methyltransferase easF that
CC methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-
CC L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine
CC (By similarity). The catalase easC and the FAD-dependent oxidoreductase
CC easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is
CC further oxidized by easD in the presence of NAD(+), resulting in the
CC formation of chanoclavine-I aldehyde (By similarity). Agroclavine
CC dehydrogenase easG then mediates the conversion of chanoclavine-I
CC aldehyde to agroclavine via a non-enzymatic adduct reaction: the
CC substrate is an iminium intermediate that is formed spontaneously from
CC chanoclavine-I aldehyde in the presence of glutathione (By similarity).
CC The presence of easA is not required to complete this reaction (By
CC similarity). Further conversion of agroclavine to paspalic acid is a
CC two-step process involving oxidation of agroclavine to elymoclavine and
CC of elymoclavine to paspalic acid, the second step being performed by
CC the elymoclavine oxidase cloA (By similarity). Paspalic acid is then
CC further converted to D-lysergic acid (By similarity). Ergovaline is
CC assembled from D-lysergic acid and three different amino acids by the
CC D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a
CC trimodular (lpsA) nonribosomal peptide synthetase subunit
CC (PubMed:17308187, PubMed:11592979). {ECO:0000250|UniProtKB:Q50EL0,
CC ECO:0000269|PubMed:11592979, ECO:0000269|PubMed:17308187}.
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000269|PubMed:17308187}.
CC -!- INDUCTION: Strongly expressed in planta but not expressed in axenic
CC culture (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) or reductase domain (R) that releases the
CC newly synthesized peptide from the enzyme (By similarity). LpsB is
CC composed of only one module which is required for the activation of D-
CC lysergic acid activation and its incorporation in the final ergot
CC alkaloid (By similarity). {ECO:0000250|UniProtKB:Q8J0L6}.
CC -!- DISRUPTION PHENOTYPE: Aolishes the production of ergovaline and its
CC stereoisomer ergovalinine but accumulates lysergic acid and its C-8
CC stereoisomer (PubMed:17308187). {ECO:0000269|PubMed:17308187}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; EF125025; ABM91454.1; -; Genomic_DNA.
DR AlphaFoldDB; A2TBU4; -.
DR SMR; A2TBU4; -.
DR UniPathway; UPA00327; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035835; P:indole alkaloid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Transferase.
FT CHAIN 1..1351
FT /note="D-lysergyl-peptide-synthetase subunit 2"
FT /id="PRO_0000439112"
FT DOMAIN 828..904
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 285..684
FT /note="Adenylation (A) domain"
FT /evidence="ECO:0000255"
FT REGION 941..1340
FT /note="Condensation (C) domain"
FT /evidence="ECO:0000255"
FT MOD_RES 865
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1351 AA; 147939 MW; 9617F81504AA66E0 CRC64;
MQSQVRLPSN GNPALSFPQN EIGGPVHWKT YLEGCSPCSF PSLRTVCPSQ SWPASVSITI
GDSIFRRLEH FSDKTGISVA TVFRASWGLV LRIYTGQDSV CFGDMTTAPG GIDAIGCVGV
CRVELSDTAV ISKVLQRIQA ASANKLAIPH VPLSDAVLSK CMPSASLFNT CMLISGGGER
PEKTSSTFEK VELGYDDQYD IIVRGSVEDS GASAALSYRT SFLSEEQATS IANTFERAVS
DLIGIENRIG QICFLSDLDK SQIYTWNKDP PLRAHSCVDT LIHERCLSQP TASAVNAWDG
ELSYEELNHL SSKLSRHLVT LGVGAEVFVP LCFEKSRWTT VAMLAVIKAG GAFVLLDPSH
PAERLLSICQ KVSARLIVAS AQHAKLAEDL VTSIVEVGDD KADWLTDKGI KAQTQTRTRR
SAAPGDALYA VFTSGSTGTP KGVIIEHGSF HAAVFPYTEA VGLNQESRVF QFSSYAFDVT
IFDTLMTLIS GGCVCVPSNT ERWSDVANAI QRFRVTHSSL TPTVARILDP KDVLTLRTLV
LGGEKLVTSD ITKWVDQVRL VHLYGASECP IMSIQSMTGV ASDFQTTDHA TGSNCWIVDP
NNHDRLVPIG TIGELVIEGT IVGRGYLDDP EKSSATFIRP PGWLCQVRGS GYHSAVYKSG
DLVQYTADGS LRYIGRKDTQ VKLRGQRVEL GEVEHHVKLT FPNATDVVVE LVVTIHASSS
RAPILVAFVL ISHEADPDPE SIRTGRGEGL SQILSEPTDR FCSQIPIVQS QLQQSLPSYM
VPGIFLPLMT LPLTSTDKIN RKLLRELAGA LSREELESYQ PSTGPVRAPQ TTTEKLLQQY
FARVLNIPVE QVGADDHFFQ RGGDSLTAMK LVAMARKDKH KLTVQDIFDS PRLSALACVV
RSGKVDGNKE PPLEPFSLVN KHRDIIRAAA QQCQLPVRVI EDVYPCTPLQ RGLISETLRD
SKAFIAHLAV SLPPDIDLQR LQEAWTTVAN ANPILRTRMV LSASHGLLQV VVREDIRWIV
SKNAEAQDFF VGVGKPLVQL VLCCHREGNE VPVQLLLMVH HAVYDGYTLP LIFEQVKAAY
NGGTLAPRPA VPFIRYVQSI PDGTGYWNSL MANLQTPIFP ALPSKSYQPL PNAIMRHTII
TPGSHRQYTP STYVRLAWAI TQAYHQGTCD IFFGTVVSGR NAPVTDIELM TIPTVATIPC
RVTLDFQSLV QSALRKIQDD AISGIPFEQL GLPHIRRLGE HAMLACSFQT LLSIQPALPP
STDAWFEQPG STIDYRANAT YAINLFFGLE GDKLKATALY DFNVVKKDKM QSMLVDFGNI
LQTMHKSPNS LIRDILAVPQ QMRGPINSAS L
