SIDL_ASPFU
ID SIDL_ASPFU Reviewed; 484 AA.
AC Q4WJX7;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Acyltransferase sidL {ECO:0000303|PubMed:21622789};
DE EC=2.3.1.- {ECO:0000305|PubMed:21622789};
DE AltName: Full=Siderophore biosynthesis protein L {ECO:0000303|PubMed:22106303};
GN Name=sidL {ECO:0000303|PubMed:21622789}; ORFNames=AFUA_1G04450;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION.
RX PubMed=15504822; DOI=10.1084/jem.20041242;
RA Schrettl M., Bignell E., Kragl C., Joechl C., Rogers T., Arst H.N. Jr.,
RA Haynes K., Haas H.;
RT "Siderophore biosynthesis but not reductive iron assimilation is essential
RT for Aspergillus fumigatus virulence.";
RL J. Exp. Med. 200:1213-1219(2004).
RN [3]
RP FUNCTION.
RX PubMed=16113265; DOI=10.1128/iai.73.9.5493-5503.2005;
RA Hissen A.H., Wan A.N., Warwas M.L., Pinto L.J., Moore M.M.;
RT "The Aspergillus fumigatus siderophore biosynthetic gene sidA, encoding L-
RT ornithine N(5)-oxygenase, is required for virulence.";
RL Infect. Immun. 73:5493-5503(2005).
RN [4]
RP FUNCTION.
RX PubMed=17845073; DOI=10.1371/journal.ppat.0030128;
RA Schrettl M., Bignell E., Kragl C., Sabiha Y., Loss O., Eisendle M.,
RA Wallner A., Arst H.N. Jr., Haynes K., Haas H.;
RT "Distinct roles for intra- and extracellular siderophores during
RT Aspergillus fumigatus infection.";
RL PLoS Pathog. 3:1195-1207(2007).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=21622789; DOI=10.1128/aem.00182-11;
RA Blatzer M., Schrettl M., Sarg B., Lindner H.H., Pfaller K., Haas H.;
RT "SidL, an Aspergillus fumigatus transacetylase involved in biosynthesis of
RT the siderophores ferricrocin and hydroxyferricrocin.";
RL Appl. Environ. Microbiol. 77:4959-4966(2011).
RN [6]
RP FUNCTION.
RX PubMed=22106303; DOI=10.1073/pnas.1106399108;
RA Yasmin S., Alcazar-Fuoli L., Gruendlinger M., Puempel T., Cairns T.,
RA Blatzer M., Lopez J.F., Grimalt J.O., Bignell E., Haas H.;
RT "Mevalonate governs interdependency of ergosterol and siderophore
RT biosyntheses in the fungal pathogen Aspergillus fumigatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E497-E504(2012).
CC -!- FUNCTION: Acyltransferase; part of the siderophore biosynthetic pathway
CC (PubMed:21622789). Aspergillus fumigatus produces 4 types of
CC siderophores, low-molecular-mass iron chelators, including excreted
CC fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and
CC intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC)
CC for conidial iron distribution and storage. TAFC consists of 3 N(2)-
CC acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically
CC linked by ester bonds; FC is a cyclic hexapeptide with the structure
CC Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of
CC all four siderophores depends on the hydroxylation of ornithine,
CC catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265).
CC Subsequently, the pathways for biosynthesis of extra- and intracellular
CC siderophores split (PubMed:17845073). For biosynthesis of extracellular
CC siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-
CC hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA
CC moiety is derived from mevalonate by CoA ligation and dehydration
CC catalyzed by sidI and sidH respectively (PubMed:22106303). The
CC acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the
CC constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to
CC HFC by an as yet uncharacterized enzyme during conidiation
CC (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed
CC by two different nonribosomal peptide synthetases (NRPS), sidD and sidC
CC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-
CC acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and
CC intracellular siderophores are crucial for growth during iron
CC limitation and virulence (PubMed:16113265).
CC {ECO:0000269|PubMed:15504822, ECO:0000269|PubMed:16113265,
CC ECO:0000269|PubMed:17845073, ECO:0000269|PubMed:21622789,
CC ECO:0000269|PubMed:22106303}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:21622789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21622789}.
CC -!- INDUCTION: Expression is not affected by iron availability and is not
CC regulated by the iron regulator sreA (PubMed:21622789).
CC {ECO:0000269|PubMed:21622789}.
CC -!- DISRUPTION PHENOTYPE: Decreases ferricrocin (FC) biosynthesis during
CC iron starvation and completely blocks FC biosynthesis during iron-
CC replete growth (PubMed:21622789). Blocks conidial accumulation of FC-
CC derived hydroxyferricrocin (HFC) under iron-replete conditions, which
CC delays germination and decreases the size of conidia and their
CC resistance to oxidative stress (PubMed:21622789).
CC {ECO:0000269|PubMed:21622789}.
CC -!- SIMILARITY: Belongs to the lysine N-acyltransferase mbtK family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000007; EAL88155.1; -; Genomic_DNA.
DR RefSeq; XP_750193.1; XM_745100.1.
DR AlphaFoldDB; Q4WJX7; -.
DR SMR; Q4WJX7; -.
DR STRING; 746128.CADAFUBP00000473; -.
DR EnsemblFungi; EAL88155; EAL88155; AFUA_1G04450.
DR GeneID; 3507316; -.
DR KEGG; afm:AFUA_1G04450; -.
DR eggNOG; ENOG502RZMI; Eukaryota.
DR HOGENOM; CLU_027095_1_0_1; -.
DR InParanoid; Q4WJX7; -.
DR OMA; PRQGETF; -.
DR OrthoDB; 985920at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR SMART; SM01006; AlcB; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="Acyltransferase sidL"
FT /id="PRO_0000444393"
FT REGION 51..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000255"
SQ SEQUENCE 484 AA; 54809 MW; EA45FA3FF7A86AEC CRC64;
MRNTICRLPN GQSYTVTPVF GGVNFKSNDM HLKDSIIPPG WTIVLYTNQN TDQPAQDSVP
PEEERGRSRY TQGEAEEKTR TTRFTTPTLN DDCFYISFIV NPPSTDFKPP VSPTRQIAMM
IWVSLYWYFH EPEPDLHLQT DAASQTPLTG KPKGEWRIHL KREGIFKGRN LLQKLERMGL
IASEESSVGL EPSETQESGA WSRMFVSRRS FWQIDPRIFV FTLVPANPLH SAPSSPFISP
RFASPSRESP IPTESPASPT GKDFPLHMPN EGPFASSSHL PTYFPPPPTQ YTFTNGLRHP
VRPKPPHQGE VFYIRFIPSV GQYLSFRVPI LSSSATPSRG HGHSHSTSSI EVPPQTTPSD
LDLLHKWMND PRVSAAWGEG GPKEKQEKFL RNNLTSRHSF PVIGCWDGKP FGYFEIYWVK
EDRLGALIGG ADNYDRGIHL LVGEQEYRGS HRVAIWLSAL VHYCWLADPR TQTVMLEPRV
DNEK
