SIDI_ASPFU
ID SIDI_ASPFU Reviewed; 590 AA.
AC Q4WR83;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Acyl-CoA ligase sidI {ECO:0000303|PubMed:22106303};
DE EC=6.2.1.- {ECO:0000305|PubMed:22106303};
DE AltName: Full=Siderophore biosynthesis protein I {ECO:0000303|PubMed:22106303};
GN Name=sidI {ECO:0000303|PubMed:22106303}; ORFNames=AFUA_1G17190;
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 INDUCTION.
RX PubMed=18721228; DOI=10.1111/j.1365-2958.2008.06376.x;
RA Schrettl M., Kim H.S., Eisendle M., Kragl C., Nierman W.C., Heinekamp T.,
RA Werner E.R., Jacobsen I., Illmer P., Yi H., Brakhage A.A., Haas H.;
RT "SreA-mediated iron regulation in Aspergillus fumigatus.";
RL Mol. Microbiol. 70:27-43(2008).
RN [6]
RP FUNCTION.
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
RN [8]
RP SUBCELLULAR LOCATION, PEROXISOMAL TARGETING SIGNAL, AND FUNCTION.
RX PubMed=23617799; DOI=10.1111/mmi.12225;
RA Gruendlinger M., Yasmin S., Lechner B.E., Geley S., Schrettl M., Hynes M.,
RA Haas H.;
RT "Fungal siderophore biosynthesis is partially localized in peroxisomes.";
RL Mol. Microbiol. 88:862-875(2013).
CC -!- FUNCTION: Acyl-CoA ligase; part of the siderophore biosynthetic pathway
CC (PubMed:22106303). 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:22106303}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23617799}.
CC Note=Targeted to peroxisomes via its PTS2-type peroxisomal targeting
CC signal and the corresponding receptor pexG (PubMed:23617799).
CC {ECO:0000269|PubMed:23617799}.
CC -!- DISRUPTION PHENOTYPE: Blocks TAFC biosynthesis, decreases resistance to
CC oxidative stress, and attenuates virulence in a murine model of
CC invasive pulmonary aspergillosis (PubMed:22106303).
CC {ECO:0000269|PubMed:22106303}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000004; EAL91049.1; -; Genomic_DNA.
DR RefSeq; XP_753087.1; XM_747994.1.
DR AlphaFoldDB; Q4WR83; -.
DR SMR; Q4WR83; -.
DR STRING; 746128.CADAFUBP00001626; -.
DR EnsemblFungi; EAL91049; EAL91049; AFUA_1G17190.
DR GeneID; 3510119; -.
DR KEGG; afm:AFUA_1G17190; -.
DR VEuPathDB; FungiDB:Afu1g17190; -.
DR eggNOG; KOG1177; Eukaryota.
DR HOGENOM; CLU_000022_59_7_1; -.
DR InParanoid; Q4WR83; -.
DR OMA; CEQYISV; -.
DR OrthoDB; 386992at2759; -.
DR PHI-base; PHI:2321; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005777; C:peroxisome; IDA:AspGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:AspGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:AspGD.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:AspGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0031171; P:ferricrocin biosynthetic process; IMP:AspGD.
DR GO; GO:1900551; P:N',N'',N'''-triacetylfusarinine C biosynthetic process; IMP:AspGD.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Peroxisome; Reference proteome.
FT CHAIN 1..590
FT /note="Acyl-CoA ligase sidI"
FT /id="PRO_0000444397"
FT MOTIF 6..14
FT /note="PTS2-type peroxisomal targeting signal"
FT /evidence="ECO:0000269|PubMed:23617799"
FT BINDING 220..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 359..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 472..474
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 543..545
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 590 AA; 64956 MW; 3867ABE9CEE36250 CRC64;
MATIRRLQQT LSHLRPPKAP QLLSIVEGPT QPELLDITLG ELLTLQSLQY GDYECLVFPW
TGARWTYTDL KDEADRVARG LLAMGIQKGD RIGIMAGNCE QYISVFFAAA RVGAILVVLN
NTYTPSELYY ALGHTDCRLL FLTPRIGRHS LEEVLAKLGP RPKEQGTSSA LEEIIILRGQ
YSGFSTYEHV IQRGLPLPSH ALQDREAELH STDVCNLQFT SGSTGNPKAA MLTHHNLVNN
SRFIGDRMNL TSFDILCCPP PLFHCFGLVL GMLAVVTHGS KIIFPSETFD PTAVLHAISD
EKCTALHGVP TMFEAILSLP KPPNFDCSNL RTGIIAGAPV PRPLMKRLLE ELNMTEYTSS
YGLTEASPTC FNALTTDSIE RRLTTVGKVM PHAKAKIIDT QGHIVPIGQR GELCIAGYQL
TKGYWNNPEK TAEALITDSD GVTWLKTGDE AIFDEEGYCS ITGRFKDIII RGGENIYPLE
IEERLAAHPA IEVASVIGIP DQKYGEVVGA FLALAADVSA RPSDEELRAW TRETLGRHKA
PQYFFVFGEE GVDRTIPVTG SGKVRKVDLR KIAASVLERR LAKTAAIKEK
