SIDF_ASPFU
ID SIDF_ASPFU Reviewed; 462 AA.
AC Q4WF55;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF {ECO:0000303|PubMed:17845073};
DE Short=Hydroxyornithine transacylase sidF {ECO:0000303|PubMed:17845073};
DE EC=2.3.1.- {ECO:0000305|PubMed:17845073};
DE AltName: Full=Siderophore biosynthesis protein F {ECO:0000303|PubMed:17845073};
GN Name=sidF {ECO:0000303|PubMed:17845073}; ORFNames=AFUA_3G03400;
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, DISRUPTION PHENOTYPE, AND INDUCTION.
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.
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: Hydroxyornithine transacylase; part of the siderophore
CC biosynthetic pathway (PubMed:17845073, PubMed:23617799). Aspergillus
CC fumigatus produces 4 types of siderophores, low-molecular-mass iron
CC chelators, including excreted fusarinine C (FsC) and
CC triacetylfusarinine C (TAFC) for iron uptake and intacellular
CC ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial
CC iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-
CC anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by
CC ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-
CC (N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four
CC siderophores depends on the hydroxylation of ornithine, catalyzed by
CC 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:17845073}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:23617799}.
CC Note=Targeted to peroxisomes via its PTS1-type peroxisomal targeting
CC signal and the corresponding receptor pexE (PubMed:23617799).
CC {ECO:0000269|PubMed:23617799}.
CC -!- INDUCTION: Expression is induced during iron starvation
CC (PubMed:17845073). {ECO:0000269|PubMed:17845073}.
CC -!- DISRUPTION PHENOTYPE: Prevents synthesis of TAFC and FsC without
CC affecting FC production (PubMed:17845073).
CC {ECO:0000269|PubMed:17845073}.
CC -!- SIMILARITY: Belongs to the lysine N-acyltransferase mbtK family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000010; EAL86622.1; -; Genomic_DNA.
DR RefSeq; XP_748660.1; XM_743567.1.
DR AlphaFoldDB; Q4WF55; -.
DR SMR; Q4WF55; -.
DR STRING; 746128.CADAFUBP00004400; -.
DR EnsemblFungi; EAL86622; EAL86622; AFUA_3G03400.
DR GeneID; 3506152; -.
DR KEGG; afm:AFUA_3G03400; -.
DR VEuPathDB; FungiDB:Afu3g03400; -.
DR eggNOG; ENOG502SMIQ; Eukaryota.
DR HOGENOM; CLU_039848_1_0_1; -.
DR InParanoid; Q4WF55; -.
DR OMA; KLHFDPH; -.
DR OrthoDB; 985920at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005777; C:peroxisome; IDA:AspGD.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:AspGD.
DR GO; GO:1900551; P:N',N'',N'''-triacetylfusarinine C biosynthetic process; IMP:AspGD.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:AspGD.
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; Peroxisome; Reference proteome; Transferase.
FT CHAIN 1..462
FT /note="N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme
FT A-N(5)-transacylase sidF"
FT /id="PRO_0000444392"
FT REGION 88..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 460..462
FT /note="PTS1-type peroxisomal targeting signal"
FT /evidence="ECO:0000269|PubMed:23617799"
SQ SEQUENCE 462 AA; 53305 MW; 1C147C3570155304 CRC64;
MATQSSTELP QINMTTAEPT SANKRTYPWV KLPHPYLTSY AIHVVSESTP RVLQLRLHDD
QKGQALPEPL HSASLTYTDI AFDEAAQEIP DNDNSPWARS RRAPGTSFHW TGQEPPTLGQ
IWNVIHALFL TYPQHEIVRL DLNGSGKDII REECLRTGLA VPFPSPRVPF GTENRPSETD
TLILLRSAFW QGAGSPVGPR PIWAVDHGIH GLLRRSGSSY PPLAQNYEFS MKFPSERIYT
RHPIRPQKPA PGSLVYSRYI PHLDQHFSLM VVDWQNEEHL QLFHKWQNDP RVAKGWNETG
DLEHHRNYLR QLHEDKHVLC LFGRFDDFPF SYFEVYWAKE DHYGAHYDAG DYDRGRHSLV
GESSVRGAYR VNAWWSSLIH YIFLDEPRTM CVVGEPKATN TTVLSYENAH GLTVQKYVDL
GHKRSVHVYC SREKWFQLCP LFWDGRERPL ESSDRMAWDA KL
