SIDG_ASPFU
ID SIDG_ASPFU Reviewed; 235 AA.
AC Q4WF30;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=FsC-acetyl coenzyme A-N(2)-transacetylase {ECO:0000303|PubMed:17845073};
DE EC=2.3.1.- {ECO:0000305|PubMed:17845073};
DE AltName: Full=Siderophore biosynthesis protein H {ECO:0000303|PubMed:17845073};
GN Name=sidG {ECO:0000303|PubMed:17845073}; ORFNames=AFUA_3G03650;
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).
CC -!- FUNCTION: FsC-acetyl coenzyme A-N(2)-transacetylase; part of the
CC siderophore biosynthetic pathway (PubMed:21622789). 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 -!- INDUCTION: Expression is induced during iron starvation
CC (PubMed:17845073). {ECO:0000269|PubMed:17845073}.
CC -!- DISRUPTION PHENOTYPE: Eliminates TAFC production and increases FsC
CC production about 10-fold (PubMed:17845073). Does not affect the
CC production of FC (PubMed:17845073). {ECO:0000269|PubMed:17845073}.
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DR EMBL; AAHF01000010; EAL86647.1; -; Genomic_DNA.
DR RefSeq; XP_748685.1; XM_743592.1.
DR AlphaFoldDB; Q4WF30; -.
DR SMR; Q4WF30; -.
DR STRING; 746128.CADAFUBP00004365; -.
DR EnsemblFungi; EAL86647; EAL86647; AFUA_3G03650.
DR GeneID; 3505887; -.
DR KEGG; afm:AFUA_3G03650; -.
DR VEuPathDB; FungiDB:Afu3g03650; -.
DR eggNOG; ENOG502SBCZ; Eukaryota.
DR HOGENOM; CLU_013985_3_1_1; -.
DR InParanoid; Q4WF30; -.
DR OMA; GWWVLAP; -.
DR OrthoDB; 1489439at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF13302; Acetyltransf_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Lyase; Reference proteome; Transferase.
FT CHAIN 1..235
FT /note="FsC-acetyl coenzyme A-N(2)-transacetylase"
FT /id="PRO_0000444395"
FT DOMAIN 14..190
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 106..108
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 114
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 146
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
FT BINDING 151..153
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q9I0Q8"
SQ SEQUENCE 235 AA; 26838 MW; AAD4AF6CEC58CDC4 CRC64;
MTIKAQPTLH TARLELVPLG HEHREFTMKL DMDPEVMKMV AFGRPFTEDE AIQVHTWLMN
CATSVPGFGT WVGFAEGEFV GWWVLAPVPT TENPKSFRTD RTEYGFRVSP KFWGQGYAKE
GAREMVRYAF EELGLAEVIG ETMTINMASR AVMAGCGLTH VETFFNKYDT PPPGIEEGEV
RYSITREEWL RMQKPSMTRS RWFPAFASWL PRLLLSRLWS YIFQGRRLAA GAASP
