SIDJ_ASPFU
ID SIDJ_ASPFU Reviewed; 354 AA.
AC Q4WF56;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Fusarinine C esterase sidJ {ECO:0000303|PubMed:24038704};
DE EC=3.1.-.- {ECO:0000269|PubMed:24038704};
GN Name=sidJ {ECO:0000303|PubMed:24038704}; ORFNames=AFUA_3G03390;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=24038704; DOI=10.1128/aem.01285-13;
RA Gruendlinger M., Gsaller F., Schrettl M., Lindner H., Haas H.;
RT "Aspergillus fumigatus SidJ mediates intracellular siderophore
RT hydrolysis.";
RL Appl. Environ. Microbiol. 79:7534-7536(2013).
CC -!- FUNCTION: Displays specific fusarinine C (FsC) esterase activity but
CC does not hydrolyze triacetylfusarinine C (TAFC), which has the same
CC core structure as fusarinine C (PubMed:24038704). Both extra- and
CC intracellular siderophores have been shown to be crucial for the
CC virulence (PubMed:24038704). Subsequent to chelation of iron and
CC uptake, FsC and TAFC are hydrolyzed and the iron is transferred to the
CC metabolism or to the intracellular siderophore ferricrocin (FC) for
CC transport and storage of iron (PubMed:24038704).
CC {ECO:0000269|PubMed:24038704}.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased growth and increased
CC intracellular accumulation of hydrolysis products of the siderophore
CC fusarinine C (PubMed:24038704). {ECO:0000269|PubMed:24038704}.
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DR EMBL; AAHF01000010; EAL86621.1; -; Genomic_DNA.
DR RefSeq; XP_748659.1; XM_743566.1.
DR PDB; 6GUP; X-ray; 1.85 A; A/B=2-354.
DR PDBsum; 6GUP; -.
DR AlphaFoldDB; Q4WF56; -.
DR SMR; Q4WF56; -.
DR ESTHER; aspfu-q4wf56; Duf_1749.
DR EnsemblFungi; EAL86621; EAL86621; AFUA_3G03390.
DR GeneID; 3506151; -.
DR KEGG; afm:AFUA_3G03390; -.
DR eggNOG; KOG4840; Eukaryota.
DR HOGENOM; CLU_049633_3_0_1; -.
DR InParanoid; Q4WF56; -.
DR OMA; TDEIAQC; -.
DR OrthoDB; 1267782at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013744; SidJ.
DR PANTHER; PTHR31591; PTHR31591; 1.
DR Pfam; PF08538; DUF1749; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..354
FT /note="Fusarinine C esterase sidJ"
FT /id="PRO_0000444413"
FT STRAND 11..21
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 62..71
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 85..107
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 184..204
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 294..306
FT /evidence="ECO:0007829|PDB:6GUP"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:6GUP"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6GUP"
FT HELIX 334..352
FT /evidence="ECO:0007829|PDB:6GUP"
SQ SEQUENCE 354 AA; 38962 MW; 73BB6D120A95AA61 CRC64;
MYSKFWPKGG LPGILHHYTE TLVTFEYTTT TTRKPHSLLF VGGLGDGLAT TSYLADLAHA
LQPTEWSLFT LTLTSSYQSW GLGHLDRDTN EIAQCLKYIK EYKTEKFGGS ASSGKIVLMG
HSTGSQCVLH YLSRPNPHTH TPAFDPYLEH VERMPLDGAI MQAPVSDREA IQWVLAEGLG
DRTPAEIRPV FEKLTSMARE AARDADAGTD VLLPLAMTSL VYPAHTPLSA RRFLSLTSPE
SPESPSEDDL FSSDLSDEQL GKTFGMIREQ GLLRGKLMVL FSGADQSVPA WVDKDTLLSR
WRNATDHNGE AAIWDENSGI IPNASHALSN DDQAEPRNFL VNKVLGYLSA LVKA
