ESTB_ASPFU
ID ESTB_ASPFU Reviewed; 292 AA.
AC Q4WF29;
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=Siderophore triacetylfusarinine C esterase {ECO:0000303|PubMed:17586718};
DE EC=3.1.-.- {ECO:0000269|PubMed:17586718};
GN Name=estB {ECO:0000303|PubMed:17586718}; ORFNames=AFUA_3G03660;
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
RC {ECO:0000312|Proteomes:UP000002530};
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, INDUCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=17586718; DOI=10.1128/ec.00066-07;
RA Kragl C., Schrettl M., Abt B., Sarg B., Lindner H.H., Haas H.;
RT "EstB-mediated hydrolysis of the siderophore triacetylfusarinine C
RT optimizes iron uptake of Aspergillus fumigatus.";
RL Eukaryot. Cell 6:1278-1285(2007).
CC -!- FUNCTION: Displays specific TAFC esterase activity but does not
CC hydrolyze fusarinine C, which has the same core structure as TAFC
CC (PubMed:17586718). Hydrolysis optimizes but is not essential for TAFC-
CC mediated iron uptake (PubMed:17586718).Both extra- and intracellular
CC siderophores have been shown to be crucial for the virulence
CC (PubMed:17586718). Subsequent to chelation of iron and uptake, FsC and
CC TAFC are hydrolyzed and the iron is transferred to the metabolism or to
CC the intracellular siderophore ferricrocin (FC) for transport and
CC storage of iron (PubMed:17586718). Hydrolyzes both TAFC and DF-TAFC
CC with equal efficiencies, suggesting that its function might not be
CC restricted to the release of iron from the siderophore but might also
CC include the degradation of the iron-free chelator to protect cells
CC (PubMed:17586718). {ECO:0000269|PubMed:17586718}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for TAFC {ECO:0000269|PubMed:17586718};
CC pH dependence:
CC Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:17586718};
CC Temperature dependence:
CC Optimum temperature is 25 to 37 degrees Celsius.
CC {ECO:0000269|PubMed:17586718};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17586718}.
CC -!- INDUCTION: Expression is induced during iron deprivation
CC (PubMed:17586718). {ECO:0000269|PubMed:17586718}.
CC -!- DISRUPTION PHENOTYPE: Eliminates TAFC esterase activity and causes
CC increased intracellular accumulation of TAFC and TAFC hydrolysis
CC products (PubMed:17586718). Reduces the intracellular transfer rate of
CC iron from TAFC to DF-FC and delays iron sensing (PubMed:17586718).
CC Causes a decreased radial growth rate under iron-depleted but not iron-
CC replete conditions (PubMed:17586718). {ECO:0000269|PubMed:17586718}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; AAHF01000010; EAL86648.1; -; Genomic_DNA.
DR RefSeq; XP_748686.1; XM_743593.1.
DR PDB; 6GUD; X-ray; 1.70 A; A/B=3-292.
DR PDB; 6GUG; X-ray; 1.45 A; A/B=3-292.
DR PDB; 6GUI; X-ray; 1.70 A; A/B=3-292.
DR PDB; 6GUL; X-ray; 2.30 A; A/B=3-292.
DR PDB; 6GUR; X-ray; 2.10 A; A/B=3-292.
DR PDBsum; 6GUD; -.
DR PDBsum; 6GUG; -.
DR PDBsum; 6GUI; -.
DR PDBsum; 6GUL; -.
DR PDBsum; 6GUR; -.
DR AlphaFoldDB; Q4WF29; -.
DR SMR; Q4WF29; -.
DR STRING; 330879.Q4WF29; -.
DR ESTHER; aspfu-q4wf29; A85-IroE-IroD-Fes-Yiel.
DR EnsemblFungi; EAL86648; EAL86648; AFUA_3G03660.
DR GeneID; 3505888; -.
DR KEGG; afm:AFUA_3G03660; -.
DR VEuPathDB; FungiDB:Afu3g03660; -.
DR eggNOG; ENOG502SII4; Eukaryota.
DR HOGENOM; CLU_039834_3_0_1; -.
DR InParanoid; Q4WF29; -.
DR OMA; QVSWPLH; -.
DR OrthoDB; 979550at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IDA:AspGD.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IMP:AspGD.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:AspGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..292
FT /note="Siderophore triacetylfusarinine C esterase"
FT /id="PRO_0000444421"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6GUD"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 137..147
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6GUD"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:6GUG"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:6GUG"
FT STRAND 255..262
FT /evidence="ECO:0007829|PDB:6GUG"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:6GUG"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:6GUG"
SQ SEQUENCE 292 AA; 32681 MW; A9744D169390F7A7 CRC64;
MGDRPTPVPL PNSEQFYLEN DRGEPYLIQV SWPLHWEDKQ TGRGPLPIIY IVDGNALFLT
ATEAAWRRAA ASHFAGGGII VAIGYPLKGK LYDARRRSFD LTPPTACAPV GYGGADVFLD
FIENSVRPAV QARFPQVSLA REALYGHSYG GLLALHALFT RPQSFDCYIA SSPSIWWNSL
CILHEAKAFV ETKKVSHDQS PSLMVSWGSW EQHPPRWADE LLDHYEARKR TAAELRMADN
ALDLCAMLHG CSRLHALIKT EYEGEDHTSV MSCSVSRGLT MFFEDWPFHQ SG
