ACON3_ASPFU
ID ACON3_ASPFU Reviewed; 811 AA.
AC Q4WBR0;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Putative aconitate hydratase;
DE AltName: Full=Aconitase 3;
DE EC=4.2.1.-;
GN Name=acoC; ORFNames=Afu8g07140;
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 INDUCTION.
RX PubMed=23106124; DOI=10.1111/mmi.12076;
RA Fazius F., Shelest E., Gebhardt P., Brock M.;
RT "The fungal alpha-aminoadipate pathway for lysine biosynthesis requires two
RT enzymes of the aconitase family for the isomerization of homocitrate to
RT homoisocitrate.";
RL Mol. Microbiol. 86:1508-1530(2012).
CC -!- INDUCTION: Very low expression levels near the detection limit.
CC {ECO:0000269|PubMed:23106124}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000013; EAL85474.1; -; Genomic_DNA.
DR RefSeq; XP_747512.1; XM_742419.1.
DR AlphaFoldDB; Q4WBR0; -.
DR SMR; Q4WBR0; -.
DR STRING; 746128.CADAFUBP00007855; -.
DR EnsemblFungi; EAL85474; EAL85474; AFUA_8G07140.
DR GeneID; 3504966; -.
DR KEGG; afm:AFUA_8G07140; -.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_006714_3_3_1; -.
DR InParanoid; Q4WBR0; -.
DR OMA; FQRNMPS; -.
DR OrthoDB; 265826at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR02087; LEUD_arch; 1.
PE 2: Evidence at transcript level;
KW Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..811
FT /note="Putative aconitate hydratase"
FT /id="PRO_0000425365"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 504
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 507
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 686..687
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 811 AA; 89266 MW; 69BCC7A5B564824A CRC64;
MSGTYNNSSV QIYRILEQTR HIRLDDTSSE SKAKYSKAKI ASAIGLLSHL RDLTEILQNL
RHVRESSALA DVLRVCIQPH DLGGLGLDDA SDLAAQQESE VLFLVSAWLE ALNSEDRARS
MPAPVASRPP GRRGMTLSEK IFAWHEVAYR GWVAPGDLIR VDVDWVIASE ASWAGMETTY
SDLGKPGIHR NDRFWLAGDH VVDPRIRQIP KVRALIDASE RAKRVFKLTE YQGMNYTILH
TEFYRERAQP GMLIIGSDSH TCSSGALGCL AIGLGAADVT LPLVTGETWV KVPESISIRL
VGVPKPGIGG KDVILYILQQ LKRNTVASDR IVEFSGAGVQ YLSADARFAI CNMTAELCGI
TGIFVPDQIT RAFVANRRLQ RHKNLITYFR PDNDAQYAAE LDIDLANVQS FFARYPRPDD
VVPVSDYAGM QLDGCFIGAC TTTEEDLILA ALVLEQGLKK GYRPVNHGKR KMVPGSLPIL
HRLRELCLTG VFEAAGFEIG VPGCSYCVGM SADQAVSGEV WLSSQNRNFE NRMGKGHLVS
SATVAASSFE MKLTDPNDLL CGIDWARWMS LRGPFGLTAR MSAASHLTYV EPNNSPAFSQ
ERPESSIFSR STQEPPFSGP LRGKIQLLGD FIDTDALAPA EFLMDMKTNE QSGLHCLQHT
HPLFRQRTLE GFNIVVAGQA FGCGSSREQA VMALLGCGIK CVIAKSFAFI FQRNMPNLGL
LGITMPNESF YAAAKDGSEV SIDLLAQVIH IEGLRFVFQL SQMEQGLYRH GGITSAFRKF
GNRLFEELTA AKNIGTSHME EKCHAPSALQ W
