ACON2_ASPFU
ID ACON2_ASPFU Reviewed; 799 AA.
AC Q4WJ90;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Putative aconitate hydratase, mitochondrial;
DE AltName: Full=Aconitase 2;
DE EC=4.2.1.-;
DE Flags: Precursor;
GN Name=acoB; ORFNames=Afu1g06810;
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 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 -!- FUNCTION: Has no detectable activity towards cis-acontiate or cis-
CC homoaconitate. {ECO:0000269|PubMed:23106124}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed on glucose medium and on ethanol.
CC {ECO:0000269|PubMed:23106124}.
CC -!- MISCELLANEOUS: The fermenting yeast S.cerevisiae has 2 aconitases, ACO1
CC essential for the citric acid cycle, and ACO2 specifically and
CC exclusively contributing to lysine biosynthesis. In contrast, in
CC respiring filamentous fungi the ACO2 homologs (acoB) seem enzymatically
CC inactive and the ACO1 homolog (acoA) is solely responsible for these
CC functions.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000007; EAL88392.1; -; Genomic_DNA.
DR RefSeq; XP_750430.1; XM_745337.1.
DR AlphaFoldDB; Q4WJ90; -.
DR SMR; Q4WJ90; -.
DR STRING; 746128.CADAFUBP00000707; -.
DR PRIDE; Q4WJ90; -.
DR EnsemblFungi; EAL88392; EAL88392; AFUA_1G06810.
DR GeneID; 3507689; -.
DR KEGG; afm:AFUA_1G06810; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; Q4WJ90; -.
DR OMA; GRASYMR; -.
DR OrthoDB; 190960at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032543; P:mitochondrial translation; IEA:EnsemblFungi.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:EnsemblFungi.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..799
FT /note="Putative aconitate hydratase, mitochondrial"
FT /id="PRO_0000425363"
FT REGION 538..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201..203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 494
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 685..686
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 799 AA; 85101 MW; CEBB02692BF63E5E CRC64;
MVRQLVWQRA TASRRLAPKC LSPQQLFARR GLATEASAAR MPPYPKIVRN LEQVRKVLGS
SRALTLAEKI LYAHLDNAEE SLLTGTNNGK DIRGKANLKL KPDRVAMQDA SAQMALLQFM
SCGLPSTAVP ASIHCDHMIV GERGADTDLP ASIEGNREVF DFLESAAKRY GIEFWPPGAG
IIHQSVLENY AAPGLMMLGT DSHTPNAGGL GAIAIGVGGA DAVDALVDAP WELKAPRILG
VRLEGRLSGW ASPKDIILHL AGKLTVRGGT GYVIEYHGPG VETLSCTGMA TCCNMGAEVG
ATTSVFPFSP SMVPYLQATH RGHVAQAAAE IAASGPKNLL RADDGAEYDQ LITIDLSTLE
PHVNGPFTPD LSVRLSDFAN TVRENKWPET LGAGLIGSCT NSSYEDMTRA EDLVKQASAA
GLKPKADFFI TPGSEQIRAT LDRDQTLASF SEAGGTVLAN ACGPCIGQWK RTDGVAKGED
NAIFTSYNRN FPGRNDGNRR TMNFLASPEI VTALAYSGST TFNPMTDTLK TPSGEEFKFR
PPQGSDLPSA GFADGNPALQ PSAGVPDASV EVIVSPTSER LALLEPFAPF PEGELSGLKV
LYKVKGQCTT DTISAAGPWL KYKGHLPNIS ANTLIGAVNA ATGETNVAYD DAGNKHSIPD
LAARWKADGI EWLVVAEDNY GEGSAREHAA LQPRYLGGRI IVAKSFARIH ETNLKKQGVV
PLTFADKADY DRIDACDQVD TVGLYETLQS GGQGSIQLQV TKKSGEKLTI PVNHTLSKDQ
CGFILAGSAL NLLAKRAHQ
