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Database: UniProt
Entry: ACON2_ASPFU
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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   24-JAN-2024, entry version 105.
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   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
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 / CBS 101355 / FGSC A1100 / Af293;
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; 330879.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; 3266779at2759; -.
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: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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 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   NCBIfam; TIGR01340; aconitase_mito; 1.
DR   PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR   PANTHER; PTHR43160:SF2; HOMOCITRATE DEHYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 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
//
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