ACON2_EMENI
ID ACON2_EMENI Reviewed; 796 AA.
AC Q5B6D6; C8V6B4;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative aconitate hydratase, mitochondrial;
DE AltName: Full=Aconitase 2;
DE EC=4.2.1.-;
DE Flags: Precursor;
GN Name=acoB; ORFNames=AN3894;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
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 -!- 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; AACD01000062; EAA59159.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75152.1; -; Genomic_DNA.
DR RefSeq; XP_661498.1; XM_656406.1.
DR AlphaFoldDB; Q5B6D6; -.
DR SMR; Q5B6D6; -.
DR STRING; 162425.CADANIAP00004807; -.
DR EnsemblFungi; CBF75152; CBF75152; ANIA_03894.
DR EnsemblFungi; EAA59159; EAA59159; AN3894.2.
DR GeneID; 2873316; -.
DR KEGG; ani:AN3894.2; -.
DR VEuPathDB; FungiDB:AN3894; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; Q5B6D6; -.
DR OMA; GRASYMR; -.
DR OrthoDB; 190960at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron; Iron-sulfur; Lyase; Metal-binding; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..796
FT /note="Putative aconitate hydratase, mitochondrial"
FT /id="PRO_0000425364"
FT REGION 540..569
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 796 AA; 85011 MW; 6E38FFEA163D1C69 CRC64;
MLRQIVSQRS AARRQLIDQL APCLRRGLAT ATDSTPTSSR MPPYSKIVQN LEQVRKVLGS
SRALTLAEKI LYSHLDNAEE SLLTGTNNGR DIRGKADLKL KPDRVAMQDA SAQMALLQFM
SCGLPSTAVP ASIHCDHMIV GERGADTDLP ASIQGNKEVF DFLESASKRY GIEFWPPGAG
IIHQSVLENY SAPGLMMLGT DSHTPNAGGL GAIAIGVGGA DAVDALVDAP WELKAPRILG
VRLEGKLQGW AAPKDIILHL AGKLTVRGGT GFVIEYHGPG VETLSTTGMA TICNMGAEVG
ATTSLFPFSP NHVPYLKATN RADVAEAAAK IASAGSSSLL RADTSAEYDE LITIDLSTLE
PHINGPFTPD LSVPLSRFAE TVRKNNWPET FNAGLIGSCT NSSYEDMTRA EHLVKQANAA
GLKPKADLFI TPGSEQIRAT LDRDQTLSTF SSAGGTVLAN ACGPCIGQWK RTDDVPKGTD
NAIFTSYNRN FPGRNDGNRR TMNFLASPEL VTALTYAGST TFNPVTDSIT TPSGSEFRFE
PPTGQDLPSK GFEAGNPAFQ PSAPVPDSSV EVKVSPTSTR LALLEPFAPF PNSDLQNLSV
LYKVKGQCTT DTISAAGPWL KYKGHLPNIS ANTLIGAVNA ATGETNVAYD EAGKQHTIPD
LAAQWKAQGR EWLVVAEENY GEGSAREHAA LQPRYLGGRV ILAKSFARIH ETNLKKQGVV
PLTFADKADY DRIDACDVVA TEGLYETLKN GGKGEVKLRV TKKSGEEIVI PVKHTLSADQ
SSFILAGSAL NVLSKR
