ACON_EMENI
ID ACON_EMENI Reviewed; 783 AA.
AC C8VG90; Q5B1Q5; Q8J267;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Aconitate hydratase, mitochondrial;
DE Short=Aconitase;
DE EC=4.2.1.3 {ECO:0000269|PubMed:23106124};
DE AltName: Full=Citrate hydro-lyase;
DE AltName: Full=Homocitrate dehydratase;
DE EC=4.2.1.- {ECO:0000269|PubMed:23106124};
DE Flags: Precursor;
GN Name=acoA; ORFNames=AN5525;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 386-783, AND INDUCTION.
RX PubMed=12406779; DOI=10.1128/aem.68.11.5769-5772.2002;
RA Oberegger H., Schoeser M., Zadra I., Schrettl M., Parson W., Haas H.;
RT "Regulation of freA, acoA, lysF, and cycA expression by iron availability
RT in Aspergillus nidulans.";
RL Appl. Environ. Microbiol. 68:5769-5772(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MISCELLANEOUS.
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: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate, a step in the citric acid cycle. Also catalyzes the
CC reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step
CC in the alpha-aminoadipate pathway for lysine biosynthesis.
CC {ECO:0000269|PubMed:23106124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000269|PubMed:23106124};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-homocitrate = cis-homoaconitate + H2O;
CC Xref=Rhea:RHEA:26101, ChEBI:CHEBI:15377, ChEBI:CHEBI:58174,
CC ChEBI:CHEBI:58884; Evidence={ECO:0000269|PubMed:23106124};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2.
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 2/5.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- INDUCTION: Down-regulated under iron limitation conditions.
CC {ECO:0000269|PubMed:12406779}.
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. {ECO:0000305|PubMed:23106124}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA62685.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000094; EAA62685.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF515630; AAN61439.1; -; mRNA.
DR EMBL; BN001305; CBF81741.1; -; Genomic_DNA.
DR RefSeq; XP_663129.1; XM_658037.1.
DR AlphaFoldDB; C8VG90; -.
DR SMR; C8VG90; -.
DR STRING; 162425.CADANIAP00003560; -.
DR PRIDE; C8VG90; -.
DR EnsemblFungi; CBF81741; CBF81741; ANIA_05525.
DR EnsemblFungi; EAA62685; EAA62685; AN5525.2.
DR GeneID; 2871810; -.
DR KEGG; ani:AN5525.2; -.
DR VEuPathDB; FungiDB:AN5525; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; C8VG90; -.
DR OMA; GCIGMGQ; -.
DR OrthoDB; 190960at2759; -.
DR UniPathway; UPA00033; UER00029.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
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; IDA:AspGD.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Iron; Iron-sulfur; Lyase; Lysine biosynthesis;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..783
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000425362"
FT REGION 524..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 610
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 673..674
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 386..395
FT /note="GSCTNSSYED -> LSSLLLLVES (in Ref. 3; AAN61439)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 84968 MW; 3BD3AD385D3C151C CRC64;
MITTRLARMG ALAPKSRLLF GTRGMATVAD LDKKVEMCNL EKGNYINYKK MSENLDVVRR
RLTRPLTYAE KILYSHLDDP QNQDIERGKS YLKLRPDRVA CQDATAQMAI LQFMSAGMPS
VATPTTVHCD HLIEAQLGGE KDLARANEIN KEVYDFLASS TAKYNIGFWK PGSGIIHQII
LENYAFPGGL MIGTDSHTPN AGGLAIAAIG VGGADAVDVM AGLPWELKAP KVIGVRLTGE
MSGWTAPKDI ILKVAGLLTV KGGTGAIIEY HGPGVNSLSA TGMATICNMG AEIGATTSLF
PFNDRMYDYL KATKRQQIGD FARSYAKDLR EDEGAEYDQL IEINLSELEP HINGPFTPDL
ATPISQFKEA VKANGWPEEL KVGLIGSCTN SSYEDMSRAA SIAQDALDHG LKAKSIFTVT
PGSEQIRATI ERDGQLKTLE EFGGVILANA CGPCIGQWDR KDVKKGTPNS IVSSYNRNFT
GRNDANPATH AFVTSPDLVV ALSIAGTLNF NPLTDTLKDK DGKEFKLKAP TGDGLPSRGY
DPGRDTYQAP PTDRSSVDVA VSPSSDRLQL LAGFQPWDGK DATGIPILIK CQGKTTTDHI
SMAGPWLKYR GHLDNISNNM LIGAVNAENG EANKIKNVFT GEYGAVPATA RDYKARGVKW
VVIGDWNYGE GSSREHAALE PRHLGGLAII TRSFARIHET NLKKQGMLPL TFSDPADYDR
IPPDATVDLL CTELAVDKPM TLRVHPKDGA SFDVKLSHTF NESQIEWFKD GSALNTMARK
SGN
