ACON_ASPFU
ID ACON_ASPFU Reviewed; 787 AA.
AC Q4WLN1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Afu6g12930;
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, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION
RP PHENOTYPE, 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: Constitutively expressed on glucose medium and increased
CC expression on ethanol. {ECO:0000269|PubMed:23106124}.
CC -!- DISRUPTION PHENOTYPE: Essential for growth.
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. {ECO:0000305|PubMed:23106124}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL89133.1; -; Genomic_DNA.
DR RefSeq; XP_751171.1; XM_746078.1.
DR AlphaFoldDB; Q4WLN1; -.
DR SMR; Q4WLN1; -.
DR STRING; 746128.CADAFUBP00000176; -.
DR SwissPalm; Q4WLN1; -.
DR PRIDE; Q4WLN1; -.
DR EnsemblFungi; EAL89133; EAL89133; AFUA_6G12930.
DR GeneID; 3508478; -.
DR KEGG; afm:AFUA_6G12930; -.
DR VEuPathDB; FungiDB:Afu6g12930; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR InParanoid; Q4WLN1; -.
DR OMA; GCIGMGQ; -.
DR OrthoDB; 190960at2759; -.
DR UniPathway; UPA00033; UER00029.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000002530; Chromosome 6.
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..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..787
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000425361"
FT REGION 529..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197..199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 612
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 675..676
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 787 AA; 85529 MW; CDDE6C7797EE5E8F CRC64;
MISTRLARAG ALAPKSRLFL GTRAFATVGD SPLDKKVEMA NTEKGNYINY KKMSENLDIV
RRRLQRPLTY AEKVLYSHLD DPHGQEIERG KSYLKLRPDR VACQDATAQM AILQFMSAGM
PSVATPTTVH CDHLIEAQVG GDKDLARANE INKEVYDFLA SATAKYNIGF WKPGSGIIHQ
IVLENYAFPG GLMIGTDSHT PNAGGLAMAA IGVGGADAVD VMAGLPWELK APKVIGVKLT
GEMSGWTTPK DVILKVAGLL TVKGGTGAII EYHGPGVTSL SCTGMGTICN MGAEIGATTS
MFPFNDRMYD YLKATKRQHI GDFAREYAKE LREDEGAEYD QLIEINLSEL EPHINGPFTP
DLATPISKFK EAVETNKWPE ELKVGLIGSC TNSSYEDMSR AASIARDALN HGLKAKSLFT
VTPGSEQIRA TIERDGQLQT LEEFGGVILA NACGPCIGQW DRRDVKKGEP NSIISSYNRN
FTGRNDANPA THAFVASPDL VVAMTIAGTL KFNPLTDKLK DKDGNEFLLQ PPTGEGLPAK
GYDPGRDTYQ APPADRSSVN VAVSPTSDRL QLLAGFEPWD GKDANGIPIL IKCQGKTTTD
HISMAGPWLK YRGHLDNISN NMLIGAVNAE NGKANSVKNK FTGEYDAVPA TARDYKARGV
KWVVIGDWNY GEGSSREHAA LEPRHLGGLA IITRSFARIH ETNLKKQGML PLTFADPADY
DKINPEDTVD LLCTQLEVGK PMTLRVHPKD GSAPFDISLN HTFNESQIEW FKDGSALNTM
ARKSGAK
