ACON_ARTBC
ID ACON_ARTBC Reviewed; 775 AA.
AC D4AT77;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000250|UniProtKB:P20004};
DE Short=Aconitase {ECO:0000250|UniProtKB:P20004};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P20004};
DE AltName: Full=Citrate hydro-lyase {ECO:0000250|UniProtKB:P20004};
DE Flags: Precursor;
GN ORFNames=ARB_07441;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000250|UniProtKB:P20004}.
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:0000250|UniProtKB:P20004};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P20004};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S]
CC cluster leads to an inactive enzyme. {ECO:0000250|UniProtKB:P20004};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:P20004}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P20004}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P20004}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABSU01000009; EFE33496.1; -; Genomic_DNA.
DR RefSeq; XP_003014136.1; XM_003014090.1.
DR AlphaFoldDB; D4AT77; -.
DR SMR; D4AT77; -.
DR STRING; 663331.D4AT77; -.
DR EnsemblFungi; EFE33496; EFE33496; ARB_07441.
DR GeneID; 9521551; -.
DR KEGG; abe:ARB_07441; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; GCIGMGQ; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 4Fe-4S; Glycoprotein; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..775
FT /note="Aconitate hydratase, mitochondrial"
FT /id="PRO_0000434923"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 188..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 381
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 444
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 447
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 603
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT BINDING 666..667
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20004"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 775 AA; 84060 MW; C04B6927F27AD67F CRC64;
MLTTLARASA MLLGARGFAS AADLDKKVEM TNWEKGNYIN YKKMAENLDI VRARLNRPLT
FAEKILYSHL DDPHGQEIER GKSYLKLRPD RVACQDATAQ MAILQFMSAG MPSVATPATV
HCDHLIEAQL GGDKDLARAN EINKEVYDFL STSCAKYNIG FWKPGSGIIH QILLENYCFP
GGLMIGTDSH TPNGGGLGMA AIGVGGADAV DVMAGLPWEL KAPNVIGVKL TGQMSGWTAP
KDIILKVAGI LTVKGGTGAI IEYHGDGVNS LSCTGMGTIC NMGAEIGATT SVFPFNDRMY
DYLKATKRQS IGDFSRVYAE GLRPDENAQY DQLIEINLSE LEPHINGPFT PDLATPISKF
KEAVKENNWP SELKVGLIGS CTNSSYEDMS RAASIARDAL NHGIKAKSLF TVTPGSEQIR
ATIERDGQLK TLEEFGGVIL ANACGPCIGQ WDRKDVKKNE ANSIISSYNR NFTGRNDANP
ATHAFVTSPD LVVALTIAGT LNFNPLTDKL KDKDGNEFML APPTGEGLPA NGYDPGRDTY
QAPPADRASI SVAVSPSSDR LQILEPFKAW DGKDAKGIPI LIKCEGKTTT DHISMAGPWL
KYRGHLDNIS NNLLIGAVNA ENGERNSVKN FETGEYDSVP ATARAYKARG IPWVVIGDWN
YGEGSSREHA ALQPRHLGGM AIITRSFARI HETNLKKQGM LPLTFADPAD YDRIPPTAMV
DLMCTELAVG KPMTLRVHPK DGASFDVKLS HTFNESQIEW FKNGSALNTM AKKAQ
