ID C5FCM2_ARTOC Unreviewed; 800 AA.
AC C5FCM2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN ORFNames=MCYG_00444 {ECO:0000313|EMBL:EEQ27556.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ27556.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU362107};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU362107}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR EMBL; DS995701; EEQ27556.1; -; Genomic_DNA.
DR RefSeq; XP_002850340.1; XM_002850294.1.
DR AlphaFoldDB; C5FCM2; -.
DR STRING; 554155.C5FCM2; -.
DR GeneID; 9225481; -.
DR VEuPathDB; FungiDB:MCYG_00444; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; KWPETFG; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000002035; 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-UniRule.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW Lyase {ECO:0000256|RuleBase:RU362107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362107};
KW Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 95..519
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 601..727
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 800 AA; 84989 MW; D4A3888F24F7DCE2 CRC64;
MQVLRQRCAA GSTLTQLPLR RSGLQYRGLA TVTSSSIAPS RSPPYPKILS KLNEVRRVLG
ASRPLTLAEK NLYSHLDNVE ESLLTGTQNG KEIRGCANLK LKPDRVAMQD ASAQMALLQF
MSCGLPSTAV PASIHCDHMI VGEKGADVDL PASIKGNKEV FDFLESAAKK YGIEFWPPGA
GIIHQTVLEN YAAPGLLMLG TDSHTPNGGG LGAIAIGVGG ADAVDALVDA PWELKAPKIL
GVRLEGALNG WASPKDIILH LAGKLTVRGG TGFIIEYHGP GVETLSCTGL ATICNMGAEV
GATTSLFPFS PSMIPYLQAT NRSEIAKTAS EIASFGPQNL LSADPNAEYD QLITIDLSTL
EPHINGPFTP DLSVPLSAFA STVREKKWPE TFGAGLIGSC TNSSYQDMTR SEDLVKQASA
AGLRPKADFF ITPGSEQIRA TLERDQTLST FSSAGGTVLA NACGPCIGQW KRTDGVKKGE
PNAILTSYNR NFRGRNDGNT ATMNFLASPE IVTAMSYAGS TTFNPMTDSL TTPSGESFKF
QAPVGSDLPS AGFAAGNPDF QPSAAVPDPS AVVVVSPTSD RLALLEPFEP FPPKDLTSLR
VLYKVKGQCT TDTISAAGPW LKYKGHLPNI SANTLIGAIN AATGETNVAY DLDGKTYSIP
DLAEKWKNEG SQWLVVAEEN YGEGSAREHA ALQPRYLGGR IIVAKSFARI HETNLKKQGV
VPLTFKDKAD YDKIDACDQV DTVGLYDVLN NDGQGEVTLK VTKKSSGKTI NIPVKHTLSK
DQCGFILAGS ALNLLAAKSR
//
