ID A0A197JJY6_9FUNG Unreviewed; 789 AA.
AC A0A197JJY6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=K457DRAFT_23233 {ECO:0000313|EMBL:OAQ25288.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ25288.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ25288.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ25288.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362107}.
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DR EMBL; KV442080; OAQ25288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JJY6; -.
DR STRING; 1314771.A0A197JJY6; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000078512; 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; PS00450; ACONITASE_1; 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:UP000078512};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 66..502
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 584..712
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 789 AA; 85434 MW; 2EF42ABB9A4AB40C CRC64;
MSFLKPLTRT PRSRWTTSTL RTLATEASTT RPARDCTRIT PPYAKLVSNL EKVKRVLDNR
PLTLSEKILY SHLTNPEEVK PVRGQTYLKL SPDRVAMQDA SAQMAILQFM LAGMPTTAVP
SSIHCDHLIV GHKGAEQDLV NSIENNKEIF NFLQSAAEKY GMSFWKPGSG IIHQIVLENY
AAPGLLMLGT DSHTPNAGGL GAIAIGVGGA DAVDAMANIP WELKAPEVIG IKLTGKLNGW
TSPKDVILHL AGKLTVRGGT GHIIEYFGPG IDTLSCSGMG TICNMGAEVG ATTSLFPFVN
SMSSYLHATG RGPVAEAARQ HANFLRADEG AHYDKVIEVN LSDLEPHING PFTPDLATPL
SKFAEVVKKN GWKDEVKVGL IGSCTNSSYE DMDRVTSLAK QAVEKGIKSK AGFFITPGSE
QIRATIERDG QTGVLEQVGG VVLANACGPC IGQWTRDDLN DKEENAILTS FNRNFKNRND
GNATTMNFLT SPELVTAMSL SGKLTFNPLT DPLIDASGNE FMLQPPYGDN LPQNGFIPGN
LSYTPPDISQ PNPAIQINVD PKSTRLQVLE PFGPGPVGEF ENLQVMLKVK GKCTTDHISA
AGPWLKYKGH LENIAHNTLN GALNADNEQV NVVKNVFTGK EGAIHEVGRE YQALGKPWIV
VTDHNYGEGS AREHAALQMR YLGCPLILAR SFARIHQTNL KKQGVLPLTF ADPADWEKMH
GGDVIESTEG VADLVAGRPG KNDTPEGGEI LLNVRRPDGE KYVIKALHTM SKDQVEWFRK
GSALNAARG
//
