ID F8MUB4_NEUT8 Unreviewed; 784 AA.
AC F8MUB4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00015940, ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN ORFNames=NEUTE1DRAFT_117841 {ECO:0000313|EMBL:EGO55596.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO55596.1};
RN [1] {ECO:0000313|EMBL:EGO55596.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO55596.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) 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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
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; GL891306; EGO55596.1; -; Genomic_DNA.
DR RefSeq; XP_009853405.1; XM_009855103.1.
DR AlphaFoldDB; F8MUB4; -.
DR GeneID; 20823404; -.
DR KEGG; nte:NEUTE1DRAFT117841; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_117841; -.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000008065; 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 CDD; cd01578; AcnA_Mitochon_Swivel; 1.
DR CDD; cd01584; AcnA_Mitochondrial; 1.
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:SF3; ACONITATE HYDRATASE, 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 Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 71..507
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 586..715
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 530..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 84954 MW; AAD442B89A719E76 CRC64;
MLASRQLLGV ARSRAAAGLG RRCMATATEN PLDRKVKQNL LEEGNFINYK KMSENLAVVR
SRLNRPLTYA EKILYSHLDN PHEQDIERGV SYLRLRPDRV ACQDATAQMA ILQFMSAGMP
SVANPTTVHC DHLIEAQVGG EKDLERAINI NKEVYDFLAS ACAKYNIGFW KPGSGIIHQI
ILENYAFPGG LLIGTDSHTP NAAGLGMAAI GVGGADAVDV MANLPWELKA PKVIGVKLTG
ALNGWTTPKD VILKLAGILT VKGGTGSIVE YYGEGASSMS ATGKATCGNM GAEIGATTSV
FPYDKAMFDY LVATKRSDIA EFAKTYQKEL QADEGAEYDQ HIEINLNELE PHINGPFTPD
LATPISKFAQ AAKENNWPEE LKVGLIGSCT NSSYEDMTRA ASIARDALDH GLKAKAAFVV
TPGSEQIRAT IARDGQLQTF EEFGGTVLAN ACGPCIGQWD RRDTPKGTPN SILSSYNRNF
TGRNDGNPAT HSFVTSPDLV VAMSIAGSLY FNPLTDSLKD KDGKEFKLQA PTGAGLPDRG
YDPGQNTYQA PPADRATVQV QVSPTSDRLQ VLSPFNAWNG KDATDMPILI KAQGKTTTDH
ISMAGPWLKY RGHLDNISNN MLIGAINAAN GEANKVQNFT TGEWDAVPAV ARDYKAKGIP
WVVIGDWNYG EGSSREHAAL EPRHLGGLAI ITRSFARIHE TNLKKQGMLP LTFADPADYD
KISPEDKVDI LCTELAVGKP ITMRVHPKNG KDFDIKLNHT FNDAQIEWFK NGSALNTMAK
NAKN
//
