ID T1JJR7_STRMM Unreviewed; 738 AA.
AC T1JJR7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU362107};
OS Strigamia maritima (European centipede) (Geophilus maritimus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR014097-PA, ECO:0000313|Proteomes:UP000014500};
RN [1] {ECO:0000313|Proteomes:UP000014500}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA Muzny D.M., Gibbs R.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:SMAR014097-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|ARBA:ARBA00003113}.
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:0000256|RuleBase:RU362107};
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; JH431789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1JJR7; -.
DR STRING; 126957.T1JJR7; -.
DR EnsemblMetazoa; SMAR014097-RA; SMAR014097-PA; SMAR014097.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; NTHAFVA; -.
DR OrthoDB; 3266779at2759; -.
DR PhylomeDB; T1JJR7; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000014500; 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:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 Reference proteome {ECO:0000313|Proteomes:UP000014500};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 25..461
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 541..669
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 476..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 80513 MW; B0697E0EA93AAD21 CRC64;
MPYEKLNQNL EIIKKRLNRP LTLSEKIVYS HLDDPQNQDI IRGESYLRLR PDRVAMQDAT
AQMAMLQFIS SGLPRVAVPS TIHCDHLIEA QLGGEKDLSR AIELNKEVYN FLSTAGAKYG
VGFWRPGSGI IHQIILENYA FPGVLLIGTD SHTPNGGGLG GVCIGVGGAD AVDVMADIPW
ELKCPKVIGV KLTGKLSGWT SPKDIILKVA GILTVKGGTG AIIEYHGPGV DSISCTGMGT
ICNMGAEIGA TTSVFPYNVR MRDYLRATKR EAIAKTADTY SHLITPDSGA QYDQLVEINL
DELAPHVNGP FTPDLATPID KLGQTAKKNG WPLDIRVGLI GSCTNSSYED MGRAASVANQ
AIKHGVRAKT QYTVTPGSEM IRATIERDGL AKSLRDIGGV VLANACGPCI GQWDRKDVQK
GEKNTIVTSY NRNFTGRNDA NPATHCFVTS PEIVTALSLA GTLDFDPRKD ELTGAKGEKF
KLTAPTGDEL PSRGFDPGQD TYQPPPVDGG EIQVNVDPKS QRLQLLEPFD TWDGRDHTDM
VILIKVKGKC TTDHISAAGP WLKYRGHLDN ISNNLLIGAI NFENNEANKI KHQIKGTWAA
VPDTARQYKA EGVKWVVIGD ENYGEGSSRE HAALEPRHLG GRAIIVKSFA RIHETNLKKQ
GLLPLTFDKP KDYDKIQPTD RISLLDLANL SPGKPVKCEI KHADGKKEVV SLNHSMNDLQ
IEWFRAGSAL NRMAQKKR
//
