ID A0A0L8HKW4_OCTBM Unreviewed; 783 AA.
AC A0A0L8HKW4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN ORFNames=OCBIM_22012436mg {ECO:0000313|EMBL:KOF89881.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF89881.1};
RN [1] {ECO:0000313|EMBL:KOF89881.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF89881.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF89881.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ417911; KOF89881.1; -; Genomic_DNA.
DR RefSeq; XP_014771485.1; XM_014915999.1.
DR AlphaFoldDB; A0A0L8HKW4; -.
DR STRING; 37653.A0A0L8HKW4; -.
DR EnsemblMetazoa; Ocbimv22012436m; Ocbimv22012436m.p; Ocbimv22012436m.g.
DR EnsemblMetazoa; XM_014915999.1; XP_014771485.1; LOC106870033.
DR GeneID; 106870033; -.
DR KEGG; obi:106870033; -.
DR OMA; NTHAFVA; -.
DR OrthoDB; 3266779at2759; -.
DR UniPathway; UPA00223; UER00718.
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; 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.
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 68..504
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 783 AA; 85460 MW; D66628CAF531BD09 CRC64;
MAYLLRSGLT KRLYTPNMVT QHLRMYSAAA SKVAMSKFET NKYIDYDKMK FNVDVVKDRL
GRPLTLSEKI VYGHLDKPKE QDIVRGESYL KLRPDRVAMQ DATAQMAMLQ FISSGLARVA
VPSTIHCDHL IEAQIGGEED LARAKDINKE VYDFLQTAGA KYGVGFWRPG SGIIHQIVLE
NYAFPGVMII GTDSHTPNGG GLGGVCVGVG GADAVDVMAD IPWELKCPKV IGVELTGKLH
GWTSPKDIIL KVAGILTVKG GTGAIVEYFG DGVDSISCTG MGTICNMGAE IGATTSIFPY
NHRMKDYLVA TNRNDIASLA DSYKSLLSAD KDAKYDQLIK INLDELEPHV NGPFTPDLAH
SISELGKTAV DMKWPLDVKV GLIGSCTNSS YEDMCRSVSI AKQALDHGLK SKAGFTITPG
SEQIRATIER DRLTETLEAI DGCVLANACG PCIGQWDRKD VAKGEKNTIV TSYNRNFTGR
NDANPATHAF VASPEIVTAL AIAGRLDFNP LTDYLTGVNG EKFKFEPPSG DELPNKGFDP
GMDTYQAPPS DSSNVFVAVD PASTRLQLLS PFAKWDGEDI KDMVVLIKAK GKCTTDHISA
AGKWLKFRGH LDNISNNLLI GAVNYENEKL NCVKNQLTGE YGGVPDTARY YKSKGIYWVV
IGDENYGEGS SREHAALEPR HLGGRAIIVK SFARIHETNL KKQGMLPLTF ADSADYDKIQ
PTDRISILGL KTFTPGKPLT CEVKHADDST DTFLLNHTFN EGQITWFKAG SALNRMFEVR
QGS
//
