ID A0A0V1I5J7_9BILA Unreviewed; 2094 AA.
AC A0A0V1I5J7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
GN Name=aco-2 {ECO:0000313|EMBL:KRZ18137.1};
GN ORFNames=T11_11853 {ECO:0000313|EMBL:KRZ18137.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ18137.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ18137.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ18137.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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 -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ18137.1}.
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DR EMBL; JYDP01000004; KRZ18137.1; -; Genomic_DNA.
DR STRING; 268475.A0A0V1I5J7; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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; 1.10.287.1490; -; 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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR NCBIfam; TIGR00606; rad50; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 1424..1521
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 1084..1111
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1177..1327
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1685..1719
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 1471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 2094 AA; 237689 MW; 4FD060A642FB72C8 CRC64;
MNISVINLFF NGTKIMGFRQ FNSARFLHKS STHFATQVPI SRFELDKFLP YDALIQRLDI
VRKRLNRPLT LAEKILYSHL DDPENAEIVR GSSYLKLRPD RVAMQDATAQ MAVLQFISSG
LNRVSVPTTI HCDHLIEANE EANSDLKRAK DVNAEVYEFL SSVAAKYGIG FWHPGSGIIH
QIILENYAFP GLLLIGTDSH TPNGGGLCGL CIGVGGADAV DVMADIPWEL KCPKVMGVKL
QGELSGWTSP KDVILKLAEI LTVKGGTGYI IEYFGPGVDS ISCTGMGTIC NMGAEVGATT
SVFPFNNRMK RYLEATGREG IATVAEKCKH LFTSDAGAGY DQLVEINLSE LEPRINGPFT
PDLGHTIHNL GQHARENGYP LEVKAGLIGS CTNSSYEDMT RAANVAQQAV EHNYKAKSIF
DVTPGSEQIR ATMERDGLTE TFRKIGATVL ANACGPCIGQ WNRKDVRKGE KNTIVTSYNR
NFTGRNDANP ATHAFVASPE IVTAIALAGR LDFDPTRDYL TANDGKKFKL KVPVGEELPS
KGFDRGQETY QAPPADGSAV KVVVQPNSKR LQLLKAFDKW DGKDFEDMFV LIKIKGKCTT
DHISAAGPWL KFRGHLDNIS NNMFIGAINE ENGEMNKVKN QLSGEWSSVP EAARFYKAKG
KKWIVFGEEN YGEGSSREHA ALEPRHLGGR AIVVKSFARI HETNLKKQGM LALTFVNPAD
YDKVLPTDSV SLVGLKDFKP GKPLKCILKH HDGSTDEFLL DHTYNDLQIE WFKAVNKMSE
LSAMMIRGFR SFGLEEKGQT IKFQKPLTLI VGSNGSGKTT IIECLKYATI GSLPPGGRGT
IFIHDPKIAN LPEVNAQVKL KFTDTLGATA VVSKSMTCFQ RKNKMESRSL DGTIQRKING
QTTSVSMRCM DIEAEMVNLL GVSKPILDSV IFCHQEESNW PLSEPKLLKM KFDEIFSAVK
YTKCVDEIRR INKGHKVQIL ECKTELKHLE QNKTKASEVK QALQSNELKL KSINDDLNIL
NGELEKMKVY LENVTKVRQE IVELTTKLDN VKSQMQIHKA TADSLRKGIG ELFKGSESEL
DYEIATFEMK IQKEKESLSQ LQLEIEKSDE QLIGRCKQRD EIVSHENKLK LEIEYWNGKL
TEFDSQISVM CSKANIPNNY GNNVALQDIR KYCKSQADFL KTKEDEYGCR LNELKQEISD
VEIKKKSEER NMSVLKEQIE NCKSEIKKIE EQLLQSKTAV DELDALAEEL KSVNEQIEVK
NQFISVSRMK DEIEELTRFS ERKHSEINDL NDQLKKAKQH SAAEMQLDMW KREKATKLKA
IEELMEKHEK FLNTHFKHTP NELLWLVCYY FQQLLIYIYT SEMRKYVESK HVELTKLNAE
METLNSAMQN CTEQLNLNNE MIKEKTNDLE TYNKKIAAAC DGDPSSYNSV LLNVTENIEK
LQLEKGNIGG TGFLYKKYVK YLKKNPCCPV CHRDFPSPEI VDSVIDELNE TITNLPNREQ
FLISNLRSQE TRRDTLVGLK PLFDIVQKLE LQTIPDLEKE RQLLIEKGES ASQQLRQCEA
RCKIADEEYR QATAILVDVI TVDSFLQYER SLCEKIAEQE EFLKASGMTM SSEDLQQKIE
HVQNMLSENE AMLQLKRKEQ SKHRDMLQNL RDCAHHLTEK KQRVLNQMQQ SASLRELESS
RRAELSRLEA NFINAMEQVE ILQQQLNEHT LELDCLRQNS AEILEPLKSG VADLTDSLRQ
LDHSADHLKQ YNVGEFESQL EQLKRKRIEN EQIIHSLETS KVDKVNKLQN IQKGVVCAEM
RKRDLHDFKK LLSEEAAQCR LAAEANHLQT ELDSKMLPSG EMDFDIVNEE YCKKLKSSHE
LIGKKSELEL TIDRLRGELD SNIYKDADVK WRDKMIAHVT LEHAQNDLYH YANALEQAIM
QFHKTKMQEV NAILKDLWET VYQGSDVDYI EIKSEEDLQD NFGKRRNYNY RVVMHVGKEV
LDMRGRCSAG QKVLASIIIR IALAEVFSTN CGFMTLDEPT TNLDSKNSAN LARALVDLLR
VRSLEKHFQL ILITHDDSFV EQITRFWPVE VFYRVKKNDS GCSKLYEETV DKLT
//
