ID A0A0V1D5L9_TRIBR Unreviewed; 2096 AA.
AC A0A0V1D5L9;
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:KRY56797.1};
GN ORFNames=T03_2600 {ECO:0000313|EMBL:KRY56797.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY56797.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY56797.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY56797.1};
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:KRY56797.1}.
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DR EMBL; JYDI01000039; KRY56797.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1D5L9; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000054653; 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; 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 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; 2.
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:UP000054653};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 1426..1523
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 1105..1132
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1198..1348
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1536..1570
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1614..1707
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1755..1782
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 1473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 2096 AA; 237303 MW; 06BC0C40EA01058A CRC64;
MNISVINLIF NGTKIMGYRQ LNSSRFLHKS STYFATQVPI SRFELDKFLP YDALIQRLDI
VRKRLNRPLT LAEKILYSHL DDPENAEIVR GSSYLKLRPD RVAMQDATAQ MAVLQFISSG
LDRVSVPTTI HCDHLIEANE EANSDLKRAK DVNAEVYDFL SSVAAKYGIG FWHPGSGIIH
QIILENYAFP GLLLIGTDSH TPNGGGLGGL CIGVGGADAV DVMADIPWEL KCPKVMGVKL
QGELSGWTSP KDVILKLAEI LTVKGGTGYI IEYFGPGVDS ISCTGMGTIC NMGAEVGATT
SVFPFNNRMK RYLEATGREG IATVAEKCKH LFSSDAGAGY DQLVEINLSE LEPRINGPFT
PDLGHTVHNL GQHARENGYP LEVKAGLIGS CTNSSYEDMT RAANVAQQAV EHNYKAKSIF
DVTPGSEQIR ATMERDGLTE TFRKIGATVL ANACGPCIGQ WNRKDVRKGE KNTIVTSYNR
NFTGRNDANP ATHAFVASPE IVTAIALAGR LDFDPTRDYL TANDGRKFKL KVPVGEELPS
KGFDRGQETY QAPPADGSAV KVVVQPNSKR LQLLKAFDKW NGKDFEDMLV LIKIKGKCTT
DHISAAGPWL KFRGHLDNIS NNMFIGAINE ENGEMNKVKN QLSGQWSSVP EAARFYKAKG
KKWIVFGEEN YGEGSSREHA ALEPRHLGGR AIVVKSFARI HETNLKKQGM LALTFVNPAD
YDRVLPTDSV SLVGLKDFKP GKPLKCILKH RDGSTDEFLL DHTYNDLQIE WFKAVSAGSI
NLILNEDFEV LYTCLVNKMS ELSAMMIRGF RSFGLEEKGQ TIKFQKPLTL IVGSNGSGKT
TIIECLKYAT IGILPPGGRG TIFIHDPKIA NLPEVNAQVK LKFTDTLGAT AVVSKSMTCY
QRKNKMESRS LDGTIQRKIN GQTTSVSMRC MDIEAEMVNL LGVSKPILDS VIFCHQEESN
WPLSEPKLLK MKFDEIFSAV KYTKCVDEIR RINKGNKVQI LECKTELKHL EQNKTKASEV
KQALQSNELK LKSINDDLNV LNGELEKMKV YLENVTKVRQ EIVELTTKLD NVKSQMQIHK
ATADSLRRGI GELFKGSESE LDYEIATFEM KIQKEKESLS QLQLEIENND EQLIGRCKQR
DEIISHENKL KLEIEYWNGK LTEFDSQISV MCSKANIPNN YGNNVALQNI RKYCQSQADF
LKTKEDEYSC RLNELKQEIS DVEIKKKSEE RNMSVLKEQI ENSRNEIKKI EEQLLQSKTA
VDELDALAEE LKSVNEQIEV KNQFISASRM KDEIEELTRF SERKHTEIND LNNQLKKAKQ
HSAAEMQLDM WKREKATKLK AVEELMEKHE KFLSTHFKHT PNELLCSEMT NKHVELTKLN
AEMETLNSTV QNCTEQLNLN DEMIKEKTND LETYNKKIAA ACDGDPSSYN SVLLNVTENI
EKLQLEKGNI GGTGFLYKKY VKYLKKNPCC PVCHRDFPSS EIVDSVIDEL NETITNLPNR
EQSLISNLRS QETRRDTLVG LKPLFDIVQK LELQTIPDLE KERKLLIEKS ESASQQLRQC
EARCKIADEE YRQASAILVD VITLDSFLQY ERSLCEKIAH QEEFLKASGM TMSSESLQQK
IQDVQNMLSE NEAMLQLKRK EQSKHRDVLQ TLRDSAHHLT EKKQRVLNQM QQSASLRELE
SSRRAELSRL ETNFTNAEKQ VEILGRQLNE RTLELDSLRQ NSAEILEPLK SGVENLTDSL
RQLDHSADHL KQYNAGKFES QLEQLKQKRM ENEQIIHSLE MSKADTVNKL QIMQKDVVRA
EMRKRDLHDL KKLLGEEAAQ CRLAAEAHHL QTELDSKIVP SGETDFDTVN EEYCKKLKIS
HELIGKKSEL ELTVDRLRGE LESNMYKDAD VKWRDKMIAH VTLEHAQNDL YHYANALEQA
IMQFHKIKMQ EVNAILKDLW EAVYQGSDVD YIEIKSEEDL QDNFGKRRNY NYRVVMHVGK
EVLDMRGRCS AGQKVLASII IRIALAEVFS TNCGFMTLDE PTTNLDSKNS ANLARALVDL
LRVRSLEKHF QLILITHDDS FVEQITRFWP VEVFYRVKKN DAGCSKLYEE TVDKLD
//
