ID A0A0V1I5J0_9BILA Unreviewed; 1959 AA.
AC A0A0V1I5J0;
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:KRZ18138.1};
GN ORFNames=T11_11853 {ECO:0000313|EMBL:KRZ18138.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ18138.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ18138.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ18138.1};
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=[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 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:KRZ18138.1}.
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DR EMBL; JYDP01000004; KRZ18138.1; -; Genomic_DNA.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000055024; 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-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; 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; 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 NCBIfam; TIGR01340; aconitase_mito; 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 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024}.
FT DOMAIN 73..509
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 590..717
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT DOMAIN 785..1028
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT COILED 1084..1111
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1177..1356
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1550..1584
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1959 AA; 221981 MW; B803A72889A53B0F 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 EQLLQSKTAI NDLNDQLKKA KQHSAAEMQL
DMWKREKATK LKAIEELMEK HEKFLNTHFK HTPNELLCSE MRNKHVELTK LNAEMETLNS
AMQNCTEQLN LNNEMIKEKT NDLETYNKKI AALNETITNL PNREQFLISN LRSQETRRDT
LVGLKPLFDI VQKLELQTIP DLEKERQLLI EKGESASQQL RQCEARCKIA DEEYRQATAI
LVDVITVDSF LQYERSLCEK IAEQEEFLKA SGMTMSSEDL QQKIEHVQNM LSENEAMLQL
KRKEQSKHRD MLQNLRDCAH HLTEKKQRVL NQMQQSASLR ELESSRRAEL SRLEANFINA
MEQVEILQQQ LNEHTLELDC LRQNSAEILE PLKSGVADLT DSLRQLDHSA DHLKQYNVGE
FESQLEQLKR KRIENEQIIH SLETSKVDKV NKLQNIQKGV VCAEMRKRDL HDFKKLLSEE
AAQCRLAAEA NHLQTELDSK MLPSGEMDFD IVNEEYCKKL KSSHELIGKK SELELTIDRL
RGELDSNIYK DADVKWRDKM IAHVTLEHAQ NDLYHYANAL EQAIMQFHKT KMQEVNAILK
DLWETVYQGS DVDYIEIKSE EDLQDNFGKR RNYNYRVVMH VGKEVLDMRG RCSAGQKVLA
SIIIRIALAE VFSTNCGFMT LDEPTTNLDS KNSANLARAL VDLLRVRSLE KHFQLILITH
DDSFVEQITR FWPVEVFYRV KKNDSGCSKL YEETVDKLT
//
