ID U6LD99_9EIME Unreviewed; 793 AA.
AC U6LD99;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=EBH_0045350 {ECO:0000313|EMBL:CDJ48387.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ48387.1};
RN [1] {ECO:0000313|EMBL:CDJ48387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ48387.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ48387.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ48387.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00023501};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; HG711107; CDJ48387.1; -; Genomic_DNA.
DR AlphaFoldDB; U6LD99; -.
DR EnsemblProtists; CDJ48387; CDJ48387; EBH_0045350.
DR VEuPathDB; ToxoDB:EBH_0045350; -.
DR OrthoDB; 176941at2759; -.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 3.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 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};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 92..539
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 691..721
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 87086 MW; 83DA21F7A9F426F6 CRC64;
MRDDSSSGKA SNVTPSCSQS RNSHPHPYAH LFERLNGFDE SIYNIQKLGK DKVCRLPHCI
RVLLESAVRN CDGFLVTQDD VERILDWDAL VNHKRTDGSV MLDVPFIPAR VILQDFTGVP
CVVDLAAMRD AMVELGSDPL KINPRVPVDL IIDHSVQVDR VRSKDAVTYN EEMEMHRNSE
RFSFLKWAAK TFSQMLIVPP GSGIVHQVNL EYLAKVVVTR NGVCFPDSLV GTDSHTTMID
GLGIVGWGVG GIEAEATMLG QPISMTLPPV LGVRLVGRLS PACTTTDLVL HVARILRMRG
VVDHFVEFFG EACASLSAPD RATLANMSPE FGATIAYFPP DEMTLKYLLN TGRSTGEVEK
IKAYLLQQGM FRTYENTGQK VSYTDVLEVD LSKIEPCIAG PKRPQDEVLL RNLKREFIVR
SGSLRLELVR KPSYMDGSRK YLQGSVVIAA ITSCTNTSNP SVMVGAGLLA RKAVDLGLSV
APYIKTSLSP GSHVVQRYLE SADLLPALEE LGFYLTGFGC MTCIGNSGDL PEEVTAAIQS
SPDLVVSAVL SGRVDIDFET EPLGICKNGK EVFLRDIWPS PSAVNEVVEK VLLPSLFKEA
YQNIQQGNER SATALQQTIF HLLEESRRIH LLVVIFLLRA LQGASSKSGR NGFENRSLES
PFCVQQACAV TVGCDLLQLY RETRTPLIVI AGVKAVIAES YERIHRSNLV GMGVLPLQFL
EGESASSLGI TGMEEFSIDL TILGVNSVLP VQLDDGRQFS VKCRLQTKVE LEYFRNGGIL
QYVLRNAASE STV
//
