ID A0A1R2D0D0_9CILI Unreviewed; 890 AA.
AC A0A1R2D0D0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN ORFNames=SteCoe_2044 {ECO:0000313|EMBL:OMJ94706.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ94706.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ94706.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ94706.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
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 ECO:0000256|RuleBase:RU361275};
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, ECO:0000256|RuleBase:RU361275}.
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:OMJ94706.1}.
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DR EMBL; MPUH01000022; OMJ94706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2D0D0; -.
DR OrthoDB; 176941at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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 NCBIfam; TIGR01341; aconitase_1; 1.
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 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000187209}.
FT DOMAIN 69..564
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 692..818
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 97490 MW; 14C84E7F11D8D7E9 CRC64;
MAGTNPFDAR CLKDLQVGEK AYKFYNIQGL NDPRLSRLPY SIRILLESAI RNCDEFEVKS
SDVENILNWE QTSKQDIEIP FKPARVLLQD FTGVPAVVDL AAMRDAFVKI GGTPSRINPL
CPVDLVIDHS IQVDVARSLE ALQQNEEFEF YRNRERFEFL KWGQKAFENL LIVPPGSGIV
HQVNLEYLAR IIFDRNGLLY PDSVVGTDSH TTMINGAGVV GWGVGGIEAE AVMLGQSISM
VLPEVVGFKL TGKLSDAATA TDLVLTVTKM LRQRGVVNKF VEFFGNGVEN LSIADRATIG
NMAPEYGATV GYFPMDGKTL DFLRTSGRSG EKIAFIEAYL KANGLFRDYN GEDPVFSGAV
LELDLGAVVP CVAGPKRPHD RVSVSDLKNE FITGLTGPVN FKGFGVPNPE AVSTFDYKGQ
TFNLKHGSVV IAAITSCTNT SNPGVMLAAG LLAKNAVAKG LKVAPYIKTS LSPGSGVVTK
YFDKAGVTGF LNELGFTVAG YGCMTCIGNS GDLEEEVLKA ISANDLVATS VLSGNRNFEG
RVHPATRANY LASPPLVVAY ALAGRVDFDF ETEPLGVFEG NPVFLRDIWP SRELVNHTVN
EIITPEMFAE VYNRIAQGTD RWNSLEAPEG TLYSWKDEST YIHNPPFFKT LTLEIPSIKD
ITNAYALLKL GDSITTDHIS PAGNIARNSP AAKYLQVRGV PPKEFNSYGA RRGNDEIMMR
GTFANIRLVN TLINHPGPQT KHIPSNEEMD IYEASAKYQQ DGVDLIVIAG KEYGSGSSRD
WAAKGPYLLG VKAVIAESYE RIHRSNLLGM GILPLQFLPD QNATSLELTG FEKFNIVLNG
HVGVQQIIEV VTDSGKNFNV KARVDTDVEV EYFRHRGILH YVLRKLAKNN
//
