ID A0A091M0P6_CARIC Unreviewed; 855 AA.
AC A0A091M0P6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Cytoplasmic aconitate hydratase {ECO:0000256|ARBA:ARBA00020255};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive element-binding protein 1 {ECO:0000256|ARBA:ARBA00033207};
DE Flags: Fragment;
GN ORFNames=N322_10622 {ECO:0000313|EMBL:KFP65041.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP65041.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP65041.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP65041.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conversely, when cellular iron levels are high, binds a 4Fe-
CC 4S cluster which precludes RNA binding activity and promotes the
CC aconitase activity, the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|ARBA:ARBA00024990}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK516903; KFP65041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091M0P6; -.
DR Proteomes; UP000054116; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; 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:0030350; F:iron-responsive element binding; IEA:UniProt.
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:SF32; 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|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275};
KW Cytoplasm {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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 28..530
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 659..784
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP65041.1"
FT NON_TER 855
FT /evidence="ECO:0000313|EMBL:KFP65041.1"
SQ SEQUENCE 855 AA; 93910 MW; 07F55D0036875B9D CRC64;
LPFSIRVLLE AAIRNCDEFL VKKGDVENIL NWKVVQHKNV EVPFKPARVI LQDFTGVPAV
VDFAAMRDAV KKLGGDPEKI NPVCPADLVI DHSIQVDFNR RSDSLQKNQD LEFERNKERF
EFLKWGSQAF KNMRIIPPGS GIIHQVNLEY LARVVMDQDG HYYPDSVVGT DSHTTMIDGL
GVLGWGVGGI EAEAVMLGQP ISMVLPEVVG YKLLGNPQPL VTSTDIVLTI TKHLRQVGVV
GKFVEFFGPG VAQLSIADRA TIANMCPEYG ATAAYFPVDD ISIGYLIQTG RDKEKVLCTK
KYLEAVGMLR DFKNSSQDPD FTQVVELDLH TVVPCCSGPK RPQDKVAVSD MKKDFETCLG
AKQGFKGFQI APDRHNSIVK FNFEGCDFEL THGSVVIAAI TSCTNTSNPS VMLGAGLLAK
KAVEAGLTVK PYVKTSLSPG SGVVTYYLRE SGVMSYLSQL GFDVVGYGCM TCIGNSGPLP
ESVVEAITQG DLVAVGVLSG NRNFEGRVHP NTRANYLASP PLVIAYAIAG TIRIDFEKEP
LGITASGKKI FLKDIWPTRN EIQAVERQFV IPGMFKEVYQ KIETVNKSWN ALDAPSDKLY
TWNPKSTYIK SPPFFDGLTL AIQSPKTIED AYVLLSFGDS VTTDHISPAG NIARNSPAAR
YLTSRGLTPR EFNSYGSRRG NDAVMARGTF ANIRLVNKFL DKQGPQTVHF PSGETLDVFD
AAERYKQAGH PLIVLAGKEY GAGSSRDWAA KGPFLLGVKA VLAESYERIH RSNLVGMGVI
PLQYLPGEDA GTLGLTGRER YTIIIPEKLK PQMNIQIKLD TGKTFHAIMR FDTDVELTYF
YNGGILNYMI RKMAS
//
