ID H3CI89_TETNG Unreviewed; 890 AA.
AC H3CI89;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
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};
GN Name=ACO1 {ECO:0000313|Ensembl:ENSTNIP00000007967.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000007967.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000007967.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; H3CI89; -.
DR STRING; 99883.ENSTNIP00000007967; -.
DR Ensembl; ENSTNIT00000008128.1; ENSTNIP00000007967.1; ENSTNIG00000005288.1.
DR GeneTree; ENSGT00940000157772; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; H3CI89; -.
DR OMA; NGGIMQY; -.
DR TreeFam; TF313476; -.
DR Proteomes; UP000007303; 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:UP000007303};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 63..564
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 694..820
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 97783 MW; C92527DE6E2C6364 CRC64;
VLSPCTRLLE PLDPSAPGQR FFNLSKLGDA RYERLPFSIR VLLEAAVRTC DCFLVKPSDV
ENILDWKRTQ TRSVEVPFRP ARVILQDFTG VPAVVDLAAM RDAVKQLGGD PERVNPVCPA
DLVIDHSIQV DFNRKSDSLR RNQDLEFERN RERFQFLKWG SRAFRNMRII PPGSGIVHQV
NLEYLARVVF QRDGLVYPDS VVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP
QVVGYRLSGV PDGFVTSTDI VLTVTKHLRQ VGVVGKFVEF FGPGVARLSI ADRATIANMC
PEYGATAAFF PVDDASIRYL EQTGREPETL ATVRDYLKAV GMLRDYADAG QDPEFTQVVE
LDLGTVAPCC SGPKRPQDRV PLSQMKEDFE SCLGAKQGFK GFQVAAEHHA ATVPFRFDGA
EYLLGHGSVV IAAITSCTNT SNPSVMLAAG LLAKKAVQRG LSVRPYIKTS LSPGSGVVTY
YLRESGVLAY LAQLGFEVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAAG VLSGNRNFEG
RVHPNTRANY LASPPLVVAY ALAGTVRMDF ERQPLGVDAE GTAVYLRDIW PSREEIQAVE
RAFVIPSMFQ EVYQKMEKVN QSWNALAASS DTLYSWDPDS TYIKSPPFFQ RAETMELRPP
ESILDARVLL NLGDSVTTDH ISPAGNIARS SAAARYLTSR GLSPRDYNSY GSRRGNDAVM
ARGTFANIRL FNKFLNKQAP QTLHLPSGET LDVFDAAERY QQAGVPLLVL AGKEYGSGSS
RDWAAKGPFL LGIKAVIAES YERIHRSNLV GMGVVPLEFL PGDTAQSLGL TGRERYSVLL
PQQLAPRMLL QVQLDDGRSF QVRMRFDTDV ELTYFRHGGI LNYMIRKMTL
//
