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Database: UniProt
Entry: G3TBD3_LOXAF
LinkDB: G3TBD3_LOXAF
Original site: G3TBD3_LOXAF 
ID   G3TBD3_LOXAF            Unreviewed;       889 AA.
AC   G3TBD3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
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:ENSLAFP00000011276.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000011276.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000011276.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011276.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000011276.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000011276.3};
RG   Ensembl;
RL   Submitted (JUL-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   -!- SUBUNIT: Interacts (when associated with the 4Fe-4S) with FBXL5.
CC       Interacts with frataxin(81-210). {ECO:0000256|ARBA:ARBA00011759}.
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; G3TBD3; -.
DR   Ensembl; ENSLAFT00000013474.3; ENSLAFP00000011276.3; ENSLAFG00000013470.3.
DR   GeneTree; ENSGT00940000157772; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; 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:UP000007646}.
FT   DOMAIN          62..564
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          693..818
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   889 AA;  98351 MW;  EB1CF0D6173967E4 CRC64;
     MSNPFIHIAE PLDPAQPGKK FFNLNKLKDS RYGRLPFSIR VLLEAAIRNC DEFLVKKNDI
     ENILNWNVMQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RNAVKKLGGD PEKINPICEG
     QLILDEGSQS HFRNRTDSLQ KNQDLEFERN RERFEFLKWG SQAFRNMRII PPGSGIIHQV
     NLEYLARVVF DQDGYYYPDS LVGTDSHTTM IDGLGILGWG VGGIEAEAVM LGQPISMVLP
     QVIGYKLMGS PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
     PEYGATAAFF PVDKVSIKYL VQTGRDEAKI KHIKKYLQAV GMFRDFSDSS QDPDFAQVVE
     LDLKTVVPCC SGPKRPQDKV AVSDMKKDFE SCLGAKQGFK GFQIAPDHHN DHKTFIYDNS
     EFTLAHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVDAG LSVKPYVKTS LSPGSGVVTY
     YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPEPVVEA ITQGDLVAVG VLSGNRNFEG
     RVHPNTRANY LASPPLVIAY AIAGTIRIDF EKEPLGVNAK GQQVFLKDIW PSRDEIQAVE
     RQYVIPGMFK EVYQKIETVN ESWNALTVSS EKLYCWNPKS TYIKSPPFFE NLTLDLQSPK
     SVVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMV
     RGTFANIRLL NKFLNKQAPQ TIHLPSGEIL DVFDAAERYQ QAGLPLIILA GKEYGSGSSR
     DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GENANTLGLT GLERYTIIIP
     EDLKPRMKVQ VKLDTGKTFQ TVMRFDTDVE LTYFHNGGIL NYMIRKMAK
//
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