ID M3XZ06_MUSPF Unreviewed; 889 AA.
AC M3XZ06;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:ENSMPUP00000004307.1,
GN ECO:0000313|RefSeq:XP_004765422.1, ECO:0000313|RefSeq:XP_044935620.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000004307.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000004307.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004765422.1, ECO:0000313|RefSeq:XP_044935620.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004765422.1,
RC ECO:0000313|RefSeq:XP_044935620.1};
RG RefSeq;
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 -!- 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 EMBL; AEYP01063318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004765422.1; XM_004765365.3.
DR RefSeq; XP_012918367.1; XM_013062913.1.
DR RefSeq; XP_044935620.1; XM_045079685.1.
DR STRING; 9669.ENSMPUP00000004307; -.
DR Ensembl; ENSMPUT00000004383.1; ENSMPUP00000004307.1; ENSMPUG00000004340.1.
DR GeneID; 101691360; -.
DR KEGG; mpuf:101691360; -.
DR CTD; 48; -.
DR eggNOG; KOG0452; Eukaryota.
DR GeneTree; ENSGT00940000157772; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR OMA; NGGIMQY; -.
DR OrthoDB; 176941at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006101; P:citrate metabolic process; IEA:Ensembl.
DR GO; GO:0010040; P:response to iron(II) ion; IEA:Ensembl.
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:UP000000715};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
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; 98322 MW; 4F817AEB45411E48 CRC64;
MSNPFAHLVE PLDLAQPGKK FFNLNKLKDS RYERLPFSIR VLLEAAVRNC DQFLVKKNDI
ENILNWNVMQ HKNIEVPFKP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPICPA
DLVIDHSIQV DFNRRTDSLQ KNQDLEFERN RERFEFLKWG SQAFRNMRII PPGSGIIHQV
NLEYLARVVF DHDGYYYPDS LVGTDSHTTM IDGLGVLGWG VGGIEAEAVM LGQPISMVLP
QVIGYKLVGN PHPLVTSTDI VLTITKHLRQ VGVVGKFVEF FGPGVAQLSI ADRATIANMC
PEYGATAAFF PVDDVSIKYL VQTGRDEEKV KQMKKYLQAV GMFRDFSDPS QDPDFAQVVE
LNLGTVVPCC SGPKRPQDKV AVTDMKKDFE SCLGAKQGFK GFQVALDHHN DHKTFIYNNS
EFTLTHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVNAG LNVKPYIKTS LSPGSGVVTY
YLRESGVMPY LSQLGFDVVG YGCMTCIGNS GPLPDPVVEA ITQGDLVAVG VLSGNRNFEG
RVHPNTRANY LASPPLVIAY AIAGTIRINF EKEPLGVNAK GEQVFLKDIW PTRDEIQAVE
RQYVIPGMFK EVYQKIETVN ESWNALAAPS DKLYCWNPKS TYIKSPPFFE NLTLALQPPK
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTNRG LTPREFNSYG SRRGNDAIMA
RGTFANIRLL NKFLNKQAPQ TIHLPSGEIL DVFDAAEQYQ QAGLPLIILA GKEYGSGSSR
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLP GETADTLGLT GRERYTIIIP
ENLTPRMKVQ VKLDTGKTFQ AIMRFDTDVE LTYFHNGGIL NYMIRKMAK
//