ID W5K4Q8_ASTMX Unreviewed; 1371 AA.
AC W5K4Q8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Cytoplasmic aconitate hydratase {ECO:0000256|ARBA:ARBA00020255};
DE EC=2.9.1.2 {ECO:0000256|ARBA:ARBA00012464};
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 AltName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase {ECO:0000256|ARBA:ARBA00021963};
DE AltName: Full=Selenocysteine synthase {ECO:0000256|ARBA:ARBA00030669};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|ARBA:ARBA00032048};
DE AltName: Full=Sep-tRNA:Sec-tRNA synthase {ECO:0000256|ARBA:ARBA00032693};
GN Name=ACO1 {ECO:0000313|Ensembl:ENSAMXP00000002569.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000002569.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000002569.2}
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 -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-
CC tRNA(Sec) required for selenoprotein biosynthesis.
CC {ECO:0000256|ARBA:ARBA00002552}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-tRNA(Sec) + selenophosphate = L-
CC selenocysteinyl-tRNA(Sec) + 2 phosphate; Xref=Rhea:RHEA:25041,
CC Rhea:RHEA-COMP:9743, Rhea:RHEA-COMP:9947, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:78573; EC=2.9.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001746};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC (archaeal/eukaryal route): step 2/2. {ECO:0000256|ARBA:ARBA00004822}.
CC -!- SUBUNIT: Homotetramer formed by a catalytic dimer and a non-catalytic
CC dimer serving as a binding platform that orients tRNASec for catalysis.
CC Each tetramer binds the CCA ends of two tRNAs which point to the active
CC sites of the catalytic dimer. {ECO:0000256|ARBA:ARBA00026053}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the SepSecS family.
CC {ECO:0000256|ARBA:ARBA00007037}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR STRING; 7994.ENSAMXP00000002569; -.
DR Ensembl; ENSAMXT00000002569.2; ENSAMXP00000002569.2; ENSAMXG00000002499.2.
DR eggNOG; KOG0452; Eukaryota.
DR GeneTree; ENSGT00940000157772; -.
DR HOGENOM; CLU_013476_2_1_1; -.
DR InParanoid; W5K4Q8; -.
DR UniPathway; UPA00906; UER00898.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000002499; Expressed in mesonephros and 14 other cell types or tissues.
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 GO; GO:0098621; F:O-phosphoseryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; IEA:InterPro.
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 Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR019872; Sec-tRNA_Se_transferase.
DR InterPro; IPR008829; SepSecS/SepCysS.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR NCBIfam; TIGR03531; selenium_SpcS; 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 Pfam; PF05889; SepSecS; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 66..564
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 693..820
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 1371 AA; 151358 MW; 7A9BA2311F9688C2 CRC64;
MSNPYAHIIE PLDPKKPEHK FFNLTKLGDP RYERLPFSIR VLLESAVRNC DEFLVKKEDV
ESILNWKQTQ TQTVEVPFRP ARVILQDFTG VPAVVDFAAM RDAVKKLGGD PEKINPVCPA
DLVIDHSIQV DFNRKSDSLQ KNQELEFERN KERFEFLKWG SKAFQNMRII PPGSGIVHQV
NLEYLARVVF QQDGHYYPDS LVGTDSHTTM INGLGVLGWG VGGIEAEAVM LGQPISMVLP
EVIGYRLKGT PNKFITSTDI VLTVTKHLRQ VGVVGKFVEF YGPGVAQLSI ADRATIANMC
PEYGATAAFF PVDHISIQYL EQTGRDVEKL SYISQYLKAV GMYRDYSNET QDPDFTKVVE
LDLCTVVPCC SGPKRPQDRV AVSEMKEDFE SCLAAKQGFK GFQLPPERHD VSVPFQYNDV
DYSLSHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAIEHG LSVKPYIKTS LSPGSGVVTY
YLKESGVMDY LVKLGFEVVG YGCMTCIGNS GPLPDPVVEA ITKGDLVAAG VLSGNRNFEG
RVHPNTRANY LASPPLVIAY AIAGTVKIDF EKEPIAVSAN GKEVYLRDIW PTREEIQAVE
REFVIPAMFK EVYEKVEKVN DRWNSLNAPS DKLYTWDVKS TYIKSPPFFD GLTKELQQPK
SIVDAYVLLN LGDSVTTDHI SPAGNIARNS PAARYLTSRG LTPREFNSYG SRRGNDAVMA
RGTFANIRLL NKFLNKQAPS TIYLPTGEMM DVYDAAEKYQ QAGHPLLVLA GKEYGSGSSR
DWAAKGPFLL GIKAVLAESY ERIHRSNLVG MGVIPLEYLN GETADSLGLT GRERYTVAIP
PQLTPRMIVD IKLDTGKTFQ ARMRFDTDVE LTYFHHGSKL ADSSRMNSEN FSLSEKIVSQ
SYVRQGLQAR RGHEQLVRLL LEQGKCPEEG WSESTIELFL NELAVMDSNN FLGNCGVGER
EGRVASSLVA RRHYRLIHGI GRSGDIAAVQ PKAAGSSLLN KITNSVVLDV LKFSGVRSVS
SCFVVPMATG MSLTLCFLTL RHRRPAACYI LWPRIDQKSC FKSMITAGFE PVVIENVLEG
DELRTDLEAV EKKIEELGAE NILCVHSTTS CFAPRVPDRL EELAFLCAKH NIPHIVNNAY
GVQSSKCMHL IQQGARVGRI DAFVQSLDKN FMVPVGGAII AGFDEDFIKE ISKMYPGRAS
ASPSLDVLIT MLTLGASGYK KLLSERKELY THLAQELKAL AERHGERLLH TPHNPISLAM
SLDGLQASCD KAVTQLGSML FTRQVSGARV VPLGVEQTVS GHTFCGFMSH ANAYPCPYLN
AASAIGITKN DVELSIKRLD KCLKALKKEG NVEKHEPVTV TSEDPNDQTV P
//
