ID Q5I0B1_XENTR Unreviewed; 781 AA.
AC Q5I0B1; F6YAS2; F7B0W0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00015940, ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU362107};
GN Name=aco2 {ECO:0000313|EMBL:AAH88528.1,
GN ECO:0000313|Ensembl:ENSXETP00000015081,
GN ECO:0000313|RefSeq:NP_001011445.1,
GN ECO:0000313|Xenbase:XB-GENE-1000785};
GN Synonyms=ACO2 {ECO:0000313|EMBL:CAJ81637.1};
GN ORFNames=TEgg058p10.1-001 {ECO:0000313|EMBL:CAJ81637.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH88528.1};
RN [1] {ECO:0000313|RefSeq:NP_001011445.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH88528.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH88528.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAJ81637.1}
RP NUCLEOTIDE SEQUENCE.
RA Amaya E., Ashurst J.L., Bonfield J.K., Croning M.D.R., Chen C-K.,
RA Davies R.M., Francis M.D., Garrett N., Gilchrist M.J., Grafham D.V.,
RA McLaren S.R., Papalopulu N., Rogers J., Smith J.C., Taylor R.G., Voigt J.,
RA Zorn A.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSXETP00000015081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000015081};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [5] {ECO:0000313|Ensembl:ENSXETP00000015081}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [6] {ECO:0000313|RefSeq:NP_001011445.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|ARBA:ARBA00003113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU362107};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU362107}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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; BC088528; AAH88528.1; -; mRNA.
DR EMBL; CR848472; CAJ81637.1; -; mRNA.
DR RefSeq; NP_001011445.1; NM_001011445.1.
DR DNASU; 496933; -.
DR Ensembl; ENSXETT00000015081; ENSXETP00000015081; ENSXETG00000006892.
DR GeneID; 496933; -.
DR KEGG; xtr:496933; -.
DR AGR; Xenbase:XB-GENE-1000785; -.
DR CTD; 50; -.
DR Xenbase; XB-GENE-1000785; aco2.
DR OMA; NTHAFVA; -.
DR OrthoDB; 3266779at2759; -.
DR Reactome; R-XTR-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000008143; Chromosome 4.
DR Bgee; ENSXETG00000006892; Expressed in skeletal muscle tissue and 21 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01578; AcnA_Mitochon_Swivel; 1.
DR CDD; cd01584; AcnA_Mitochondrial; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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 2: Evidence at transcript level;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW Lyase {ECO:0000256|RuleBase:RU362107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362107};
KW Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 69..505
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 584..713
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 520..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 85223 MW; 39256A406E43D39A CRC64;
MASYCLLASR LQQALGHGAR RYHVSSVLCQ RAKVAMSHFE ANEYINYERL DKNINIVRKR
LDRPLTLSEK IVYGHIDDPV TQEVVRGKTY LRLRPDRVAM QDATAQMAML QFISSGLPRV
AVPSTIHCDH LIEAQLGGEK DLKRAKDINQ EVYNFLATAA AKYGVGFWKP GSGIIHQIIL
ENYAFPGVLL IGTDSHTPNG GGLGGICIGV GGADAVDVMA GIPWELKCPN VIGVKLTGQL
SGWTSPKDVI LKVAGILTVK GGTGAIVEYH GPGVDSISCT GMATICNMGA EIGATTSVFP
YNHRMKKYLD KTGRSAIASL ADEFKSHLVP DEGCEYDQLI EINLDELKPH INGPFTPDLA
NPVSEVGAVA EQKGWPLDIR VGLIGSCTNS SYEDMGRAAA VAKQALAHGL KCKSQFTITP
GSEQIRATIE RDGYAAVLRD VGGVVLANAC GPCIGQWDRK DIKKGEKNTI VTSYNRNFTG
RNDANPETHA FVTSPEIVTA LSIAGTLKFD PEKDFLTGAD GKKFKLQPPD ADELPKSSFD
PGQDTYQHPP KEGSSLKVDV SPTSQRLQLL EPFDKWDGKD LENMQILVKV KGKCTTDHIS
AAGPWLKFRG HLDNISNNLL IGAINLENNK ANSVKNCVNQ EYGAVPDTAR YYKAHGIKWV
VIGDENYGEG SSREHAALEP RHLGGRAIIT KSFARIHETN LKKQGLLPLT FSDPADYDKI
HPEDKITIAE LKHLAPGKPV KCIITHQNGS QETILLNHTF NETQIEWFQA GSALNRMKEL
Q
//
