ID R7SBT8_TREMS Unreviewed; 790 AA.
AC R7SBT8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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.- {ECO:0000256|RuleBase:RU362107};
GN ORFNames=TREMEDRAFT_40787 {ECO:0000313|EMBL:EIW66789.1};
OS Tremella mesenterica (strain ATCC 24925 / CBS 8224 / DSM 1558 / NBRC 9311 /
OS NRRL Y-6157 / RJB 2259-6 / UBC 559-6) (Jelly fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Tremellaceae; Tremella.
OX NCBI_TaxID=578456 {ECO:0000313|EMBL:EIW66789.1, ECO:0000313|Proteomes:UP000054539};
RN [1] {ECO:0000313|Proteomes:UP000054539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fries {ECO:0000313|Proteomes:UP000054539};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH711540; EIW66789.1; -; Genomic_DNA.
DR RefSeq; XP_007007289.1; XM_007007227.1.
DR AlphaFoldDB; R7SBT8; -.
DR GeneID; 18493188; -.
DR KEGG; tms:TREMEDRAFT_40787; -.
DR VEuPathDB; FungiDB:TREMEDRAFT_40787; -.
DR eggNOG; KOG0453; Eukaryota.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000054539; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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 3: Inferred from homology;
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:UP000054539};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 73..509
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 589..717
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 790 AA; 85437 MW; 1FD5512B3CDE3D21 CRC64;
MATSRMISSP LRTARYRLPT LSRRSMATVQ SSIGDKKVEM SNLEQGRYIN YQRIEDNLQI
VRSRLNRPLT LAEKIVYGHL DNPHEQDIER GVSYLKLRPD RVACQDATAQ MAILQFMSAG
LPQTAVPTSV HCDHLIQAQV GGVKDLARAI EINKEVYDFL ATACAKYGIG FWKPGSGIIH
QIILENYAIP GLMMIGTDSH TPNAGGLGMV ACGVGGADAV DVMADIPWEL KAPKVIGVRL
DGQMSGWTTP KDVILKVAGI LTVKGGTGAI IEYHGPGVES LSCTGMATIC NMGAEIGATT
SLFPFNHRMS KYLEATRRPA IARYAEEFNH NLQPDEGCEY DQLININLNE LEPHINGPFT
PDLATPISKF ASEVKKHSWP AELKVGLIGS CTNSSYEDMT RSASIATEAA SHGLKAKSLF
TITPGSEQVR ATIERDGVVK AFEDVGGVVL ANACGPCIGQ WDRKDVKKGE ANSIVTSYNR
NFTGRNDANP ATHAFVTSPD LVTAMVFAGD LTFNPLTDTL KGADGKEFKF SEPSGFELPA
KGYDAGENTF QAPPKDGASV QVAVSPTSDR LQLLKPFASW DGKDIIEAPV LIKAKGKCTT
DHISAGGPWL KYRGHLENIS QNCLIGAINA DNGEANKVLN QFTGEYGPVP TVGASYRDQG
VPWVVIGDEN YGEGSSREHA ALEPRFLGGR AVICRSFARI HETNLKKQGM LPLWFKNPAD
YDKISGSDKI SILGLNEFKP GQDITVEITH KDGSKEKFLC TSSINEGQWG WFKAGSALNM
MAAAAKARGA
//
