ID A0A0E9N9M0_SAICN Unreviewed; 1233 AA.
AC A0A0E9N9M0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00015940};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Mitochondrial transcription factor 1 {ECO:0000256|ARBA:ARBA00013836};
GN ORFNames=G7K_0816-t2 {ECO:0000313|EMBL:GAO46587.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO46587.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO46587.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO46587.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO46587.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO46587.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
CC -!- FUNCTION: Mitochondrial transcription factor that confers selective
CC promoter recognition on the core subunit of the yeast mitochondrial RNA
CC polymerase. Interacts with DNA in a non-specific manner.
CC {ECO:0000256|ARBA:ARBA00024915}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01026}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO46587.1}.
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DR EMBL; BACD03000004; GAO46587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9N9M0; -.
DR STRING; 698492.A0A0E9N9M0; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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 Gene3D; 1.10.8.100; Ribosomal RNA adenine dimethylase-like, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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 Pfam; PF00398; RrnaAD; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Reference proteome {ECO:0000313|Proteomes:UP000033140};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01026};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 827..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..546
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 626..753
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 1210..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 903
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 953
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 1014
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 1233 AA; 136268 MW; 078637A7DC3AD456 CRC64;
MISFPPSHLR ITPPPPPPPT LGFRGITFHT RGHWFRFPNQ YPPYIATMFR ALKTASSAAR
NVRSLATVAD ASGKVQLSNL EKGKYINYEK LSENIDIVRQ RLNRPLTYSE KVVYGHLDNP
HEQDIERGKS YLKLRPDRVA CQDATAQMAI LQFMSAGMPS VAVPTTVHCD HLIEAQVGGV
KDLARAKDIN KEVYNFLSTA CAKYNIGFWR PGSGIIHQII LENYAFPGGM MIGTDSHTPN
GGGLGMIAVG VGGADAVDVM ADIPWELKCP KVIGVKLTGK LSGWTAPKDV ILKVAGILTV
KGGTGAIVEY FGPGVDSLSS TGMGTICNMG AEIGATTSIF PFNKSMSDYL VATGRESIAK
HAQKFQHVLR ADEGAEYDQV IEINLNELEP HINGPFTPDL ATPLSKFAET AEKNGWPLDL
KVGLIGSCTN SSYEDMSRSA SIADQALAHG LKAKSGFLVT PGSEQIRATI ARDGQLETFE
KIGGSVLANA CGPCIGQWDR RDVEKGTPNS IFSSYNRNFT GRNDANPKTH SFVTSPDLVT
AFIFAGDLRF NPLTDTLKGA DGKEFKFEAP TGAALPARGY DPGENTYQAP PEERTSVQVD
VAPTSDRLQL LSPFKAWDGK DLTDAKILIK AKGKCTTDHI SMAGPWLKYR GHLDNISNNY
MIGAINAENG EANTLKNQLT GEYQPVPDVA RAYKAQDIPW VVIGEDNLGE GSSREHAALE
PRHLGGRAII VKSFARIHET NLKKQGLLPL TFVDGSAYDK INPTDVVDIV GLPEFAPGKQ
LTLRVKPQNG EAWETKLDHT FNEEQGISEV MSRKTIRVGC VNYGVCVFYQ LLAFFLVTFY
CGIRYVAYTY LIALLFFGDF QPTTPRRQLD MRGTQLLRTS FEALPSQARL STYATGVPKR
TLMVNQDLAN RLAEAYDWSY YKNGDILEMN PGFGLFTRAI WNVAKPRRHV LMEPHKKFIP
IMEDFDAKTE GRIKYTSLEG YDWATYDKLI ADGTITPENQ SMERVNDSLL LFASMPNGAT
GEALAVQFLC TLPRRNWIQK YGRVRMLIWM KTKSADRLLV GPGGHTRARP TIIAQACADM
RVIASPKDAH MGAFNYDEAA MKDVIETTPD DWRQRGDYTL VEFTPKEKPL FNSDFAEFDY
VLRNLFILRA TAMEKSLMML GSGSDSLIKC MPSGLDLSKP VNAYTVEEFD QVTQAFSKWP
FKPTELFEKG WTNDREKDPK GENGVVKNIG KKK
//
