ID G8BZK2_TETPH Unreviewed; 784 AA.
AC G8BZK2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Name=TPHA0K01970 {ECO:0000313|EMBL:CCE65330.1};
GN OrderedLocusNames=TPHA_0K01970 {ECO:0000313|EMBL:CCE65330.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65330.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65330.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR EMBL; HE612866; CCE65330.1; -; Genomic_DNA.
DR RefSeq; XP_003687764.1; XM_003687716.1.
DR AlphaFoldDB; G8BZK2; -.
DR STRING; 1071381.G8BZK2; -.
DR GeneID; 11533382; -.
DR KEGG; tpf:TPHA_0K01970; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; NTHAFVA; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000005666; Chromosome 11.
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:UP000005666};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 70..507
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 586..715
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 784 AA; 85889 MW; 90B122323DC68AE8 CRC64;
MLSARSVLRK HVSSNASRNF SSTAIKSSLT RDSKVNQNLL EDHSFINYKQ NLEYVDIVRK
RLNRPLTYAE KILYGHLDKP HEQEIIRGTS YLKLRPDRVA CQDATAQMAI LQFMSAGLPE
VAKPVTVHCD HLIQAQIGGD KDLKRAIDLN KEVYDFLASS TAKYNMGFWK PGSGIIHQIV
LENYAFPGAL IIGTDSHTPN AGGLGQLAIG VGGADAVDVM SNLAWELKAP KILGVKLTGK
MNGWTSPKDI ILKLAGITTV KGGTGKIVEY FGEGVDTFSA TGMGTICNMG AEIGATTSVF
PFNKSMVDYL DATKRNKIAE FAQLYKGDLL SADKGAEYDE VIEIDLNTLE PYVNGPFTPD
LATPISKMKD VAVKNNWPLE VKVGLIGSCT NSSYEDMSRA ASIVKDAAKH GLKSKSIFTV
TPGSEQIRAT IQRDGQLATF EEFGGTVLAN ACGPCIGQWD RKDIKKGDKN TIVSSFNRNF
TSRNDGNPDT HSFVASPEIT TAFAIAGDLR FNPLTDKLKD KDGNEFLLKP PSGVGLPVNG
YDPGENTYQA PPQERAKVTV KVSPTSDRLQ LLQPFAPWDG KDALNMPILI KALGKTTTDH
ISMAGPWLKY RGHLENISNN YMIGAINAEN KKANSVKNVY TGEYKGVPDT ARDYRDTNHK
WVVIGDENFG EGSSREHAAL EPRFLGAFAI ITKSFARIHE TNLKKQGLLP LNFKNTADYD
KINPDDKIDI LGLAELAPGK IVTMRVHPKS GEAWDCPLTH TFNEEQIEWF KAGSALNKIK
NDKA
//
