ID A0A0B1PAB8_UNCNE Unreviewed; 817 AA.
AC A0A0B1PAB8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.- {ECO:0000256|RuleBase:RU362107};
GN ORFNames=EV44_g2276 {ECO:0000313|EMBL:KHJ33614.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ33614.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ33614.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
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 -!- 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 -!- 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:KHJ33614.1}.
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DR EMBL; JNVN01001334; KHJ33614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1PAB8; -.
DR STRING; 52586.A0A0B1PAB8; -.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; KWPETFG; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000030854; 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 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:SF2; HOMOCITRATE DEHYDRATASE, 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:UP000030854};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 100..525
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 607..732
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 817 AA; 88412 MW; C4D26F02F62A89A8 CRC64;
MLTLLPKFST KIGIIVASQH RFCVSRTLAT IATESRASSF SNNTDSRTPP YARLKKRLSQ
VRKILGDSRK LTLAEKILYS HLDNPEESLL SNTDNGLHIR GNANLKLKPD RVAMQDASAQ
MALLQFMTCN LTSTAVPTSI HCDHMIVAEG GADFDLQESI TDNKEIFDFL ESAARKYGIE
FWPPGAGIIH QTVLENYAAP ALMILGTDSH TPNAGGLASI AIGVGGADAV DAMVDAPWEL
KAPKILGVRL EGQLSDWTSP KDVILYLAGK LTVRGGTGYI IEYFGPGVNT LSATGMATIT
NMGAEVGATT SIFPYSPRHF HYLASTNRLS IAKKASEIFA SPPKLNLLAA DEDVEYDEVI
TINLSTLEPH INGPFTPDLS TPLSIFSSAV SSNKWPEKIS AGLIGSCTNS SYQDMTRAED
LVKQATSVGL KPTADILITP GSEQIRATLQ RDNTLATFED AGGVVLANAC GPCIGQWSRK
NTSKNHSNAI FTSYNRNFRG RNDGNPETMN FIASPEIVIA MSYAGTTKFN PILDSIETPT
GGQFRFKPPK GSELPSSGFE TGNPAFFVAT ATPSPETEIV ISPTSTRLAK LESFDPFPNS
DLQALRVLYK VSGKCTTDTI SAAGPWLKYK GHLPNISANT LIGATNASTG EVNTAYDIDG
TRYSIPELAQ KWKSQKISWL VVAEDNYGEG SAREHAALQP RYLGGRIILA KSLARIHETN
LKKQGILPLT FVDPTDYARI DACDEVETVG LYDLLKKGCR GSLSRTNSFV TLLVKKAKTA
EKFDILTKHT LSADQCEYIL AGSALNLMAM KKRGDFK
//
