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Database: UniProt
Entry: A0A2B7XGQ6_9EURO
LinkDB: A0A2B7XGQ6_9EURO
Original site: A0A2B7XGQ6_9EURO 
ID   A0A2B7XGQ6_9EURO        Unreviewed;      1277 AA.
AC   A0A2B7XGQ6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Aconitate hydratase, mitochondrial {ECO:0000313|EMBL:PGH07808.1};
GN   ORFNames=GX51_01518 {ECO:0000313|EMBL:PGH07808.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH07808.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH07808.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH07808.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
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:PGH07808.1}.
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DR   EMBL; PDNC01000012; PGH07808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XGQ6; -.
DR   STRING; 2060905.A0A2B7XGQ6; -.
DR   OrthoDB; 3266779at2759; -.
DR   Proteomes; UP000224080; Unassembled WGS sequence.
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: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   InterPro; IPR018810; UPF0662.
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   Pfam; PF10303; DUF2408; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224080};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          567..993
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          1075..1201
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          424..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1277 AA;  139895 MW;  653DA9808145DA19 CRC64;
     MADSPAVSVP LDPKEQPILD QLLVIRDALL LLKQDKSRYI KSQDVLHYHD QVVEQVQRLN
     AIRTEHTVKH NRVDNVLDDC FQLISLLFLT VGRNNEAPAA YAMASTIKRL LDHLKEAAFY
     SQKDLDSVAK TLDTMQENIN RGKETYSPDI LKLLEVRLET CRKQLAELQH ELSFLSPKLA
     PTHETLVSIL RSTSAANTRS KFSASEVASF QEQLKVIQDS MKDGNFVEPD GSIPEGQEIV
     KALLDRCWKW SEIVLERRGQ IDERFKDPYS KLLEIRNQLD RLVMTQAWSL RETDLFMYQR
     KLNKIDESRV DGNFLDSYGK PADIHAQRTL LYLIRRSYAL IYGLLISSEP VSEALLPIYN
     QLQTLRKCLI EVKESGGVSN TRELYPYSMK LNSIDNMRVD VLFAFPCIPP HNFYREVPPL
     PRPGIGLSQP QPANQRSPKK FTPKVRQHRI SNGDIFNFFL AIAADISKMM RQYFCQRAAA
     SRKLAQCLPL GARIRSRGLA TEADPQSSAN SSSSRSPPYP KILNNLREVR RVLGTERSLT
     LAEKILYSHL DNVEESLLSD TQNGKNIRGQ ANLKLKPDRV AMQDASAQMA LLQFMTCGLP
     STAVPASIHC DHMIVGEKGA DVDLPASIKG NKEVFDFLES AAKKYGIEFW PPGAGIIHQT
     VLENYAAPGL VMLGTDSHTP NGGGLGAIAI GVGGADAVDA LVDAPWELKA PKVLGVRLEG
     KLSGWTAPKD IILHLAGKLT VRGGTGYIIE YYGPGVESLS CTGMATICNM GAEVGATTSL
     FPFSPSMVPY LRATNRGDIA DAAAAIASSG PQNLLRADIN AEYDQNITID LSILEPHING
     PFTPDLSIPL SSFAQTVREK KWPETFGAGL IGSCTNSSYE DMTRAEDLVK QASEAGLKPK
     ADFFITPGSE QIRATLDRDQ TLATFSAAGG TVLANACGPC IGQWKRTDGV KKGESNAILT
     SYNRNFRGRN DGNTATMNFL ASPEIVTAMT YAGSTTFNPM TDTLPTPSGK PFKFRAPTGF
     DLPKSGFESG NPDFQPSLAA PSPSCPVVIS PTSDRLAVLE PFSPFPSHNL TSLRVLYKVK
     GQCTTDTISA AGPWLKYKGH LPNISANTLI GAINAATDET NVAYDIDGST HSIPDLASKW
     KAEGTEWLVV AEDNYGEGSA REHAALQPRY LGGRIIAAKS FARIHETNLK KQGVVPLTFK
     DKADYDRIDA CDTVDTVGLY EVLTSGGQGG QEVKLRVTKK GSGEVFDIPM KHTLSKDQCG
     FILAGSALNL LAKKANK
//
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