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
//