ID H6CBU4_EXODN Unreviewed; 824 AA.
AC H6CBU4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Aconitase {ECO:0000313|EMBL:EHY61241.1};
GN ORFNames=HMPREF1120_09177 {ECO:0000313|EMBL:EHY61241.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY61241.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY61241.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY61241.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; JH226138; EHY61241.1; -; Genomic_DNA.
DR RefSeq; XP_009161702.1; XM_009163454.1.
DR AlphaFoldDB; H6CBU4; -.
DR STRING; 858893.H6CBU4; -.
DR GeneID; 20313816; -.
DR VEuPathDB; FungiDB:HMPREF1120_09177; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_3_1; -.
DR InParanoid; H6CBU4; -.
DR OMA; WAGMETT; -.
DR OrthoDB; 1326656at2759; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901607; P:alpha-amino acid biosynthetic process; IEA:UniProt.
DR CDD; cd01577; IPMI_Swivel; 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; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033940; IPMI_Swivel.
DR InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR NCBIfam; TIGR02087; LEUD_arch; 1.
DR PANTHER; PTHR43822:SF2; 3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
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; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT DOMAIN 216..433
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 433..558
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 674..744
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 609..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 90926 MW; 380FBFC61D2DABE2 CRC64;
MTARIVPQQV HLDLKPEDLT PSQSKCILLF EDAFQTQIVF TSQSREEPRS NLIVFLGILA
ESLRSTNSDQ LAAMLEEVIW RCKEHPDFGG YGFSDKDDLQ PGEEGEIIFL FSAYLEAFKH
AARASQRPAP SSLKPPGRRS MTMTEKIFAF HDVSQRGYVR PGDIIQVDVD WVIASELSWQ
GMERVYSAIG RPGIFRNDRF WLAGDHRVEP PLYNEPKVKA LMDNCRKAKT DFKMTEFQGF
NYTIMHTEFV RERAQPGMLI IGADSHTCSA GAVSCLAIGM GATDVCMPLV TGQTWFTVPK
TVQLRMINKP PRGVGGKDTI LYILKQFKRN TIASDRVVEF TGPGMKYLSC DARFAISNMC
TEFGAVTAIF ESDERTVDFI EGRRLKRHKS ESVYFKADPG AEYAATVDVD LSEVRPFVAI
NPSPDNVVPV NEVEGTSLDG CFIGACTTAE EDLVIGALVL RAGLDQGLTP VPHGRRLVVP
GSKPIRRKLE QFGLLDVYRR AGFKIGVPGC SMCVGQGVDQ AAPGEVWLSS QNRNFKNRMG
PGSHANLGSA ATVAVSSFSM KMTDPTKLLE LIDMDLLERY LGYQPFADIE VSPWSDVVQY
SEPYGQDLEV DNCAESNPES PAPTSDEGGN PDSVNKVISG KVLRLGDFID TDAIIPSKFL
ASCTTNEALG DHCMEFFMPE FRQRVKDGFN VVVGGHGFGC GSSRDVAVNA LLGCGVKCVI
ARSFAFIYAR NQPNIGLLGI VIEDESFYLA AQDGREINVD LEQNSVHCGA QTFKFSLSQM
EKQLIAAGGL TEAFRRFGTR LFDVMCQRRE VAATGHRTKD IESF
//
