ID W9XXN0_9EURO Unreviewed; 881 AA.
AC W9XXN0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aconitate hydratase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O5_01715 {ECO:0000313|EMBL:EXJ75019.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ75019.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ75019.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ75019.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:EXJ75019.1}.
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DR EMBL; AMGX01000002; EXJ75019.1; -; Genomic_DNA.
DR RefSeq; XP_007740521.1; XM_007742331.1.
DR AlphaFoldDB; W9XXN0; -.
DR STRING; 1182543.W9XXN0; -.
DR GeneID; 19186448; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_3_3_1; -.
DR OrthoDB; 1326656at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; 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 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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
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.
PE 4: Predicted;
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:UP000019471}.
FT DOMAIN 232..439
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 439..564
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 721..782
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 593..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 881 AA; 97626 MW; 3D8DE2FA9359B0C7 CRC64;
MPSFTHTAAC ITVPEPVSLQ LDNLLHILKD TRKIKILSPD RVNGQGVQPT EREAKPLLDE
IQYLADVLVG AGHPADAAAF RDVRELAILS TDFGGLGLRP DCENLSVQDT SELLFLISAH
LEAVNSAERA RSQLHPLSWR PQERRGMTLA EKIFAAHDID QRGEVKPGDV IRVDVDWILA
SELSWKGMER WYDQLGQPGI YRNDRFWLAG DHLVDPRVID TPKIRSFVKS NERARKEFKM
TDSQRMNYTI MHTEFCRERA QPGMFVIGSD SHTCSAGSVS CLAIGLGVAD VILPLITGET
WFKIPETVEI RFINQPKPGI SGKDVILYVL KELKRNTVAS DRVVEYTGPG VQYLSCDARF
AIANMTTEFG GVTGIFVPDA ITQTFINRRV QTKHRSNALY FRPDDDATYA ETHILDLAQV
EPFVARYPKP DDVVPVTEVE GLELQGCFIG ACTTTEEDLV LAALVLEKAM KLGAKPRSSG
KRKVVPGSMP ILHNLRKHGL IDIFENAGWE VGVPGCSYCV GMSADQAGKG EIWLTSQNRN
FENRMGPGAF GNLASAVTVA ASSFDMKVTN PASLLNLIDM SRVDAILDRE SKRDSPVGPD
FVEPGSRSSV HRTSDCQQML PNFAIRESRE AKLTLMAKSN SYPMHSDLQV NVDTATTESI
TPKARKLEIA SSIIRGKVAR LGDFIDTDAL APNEAISKPN ITREQLGTYC LYHTHPEFRR
QVRELGHNIV VAGEAFGCGS SREDAVGALQ GAGVQCVIAK SFAFIYGRNQ SNLGLLGFEM
KDPRFWEVIA DGREMKIYLD RSLLQLEVDD NGTYETFHFG LSPMQRRLME CGGAAKAFGR
WGKGLWEALT SQTPNHDIKN PLTASDFGTL EEDREQAKLQ W
//
