ID A0A066XLX6_COLSU Unreviewed; 817 AA.
AC A0A066XLX6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CSUB01_03108 {ECO:0000313|EMBL:KDN68649.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN68649.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(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:KDN68649.1}.
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DR EMBL; JMSE01000640; KDN68649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066XLX6; -.
DR STRING; 1173701.A0A066XLX6; -.
DR eggNOG; KOG0453; Eukaryota.
DR HOGENOM; CLU_006714_2_2_1; -.
DR OMA; KWPETFG; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000027238; 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; 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:UP000027238};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 87..535
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 617..745
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 817 AA; 88391 MW; A7FC19832495D7EE CRC64;
MAPIELASRS GGAARRLLTH TRPCLSASSC LPIRRAFATA QDVDQQDSEM RRLLPKSIKP
DTYRKLHDNL LKVRHVLGQQ RLTLAEKILY SHLDNVEDSL LTDTENGRNI RGRANLKLNP
DRVNMQDASA QMALLQFMSC NLAKPAIPAS IHCDHLIVGS KGAESDLTDG ISVNKEVFDF
LESAGRKYGM DFWPPGAGII HQTVLEVYAL PGIMMLGTDS HSPNAGGLST ITIGVGGADA
VEALVGAPWE LKAPRVLGVK LTGKLNDWVS PKDVILNLAG KLTVRGGTGF IVEYFGEGVE
TLSATGMATI CNMGAEVGAT TSIFPYTAAS ERYLLQTRRG AQHHALDDYK KWGSFDFKAD
EGAQYDQVIE INLSELEPHI NGPFTPDLAT PLSAFKDTIQ QEQWPEVLSA GLIGSCTNSS
YEDMTKVESM VKQAEKAGLK PKAPFYITPG SEQIRATLER DGTLQTLEGA GGIILSNACG
PCIGQWKRQD DIPKGQLNAI LTSYNRNFKG RNDGNPGTMN FLASPEIVTA MAYAGATTFN
PMTDKLQTPD GKEFKFEAPQ GLENPKAPFE SGVASLQAIT PEAHNPDVQV AIAPTSERLA
FLEPFAPFPE SDLSGLKVLV KITGKCTTDT ISAAGPWLKY KGHLPNISTN TLNTAVNKET
GEVNAAYDVD GSKHTIPELA QKWKERGQEW LVVAEHNYGE GSAREHAALQ PRYLGARVVL
TKSFARIHET NLKKQGVVPL TFANEADYDK IAACDEVSTV GLYEMLQNGG QGKVQLLVKK
KDGSEVLIPT NHAVTKDQAG FILAGSALSM LAKRNQA
//
