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Database: UniProt
Entry: A0A066XP37_COLSU
LinkDB: A0A066XP37_COLSU
Original site: A0A066XP37_COLSU 
ID   A0A066XP37_COLSU        Unreviewed;       880 AA.
AC   A0A066XP37;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Putative aconitase {ECO:0000313|EMBL:KDN70973.1};
GN   ORFNames=CSUB01_11701 {ECO:0000313|EMBL:KDN70973.1};
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:KDN70973.1, 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   -!- 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:KDN70973.1}.
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DR   EMBL; JMSE01000270; KDN70973.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XP37; -.
DR   STRING; 1173701.A0A066XP37; -.
DR   eggNOG; KOG0454; Eukaryota.
DR   HOGENOM; CLU_006714_3_3_1; -.
DR   OMA; FLSCDAR; -.
DR   OrthoDB; 1326656at2759; -.
DR   Proteomes; UP000027238; 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:UP000027238}.
FT   DOMAIN          187..469
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          471..592
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          731..782
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   880 AA;  95988 MW;  206BFC7A180E6E2D CRC64;
     MMAVESSPSQ FMANVLSALK RIRGVDLDEA KQSYLGEHTS GPLEYGPGLD SSFSNLGQFF
     RFVHSELRSR DHVAEAEAIA HVAELCATDP ELGGLGIVGF VTGAVGWGPE SASTGSITNS
     SVLHKVEFLV DAWLSAVSSR EAASRQARPV MRKQLGGTPS NAYPMTLTEK ILAHHAFSLP
     SSRGVKPGDV VRVSLDWVIA SEVAWLGMLH SMRSIGQQSQ AWRNDRFWLT GDHAVDPRNY
     HLEKSRMLRR EMETAKRNLK MTENQGSNVH APPQDYKDIP PARLVPKRAE PGMLVVGADS
     HTCSGGAVSS LSIGLGATDN MIGLATGQTW FKVPESIRVN FTGKPAWHIK GKDVILFILR
     QLRRNTFAAD RVVEFGGSGA EYLSCDARFA ICNMCTELGA ITGIFVPDKV TRSFLEGRKF
     KVYKSNSVYF TPDKDAEYAA MFDIDLSRVE SAIAIYPSPD DVYPVTDHLG MKFDGCFIGA
     CTTTEEDLVL AALVLEVGLK RGLAIVPGKR LVVPGSRPIA RNLRILGLMD IYESAGFEQP
     SPGCSMCLGM GVDVAEEGSN WLSSQNRNFK NRMGKGSVGH ICSAATVAAA SFSMTLSDPT
     ELLREVDKSR YNELLEQCKA WRNRKHAAPQ RKHAHGDFLN EDVEYVEPAL TAGTVQQGEG
     QLSPKGTTAF ETSSGQLDGA SVIRGRVFTM GDFVDTDAII PAPFCSSPTD EALGSHCFEY
     VCPDFRDHVR QGYTVVVGGK AFGCGSSREE AARALKGIGV KCVIARSFSF IFGRNMPSIG
     LIGFIITDDE FYRMTNHGAD IQIDVQGRCV KVGGKEFGFR LDDMELRLVE NQGLAEAFRR
     HRKDVYDTLC CGKGASVELP SPASLADVSM ERRKPEELAW
//
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