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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//