ID A0A1M4WKX9_9CLOT Unreviewed; 763 AA.
AC A0A1M4WKX9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:SHE81857.1};
GN ORFNames=SAMN02745158_01665 {ECO:0000313|EMBL:SHE81857.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE81857.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHE81857.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE81857.1,
RC ECO:0000313|Proteomes:UP000184245};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; FQVI01000006; SHE81857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M4WKX9; -.
DR STRING; 1122155.SAMN02745158_01665; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000184245; Unassembled WGS sequence.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015932; Aconitase_dom2.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, 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.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184245}.
FT DOMAIN 51..480
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 651..696
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 763 AA; 82177 MW; 787626688F3AD44F CRC64;
MIQLYDTGAY LVNGTEIIPD TGDAQAALKS KLGGQAPTKE EAARNTIAYG ILKEHNTSGN
MEKLTVKFDK LTSHDITFVG IIQTARASGL EKFPVPYVLT NCHNSLCAVG GTINEDDHMF
GLTCAKKYGG VYVPPHQAVI HQFAREMLAG GGKMILGSDS HTRYGALGTM AMGEGGPELV
KQLLGQTYDI TMPGVVGVYL TGEPIPGVGP QDVALAIIGA VFANGYVKNK VMEFVGPGVE
KLSADFRIGV DVMTTETTCL SSIWKTDDAI REFYEIHKRP EEYKELAPGA VAYYDGMVYV
DLGKIRPMIA MPFHPSNTYT IDELNANLMD ILDDVEKKAQ VSLDGKVPFT LKDKVRDGRL
YVEQGIIAGC AGGGFENICD AADILKGASI GADAFTLSVY PASTPIYMEL AKNGTLATLI
ETGAIVKTAF CGPCFGAGDT PANNAFSIRH STRNFPNREG SKIQNGQISS VALMDARSIA
ATAANKGYLT AATEYAGSYR KPQYHFDKTI YDNRVFDSKG VADPNVEIQF GPNIKDWPQM
SPLAENLILK VVSEIHDPVT TTDELIPSGE TSSYRSNPLG LAEFTLSRKD PAYVGKAKEV
QKAQKAIEAG TCPLEALPEL KPVMETIQAQ YPEIGKGNIG VGSTIFAVKP GDGSAREQAA
SCQKVLGGWA NIANEYATKR YRSNLINWGM LPFLIQEGEL PFANGSYILV PGIKSAVENK
VPEITAYAVG EGLTPFTLTL GELTDDEREI ILKGCLINYN RRG
//
