ID A0A179D5I8_9BACT Unreviewed; 645 AA.
AC A0A179D5I8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:OAQ21233.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:OAQ21233.1};
GN ORFNames=TDIS_0453 {ECO:0000313|EMBL:OAQ21233.1};
OS Thermosulfurimonas dismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Thermosulfurimonas.
OX NCBI_TaxID=999894 {ECO:0000313|EMBL:OAQ21233.1, ECO:0000313|Proteomes:UP000078390};
RN [1] {ECO:0000313|EMBL:OAQ21233.1, ECO:0000313|Proteomes:UP000078390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S95 {ECO:0000313|EMBL:OAQ21233.1,
RC ECO:0000313|Proteomes:UP000078390};
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Slobodkin A.I., Ravin N.V.;
RT "Genome analysis of Thermosulfurimonas dismutans, the first thermophilic
RT sulfur-disproportionating bacterium of the phylum Thermodesulfobacteria.";
RL Submitted (APR-2016) 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:OAQ21233.1}.
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DR EMBL; LWLG01000002; OAQ21233.1; -; Genomic_DNA.
DR RefSeq; WP_068668894.1; NZ_LWLG01000002.1.
DR AlphaFoldDB; A0A179D5I8; -.
DR STRING; 999894.TDIS_0453; -.
DR PATRIC; fig|999894.6.peg.456; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000078390; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR006250; Aconitase_put.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01342; acon_putative; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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:0000313|EMBL:OAQ21233.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 7..284
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 282..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 511..581
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 645 AA; 70145 MW; 599270D877E134DE CRC64;
MGLTVAEKII ERHLVSGSLK RGEPIAIRID QTLTQDATGT MAYLEFEAIG IDRVRTELSV
SYVDHNLLQT DFRNADDHRF LQTVAARYGL WFSRPGNGIC HQVHLERFAR PGRTLLGSDS
HTPTAGGCGM IAIGAGGLDV AMAMAGEPFH LIMPKILGVH LTGKLPPWVS ARDVALWLLR
KLTVKGGLGK ILEYFGPGVK ELSVPDRATI ANLGTEMGAT TSVFPADEVT RAWLYAQGRE
GDFEEILPDE DARYDEVIEL DLSSLEPLAA CPSSPDNVKP VAEIAGKPVA QVIIGSCANS
SLRDLLVVAE VLGRHPVHRD TCLEINPGSL QVVENLEALG KFQSLVHGGA RIHQSGCLGC
IGMGQAPPTE AISLRTFTRN FPGRSGTRPD YVYLVSPETA VASAVRGVIT DPRELGDYPE
ISLPEKFILN DTLLVPPLPD EEALKVEILR GPNIVPLPKF DPLPEDLEGE ILLKVGDNIT
TDHIMPAGAK ILPLRSNLPA ISEYVFSAID PEFSKKALAL KEKGTAVVIL GGENYGQGSS
REHAALAPRY LGVRLKIAKS FARIHKANLI NFGILPVVLE NPEDYDRLAA GDRIRVPDIR
KALSEGAERL RIEVPGKEEI WGRLELTERD REIILSGCLL NMVKK
//
