ID A0A1F9EU32_9DELT Unreviewed; 651 AA.
AC A0A1F9EU32;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=3-isopropylmalate dehydratase {ECO:0000313|EMBL:OGQ10575.1};
GN ORFNames=A2138_26560 {ECO:0000313|EMBL:OGQ10575.1};
OS Deltaproteobacteria bacterium RBG_16_71_12.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1797848 {ECO:0000313|EMBL:OGQ10575.1, ECO:0000313|Proteomes:UP000176731};
RN [1] {ECO:0000313|EMBL:OGQ10575.1, ECO:0000313|Proteomes:UP000176731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGQ10575.1}.
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DR EMBL; MGQY01000390; OGQ10575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9EU32; -.
DR Proteomes; UP000176731; 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 GO; GO:1901607; P:alpha-amino acid biosynthetic process; IEA:UniProt.
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; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR43822:SF2; 3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 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 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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}.
FT DOMAIN 78..131
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT DOMAIN 223..641
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 651 AA; 69912 MW; 241FEB583CAC6B56 CRC64;
MVRFSGRVLY LADDLDLLER QLKGEILQHD PGRKLIDNIS TDELTPGWVC FWYDETLGDY
CLVGLRGGKV GKDSIKNAKP AVIVSGLSKG CGSSRETAPY AEKVAGVQLV VAKTIEKIYG
QNCRNIGLLT TTSESVLPRI ERGEAIPLAE FTEGLNEIER GIVEYGGLFN YNKARLAGEV
TPPPVTTPPR PMTLVEKIIA SRAIADAKTG KVGLPAVKPG DALFCRTDVR FSHDYTTAMC
DSLFTAGYGD DAKLRDPSSV FAMRDHLTFR NKIMSDADRA KGLHVLVDNL GTEQERFVKK
HGIRYFGLAP DGTGSEAICH NAVMEELGGP GDIIVGTDSH TCTAGALGAF AFGVGSTDMA
NAWYTADIQV KVPASVKYVL TGMPAKGVTA KDVMLYVMSQ QYAKDGNCIG KVLELSGPGL
AHLNMDERAT LTNLAVECGA TTGIIEADDV TKQYLMKFRG WPEQRAARGH LRADHGAQYD
ATFTIDLAAV PQMVATPGDP RNGVAVEELR KAHGAVKIDI AYGGSCTGGK MADMDMYAEV
LARGLERGMK VKEGVQLFIQ FGSQRIKRYA IERGYPELFK QAGAQVIEPS CGACINAGPG
VSKGKDQVTV SAINRNFPGR SGPGQVYLAS PRVVAASALS GTIVTPEELF R
//
