ID A0A1F4ACP3_9PROT Unreviewed; 422 AA.
AC A0A1F4ACP3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=3-isopropylmalate dehydratase {ECO:0000313|EMBL:OGA09859.1};
GN ORFNames=A3H33_03285 {ECO:0000313|EMBL:OGA09859.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_02_FULL_65_20.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797488 {ECO:0000313|EMBL:OGA09859.1, ECO:0000313|Proteomes:UP000176396};
RN [1] {ECO:0000313|EMBL:OGA09859.1, ECO:0000313|Proteomes:UP000176396}
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:OGA09859.1}.
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DR EMBL; MEQZ01000167; OGA09859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4ACP3; -.
DR Proteomes; UP000176396; Unassembled WGS sequence.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd01583; IPMI; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR InterPro; IPR033941; IPMI_cat.
DR NCBIfam; TIGR01343; hacA_fam; 1.
DR NCBIfam; TIGR02086; IPMI_arch; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 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 23..286
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 290..412
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 422 AA; 44439 MW; 986B9F90E9608362 CRC64;
MATQTLSQKI IARAAGRKSV APGEIVTCRV DLAMMHDSGG PRRVKPMLEK LGAKVWDPDK
IVVITDHYLP ANDDESRRII HIAREWVKEA GVTRFHDGEG ICHVVLPQKG YLHPGMFVVG
GDSHSPTGGA FGAYMFGVGA TEMLGVLVTG EIWLKVPHTI LVDWSGKLGP AVSAKDMMLA
LCGRLGLDGG QYQAIQYAGD AISALPMQER MTLCNMAPEV GAQTGLVAPD AVTRDFLESV
GASGTDGETW QGDPGAPLLA HHRFDASTLE PQVAAPHSPA NAAPIGRHAG TRIDTAYIGA
CTGAKIEDLR MAARVLGGRR AAAHVRFVVA PASAHDQAIA AREGTLQILV DAGAELLANS
CGICAGYGDD RLGENEVAIT STARNFKGRM GAASSQVYLA SPYTVAASAI AGKICDPREF
FK
//
