ID A0A1Q7EBN0_9CHLR Unreviewed; 451 AA.
AC A0A1Q7EBN0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Homoaconitate hydratase {ECO:0000256|ARBA:ARBA00032706};
GN ORFNames=AUH39_00730 {ECO:0000313|EMBL:OLC10963.1};
OS Chloroflexi bacterium 13_1_40CM_67_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805082 {ECO:0000313|EMBL:OLC10963.1, ECO:0000313|Proteomes:UP000187329};
RN [1] {ECO:0000313|EMBL:OLC10963.1, ECO:0000313|Proteomes:UP000187329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OLC10963.1}.
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DR EMBL; MNEQ01000011; OLC10963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7EBN0; -.
DR Proteomes; UP000187329; 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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok.
DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu.
DR NCBIfam; TIGR01343; hacA_fam; 1.
DR NCBIfam; TIGR02086; IPMI_arch; 1.
DR PANTHER; PTHR43822:SF25; HOMOACONITASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 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 4..230
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 271..392
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 451 AA; 47448 MW; 7D4F197C24173CE7 CRC64;
MAEKILSRVA LRDATAGDLV IAPVSRVMVH DSVIDAVIAG LRDLGKERVW DTTKVAVFVD
HAAPAPTPVV ADSHRVLREW VRAQGIATFY DAGEGVCHQI MVEEGYCESG TVIVGSDSHS
NSYGAVGAFG AGMGATDVAV ALALGRTWLR VPESIKVTFT GRPRKGVTMK DAIMRVVREV
GTDGARYKCV EFHGAGALPQ GDRITLAGMT TEMGAKAGIV VATPEAPDWL FPDHGAAYVN
EVTVDLSALE PQIAVPPRVD QVVDVSEAVG QPVDVVFLGS CTNGRLVDMR QAAAVLRGRR
ISPEVRLEVV PSSRRQFEDA MADGTLLALS AAGAVIGSSG CGPCLGRTGG VLAGQEICLS
TANRNYRGRM GSPDASIFIG SPYVAAVAAL TGVIDDPRPY LEASDDEFDN LVAQRRSERA
GRGASSVRSG DRARELMVAV ARRGVAAEID D
//
