ID A0A1U7PP05_9BACI Unreviewed; 709 AA.
AC A0A1U7PP05;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aconitase {ECO:0000313|EMBL:SIT75174.1};
GN ORFNames=SAMN05428946_1140 {ECO:0000313|EMBL:SIT75174.1};
OS Edaphobacillus lindanitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Edaphobacillus.
OX NCBI_TaxID=550447 {ECO:0000313|EMBL:SIT75174.1, ECO:0000313|Proteomes:UP000187550};
RN [1] {ECO:0000313|EMBL:SIT75174.1, ECO:0000313|Proteomes:UP000187550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MNA4 {ECO:0000313|EMBL:SIT75174.1,
RC ECO:0000313|Proteomes:UP000187550};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR EMBL; FTPL01000001; SIT75174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7PP05; -.
DR STRING; 550447.SAMN05428946_1140; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000187550; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 6.20.20.10; -; 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; IPR006250; Aconitase_put.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
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; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 9..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 515..581
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 709 AA; 77395 MW; E5574D8F7B51B361 CRC64;
MRMNVTQKLI KSHLLSGEMV SGREIGLKID QTLTQDATGT MVMLELEAMG IERAQTEASA
QYVDHNVIQV DNKNADDHLF LQSATRRFGL YYSRPGNGVS HPVHMQRLAV PGKTLLGSDS
HTCANGCMGM LAMGAGGIDV AMAIAGEPIY IKMPQVWGVK LTGELPEWVS AKDVILEMLR
RHDVKGGVGK IIEYYGPGLE NLSAMDRHVI ANMGAELGAT TTVFPSDGEI RHFLKTQGRE
GDWVELLADE GAEYDLHEEI NLSELEPLIA LPSSPGNVVT VREVADEPIY QSYIGSSANP
GYRDFAVASK IVEGNRVPDN VSFDINPTSR QLLTDLVKEG HIANLLTAGG RLHQAGCNGC
IGMGQAPATH ENSLRTTPRN FPGRSGTLED KVFLCSPETA AASALAGKIT DPRTLNMPYP
RVHDPEEPTV DVKLLDEPIP LEEARKVELH KGPNIASIPD MDPLHDRLEV PVLLKMKDNI
STDEILAGGA RVLPYRSNLP EISKFAFEIV DPTYYKRAME QRGAGGHAVV AGYNYGQGSS
REHAALAPRY LGLRVALAKD FARIHWQNLV NFGILPVTFM NPEDYDALEQ GDILVLENLK
EKIRNGNEFM ISVKNSNRRI PVQHALSPRQ IEIMIEGGLI NWVKKNNENA GNADVGEKVV
CSACHGTGKQ SDEEGWQYAC TVCNGTGYVT PGDTTARVAD VDATKRILD
//
