ID A0QRG9_MYCS2 Unreviewed; 654 AA.
AC A0QRG9;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Aconitate hydratase, putative {ECO:0000313|EMBL:ABK69737.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:ABK69737.1};
GN OrderedLocusNames=MSMEG_1112 {ECO:0000313|EMBL:ABK69737.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK69737.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK69737.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000480; ABK69737.1; -; Genomic_DNA.
DR RefSeq; WP_011727420.1; NZ_SIJM01000011.1.
DR RefSeq; YP_885507.1; NC_008596.1.
DR AlphaFoldDB; A0QRG9; -.
DR STRING; 246196.MSMEG_1112; -.
DR PaxDb; 246196-MSMEI_1081; -.
DR GeneID; 66732576; -.
DR KEGG; msm:MSMEG_1112; -.
DR PATRIC; fig|246196.19.peg.1102; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000000757; Chromosome.
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:ABK69737.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT DOMAIN 10..284
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 285..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 521..582
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 654 AA; 70769 MW; 44B5932685B84AE8 CRC64;
MSQSVTHKLI GSHLVSGDMT PGDEIAIRID QTLTQDATGT LVMQELEALQ LDRARTEVSV
QYVDHNLLQT DEKNAEDHEY LRTAAQRFGL WFSKPGNGVS HPTHMQRFGI PGKTMVGSDS
HTPAAGSLGM LAIGVGGLEV ALAIAGEPLH LRMPEVWGIR LEGELPQWCS AKDVILEMLR
RHDVKGGLNR ILEYHGPGLD SLSAMDRHVI ANMGAELGAT TTVFPSDEAV REFLVAEDRG
DDWVELLADE GAEYDIEETI DLSEIEPLIA KPSSPGNVVT VAEVAGEPVS QVVIGSSANP
GLRDFAIAAA MVRGRQTSPE VSFDVNPTSR EILTDLTKMG ATTDLVINGA RIHQAGCMGC
IGMGQAPATG RNSLRTMPRN FPGRSGTRED SVWLCSPETA AASAITGVIT DPRQWAKDND
VDYPALDLPS HHTVNTAMLV EPPPPEEAKA VEVVKGPNIS DLPDLRPLGD TIEAPVLLKV
GDNISTDEIS PAGARALPYR SNIPKLAMFS FTQVDETYPE RAKSTPQGHI VVGGDNYGQG
SSREHAAIAP RHLGLLAVIA KSFARIHWQN LANFGVLALE FVDDADYDRI DQDDVLTLSD
VWQTLHDDQP LIVTNTTKNT TFSVCHRLSS RQIDHVLAGG LIPWLAREKD HAKH
//