Comparing RR42_RS23515 RR42_RS23515 bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
P36683 Aconitate hydratase B; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; 2-methyl-cis-aconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Escherichia coli (strain K12) (see 2 papers)
74% identity, 100% coverage: 1:859/861 of query aligns to 1:859/865 of P36683
1l5jA Crystal structure of e. Coli aconitase b. (see paper)
74% identity, 100% coverage: 1:859/861 of query aligns to 1:859/862 of 1l5jA
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
28% identity, 51% coverage: 379:820/861 of query aligns to 1:417/423 of 4kp1A
4nqyA The reduced form of mj0499 (see paper)
28% identity, 51% coverage: 380:820/861 of query aligns to 1:404/409 of 4nqyA
O14289 3-isopropylmalate dehydratase; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 43% coverage: 489:854/861 of query aligns to 131:503/758 of O14289
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 43% coverage: 452:818/861 of query aligns to 138:505/789 of P39533
Sites not aligning to the query:
Q9SIB9 Aconitate hydratase 3, mitochondrial; Aconitase 3; mACO1; Citrate hydro-lyase 3; EC 4.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 26% coverage: 475:698/861 of query aligns to 268:481/990 of Q9SIB9
Sites not aligning to the query:
>RR42_RS23515 RR42_RS23515 bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase
MLENYRAHVAERAALGIPPLPLTAKQTAELIELLKSPPAGEEQVLVDLITHRVPAGVDDA
AKVKASYLAAVALGKEACALISRAKAAELLGTMLGGYNISPLIELLDDAEIGPVAAEALK
KTLLMFDAFHDVKEKADKGNAIAKSVLQSWADAEWFTSRPEVPQSLTVTVFKVTGETNTD
DLSPAPDATTRPDIPLHALAMLKNARPGITPEEDGKRGPVKFIESLKEKGNLVAYVGDVV
GTGSSRKSATNSVLWFTGEDIPFVPNKRFGGVCLGSKIAPIFYNTMEDAGALPIELDVSQ
MEMGDVVELRPYDGKALKNGQVIAEFTVKSDVLFDEVRAGGRIPLIVGRGLTAKAREALG
LAPSTLFRLPHNPADTGRGFTLAQKMVGRACGLPEGKGIRPGTYCEPKMTSVGSQDTTGP
MTRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVKTHHTLPQFISTRGGISLRPGDGVI
HSWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGK
MQPGVTLRDLVNAIPLYAIKSGLLTVAKQGKKNIFSGRVLEIEGLPDLKVEQAFELSDAS
AERSAAGCSVRLNKEPIIEYINSNITLLKWMIAEGYQDPRSLSRRIQAMEAWLADPKLLE
PDADAEYAAVIEIDLADVHEPIVACPNDPDDVKTLSEVAGAKIDEVFIGSCMTNIGHFRA
ASKLLEGKRDIPVKLWVAPPTKMDAKQLTEEGHYGVFGTAGARTEMPGCSLCMGNQAQVR
EGATVMSTSTRNFPNRLGKNTNVYLGSAELAAICSRLGRIPTKEEYMSDMGVLATNGDQI
YKYLNFDKIEDFKGVADTVTV
Or try a new SitesBLAST search
SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory