Comparing WP_019896250.1 NCBI__GCF_000384235.1:WP_019896250.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
67% identity, 98% coverage: 1:844/860 of query aligns to 1:852/865 of P36683
1l5jA Crystal structure of e. Coli aconitase b. (see paper)
67% identity, 98% coverage: 1:844/860 of query aligns to 1:852/862 of 1l5jA
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
29% identity, 51% coverage: 374:812/860 of query aligns to 1:417/423 of 4kp1A
4nqyA The reduced form of mj0499 (see paper)
29% identity, 51% coverage: 376:812/860 of query aligns to 2:404/409 of 4nqyA
P19414 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
25% identity, 40% coverage: 466:812/860 of query aligns to 163:502/778 of P19414
Sites not aligning to the query:
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 40% coverage: 467:810/860 of query aligns to 165:505/789 of P39533
Sites not aligning to the query:
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)
23% identity, 48% coverage: 415:823/860 of query aligns to 76:483/758 of O14289
Sites not aligning to the query:
>WP_019896250.1 NCBI__GCF_000384235.1:WP_019896250.1
MLKAYREHVAEREAQNIPPLPMDAQQTAELVEYIKNPSQLSDAEKDMVMDLFVNRVPPGV
DDASYVKAGFLADVAAEKVSVDAITPVKAVFYLGTMLGGYNVQPLVDLLESPNDAVAAEA
VKALSQTLLVYDAYNDVLEKSKTNANAKKVLESWAEAEWFKAKPKMPEQITVTVFKVDGE
TNTDDLSPATAAWSRPDIPLHAKEMLKTRLDDLDATIAELEAKGHPVAYVGDVVGTGSSR
KSAMNSVMWFFGDDIPYVPNKRKGGVVLGGKIAPIFFNTAEDSGSMPIECDVEKLEMGDV
ITIYPYDGKIVNEQGETVSTFELAPDTMPDEVRAGGRVPLIIGRGLTDKSREALGLEPSD
VFIRPQDKSQADHGYTLAQKMVGKACGVAGVRPGMYCEPRMTTVGSQDTTGAMTRDEMKE
LACLGFNADLVMQSFCHTAAYPKPVDVKLQHTLPEFFTSRGGVSLRPGDGVIHSWLNRLL
LPDTVGTGGDSHTRFPIGISFPAGSGLVAFGATLGVMPLNMPESVLVRFKGEMQPGVTLR
DLVNAIPYQAIQDGLLTVEKKGKQNVFNGRVLEIEGLEHLKVEQAFELSDASAERSANGC
VVKLGQEPIIEYLKSNMALIDWMVENGYQDARTLLRRRDAMQAWIDNPELMEADADANYK
EVIEIDLNTIKEPIVACPNDPDDVKLMSEVEGTQIDEVFIGSCMTNIGHYRAAGKVLEQM
GTVPTRLWVAPPTKMDERQLIEEGYYSIFGKVGARTEMPGCSLCMGNQARVADGATVFST
STRNFPNRLGNGANVYLGSAELAAVCSVLGRIPTQAEYMDAVSMLNTMSSEVYRYLQFDQ
MADYKVESPKQLSDIGVAVA
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