Comparing WP_019622309.1 NCBI__GCF_000381785.1:WP_019622309.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 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)
30% identity, 97% coverage: 6:910/931 of query aligns to 4:836/865 of P36683
1l5jA Crystal structure of e. Coli aconitase b. (see paper)
30% identity, 96% coverage: 19:910/931 of query aligns to 16:836/862 of 1l5jA
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
23% identity, 50% coverage: 404:865/931 of query aligns to 1:392/423 of 4kp1A
4nqyA The reduced form of mj0499 (see paper)
23% identity, 50% coverage: 405:865/931 of query aligns to 1:379/409 of 4nqyA
>WP_019622309.1 NCBI__GCF_000381785.1:WP_019622309.1
MSYYSDYLEEIEVRKKDLGLNPKPIDSAELLSEIIAQIKDVGNEHREASLNFFIYNILPG
TTPAAGVKATFLKDIALGKETVAEISAEFALEQLSHMKGGPSVEALLDIALSDDAQAAAA
AEVLKSQVFLYDADSARLADAFKAGNAIAKDILESYSKAEFFTKLSDIPETIKVITYIAG
EGDISTDLLSPGNQSHSRADRELHGKCMISPEAQQEIAEMGKQNPDAKVMLIAEKGTMGV
GSSRMSGVNNVALWAGEKTSPYIPFINNNPVVAGTNGIAPIFLTTVGVTGGIGLDLKNWV
KKTDANGEVVRDANGDPVLEEAYSVATGTVLTIDTKAKKLYNGDQELVDIADAFTPQKVE
FMKAGGSYAVTFGKKLQTFAAETLGVEAPAVYAQSKEISHEGQGLTAVEKIFNRNAVGVT
SKTPLHTGSDVRVKVNIVGSQDTTGPMTCQELEAMAASTISTSVDGAFQSGCHTASVWDN
KAKANTPKLMAFMNAFGAITARDPKHVYHSMTDVIHKVLNDITVDDRAIIIGGDSHTRMS
KGVAFGADSGTVAIALATGESAMPIPESVKVTFKGSMKPHMDFRDIVHATQAQMLKKFGG
ENVFQGRVIEVQIGTLLADQAFTFTDWTAEMKAKASICISTDDTLIQSLELAKSRIQIMI
NKGMENEAGMLQGLIDLADKRIAEVKSGEAPALAPDDNAKYYAELVVDLDVIEEPMIADP
DVNNEDVSKRYTHDVIRPASYYDGRKVDLGFVGSCMVHKGDMQIIAAMLRNLEKKGPITF
KAPLVVAPPTYNIVDELKAEGDWELLEKFAGFEFSDENPKEAARTKYENILYLERPGCNL
CMGNQEKAEAGDTVLATSTRLFQGRVVEDTAEKKGESLLGSTPMVVLSCVLGRFPTLEEY
KEAVEGIDLTTFAPPSEDLSVASTAIPAARI
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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