Comparing WP_012383230.1 NCBI__GCF_000019845.1:WP_012383230.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 6 hits to proteins with known functional sites (download)
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)
60% identity, 100% coverage: 1:201/201 of query aligns to 537:734/758 of O14289
Sites not aligning to the query:
P9WK95 3-isopropylmalate dehydratase small subunit; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 95% coverage: 1:191/201 of query aligns to 1:184/198 of P9WK95
Q58667 Methanogen homoaconitase small subunit; HACN; Homoaconitate hydratase; EC 4.2.1.114 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
39% identity, 54% coverage: 18:126/201 of query aligns to 13:110/170 of Q58667
2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
39% identity, 54% coverage: 18:126/201 of query aligns to 13:110/167 of 2pkpA
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
47% identity, 27% coverage: 65:119/201 of query aligns to 650:707/780 of P20004
Sites not aligning to the query:
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
40% identity, 25% coverage: 70:119/201 of query aligns to 631:680/754 of 5acnA
Sites not aligning to the query:
>WP_012383230.1 NCBI__GCF_000019845.1:WP_012383230.1
MEKFTTLTGVAAPLKITNVDTDMIIPKQYLKTIKRTGLGEGLFSELRFKDDGTENPDFVL
NQPAYRKASILVAGDNFGCGSSREHAPWALLDFGIRCVISTSFADIFYNNCFKNGILPIK
VTPEQLALLMEDAERGANATLTVDLENQTIRGPDGGSIPFNIDPFRKHCLLNGLDDIGLT
MQKADEISAYEERQAKQHAWL
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