SitesBLAST – Find functional sites

 

SitesBLAST

Comparing Synpcc7942_2548 Synpcc7942_2548 isopropylmalate isomerase small subunit 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 4 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)
37% identity, 76% coverage: 8:160/202 of query aligns to 543:697/758 of O14289

query
sites
O14289
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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)
34% identity, 67% coverage: 9:144/202 of query aligns to 8:141/198 of P9WK95

query
sites
P9WK95
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D

Sites not aligning to the query:

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)
36% identity, 58% coverage: 8:125/202 of query aligns to 3:112/170 of Q58667

query
sites
Q58667
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2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
36% identity, 58% coverage: 8:125/202 of query aligns to 3:112/167 of 2pkpA

query
sites
2pkpA
V
 
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D

Query Sequence

>Synpcc7942_2548 Synpcc7942_2548 isopropylmalate isomerase small subunit
MGSEILEVTGRAVPLVGNDIDTDRIIPARFLRSVTFDGLGANVFIDDRQQLQGQHPFDQA
QYQGATVLVVNRNFGCGSSREHAPQAIAKWGIQAIVGESFAEIFFGNCLSLGIPCVTAGA
AAVAELQAAIASDPSQPVTVDLEELQVRRGAWSAELTLAPGPLQMLRSGQWDATGQLVAN
AEAIAQTAANLPYVGWQAIAAS

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory