SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CCNA_00195 FitnessBrowser__Caulo:CCNA_00195 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 5 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)
54% identity, 98% coverage: 4:200/202 of query aligns to 540:734/758 of O14289

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Sites not aligning to the query:

486 modified: Phosphoserine
488 modified: Phosphoserine

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)
40% identity, 98% coverage: 1:198/202 of query aligns to 1:192/198 of P9WK95

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K154 (≠ D160) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

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)
33% identity, 89% coverage: 18:196/202 of query aligns to 13:163/170 of Q58667

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R26 (≠ K31) mutation R->K,V: Allows the recognition of substrates of IPMI enzymes since it becomes able to efficiently catalyze citraconate hydration and 3-isopropylmalate dehydration. Largely decreases substrate affinity for cis-homo(1-3)-aconitate.
T27 (= T32) mutation to A: Largely decreases substrate affinity for cis-homo(1-3)-aconitate while slightly increases activity on these substrates, and also decreases substrate affinity for maleate. Gains the ability to hydrate citraconate, an IPMI substrate.

2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
34% identity, 89% coverage: 18:196/202 of query aligns to 13:163/167 of 2pkpA

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binding zinc ion: D13 (≠ N18), C63 (= C79)

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)
46% identity, 25% coverage: 70:119/202 of query aligns to 655:704/778 of P19414

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Sites not aligning to the query:

1:16 modified: transit peptide, Mitochondrion
604 R→K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.

Query Sequence

>CCNA_00195 FitnessBrowser__Caulo:CCNA_00195
MKAFTRLDGRAAPLELANIDTDQIIPKQFLKTVEREGLAKGLFYDFRFDADGNEISDFVL
NKPEYKSASVLIAGDNFGCGSSREHAPWALMDFGIMCVISTSFADIFNNNCFNNGLLPVV
VSPEDLALLMDEAKGGNHMVSVDLEAQTVISPSGKTIGFDIDPVRKEKMLKGLDAIGETM
MHGGDIDLFESKRAISQPWLEA

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