SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_245526003.1 NCBI__GCF_000023265.1:WP_245526003.1 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 6 hits to proteins with known functional sites (download)

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)
49% identity, 94% coverage: 5:192/199 of query aligns to 8:193/198 of P9WK95

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K154 (≠ A153) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

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)
43% identity, 93% coverage: 6:191/199 of query aligns to 545:732/758 of O14289

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Sites not aligning to the query:

486 modified: Phosphoserine
488 modified: Phosphoserine

2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
35% identity, 54% coverage: 8:114/199 of query aligns to 1:107/167 of 2pkpA

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binding zinc ion: D13 (= D15), C63 (≠ V70)

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)
35% identity, 54% coverage: 8:114/199 of query aligns to 1:107/170 of Q58667

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R26 (≠ K28) 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 (≠ R29) 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.

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
38% identity, 26% coverage: 61:112/199 of query aligns to 658:709/780 of P20004

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P20004

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SR 670:671 (= SR 73:74) binding substrate

Sites not aligning to the query:

99 binding substrate
192:194 binding substrate
385 binding [4Fe-4S] cluster
448 binding [4Fe-4S] cluster
451 binding [4Fe-4S] cluster
474 binding substrate
479 binding substrate
607 binding substrate

5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
37% identity, 26% coverage: 61:112/199 of query aligns to 631:682/754 of 5acnA

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active site: S642 (= S72), R644 (= R74)
binding tricarballylic acid: R666 (≠ D96)

Sites not aligning to the query:

active site: 100, 101, 165, 447
binding fe3-s4 cluster: 145, 147, 167, 358, 421, 424, 446
binding tricarballylic acid: 198, 235

Query Sequence

>WP_245526003.1 NCBI__GCF_000023265.1:WP_245526003.1
MREWAGRMVPLGRSDVDTDQIIPSEWLKRISRTGFGEGLFSEWREDPTFVLNDPRMAGAT
ILVARENFGVGSSREHAVWALTDYGFRVVVSPRFGDIFRQNATKNGLLPVVLDTAIVERL
LEASASDPTIVARVDVVSGRFEVPELGLEASFALDPAVRHRFIHGLDDIGISLQHEAEIE
AFEARRPSWLPRLEGSASA

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