SitesBLAST
Comparing WP_013706496.1 NCBI__GCF_000195295.1:WP_013706496.1 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 20 (the maximum) hits to proteins with known functional sites (download)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
35% identity, 92% coverage: 3:592/641 of query aligns to 55:731/789 of P39533
- K610 (≠ R492) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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)
35% identity, 91% coverage: 3:587/641 of query aligns to 60:721/778 of P19414
- R604 (= R492) mutation to K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.
Sites not aligning to the query:
- 1:16 modified: transit peptide, Mitochondrion
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
35% identity, 92% coverage: 3:593/641 of query aligns to 64:730/780 of P20004
- Q99 (= Q34) binding substrate
- DSH 192:194 (= DSH 118:120) binding substrate
- C385 (= C296) binding [4Fe-4S] cluster
- C448 (= C356) binding [4Fe-4S] cluster
- C451 (= C359) binding [4Fe-4S] cluster
- R474 (= R378) binding substrate
- R479 (= R383) binding substrate
- R607 (= R492) binding substrate
- SR 670:671 (= SR 533:534) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 8acnA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding nitroisocitric acid: Q71 (= Q34), T74 (= T37), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), I424 (= I360)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1fghA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding 4-hydroxy-aconitate ion: Q71 (= Q34), T74 (= T37), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), I424 (= I360), R451 (= R383)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1amjA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding iron/sulfur cluster: I144 (= I98), H166 (= H120), C357 (= C296), C420 (= C356), C423 (= C359)
- binding sulfate ion: Q71 (= Q34), R579 (= R492), R643 (= R534)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
35% identity, 92% coverage: 3:593/641 of query aligns to 36:702/753 of 1amiA
- active site: D99 (= D63), H100 (= H64), D164 (= D118), R446 (= R378), S641 (= S532), R643 (= R534)
- binding alpha-methylisocitric acid: Q71 (= Q34), T74 (= T37), H100 (= H64), D164 (= D118), S165 (= S119), R446 (= R378), R451 (= R383), R579 (= R492), S641 (= S532), S642 (= S533), R643 (= R534)
- binding iron/sulfur cluster: H100 (= H64), I144 (= I98), D164 (= D118), H166 (= H120), S356 (= S295), C357 (= C296), C420 (= C356), C423 (= C359), N445 (≠ P377)