SitesBLAST
Comparing WP_010964289.1 NCBI__GCF_000008765.1:WP_010964289.1 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, 93% coverage: 3:598/642 of query aligns to 54:735/789 of P39533
- K610 (≠ R494) 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, 100% coverage: 3:642/642 of query aligns to 59:777/778 of P19414
- R604 (= R494) 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: 3:591/642 of query aligns to 63:726/780 of P20004
- Q99 (= Q35) binding substrate
- DSH 192:194 (= DSH 119:121) binding substrate
- C385 (= C297) binding [4Fe-4S] cluster
- C448 (= C357) binding [4Fe-4S] cluster
- C451 (= C360) binding [4Fe-4S] cluster
- R474 (= R379) binding substrate
- R479 (= R384) binding substrate
- R607 (= R494) binding substrate
- SR 670:671 (= SR 535:536) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
34% identity, 92% coverage: 3:592/642 of query aligns to 35:699/753 of 8acnA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S534), R643 (= R536)
- binding nitroisocitric acid: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R494), S641 (= S534), S642 (= S535), R643 (= R536)
- binding iron/sulfur cluster: H100 (= H65), D164 (= D119), H166 (= H121), S356 (= S296), C357 (= C297), C420 (= C357), C423 (= C360), I424 (= I361)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
34% identity, 92% coverage: 3:592/642 of query aligns to 35:699/753 of 1fghA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S534), R643 (= R536)
- binding 4-hydroxy-aconitate ion: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R579 (= R494), S641 (= S534), S642 (= S535), R643 (= R536)
- binding iron/sulfur cluster: H100 (= H65), D164 (= D119), H166 (= H121), S356 (= S296), C357 (= C297), C420 (= C357), C423 (= C360), I424 (= I361), R451 (= R384)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
34% identity, 92% coverage: 3:592/642 of query aligns to 35:699/753 of 1amjA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S534), R643 (= R536)
- binding iron/sulfur cluster: I144 (= I99), H166 (= H121), C357 (= C297), C420 (= C357), C423 (= C360)
- binding sulfate ion: Q71 (= Q35), R579 (= R494), R643 (= R536)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
34% identity, 92% coverage: 3:592/642 of query aligns to 35:699/753 of 1amiA
- active site: D99 (= D64), H100 (= H65), D164 (= D119), R446 (= R379), S641 (= S534), R643 (= R536)
- binding alpha-methylisocitric acid: Q71 (= Q35), T74 (= T38), H100 (= H65), D164 (= D119), S165 (= S120), R446 (= R379), R451 (= R384), R5