SitesBLAST
Comparing 6936601 FitnessBrowser__SB2B:6936601 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3oceA Crystal structure of fumarate lyase:delta crystallin from brucella melitensis bound to cobalt
58% identity, 97% coverage: 3:462/472 of query aligns to 2:460/461 of 3oceA
6wngA Crystal structure of an aspartate ammonia-lyase from elizabethkingia anophelis nuhp1
55% identity, 98% coverage: 2:462/472 of query aligns to 2:462/466 of 6wngA
- binding fumaric acid: T101 (= T101), S140 (= S140), T141 (= T141), N142 (= N142), T187 (= T187), Q188 (= Q188), G317 (= G317), S318 (= S318), S319 (= S319), I320 (= I320), M321 (= M321), K324 (= K324), N326 (= N326)
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
49% identity, 98% coverage: 2:462/472 of query aligns to 1:459/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
49% identity, 97% coverage: 4:462/472 of query aligns to 2:458/462 of 3r6qA
P0AC38 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Escherichia coli (strain K12) (see 2 papers)
54% identity, 98% coverage: 2:462/472 of query aligns to 4:465/478 of P0AC38
- D10 (= D8) mutation to A: Loss of activity.; mutation to N: Reduces Kcal by 80%. Increases KM for aspartic acid 3-fold.
- R15 (≠ A13) mutation to A: No effect on kcat. Increases KM for aspartic acid 2.5-fold.
- H26 (≠ Q24) mutation to N: No effect on kcat. Increases KM for aspartic acid 3-fold.
- R29 (= R27) mutation to A: No effect on kcat. Increases KM for aspartic acid 40-fold.
- K55 (= K53) mutation to R: Loss of activity.
- H124 (= H121) mutation to L: Reduces activity by 30%.
- S143 (= S140) mutation to G: Reduces kcat by 90%. Increases KM for aspartic acid 4-fold.; mutation to T: Reduces kcat by 98.5%. Increases KM for aspartic acid 2-fold.
- K327 (= K324) mutation to R: Reduces activity by 99.7%. Increases KM for aspartic acid 5-fold.
1jswA Native l-aspartate ammonia lyase (see paper)
55% identity, 96% coverage: 2:455/472 of query aligns to 4:458/459 of 1jswA
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
43% identity, 97% coverage: 4:460/472 of query aligns to 4:460/464 of 7c18B
- binding fumaric acid: T100 (= T101), S139 (= S140), S140 (≠ T141), N141 (= N142), T187 (= T187), H188 (≠ Q188), G317 (= G317), C318 (≠ S318), S319 (= S319), I320 (= I320), M321 (= M321), K324 (= K324), N326 (= N326)
Q9ZCQ4 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Rickettsia prowazekii (strain Madrid E) (see paper)
41% identity, 97% coverage: 2:461/472 of query aligns to 3:461/461 of Q9ZCQ4
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
41% identity, 97% coverage: 4:462/472 of query aligns to 29:487/488 of P08417
- 29:44 (vs. 4:19, 44% identical) mutation Missing: Does not affect subcellular location.
- H154 (= H130) mutation to R: Abolished fumarate hydratase activity and ability to participate in DNA repair.
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 24 M→S: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.; mutation M->V,I: Abolishes processing by the mitochondrial processing peptidase. Mainly localizes in the cytosol, with a small fraction in the mitochondrion. Reduced fumarate hydratase activity.
- 24:25 MN→SF: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.
P05042 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Escherichia coli (strain K12) (see 4 papers)
41% identity, 97% coverage: 1:460/472 of query aligns to 1:460/467 of P05042
- R126 (= R127) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ H128) mutation to D: No effect.
- H129 (= H130) mutation to N: No effect on fumarase activity and essentially same conformation compared to the wild-type, but appears to dramatically reduce binding of ligands at the B-site.
- HPND 129:132 (≠ HPNN 130:133) binding in site B
- SSN 139:141 (≠ STN 140:142) binding
- H188 (≠ Q188) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (≠ Q315) mutation to Q: There is essentially no effect on the affinity values for both S-malate and fumarate. In contrast, the catalytic efficiency values have been lowered by 10-fold in both directions.
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
41% identity, 97% coverage: 4:459/472 of query aligns to 2:456/456 of 1fuqA