SitesBLAST
Comparing GFF2631 FitnessBrowser__psRCH2:GFF2631 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)
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)
58% identity, 98% coverage: 3:458/464 of query aligns to 5:460/461 of Q9ZCQ4
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)
59% identity, 99% coverage: 2:460/464 of query aligns to 4:462/467 of P05042
- R126 (≠ S124) binding ; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ P125) mutation to D: No effect.
- H129 (= H127) 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 (= HPND 127:130) binding in site B
- SSN 139:141 (= SSN 137:139) binding
- H188 (= H186) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (= E313) 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)
59% identity, 98% coverage: 2:457/464 of query aligns to 1:456/456 of 1fuqA
- active site: N104 (= N105), T184 (= T185), H185 (= H186), S315 (= S316), K321 (= K322), E328 (= E329)
- binding citric acid: T97 (= T98), S136 (= S137), S137 (= S138), N138 (= N139)
- binding 3-trimethylsilylsuccinic acid: R123 (≠ S124), H126 (= H127), P127 (= P128), N128 (= N129), D129 (= D130)
1fuoA FumarasE C with bound citrate (see paper)
59% identity, 98% coverage: 2:457/464 of query aligns to 1:456/456 of 1fuoA
1fupA Fumarase with bound pyromellitic acid (see paper)
59% identity, 98% coverage: 3:457/464 of query aligns to 1:455/455 of 1fupA
7lubB Crystal structure of recombinant human fumarase in complex with d-2- amino-3-phosphono-propionic acid (see paper)
58% identity, 98% coverage: 3:458/464 of query aligns to 3:459/462 of 7lubB
P07954 Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2 from Homo sapiens (Human) (see 4 papers)
58% identity, 98% coverage: 3:458/464 of query aligns to 51:507/510 of P07954
- T147 (= T98) mutation to A: Does not affect phosphorylation by PRKDC.
- S187 (= S138) mutation to A: Does not affect phosphorylation by PRKDC.
- K230 (= K181) to R: in FMRD and HLRCC; dbSNP:rs752232718
- R233 (= R184) to H: in HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair; dbSNP:rs121913123
- T236 (≠ M187) modified: Phosphothreonine; by PRKDC; mutation to A: Abolished interaction with H2AZ1 and localization to chromatin in response to DNA damage.; mutation to D: Phosphomimetic mutant; promotes interaction with H2AZ1, leading to increased localization to chromatin in response to DNA damage.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 1:43 modified: Variant sequence, Missing (in isoform Cytoplasmic)
- 46 S→A: Does not affect phosphorylation by PRKDC.
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
56% identity, 99% coverage: 3:460/464 of query aligns to 4:462/464 of 7c18B
- binding fumaric acid: T100 (= T98), S139 (= S137), S140 (= S138), N141 (= N139), T187 (= T185), H188 (= H186), C318 (≠ S316), S319 (= S317), M321 (= M319), K324 (= K322), N326 (= N324)
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
55% identity, 98% coverage: 3:458/464 of query aligns to 29:485/488 of P08417
- 29:44 (vs. 3:18, 50% identical) mutation Missing: Does not affect subcellular location.
- H154 (= H127) 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.
P9WN93 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
47% identity, 97% coverage: 3:450/464 of query aligns to 11:456/474 of P9WN93
- SGT 104:106 (= SGT 96:98) binding
- SSN 138:140 (= SSN 137:139) binding
- T186 (= T185) binding
- S318 (= S316) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S317) binding
- KVN 324:326 (= KVN 322:324) binding
4adlA Crystal structures of rv1098c in complex with malate (see paper)
47% identity, 97% coverage: 3:450/464 of query aligns to 3:448/459 of 4adlA