SitesBLAST
Comparing 209008 MicrobesOnline__882:209008 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)
7lubB Crystal structure of recombinant human fumarase in complex with d-2- amino-3-phosphono-propionic acid (see paper)
58% identity, 98% coverage: 5:464/468 of query aligns to 1:461/462 of 7lubB
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, 97% coverage: 6:461/468 of query aligns to 4:459/467 of P05042
- R126 (≠ K128) binding substrate; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ L129) mutation to D: No effect.
- H129 (= H131) 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 131:134) binding in site B
- SSN 139:141 (= SSN 141:143) binding substrate
- H188 (= H190) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (= E317) 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, 97% coverage: 6:461/468 of query aligns to 1:456/456 of 1fuqA
- active site: N104 (= N109), T184 (= T189), H185 (= H190), S315 (= S320), K321 (= K326), E328 (= E333)
- binding citric acid: T97 (= T102), S136 (= S141), S137 (= S142), N138 (= N143)
- binding 3-trimethylsilylsuccinic acid: R123 (≠ K128), H126 (= H131), P127 (= P132), N128 (= N133), D129 (= D134)
1fuoA FumarasE C with bound citrate (see paper)
59% identity, 97% coverage: 6:461/468 of query aligns to 1:456/456 of 1fuoA
P07954 Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2 from Homo sapiens (Human) (see 4 papers)
58% identity, 98% coverage: 5:464/468 of query aligns to 49:509/510 of P07954
- T147 (= T102) mutation to A: Does not affect phosphorylation by PRKDC.
- S187 (= S142) mutation to A: Does not affect phosphorylation by PRKDC.
- K230 (= K185) to R: in FMRD and HLRCC; dbSNP:rs752232718
- R233 (= R188) to H: in HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair; dbSNP:rs121913123
- T236 (≠ L191) 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.
1fupA Fumarase with bound pyromellitic acid (see paper)
59% identity, 97% coverage: 7:461/468 of query aligns to 1:455/455 of 1fupA
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
54% identity, 98% coverage: 5:461/468 of query aligns to 2:459/464 of 7c18B
- binding fumaric acid: T100 (= T102), S139 (= S141), S140 (= S142), N141 (= N143), T187 (= T189), H188 (= H190), C318 (≠ S320), S319 (= S321), M321 (= M323), K324 (= K326), N326 (= N328)
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
54% identity, 99% coverage: 2:464/468 of query aligns to 24:487/488 of P08417
- M24 (= M2) mutation to 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.
- MN 24:25 (≠ MT 2:3) mutation to SF: Does not affect processing by the mitochondrial processing peptidase. Localizes both in the mitochondrion and cytosol. Exhibits high fumarate hydratase activity.
- 29:44 (vs. 7:22, 50% identical) mutation Missing: Does not affect subcellular location.
- H154 (= H131) 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
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)
52% identity, 97% coverage: 7:461/468 of query aligns to 5:459/461 of Q9ZCQ4
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
41% identity, 99% coverage: 2:464/468 of query aligns to 1:462/468 of Q9LCC6