SitesBLAST
Comparing WP_013532412.1 NCBI__GCF_000185905.1:WP_013532412.1 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)
7lubB Crystal structure of recombinant human fumarase in complex with d-2- amino-3-phosphono-propionic acid (see paper)
65% identity, 98% coverage: 7:464/465 of query aligns to 3:461/462 of 7lubB
P07954 Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2 from Homo sapiens (Human) (see 4 papers)
65% identity, 98% coverage: 7:464/465 of query aligns to 51:509/510 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 (= T191) 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.
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
64% identity, 98% coverage: 7:464/465 of query aligns to 29:487/488 of P08417
- 29:44 (vs. 7:22, 69% 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
- 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.
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
60% identity, 98% coverage: 7:461/465 of query aligns to 4:459/464 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)
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, 98% coverage: 7:461/465 of query aligns to 5:459/467 of P05042
- R126 (≠ K128) binding substrate; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ P129) 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.
1fupA Fumarase with bound pyromellitic acid (see paper)
59% identity, 98% coverage: 7:461/465 of query aligns to 1:455/455 of 1fupA
1fuqA Fumarase with bound 3-trimethylsilylsuccinic acid (see paper)
59% identity, 98% coverage: 7:461/465 of query aligns to 2:456/456 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, 98% coverage: 7:461/465 of query aligns to 2:456/456 of 1fuoA
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)
57% identity, 98% coverage: 7:461/465 of query aligns to 5:459/461 of Q9ZCQ4
A0A3Q0KQY7 Fumarate hydratase; Fumarase; Class II fumarase; SmFHII; EC 4.2.1.2 from Schistosoma mansoni (Blood fluke) (see paper)
46% identity, 99% coverage: 3:464/465 of query aligns to 6:484/488 of A0A3Q0KQY7
- S105 (= S100) binding (S)-malate
- S147 (= S142) binding (S)-malate
- N148 (= N143) binding (S)-malate
- T194 (= T189) binding (S)-malate
- H195 (= H190) binding (S)-malate
- 263:277 (vs. 251:257, 7% identical) mutation Missing: Remains as a tetramer. 17.35 degrees Celsius lower melting temperature (Tm) than wild-type with the highest thermal stability around pH 6.5. Similarly to wild-type, thermal stability increases with increasing NaCl concentration, in addition, acetate induces a positive thermoshift. No change in optimum pH. No effect in catalytic constants other than subtle differences for L-malate constants.
- S341 (= S321) binding (S)-malate
- K346 (= K326) binding (S)-malate
- N348 (= N328) binding (S)-malate
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)
50% identity, 97% coverage: 3:454/465 of query aligns to 7:456/474 of P9WN93
- SGT 104:106 (= SGT 100:102) binding substrate
- SSN 138:140 (= SSN 141:143) binding substrate
- T186 (= T189) binding substrate
- S318 (= S320) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S321) binding substrate
- KVN 324:326 (= KVN 326:328) binding substrate
4adlA Crystal structures of rv1098c in complex with malate (see paper)
50% identity, 96% coverage: 7:454/465 of query aligns to 3:448/459 of 4adlA
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
50% identity, 96% coverage: 7:454/465 of query aligns to 3:448/462 of 4apbD
- active site: H179 (= H190), C310 (≠ S320), K316 (= K326), E323 (= E333)
- binding fumaric acid: T98 (= T102), S130 (= S141), S131 (= S142), N132 (= N143), T178 (= T189), H179 (= H190), C310 (≠ S320), S311 (= S321), M313 (= M323), K316 (= K326), N318 (= N328)
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
43% identity, 99% coverage: 7:465/465 of query aligns to 6:463/468 of Q9LCC6
- T101 (= T102) binding L-aspartate; mutation to A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 80-fold decrease in catalytic efficiency.
- H134 (= H135) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
- S140 (= S141) binding L-aspartate; mutation to A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
- T141 (≠ S142) binding L-aspartate; mutation to A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
- N142 (= N143) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation to Q: 3000-fold decrease in catalytic efficiency.
- K183 (= K185) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T189) binding L-aspartate; mutation to A: 6280-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 2.3-fold decrease in catalytic efficiency.
- H188 (= H190) binding L-aspartate; mutation to A: 100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation H->K,Q,R: Loss of activity.
- S318 (= S320) mutation to A: Loss of activity.
- S319 (= S321) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I322) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M323) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P324) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K326) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation K->D,H,R,S,V: Loss of activity.
- N326 (= N328) mutation to A: 22500-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to Q: 168750-fold decrease in catalytic efficiency.
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
43% identity, 99% coverage: 6:465/465 of query aligns to 1:459/462 of 3r6qA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
43% identity, 99% coverage: 6:465/465 of query aligns to 2:460/463 of 3r6vG
6s88A Fumarate hydratase of mycobacterium tuberculosis in complex with formate and allosteric modulator n-(2-methoxy-5-((1,2,4,5-tetrahydro- 3h-benzo[d]azepin-3-yl)sulfonyl)phenyl)-2-(4-oxo-3,4- dihydrophthalazin-1-yl)acetamide (see paper)
48% identity, 96% coverage: 7:454/465 of query aligns to 2:439/450 of 6s88A
6s7wA Fumarate hydratase of mycobacterium tuberculosis in complex with formate and allosteric modulator n-(5-(azepan-1-ylsulfonyl)-2- methoxyphenyl)-2-(quinolin-4-yl)acetamide (see paper)
48% identity, 96% coverage: 7:454/465 of query aligns to 2:439/450 of 6s7wA
6s7sA Fumarate hydratase of mycobacterium tuberculosis in complex with formate and allosteric modulator n-(2-methoxy-5-(n-phenylsulfamoyl) phenyl)-2-(4-oxo-3,4-dihydrophthalazin-1-yl)acetamide (see paper)
48% identity, 96% coverage: 7:454/465 of query aligns to 2:439/450 of 6s7sA
6s7uA Fumarate hydratase of mycobacterium tuberculosis in complex with formate and allosteric modulator n-(5-(azepan-1-ylsulfonyl)-2- methoxyphenyl)-2-(1h-indol-3-yl)acetamide (see paper)
48% identity, 96% coverage: 7:454/465 of query aligns to 2:439/450 of 6s7uA
Query Sequence
>WP_013532412.1 NCBI__GCF_000185905.1:WP_013532412.1
MTAAKTRTETDTFGPIEVAADRYWGAQAQRSLGNFKIGWEKQPASIVRALGIVKRAAAEA
NMELKRLDPAIGKTIVEAAQEVIDGKLDEHFPLVVWQTGSGTQSNMNANEVISNRAIEML
GGVMGSKKPVHPNDHVNMSQSSNDTYPTAMHIACAERIVHDLLPALKHLHKALAAKSREF
NHIIKIGRTHTQDATPLTLGQEFSGYAAQVASSIKRIELTLPGLQELAQGGTAVGTGLNA
PVGFAERVADRIASITGIAFVTAPNKFEALAAHDSMVFSHGAINAAAAALFKIANDIRFL
GSGPRSGLGELSLPENEPGSSIMPGKVNPTQCEALTQVCVQVFGNNAALTFAGSQGHFEL
NVYNPLMAYNFLQSVKLLCDASVSFTDNCVVGIEAREDNIKAALDRSLMLVTALAPTIGY
DNAAKIAKTAHKKGTTLREEALATGLVSEADYDRLVRPEDMTHPG
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory