SitesBLAST
Comparing AZOBR_RS06120 FitnessBrowser__azobra:AZOBR_RS06120 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)
P07954 Fumarate hydratase, mitochondrial; Fumarase; HsFH; EC 4.2.1.2 from Homo sapiens (Human) (see 4 papers)
68% identity, 100% coverage: 1:466/466 of query aligns to 44:510/510 of P07954
- S46 (≠ G3) mutation to A: Does not affect phosphorylation by PRKDC.
- T147 (= T103) mutation to A: Does not affect phosphorylation by PRKDC.
- S187 (= S143) mutation to A: Does not affect phosphorylation by PRKDC.
- K230 (= K186) to R: in FMRD and HLRCC; dbSNP:rs752232718
- R233 (= R189) to H: in HLRCC; catalytically inactive mutant; abolished ability to promote DNA repair; dbSNP:rs121913123
- T236 (≠ L192) 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)
7lubB Crystal structure of recombinant human fumarase in complex with d-2- amino-3-phosphono-propionic acid (see paper)
68% identity, 99% coverage: 7:466/466 of query aligns to 2:462/462 of 7lubB
P08417 Fumarate hydratase, mitochondrial; Fumarase; EC 4.2.1.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
65% identity, 99% coverage: 5:466/466 of query aligns to 26:488/488 of P08417
- 29:44 (vs. 8:23, 69% identical) mutation Missing: Does not affect subcellular location.
- H154 (= H132) 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.
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)
63% identity, 98% coverage: 8:463/466 of query aligns to 5:460/461 of Q9ZCQ4
7c18B Crystal structure of fumarasec from mannheimia succiniciproducens in complex with fumarate
62% identity, 98% coverage: 5:463/466 of query aligns to 1:460/464 of 7c18B
- binding fumaric acid: T100 (= T103), S139 (= S142), S140 (= S143), N141 (= N144), T187 (= T190), H188 (= H191), C318 (≠ S321), S319 (= S322), M321 (= M324), K324 (= K327), N326 (= N329)
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)
63% identity, 98% coverage: 7:463/466 of query aligns to 4:460/467 of P05042
- R126 (≠ K129) binding substrate; mutation to A: 10-fold decrease of fumarase activity.
- K127 (≠ P130) mutation to D: No effect.
- H129 (= H132) 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 132:135) binding in site B
- SSN 139:141 (= SSN 142:144) binding substrate
- H188 (= H191) active site, Proton donor/acceptor; mutation to N: 200-fold decrease of fumarase activity.
- E315 (= E318) 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)
63% identity, 98% coverage: 7:462/466 of query aligns to 1:456/456 of 1fuqA
- active site: N104 (= N110), T184 (= T190), H185 (= H191), S315 (= S321), K321 (= K327), E328 (= E334)
- binding citric acid: T97 (= T103), S136 (= S142), S137 (= S143), N138 (= N144)
- binding 3-trimethylsilylsuccinic acid: R123 (≠ K129), H126 (= H132), P127 (= P133), N128 (= N134), D129 (= D135)
1fuoA FumarasE C with bound citrate (see paper)
63% identity, 98% coverage: 7:462/466 of query aligns to 1:456/456 of 1fuoA
1fupA Fumarase with bound pyromellitic acid (see paper)
63% identity, 98% coverage: 8:462/466 of query aligns to 1:455/455 of 1fupA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
45% identity, 98% coverage: 7:465/466 of query aligns to 2:459/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
45% identity, 98% coverage: 7:465/466 of query aligns to 1:458/462 of 3r6qA
Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
45% identity, 99% coverage: 5:465/466 of query aligns to 3:462/468 of Q9LCC6
- T101 (= T103) 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 (= H136) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
- S140 (= S142) 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 (≠ S143) 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 (= N144) 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 (= K186) mutation to A: Loss of activity. Does not affect tertiary structure.
- T187 (= T190) 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 (= H191) 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 (= S321) mutation to A: Loss of activity.
- S319 (= S322) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
- I320 (= I323) mutation to A: 50-fold decrease in catalytic efficiency.
- M321 (= M324) mutation to A: 338-fold decrease in catalytic efficiency.
- P322 (= P325) mutation to A: Almost no change in catalytic efficiency.
- K324 (= K327) 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 (= N329) 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.
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)
51% identity, 98% coverage: 8:464/466 of query aligns to 11:465/474 of P9WN93
- SGT 104:106 (= SGT 101:103) binding substrate
- SSN 138:140 (= SSN 142:144) binding substrate
- T186 (= T190) binding substrate
- S318 (= S321) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S322) binding substrate
- KVN 324:326 (= KVN 327:329) binding substrate
4adlA Crystal structures of rv1098c in complex with malate (see paper)
51% identity, 98% coverage: 8:464/466 of query aligns to 3:457/459 of 4adlA
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
51% identity, 98% coverage: 8:464/466 of query aligns to 3:457/462 of 4apbD
- active site: H179 (= H191), C310 (≠ S321), K316 (= K327), E323 (= E334)
- binding fumaric acid: T98 (= T103), S130 (= S142), S131 (= S143), N132 (= N144), T178 (= T190), H179 (= H191), C310 (≠ S321), S311 (= S322), M313 (= M324), K316 (= K327), N318 (= N329)
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)
50% identity, 98% coverage: 8:464/466 of query aligns to 2:448/450 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)
50% identity, 98% coverage: 8:464/466 of query aligns to 2:448/450 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)
50% identity, 98% coverage: 8:464/466 of query aligns to 2:448/450 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)
50% identity, 98% coverage: 8:464/466 of query aligns to 2:448/450 of 6s7uA
6s7kA Fumarate hydratase of mycobacterium tuberculosis in complex with formate and allosteric modulator n-(2-methoxy-5-(n-methylsulfamoyl) phenyl)-2-(4-oxo-3,4-dihydrophthalazin-1-yl)acetamide (see paper)
50% identity, 98% coverage: 8:464/466 of query aligns to 2:448/450 of 6s7kA
Query Sequence
>AZOBR_RS06120 FitnessBrowser__azobra:AZOBR_RS06120
MTGKTGMRTETDSFGPIEVAADRYWGAQTQRSLRNFRIGGERMPPALVRALGIQKKASAL
ANMALEVLDPRLGRAIVEAAEEVIDGTLADHFPLVVWQTGSGTQTNMNANEVISNRAIEA
LGGEMGSKKPVHPNDHVNMGQSSNDSFPTAMHIAAAEQIHHELLPALEHLHAALAAKAAE
FADIVKIGRTHLQDATPLTLGQEFSGYAAQIAYGIERVKASLPQLYRLAQGGTAVGTGLN
AKTGFAEAFAAEVASITGLPFVTAENKFEALATHDALVDAHGSLNTLAVSLMKIANDIRL
LGSGPRCGIGEIALPENEPGSSIMPGKVNPTQSEAMTMVCAQVMGNQTTVSIAGATGHFE
LNVFKPVIAYNVLQSIRLLADACNSFTDNAVVGIEANRERIGQLLNESLMLVTALNPHIG
YDNAAKIAKKAHKEGTTLKQAGVALGLLTEEQFDQWVKPETMVKPR
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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