SitesBLAST
Comparing 6938034 FitnessBrowser__SB2B:6938034 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)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
58% identity, 99% coverage: 5:706/706 of query aligns to 4:703/707 of 6yswA
- active site: A66 (= A67), I71 (≠ L72), A84 (≠ S85), Q88 (≠ H89), G112 (= G113), E115 (= E116), P136 (= P137), E137 (= E138), G145 (= G146), D264 (≠ E268), S422 (= S427), H443 (= H448), E455 (= E460), N493 (= N498)
- binding coenzyme a: E23 (= E24), M25 (= M26), A66 (= A67), D67 (= D68), I68 (= I69), P136 (= P137), E137 (= E138), L140 (= L141), T290 (= T294), K293 (= K297)
P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
44% identity, 98% coverage: 14:706/706 of query aligns to 49:762/763 of P40939
- V282 (≠ M229) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (= I252) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ I289) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E460) active site, For hydroxyacyl-coenzyme A dehydrogenase activity; to Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
39% identity, 100% coverage: 3:706/706 of query aligns to 6:714/715 of 1wdlA
- active site: A69 (= A67), N89 (≠ S85), N93 (≠ H89), G117 (= G113), E120 (= E116), P139 (= P137), E140 (= E138), P147 (= P145), G148 (= G146), S430 (= S427), H451 (= H448), E463 (= E460), N501 (= N498)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G318), I324 (≠ L320), M325 (= M321), D344 (= D341), I345 (= I342), A400 (= A397), V401 (= V398), E403 (= E400), N428 (= N425), T429 (= T426), S430 (= S427)
P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
39% identity, 100% coverage: 3:706/706 of query aligns to 6:714/715 of P28793
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
39% identity, 100% coverage: 3:706/706 of query aligns to 6:706/707 of 1wdmA
- active site: A69 (= A67), N89 (≠ S85), N93 (≠ H89), G117 (= G113), E120 (= E116), P139 (= P137), E140 (= E138), P147 (= P145), G148 (= G146), S430 (= S427), H451 (= H448), E463 (= E460), N501 (= N498)
- binding acetyl coenzyme *a: K142 (≠ Q140), D297 (≠ T293), M459 (= M456), N501 (= N498), P534 (= P531), Y652 (≠ F651), L658 (≠ P657)
- binding nicotinamide-adenine-dinucleotide: G321 (= G317), A322 (≠ G318), I324 (≠ L320), M325 (= M321), D344 (= D341), V401 (= V398), E403 (= E400), N428 (= N425), S430 (= S427), N454 (≠ S451)
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
39% identity, 96% coverage: 4:682/706 of query aligns to 7:691/719 of 6tnmA
- active site: A68 (= A67), F73 (≠ L72), G116 (= G113), E119 (= E116), P138 (= P137), E139 (= E138), G147 (= G146), N271 (≠ E268), S429 (= S427), H450 (= H448), E462 (= E460), N500 (= N498)
- binding adenosine-5'-triphosphate: D343 (= D341), I344 (= I342), V400 (= V398), V401 (≠ F399), V406 (≠ L404), K584 (= K579)
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 96% coverage: 4:682/706 of query aligns to 7:691/729 of P21177
- G116 (= G113) mutation to F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
- G322 (= G319) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H448) active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
36% identity, 98% coverage: 12:705/706 of query aligns to 8:690/692 of 6iunB
- active site: A60 (= A67), F65 (≠ L72), E73 (≠ D80), H77 (= H89), G101 (= G113), E104 (= E116), E124 (= E138), G132 (= G146), K248 (≠ E268), S407 (= S427), H428 (= H448), E440 (= E460), N478 (= N498)
- binding nicotinamide-adenine-dinucleotide: G300 (= G319), T301 (≠ L320), M302 (= M321), E321 (≠ D341), T322 (≠ I342), Y365 (= Y385), A377 (= A397), V378 (= V398), E380 (= E400), V384 (≠ L404), V388 (≠ M408), N405 (= N425), S407 (= S427)
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
34% identity, 99% coverage: 8:703/706 of query aligns to 5:706/723 of Q08426
- V40 (≠ K45) to G: in dbSNP:rs1062551
- I41 (≠ A46) to R: in dbSNP:rs1062552
- T75 (≠ Q87) to I: in dbSNP:rs1062553
- K165 (= K179) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- K171 (≠ D185) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
- A274 (= A292) to T: in dbSNP:rs2302819
- A325 (≠ V339) to G: in dbSNP:rs1062555
- K346 (= K360) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- K584 (= K589) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- K598 (≠ S603) to T: in dbSNP:rs1042437
- T606 (vs. gap) to P: in dbSNP:rs1042438
Sites not aligning to the query:
- 3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
7o4uA Structure of the alpha subunit of mycobacterium tuberculosis beta- oxidation trifunctional enzyme in complex with oxidized nicotinamide adenine dinucleotide (see paper)
34% identity, 98% coverage: 2:691/706 of query aligns to 1:705/711 of 7o4uA
8oqvA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-109
34% identity, 98% coverage: 2:691/706 of query aligns to 10:721/726 of 8oqvA
- binding 4-nitrobenzenesulfonic acid: E39 (≠ A31), G74 (= G66), M80 (≠ L72), V91 (≠ T77), T94 (≠ D80), T94 (≠ D80), E148 (= E138), L151 (= L141), R182 (≠ Q171), S448 (= S427), S519 (≠ N498), R520 (= R499), L562 (≠ V541), L566 (≠ V545), I570 (= I549)
Sites not aligning to the query:
8pf8A Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-72
34% identity, 98% coverage: 2:691/706 of query aligns to 12:723/729 of 8pf8A
- binding [2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boronic acid: G76 (= G66), F169 (≠ I157), N173 (≠ K161), S177 (≠ D164), I193 (≠ M180), F313 (= F291)
- binding bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]-bis(oxidanyl)boranuide: M39 (≠ L29), N40 (≠ K30), E41 (≠ A31), T81 (≠ M71), D92 (≠ E76), V93 (≠ T77)
- binding [(2~{R})-2,3-bis(oxidanyl)propoxy]-[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]borinic acid: M39 (≠ L29), G77 (≠ A67), D78 (= D68), M82 (≠ L72), V93 (≠ T77)
- binding (2~{R})-3-bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boranyloxypropane-1,2-diol: T152 (≠ Q140), R184 (≠ Q171), A311 (≠ I289), F312 (= F290), I673 (= I647)
Sites not aligning to the query:
8oquA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-92
34% identity, 98% coverage: 2:691/706 of query aligns to 13:724/730 of 8oquA
- binding 4-chloranylbenzenesulfonic acid: M40 (≠ L29), N41 (≠ K30), E42 (≠ A31), G77 (= G66), G78 (≠ A67), D79 (= D68), V80 (≠ I69), D90 (= D73), V94 (≠ T77), L124 (= L111), G125 (= G112), P150 (= P137), E151 (= E138)
8oqtA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-91
34% identity, 98% coverage: 2:691/706 of query aligns to 12:723/729 of 8oqtA
- binding 4-bromanylbenzenesulfonic acid: E41 (≠ A31), G76 (= G66), G77 (≠ A67), D78 (= D68), V79 (≠ I69), M82 (≠ L72), D89 (= D73), V93 (≠ T77), T96 (≠ D80), T96 (≠ D80), P149 (= P137), E150 (= E138)
Sites not aligning to the query:
8oqnA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-53
34% identity, 98% coverage: 2:691/706 of query aligns to 12:723/729 of 8oqnA
- binding 1-benzyl-1H-pyrazole-4-carboxylic acid: M39 (≠ L29), M82 (≠ L72), E150 (= E138), Q172 (≠ A160), F175 (≠ L163), V176 (vs. gap), Q181 (≠ T168), T241 (= T222), F254 (≠ A233), N257 (≠ Q236), Q261 (≠ K240), L262 (≠ T241), P266 (vs. gap), P268 (= P246), Q282 (≠ A260), V283 (≠ K261), G302 (≠ T280), Q303 (≠ P281), V304 (≠ E282), S521 (≠ N498), G525 (≠ A502)
8opvA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with resveratrol (fragment-b-h11)
34% identity, 98% coverage: 2:691/706 of query aligns to 12:723/729 of 8opvA
- binding resveratrol: M39 (≠ L29), A75 (= A65), G76 (= G66), M82 (≠ L72), E128 (= E116), P149 (= P137), E150 (= E138), T152 (≠ Q140), L153 (= L141), R184 (≠ Q171), F296 (= F274)
8opuA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with sulfamethoxazole (fragment-b-e1)
34% identity, 98% coverage: 2:691/706 of query aligns to 12:723/729 of 8opuA
8oqoA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-49
34% identity, 98% coverage: 2:691/706 of query aligns to 11:722/727 of 8oqoA
8oqlA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-1
34% identity, 98% coverage: 2:691/706 of query aligns to 11:722/728 of 8oqlA
- binding Hexafluorophosphate anion: V37 (≠ T28), N39 (≠ K30), G75 (= G66), D77 (= D68), M81 (≠ L72), V92 (≠ T77), T95 (≠ D80), P148 (= P137), E149 (= E138), L152 (= L141), Q180 (≠ T168), Q260 (≠ K240), K362 (= K340), D363 (= D341), V364 (≠ I342), V430 (≠ M408), D476 (≠ E454), K477 (= K455), M478 (= M456), P479 (= P457), K506 (= K484)
- binding formamide: V78 (≠ I69), K79 (≠ S70)
4b3iA Crystal structure of mycobacterium tuberculosis fatty acid beta-oxidation complex with coenzymea bound at the hydratase active sites (see paper)
34% identity, 98% coverage: 2:691/706 of query aligns to 14:725/731 of 4b3iA
- active site: G79 (≠ A67), E100 (≠ R82), R104 (= R86), G127 (= G113), E130 (= E116), P151 (= P137), E152 (= E138), G160 (= G146), S452 (= S427), H473 (= H448), E485 (= E460), S523 (≠ N498)
- binding adenosine-5'-diphosphate: Q640 (≠ A615), P641 (≠ G616), P642 (≠ E617), L643 (≠ I618), Q644 (≠ A619)
- binding coenzyme a: T38 (≠ M26), V40 (≠ T28), A77 (= A65), G79 (≠ A67), D80 (= D68), V81 (≠ I69), E152 (= E138), F315 (= F291), Q319 (≠ E295)
Query Sequence
>6938034 FitnessBrowser__SB2B:6938034
MEKTFSLSRRDDGIALLTMDVPGETMNTLKAQFAPEITAILQEIKADSSIKGLVLISGKA
DSFVAGADISMLDACETAEDARLLSRQGHHVFAELEGLNIPVVAAIHGACLGGGLELALA
CHQRVCSDSSKTMLGVPEVQLGLLPGGGGTQRLPRLIGIAKALDLMLTGKQVRPKQAVKM
GLVDDVVPESILLDTAIEMALAGKKTRKPLKQPLVTKLLEGTPVGRNIMFDQATKQVLKK
TQGNYPSPLKIIDCVREGMAKGMEKGLEVEAAHFGALVATPESAALRSIFFATTEMKKET
GAGDAKPRKVAKAVVLGGGLMGGGIASVTTTKAKVPVRVKDISDKGLSNALGYAYKLLDK
GVKRRHMTSAERDKLMALMTTTTEYRGVKDADIVVEAVFEDLNLKHQMVRDIERECGEHT
IFASNTSSLPITQIAAAASRPENVIGLHYFSPVEKMPLVEVIAHEKTSPETIATTVAFAR
KQGKTPIVVKDCAGFYVNRILALYMNEAAQLLLEGQAVDHLDKALVKFGFPVGPMTLLDE
VGIDVGAKISPILEKELGERFKAPAAFDKLMADDRKGRKNGKGFYLYGKAAKKGKKVDES
VYSLLGLTPATGKEAGEIAERCVVQMLNEAVRCLEEGIIASPRDGDIGAIFGIGFPPFLG
GPFRYMDTLGAAKMVRLLEGYQSKYGDRFAPAALLKAMAAEGKTFY
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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