SitesBLAST
Comparing 3610445 FitnessBrowser__Dino:3610445 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)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
41% identity, 94% coverage: 14:647/673 of query aligns to 9:654/692 of 6iunB
- active site: A60 (≠ G62), F65 (= F67), E73 (≠ P73), H77 (≠ P77), G101 (= G101), E104 (= E104), E124 (= E124), G132 (= G132), K248 (≠ R241), S407 (= S399), H428 (= H420), E440 (= E432), N478 (= N470)
- binding nicotinamide-adenine-dinucleotide: G300 (= G292), T301 (≠ L293), M302 (= M294), E321 (= E313), T322 (= T318), Y365 (≠ I357), A377 (= A369), V378 (= V370), E380 (= E372), V384 (≠ T376), V388 (≠ A380), N405 (= N397), S407 (= S399)
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)
38% identity, 97% coverage: 13:663/673 of query aligns to 9:687/723 of Q08426
- V40 (= V40) to G: in dbSNP:rs1062551
- I41 (≠ V43) to R: in dbSNP:rs1062552
- T75 (≠ D75) to I: in dbSNP:rs1062553
- K165 (≠ A165) 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 (≠ A171) 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 (= A265) to T: in dbSNP:rs2302819
- A325 (≠ E313) to G: in dbSNP:rs1062555
- K346 (≠ R336) 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 (≠ E561) 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 (≠ A574) to T: in dbSNP:rs1042437
- T606 (≠ A582) 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
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 17:685/716 of 6z5oAAA
- active site: A67 (≠ G62), F72 (= F67), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), G137 (= G132), K255 (≠ R241), S409 (= S399), H430 (= H420), E442 (= E432), N480 (= N470)
- binding coenzyme a: P26 (= P24), V27 (= V25), A65 (= A60), D68 (= D63), I69 (≠ M64), P128 (= P123), Y162 (≠ L157), F277 (= F263), K281 (≠ R267)
- binding nicotinamide-adenine-dinucleotide: G309 (= G290), G311 (= G292), T312 (≠ L293), M313 (= M294), E332 (= E313), S333 (≠ R314), Q337 (≠ T318), A379 (= A369), V380 (= V370), F381 (= F371), E382 (= E372), K387 (= K377), N407 (= N397), S409 (= S399), H430 (= H420)
- binding nicotinamide: A67 (≠ G62), E109 (= E104), E129 (= E124), P136 (= P131), F261 (≠ H247)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 17:692/727 of 3zwaA
- active site: A67 (≠ G62), F72 (= F67), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), P136 (= P131), G137 (= G132), K255 (≠ R241), S416 (= S399), H437 (= H420), E449 (= E432), N487 (= N470)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V25), A65 (= A60), G66 (= G61), A67 (≠ G62), D68 (= D63), I69 (≠ M64), L104 (= L99), E109 (= E104), R124 (= R119), E129 (= E124), L132 (≠ V127), G137 (= G132), Y162 (≠ L157)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
36% identity, 96% coverage: 15:663/673 of query aligns to 16:689/723 of 6zicAAA
- active site: A66 (≠ G62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ R241), S413 (= S399), H434 (= H420), E446 (= E432), N484 (= N470)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P24), V26 (= V25), A28 (= A27), A66 (≠ G62), D67 (= D63), I68 (≠ M64), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), Y161 (≠ L157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G290), G310 (= G292), T311 (≠ L293), M312 (= M294), E331 (= E313), S332 (≠ R314), Q336 (≠ T318), A383 (= A369), V384 (= V370), F385 (= F371), E386 (= E372), L390 (≠ T376), K391 (= K377), N411 (= N397), S413 (= S399), H434 (= H420)
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2- methylbutanoyl-coa (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 14:689/723 of 3zw9A
- active site: A64 (≠ G62), F69 (= F67), G79 (≠ P77), G103 (= G101), E106 (= E104), P125 (= P123), E126 (= E124), P133 (= P131), G134 (= G132), K252 (≠ R241), S413 (= S399), H434 (= H420), E446 (= E432), N484 (= N470)
- binding nicotinamide-adenine-dinucleotide: L305 (≠ M289), G306 (= G290), G308 (= G292), T309 (≠ L293), M310 (= M294), E329 (= E313), Q334 (≠ T318), A383 (= A369), V384 (= V370), F385 (= F371), E386 (= E372), N411 (= N397), S413 (= S399), H434 (= H420)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V25), A62 (= A60), G63 (= G61), A64 (≠ G62), I66 (≠ M64), G102 (= G100), G103 (= G101), E106 (= E104), E126 (= E124), P133 (= P131), Y159 (≠ L157)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
36% identity, 96% coverage: 15:663/673 of query aligns to 16:691/725 of 5omoA
- active site: A66 (≠ G62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R241), S415 (= S399), H436 (= H420), E448 (= E432), N486 (= N470)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P24), V26 (= V25), A28 (= A27), P31 (≠ T30), A64 (= A60), A66 (≠ G62), D67 (= D63), I68 (≠ M64), L103 (= L99), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), Y161 (≠ L157), F260 (≠ H247), K280 (≠ R267)
- binding 3-keto-decanoyl-coa: S415 (= S399), N486 (= N470), K519 (≠ A503), M520 (= M504), V525 (≠ A509), Y658 (= Y630)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 16:691/725 of 5mgbA
- active site: A66 (≠ G62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R241), S415 (= S399), H436 (= H420), E448 (= E432), N486 (= N470)
- binding acetoacetyl-coenzyme a: P25 (= P24), V26 (= V25), A64 (= A60), G65 (= G61), A66 (≠ G62), D67 (= D63), I68 (≠ M64), G105 (= G101), E128 (= E124), Y161 (≠ L157)
- binding nicotinamide-adenine-dinucleotide: L307 (≠ M289), G308 (= G290), G310 (= G292), T311 (≠ L293), M312 (= M294), E331 (= E313), S332 (≠ R314), Q336 (≠ T318), V386 (= V370), F387 (= F371), E388 (= E372), N413 (= N397), S415 (= S399), H436 (= H420)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 16:691/725 of 3zwcA
- active site: A66 (≠ G62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R241), S415 (= S399), H436 (= H420), E448 (= E432), N486 (= N470)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V25), A64 (= A60), G65 (= G61), A66 (≠ G62), D67 (= D63), I68 (≠ M64), G77 (≠ P73), L78 (≠ P74), L80 (= L76), V101 (≠ T97), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), F260 (≠ H247)
- binding nicotinamide-adenine-dinucleotide: G308 (= G290), G310 (= G292), T311 (≠ L293), M312 (= M294), E331 (= E313), Q336 (≠ T318), A385 (= A369), V386 (= V370), F387 (= F371), E388 (= E372), K393 (= K377), N413 (= N397), S415 (= S399), H436 (= H420)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 16:691/725 of 2x58A
- active site: A66 (≠ G62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R241), S415 (= S399), H436 (= H420), E448 (= E432), N486 (= N470)
- binding adenosine-5'-diphosphate: G310 (= G292), T311 (≠ L293), M312 (= M294), E331 (= E313), S332 (≠ R314), Q336 (≠ T318), V386 (= V370), L392 (≠ T376)
- binding coenzyme a: V26 (= V25), A28 (= A27), A64 (= A60), A66 (≠ G62), D67 (= D63), I68 (≠ M64), E128 (= E124)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
36% identity, 96% coverage: 15:663/673 of query aligns to 16:689/723 of 6zibAAA
- active site: A66 (≠ G62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ R241), S413 (= S399), H434 (= H420), E446 (= E432), N484 (= N470)
- binding acetoacetyl-coenzyme a: P25 (= P24), V26 (= V25), A64 (= A60), G65 (= G61), A66 (≠ G62), D67 (= D63), I68 (≠ M64), G104 (= G100), G105 (= G101), E128 (= E124), Y161 (≠ L157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G292), T311 (≠ L293), M312 (= M294), E331 (= E313), S332 (≠ R314), Q336 (≠ T318), A383 (= A369), V384 (= V370), F385 (= F371), E386 (= E372), N411 (= N397), H434 (= H420)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
36% identity, 96% coverage: 15:663/673 of query aligns to 16:691/725 of 3zwbA
- active site: A66 (≠ G62), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), A128 (≠ E124), P135 (= P131), G136 (= G132), S415 (= S399), H436 (= H420), E448 (= E432), N486 (= N470)
- binding (2E)-Hexenoyl-CoA: P25 (= P24), V26 (= V25), A28 (= A27), A64 (= A60), G65 (= G61), A66 (≠ G62), D67 (= D63), I68 (≠ M64), V101 (≠ T97), L103 (= L99), G105 (= G101), E108 (= E104), G136 (= G132), Y161 (≠ L157), K280 (≠ R267)
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)
26% identity, 99% coverage: 5:670/673 of query aligns to 41:748/763 of P40939
- V282 (vs. gap) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (≠ L226) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ A262) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E432) 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
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)
30% identity, 93% coverage: 12:638/673 of query aligns to 14:670/729 of P21177
- G116 (= G101) 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 (= G292) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H420) active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
30% identity, 93% coverage: 12:638/673 of query aligns to 14:670/719 of 6tnmA
- active site: A68 (≠ G62), F73 (= F67), G116 (= G101), E119 (= E104), P138 (= P123), E139 (= E124), G147 (= G132), N271 (≠ R241), S429 (= S399), H450 (= H420), E462 (= E432), N500 (= N470)
- binding adenosine-5'-triphosphate: D343 (≠ E313), I344 (≠ R314), V400 (= V370), V401 (≠ F371), V406 (≠ T376), K584 (≠ R551)
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
29% identity, 91% coverage: 28:640/673 of query aligns to 36:672/715 of 1wdlA
- active site: A69 (≠ G62), N89 (≠ A82), N93 (≠ S86), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S399), H451 (= H420), E463 (= E432), N501 (= N470)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G291), I324 (≠ L293), M325 (= M294), D344 (= D310), I345 (≠ L311), A400 (= A369), V401 (= V370), E403 (= E372), N428 (= N397), T429 (= T398), S430 (= S399)
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)
29% identity, 91% coverage: 28:640/673 of query aligns to 36:672/715 of P28793
8oqqA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-79
30% identity, 93% coverage: 14:638/673 of query aligns to 17:681/723 of 8oqqA
8oqpA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-76
30% identity, 93% coverage: 14:638/673 of query aligns to 17:681/723 of 8oqpA
- binding 2-azanyl-5-sulfo-benzoic acid: G28 (vs. gap), S29 (vs. gap), A63 (= A54), K64 (≠ G55), K64 (≠ G55), K65 (≠ R56), P143 (= P123), E144 (= E124), L147 (≠ V127), F307 (= F264), M473 (= M428), P548 (≠ A503), S599 (≠ T548), L602 (≠ R551), K603 (≠ A552), S661 (= S618), T662 (≠ D619), G674 (= G631)
Sites not aligning to the query:
8oqrA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-80
30% identity, 93% coverage: 14:638/673 of query aligns to 23:687/728 of 8oqrA
- binding 4-cyanobenzenesulfonic acid: G76 (= G61), G77 (= G62), T81 (≠ E66), M82 (≠ F67), M82 (≠ F67), A85 (≠ P71), D89 (= D75), T96 (≠ A82), L123 (= L99), G124 (= G100), P149 (= P123), E150 (= E124), S366 (≠ D315), L367 (≠ A316), E368 (≠ A317), A420 (= A369), V421 (= V370), F422 (= F371)
Query Sequence
>3610445 FitnessBrowser__Dino:3610445
MGGIVDTRVDTDTGLAWVTVDNPPVNATSTAVRQGLLDAVTRVQGARLAILRCAGRTFIA
GGDMREFDAPPQPPDLPDVVDAIEASATPFVAVMQGTVLGGGLEIAMGCAYRIAAPGTRF
GLPEVTVGLIPGAGGTQRAPRLFGWDAAIDMACAGKLLSAQEAHARGALDAIADDPEAAA
RALVPEPRIPVSERPAPPPPDSARIAAHRRTLAARARGQTAPLQALDALLWATGPFREGQ
RKERALHLSLRASDQSRALRHAFFAERTVARPAVIRDRTPREIARIAVMGGGLMGAGIAA
ACLGAGYRVDLLERDAATAEAARDRVRGLIAGALRRGKIDQARHDAHCAALRTGVGIGHA
AEADLAIEAVFEETATKRAAFAALAQVMAPDAILATNTSYLDPREIFAGIPAPDRCLGLH
FFAPAHVMKLLEVVRLPETSAETLATAFALAGRLRKVAVLSGICDGFIGNRMLAAYRRAA
EYMLADGALPEQIDGAMRAYGMAMGPFEAQDLSGLHIAEANRRRQDATRPARERYVTLSD
QLCALGRTGQRAGKGWYAYAEGDRRPRVDPAVTALITDYSAAHGLPRRTHDAGEIQARLL
AVLANEGARLVEEGIADSDAAVDMVKLHGYGFPRWRGGPLFAARQAGDATIRAALDALDA
ASPGSWVRAQRYR
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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