SitesBLAST
Comparing GFF400 FitnessBrowser__Phaeo:GFF400 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)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
44% identity, 98% coverage: 7:690/697 of query aligns to 4:691/692 of 6iunB
- active site: A60 (= A62), F65 (= F67), E73 (= E73), H77 (≠ P77), G101 (= G101), E104 (= E104), E124 (= E124), G132 (= G132), K248 (≠ R247), S407 (= S406), H428 (= H427), E440 (= E439), N478 (= N477)
- binding nicotinamide-adenine-dinucleotide: G300 (= G298), T301 (= T299), M302 (= M300), E321 (= E319), T322 (≠ R320), Y365 (= Y364), A377 (= A376), V378 (= V377), E380 (= E379), V384 (= V383), V388 (= V387), N405 (= N404), S407 (= S406)
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, 98% coverage: 7:686/697 of query aligns to 4:705/723 of Q08426
- V40 (≠ E42) to G: in dbSNP:rs1062551
- I41 (≠ K43) to R: in dbSNP:rs1062552
- T75 (≠ G75) to I: in dbSNP:rs1062553
- K165 (≠ D165) 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 (≠ R171) 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 (≠ S271) to T: in dbSNP:rs2302819
- A325 (≠ L317) to G: in dbSNP:rs1062555
- K346 (= K341) 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 (≠ E568) 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 (≠ E581) to T: in dbSNP:rs1042437
- T606 (≠ D589) 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
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2- methylbutanoyl-coa (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 13:707/723 of 3zw9A
- active site: A64 (= A62), F69 (= F67), G79 (≠ P77), G103 (= G101), E106 (= E104), P125 (= P123), E126 (= E124), P133 (= P131), G134 (= G132), K252 (≠ R247), S413 (= S406), H434 (= H427), E446 (= E439), N484 (= N477)
- binding nicotinamide-adenine-dinucleotide: L305 (≠ I295), G306 (= G296), G308 (= G298), T309 (= T299), M310 (= M300), E329 (= E319), Q334 (≠ A324), A383 (= A376), V384 (= V377), F385 (= F378), E386 (= E379), N411 (= N404), S413 (= S406), H434 (= H427)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V23), A62 (= A60), G63 (= G61), A64 (= A62), I66 (= I64), G102 (= G100), G103 (= G101), E106 (= E104), E126 (= E124), P133 (= P131), Y159 (≠ H157)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 16:710/727 of 3zwaA
- active site: A67 (= A62), F72 (= F67), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), P136 (= P131), G137 (= G132), K255 (≠ R247), S416 (= S406), H437 (= H427), E449 (= E439), N487 (= N477)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V23), A65 (= A60), G66 (= G61), A67 (= A62), D68 (= D63), I69 (= I64), L104 (= L99), E109 (= E104), R124 (≠ K119), E129 (= E124), L132 (= L127), G137 (= G132), Y162 (≠ H157)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
38% identity, 97% coverage: 12:686/697 of query aligns to 15:709/725 of 5omoA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R247), S415 (= S406), H436 (= H427), E448 (= E439), N486 (= N477)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P22), V26 (= V23), A28 (= A25), P31 (≠ I28), A64 (= A60), A66 (= A62), D67 (= D63), I68 (= I64), L103 (= L99), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), Y161 (≠ H157), F260 (= F253), K280 (≠ R273)
- binding 3-keto-decanoyl-coa: S415 (= S406), N486 (= N477), K519 (≠ A510), M520 (= M511), V525 (= V516), Y658 (= Y637)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 15:709/725 of 5mgbA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R247), S415 (= S406), H436 (= H427), E448 (= E439), N486 (= N477)
- binding acetoacetyl-coenzyme a: P25 (= P22), V26 (= V23), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), G105 (= G101), E128 (= E124), Y161 (≠ H157)
- binding nicotinamide-adenine-dinucleotide: L307 (≠ I295), G308 (= G296), G310 (= G298), T311 (= T299), M312 (= M300), E331 (= E319), S332 (≠ R320), Q336 (≠ A324), V386 (= V377), F387 (= F378), E388 (= E379), N413 (= N404), S415 (= S406), H436 (= H427)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 15:709/725 of 3zwcA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R247), S415 (= S406), H436 (= H427), E448 (= E439), N486 (= N477)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V23), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), G77 (≠ E73), L78 (≠ P74), L80 (= L76), V101 (≠ T97), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), F260 (= F253)
- binding nicotinamide-adenine-dinucleotide: G308 (= G296), G310 (= G298), T311 (= T299), M312 (= M300), E331 (= E319), Q336 (≠ A324), A385 (= A376), V386 (= V377), F387 (= F378), E388 (= E379), K393 (= K384), N413 (= N404), S415 (= S406), H436 (= H427)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 15:709/725 of 2x58A
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ R247), S415 (= S406), H436 (= H427), E448 (= E439), N486 (= N477)
- binding adenosine-5'-diphosphate: G310 (= G298), T311 (= T299), M312 (= M300), E331 (= E319), S332 (≠ R320), Q336 (≠ A324), V386 (= V377), L392 (≠ V383)
- binding coenzyme a: V26 (= V23), A28 (= A25), A64 (= A60), A66 (= A62), D67 (= D63), I68 (= I64), E128 (= E124)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
38% identity, 97% coverage: 12:686/697 of query aligns to 15:707/723 of 6zicAAA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ R247), S413 (= S406), H434 (= H427), E446 (= E439), N484 (= N477)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P22), V26 (= V23), A28 (= A25), A66 (= A62), D67 (= D63), I68 (= I64), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), Y161 (≠ H157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G296), G310 (= G298), T311 (= T299), M312 (= M300), E331 (= E319), S332 (≠ R320), Q336 (≠ A324), A383 (= A376), V384 (= V377), F385 (= F378), E386 (= E379), L390 (≠ V383), K391 (= K384), N411 (= N404), S413 (= S406), H434 (= H427)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
38% identity, 97% coverage: 12:686/697 of query aligns to 15:707/723 of 6zibAAA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ R247), S413 (= S406), H434 (= H427), E446 (= E439), N484 (= N477)
- binding acetoacetyl-coenzyme a: P25 (= P22), V26 (= V23), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), G104 (= G100), G105 (= G101), E128 (= E124), Y161 (≠ H157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G298), T311 (= T299), M312 (= M300), E331 (= E319), S332 (≠ R320), Q336 (≠ A324), A383 (= A376), V384 (= V377), F385 (= F378), E386 (= E379), N411 (= N404), H434 (= H427)
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 16:703/716 of 6z5oAAA
- active site: A67 (= A62), F72 (= F67), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), G137 (= G132), K255 (≠ R247), S409 (= S406), H430 (= H427), E442 (= E439), N480 (= N477)
- binding coenzyme a: P26 (= P22), V27 (= V23), A65 (= A60), D68 (= D63), I69 (= I64), P128 (= P123), Y162 (≠ H157), F277 (= F269), K281 (≠ R273)
- binding nicotinamide-adenine-dinucleotide: G309 (= G296), G311 (= G298), T312 (= T299), M313 (= M300), E332 (= E319), S333 (≠ R320), Q337 (≠ A324), A379 (= A376), V380 (= V377), F381 (= F378), E382 (= E379), K387 (= K384), N407 (= N404), S409 (= S406), H430 (= H427)
- binding nicotinamide: A67 (= A62), E109 (= E104), E129 (= E124), P136 (= P131), F261 (= F253)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
38% identity, 97% coverage: 12:686/697 of query aligns to 15:709/725 of 3zwbA
- active site: A66 (= A62), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), A128 (≠ E124), P135 (= P131), G136 (= G132), S415 (= S406), H436 (= H427), E448 (= E439), N486 (= N477)
- binding (2E)-Hexenoyl-CoA: P25 (= P22), V26 (= V23), A28 (= A25), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (= I64), V101 (≠ T97), L103 (= L99), G105 (= G101), E108 (= E104), G136 (= G132), Y161 (≠ H157), K280 (≠ R273)
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)
31% identity, 89% coverage: 47:665/697 of query aligns to 53:690/729 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 (= G298) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H427) 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)
31% identity, 89% coverage: 47:665/697 of query aligns to 53:690/719 of 6tnmA
- active site: A68 (= A62), F73 (= F67), G116 (= G101), E119 (= E104), P138 (= P123), E139 (= E124), G147 (= G132), N271 (≠ R247), S429 (= S406), H450 (= H427), E462 (= E439), N500 (= N477)
- binding adenosine-5'-triphosphate: D343 (≠ E319), I344 (≠ R320), V400 (= V377), V401 (≠ F378), V406 (= V383), K584 (= K558)
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
31% identity, 92% coverage: 47:689/697 of query aligns to 54:713/715 of 1wdlA
- active site: A69 (= A62), N89 (≠ R82), N93 (≠ A86), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S406), H451 (= H427), E463 (= E439), N501 (= N477)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G297), I324 (≠ T299), M325 (= M300), D344 (≠ E319), I345 (≠ R320), A400 (= A376), V401 (= V377), E403 (= E379), N428 (= N404), T429 (= T405), S430 (= S406)
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)
31% identity, 92% coverage: 47:689/697 of query aligns to 54:713/715 of P28793
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
32% identity, 98% coverage: 9:689/697 of query aligns to 9:702/707 of 6yswA
- active site: A66 (= A62), I71 (≠ F67), A84 (≠ P77), Q88 (vs. gap), G112 (= G101), E115 (= E104), P136 (= P123), E137 (= E124), G145 (= G132), D264 (≠ R247), S422 (= S406), H443 (= H427), E455 (= E439), N493 (= N477)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V23), A66 (= A62), D67 (= D63), I68 (= I64), P136 (= P123), E137 (= E124), L140 (= L127), T290 (≠ R273), K293 (≠ S276)
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
31% identity, 92% coverage: 47:689/697 of query aligns to 54:705/707 of 1wdmA
- active site: A69 (= A62), N89 (≠ R82), N93 (≠ A86), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S406), H451 (= H427), E463 (= E439), N501 (= N477)
- binding acetyl coenzyme *a: K142 (≠ H126), D297 (≠ E272), M459 (= M435), N501 (= N477), P534 (≠ A510), Y652 (≠ F635), L658 (≠ R641)
- binding nicotinamide-adenine-dinucleotide: G321 (= G296), A322 (≠ G297), I324 (≠ T299), M325 (= M300), D344 (≠ E319), V401 (= V377), E403 (= E379), N428 (= N404), S430 (= S406), N454 (≠ S430)
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)
29% identity, 97% coverage: 5:679/697 of query aligns to 41:750/763 of P40939
- V282 (≠ T212) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (≠ V230) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (= L265) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E439) 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
3k6jA Crystal structure of the dehydrogenase part of multifuctional enzyme 1 from c.Elegans
32% identity, 55% coverage: 288:671/697 of query aligns to 45:420/430 of 3k6jA
Sites not aligning to the query:
Query Sequence
>GFF400 FitnessBrowser__Phaeo:GFF400
MTEAIVYERIGDIAVLAAQNPPVNALGIDVRRGLLAGIERAEKEGARAVLIYGEGRTYFA
GADIREFGKPMEEPGLPDLCNRIEAAKLIVVSALHGTALGGGLEVALSSHYRIAVPGAKM
GLPEVHLGIIPGAGGTQRLPRVAGTEAALEMITTGRHVAAAEAFDKGVIDRIAEGNPREV
GLAYTRELLEQNAPRRPVCDMPAPEPVDFDATYERVLVRGRGQLSPAIAVRAVQAACEAP
SFLDGVRQERELFMKLMESDQRQGLIHAFFSERAVSKLPELVDVFPRDVAAMGVIGGGTM
GAGIATAALLAGLSVVLIERDEAASVAARERIEGNLRGALKRGKISQSQFDAILNETLKL
ATDYAALSQVDLVVEAVFEDMDVKRDVFAALDEHCKPGAILASNTSYLDINDIAAATSRP
SDVIGLHFFSPAHVMKLLEVVVADQTAPDVVATGFALGKRLKKTSVRSGVCDGFIGNRIM
NSYRKAADYMVLDGASPYQIDKVMTGFGFAMGPFAVADLAGLDIGWAARKRRAPTLDPRE
RVVHFSDMLCEGGDFGQKTGRGFYVYEEGKRGGTPNPQVAEYIERDQRDQGVTPQIFAND
EVLRRYMCAMVNEAAKVVGEGIARRPLDVDMVLLFGYGFPRFWGGPLKWADLQGPDSILK
DIRRYAKEDAFFWQPAPLLEQMVAEGRSFDDLNKEAR
Or try a new SitesBLAST search
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