SitesBLAST
Comparing GFF2242 FitnessBrowser__Phaeo:GFF2242 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
49% identity, 97% coverage: 8:692/706 of query aligns to 8:687/692 of 6iunB
- active site: A60 (= A60), F65 (= F65), E73 (≠ K73), H77 (≠ P77), G101 (= G101), E104 (= E104), E124 (= E124), G132 (= G132), K248 (≠ E251), S407 (= S410), H428 (= H431), E440 (= E443), N478 (= N481)
- binding nicotinamide-adenine-dinucleotide: G300 (= G303), T301 (= T304), M302 (= M305), E321 (= E324), T322 (= T325), Y365 (= Y368), A377 (= A380), V378 (≠ A381), E380 (= E383), V384 (= V387), V388 (≠ I391), N405 (= N408), S407 (= S410)
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)
39% identity, 97% coverage: 10:692/706 of query aligns to 11:705/723 of Q08426
- V40 (≠ D39) to G: in dbSNP:rs1062551
- I41 (≠ A40) to R: in dbSNP:rs1062552
- T75 (≠ D75) to I: in dbSNP:rs1062553
- K165 (≠ S165) 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 (= A275) to T: in dbSNP:rs2302819
- A325 (≠ L322) to G: in dbSNP:rs1062555
- K346 (≠ R343) 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 (vs. gap) 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 (≠ Q583) to T: in dbSNP:rs1042437
- T606 (≠ L591) 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)
40% identity, 94% coverage: 10:670/706 of query aligns to 14:688/723 of 3zw9A
- active site: A64 (= A60), F69 (= F65), G79 (≠ P77), G103 (= G101), E106 (= E104), P125 (= P123), E126 (= E124), P133 (= P131), G134 (= G132), K252 (≠ E251), S413 (= S410), H434 (= H431), E446 (= E443), N484 (= N481)
- binding nicotinamide-adenine-dinucleotide: L305 (≠ I300), G306 (= G301), G308 (= G303), T309 (= T304), M310 (= M305), E329 (= E324), Q334 (≠ A329), A383 (= A380), V384 (≠ A381), F385 (= F382), E386 (= E383), N411 (= N408), S413 (= S410), H434 (= H431)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V20), A62 (≠ G58), G63 (= G59), A64 (= A60), I66 (= I62), G102 (= G100), G103 (= G101), E106 (= E104), E126 (= E124), P133 (= P131), Y159 (≠ P157)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
40% identity, 94% coverage: 10:670/706 of query aligns to 16:690/725 of 5omoA
- active site: A66 (= A60), F71 (= F65), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ E251), S415 (= S410), H436 (= H431), E448 (= E443), N486 (= N481)
- binding (s)-3-hydroxydecanoyl-coa: P25 (≠ S19), V26 (= V20), A28 (= A22), P31 (≠ L25), A64 (≠ G58), A66 (= A60), D67 (= D61), I68 (= I62), L103 (≠ M99), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), Y161 (≠ P157), F260 (= F257), K280 (≠ R277)
- binding 3-keto-decanoyl-coa: S415 (= S410), N486 (= N481), K519 (≠ A514), M520 (= M515), V525 (≠ M520), Y658 (= Y639)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
40% identity, 94% coverage: 10:670/706 of query aligns to 16:690/725 of 5mgbA
- active site: A66 (= A60), F71 (= F65), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ E251), S415 (= S410), H436 (= H431), E448 (= E443), N486 (= N481)
- binding acetoacetyl-coenzyme a: P25 (≠ S19), V26 (= V20), A64 (≠ G58), G65 (= G59), A66 (= A60), D67 (= D61), I68 (= I62), G105 (= G101), E128 (= E124), Y161 (≠ P157)
- binding nicotinamide-adenine-dinucleotide: L307 (≠ I300), G308 (= G301), G310 (= G303), T311 (= T304), M312 (= M305), E331 (= E324), S332 (≠ T325), Q336 (≠ A329), V386 (≠ A381), F387 (= F382), E388 (= E383), N413 (= N408), S415 (= S410), H436 (= H431)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
40% identity, 94% coverage: 10:670/706 of query aligns to 16:690/725 of 3zwcA
- active site: A66 (= A60), F71 (= F65), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ E251), S415 (= S410), H436 (= H431), E448 (= E443), N486 (= N481)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V20), A64 (≠ G58), G65 (= G59), A66 (= A60), D67 (= D61), I68 (= I62), G77 (≠ K73), L78 (≠ P74), L80 (= L76), V101 (≠ P97), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), F260 (= F257)
- binding nicotinamide-adenine-dinucleotide: G308 (= G301), G310 (= G303), T311 (= T304), M312 (= M305), E331 (= E324), Q336 (≠ A329), A385 (= A380), V386 (≠ A381), F387 (= F382), E388 (= E383), K393 (= K388), N413 (= N408), S415 (= S410), H436 (= H431)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
40% identity, 94% coverage: 10:670/706 of query aligns to 16:690/725 of 2x58A
- active site: A66 (= A60), F71 (= F65), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ E251), S415 (= S410), H436 (= H431), E448 (= E443), N486 (= N481)
- binding adenosine-5'-diphosphate: G310 (= G303), T311 (= T304), M312 (= M305), E331 (= E324), S332 (≠ T325), Q336 (≠ A329), V386 (≠ A381), L392 (≠ V387)
- binding coenzyme a: V26 (= V20), A28 (= A22), A64 (≠ G58), A66 (= A60), D67 (= D61), I68 (= I62), E128 (= E124)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
40% identity, 94% coverage: 10:670/706 of query aligns to 17:691/727 of 3zwaA
- active site: A67 (= A60), F72 (= F65), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), P136 (= P131), G137 (= G132), K255 (≠ E251), S416 (= S410), H437 (= H431), E449 (= E443), N487 (= N481)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V20), A65 (≠ G58), G66 (= G59), A67 (= A60), D68 (= D61), I69 (= I62), L104 (≠ M99), E109 (= E104), R124 (≠ V119), E129 (= E124), L132 (= L127), G137 (= G132), Y162 (≠ P157)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
40% identity, 94% coverage: 10:670/706 of query aligns to 16:690/725 of 3zwbA
- active site: A66 (= A60), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), A128 (≠ E124), P135 (= P131), G136 (= G132), S415 (= S410), H436 (= H431), E448 (= E443), N486 (= N481)
- binding (2E)-Hexenoyl-CoA: P25 (≠ S19), V26 (= V20), A28 (= A22), A64 (≠ G58), G65 (= G59), A66 (= A60), D67 (= D61), I68 (= I62), V101 (≠ P97), L103 (≠ M99), G105 (= G101), E108 (= E104), G136 (= G132), Y161 (≠ P157), K280 (≠ R277)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
40% identity, 94% coverage: 10:670/706 of query aligns to 16:688/723 of 6zicAAA
- active site: A66 (= A60), F71 (= F65), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ E251), S413 (= S410), H434 (= H431), E446 (= E443), N484 (= N481)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (≠ S19), V26 (= V20), A28 (= A22), A66 (= A60), D67 (= D61), I68 (= I62), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), Y161 (≠ P157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G301), G310 (= G303), T311 (= T304), M312 (= M305), E331 (= E324), S332 (≠ T325), Q336 (≠ A329), A383 (= A380), V384 (≠ A381), F385 (= F382), E386 (= E383), L390 (≠ V387), K391 (= K388), N411 (= N408), S413 (= S410), H434 (= H431)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
40% identity, 94% coverage: 10:670/706 of query aligns to 16:688/723 of 6zibAAA
- active site: A66 (= A60), F71 (= F65), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ E251), S413 (= S410), H434 (= H431), E446 (= E443), N484 (= N481)
- binding acetoacetyl-coenzyme a: P25 (≠ S19), V26 (= V20), A64 (≠ G58), G65 (= G59), A66 (= A60), D67 (= D61), I68 (= I62), G104 (= G100), G105 (= G101), E128 (= E124), Y161 (≠ P157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G303), T311 (= T304), M312 (= M305), E331 (= E324), S332 (≠ T325), Q336 (≠ A329), A383 (= A380), V384 (≠ A381), F385 (= F382), E386 (= E383), N411 (= N408), H434 (= H431)
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
40% identity, 94% coverage: 10:670/706 of query aligns to 17:684/716 of 6z5oAAA
- active site: A67 (= A60), F72 (= F65), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), G137 (= G132), K255 (≠ E251), S409 (= S410), H430 (= H431), E442 (= E443), N480 (= N481)
- binding coenzyme a: P26 (≠ S19), V27 (= V20), A65 (≠ G58), D68 (= D61), I69 (= I62), P128 (= P123), Y162 (≠ P157), F277 (= F273), K281 (≠ R277)
- binding nicotinamide-adenine-dinucleotide: G309 (= G301), G311 (= G303), T312 (= T304), M313 (= M305), E332 (= E324), S333 (≠ T325), Q337 (≠ A329), A379 (= A380), V380 (≠ A381), F381 (= F382), E382 (= E383), K387 (= K388), N407 (= N408), S409 (= S410), H430 (= H431)
- binding nicotinamide: A67 (= A60), E109 (= E104), E129 (= E124), P136 (= P131), F261 (= F257)
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)
32% identity, 97% coverage: 10:691/706 of query aligns to 49:756/763 of P40939
- V282 (≠ G212) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (≠ L235) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (= L272) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E443) 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)
33% identity, 96% coverage: 13:692/706 of query aligns to 22:710/715 of 1wdlA
- active site: A69 (= A60), N89 (≠ M82), N93 (≠ S86), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S410), H451 (= H431), E463 (= E443), N501 (= N481)
- binding nicotinamide-adenine-dinucleotide: A322 (= A302), I324 (≠ T304), M325 (= M305), D344 (≠ E324), I345 (≠ T325), A400 (= A380), V401 (≠ A381), E403 (= E383), N428 (= N408), T429 (= T409), S430 (= S410)
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)
33% identity, 96% coverage: 13:692/706 of query aligns to 22:710/715 of P28793
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
33% identity, 96% coverage: 13:692/706 of query aligns to 22:702/707 of 1wdmA
- active site: A69 (= A60), N89 (≠ M82), N93 (≠ S86), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S410), H451 (= H431), E463 (= E443), N501 (= N481)
- binding acetyl coenzyme *a: K142 (= K126), D297 (≠ E276), M459 (= M439), N501 (= N481), P534 (≠ A514), Y652 (≠ N637), L658 (≠ N643)
- binding nicotinamide-adenine-dinucleotide: G321 (= G301), A322 (= A302), I324 (≠ T304), M325 (= M305), D344 (≠ E324), V401 (≠ A381), E403 (= E383), N428 (= N408), S430 (= S410), N454 (≠ S434)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
32% identity, 97% coverage: 8:692/706 of query aligns to 11:699/707 of 6yswA
- active site: A66 (= A60), I71 (vs. gap), A84 (≠ D75), Q88 (≠ L79), G112 (= G101), E115 (= E104), P136 (= P123), E137 (= E124), G145 (= G132), D264 (≠ E251), S422 (= S410), H443 (= H431), E455 (= E443), N493 (= N481)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V20), A66 (= A60), D67 (= D61), I68 (= I62), P136 (= P123), E137 (= E124), L140 (= L127), T290 (≠ R277), K293 (≠ T280)
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)
32% identity, 95% coverage: 8:677/706 of query aligns to 15:699/729 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 (= G303) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H431) 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)
32% identity, 95% coverage: 8:677/706 of query aligns to 15:699/719 of 6tnmA
- active site: A68 (= A60), F73 (= F65), G116 (= G101), E119 (= E104), P138 (= P123), E139 (= E124), G147 (= G132), N271 (≠ E251), S429 (= S410), H450 (= H431), E462 (= E443), N500 (= N481)
- binding adenosine-5'-triphosphate: D343 (≠ E324), I344 (≠ T325), V400 (≠ A381), V401 (≠ F382), V406 (= V387), K584 (= K562)
3k6jA Crystal structure of the dehydrogenase part of multifuctional enzyme 1 from c.Elegans
37% identity, 53% coverage: 293:667/706 of query aligns to 45:410/430 of 3k6jA
Sites not aligning to the query:
Query Sequence
>GFF2242 FitnessBrowser__Phaeo:GFF2242
MISIKHTEGVAFIELNAPSVNALGLKMRQVLSSAIHELDADEQVKAIVLCSALPLFCGGA
DIVEFRTGAVWDKPDLPDLCVMIETSKKPIIAAIAGPAMGGALEIALACDYRVATPDAVM
GLPEIKLGLLPGAGGTQRLPRIAGLEAATQMILSGDPVKGEYALSCGLVDALFENDQDFR
AHVLGFATRVSHEGDPKRSCADMTVRHPDPKGYLTGFRDQIAHTSKNLVAPERCLVSIEA
ACEMPLAEGLEQEKAGFAELLDTPQSRAGRHLFFAERECTKVPGVTRADRPRDIASVAVI
GAGTMGRGIAIAFLQAGYPVTLLETTQGALEQGLEKVREHFQRAAQKGRLSADRAEAISA
NATGTLSYAGLAKADLIIEAAFESMNVKRQIFEALDLHAKPGAILASNTSTLDLDEIATV
TSRPEDVIGLHFFSPANVMRLLEVVRGAKTAPDVIATAITVAKKIRKLPVTVGVCYGFVG
NRMLEPYFREGSRLLLEGATPKQVDDVLEGFGMAMGIHAMADLAGVDVGARVRQERRSEI
AHDPTYQAVQDRLFELGRLGQKTGRGSYVYEGRTRVEDPEMVQISSELADLHGVKRRDID
DQEILERCLFPLINEGFLILEEGIATRPGDCDLIWVNGYGFPNWRGGPMHYADEIGLSQI
MERMTHYRQSLGAYGEMWFTPAPLLEQLATSGVTLDAHFDAKKEKT
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