SitesBLAST
Comparing WP_034990821.1 NCBI__GCF_000745425.1:WP_034990821.1 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
43% identity, 97% coverage: 11:676/686 of query aligns to 8:687/692 of 6iunB
- active site: A60 (= A62), F65 (= F67), E73 (≠ P73), H77 (≠ P77), G101 (= G101), E104 (= E104), E124 (= E124), G132 (= G132), K248 (≠ A241), S407 (= S397), H428 (= H418), E440 (= E430), N478 (= N468)
- binding nicotinamide-adenine-dinucleotide: G300 (= G289), T301 (≠ S290), M302 (= M291), E321 (= E310), T322 (= T311), Y365 (= Y355), A377 (= A367), V378 (= V368), E380 (= E370), V384 (= V374), V388 (= V378), N405 (= N395), S407 (= S397)
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)
37% identity, 98% coverage: 6:679/686 of query aligns to 4:708/723 of Q08426
- V40 (≠ A37) to G: in dbSNP:rs1062551
- I41 (≠ L38) to R: in dbSNP:rs1062552
- T75 (vs. gap) to I: in dbSNP:rs1062553
- K165 (≠ R165) 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 (≠ G171) 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 (≠ V308) to G: in dbSNP:rs1062555
- K346 (≠ E329) 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 (≠ N560) 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 (≠ S571) to T: in dbSNP:rs1042437
- T606 (≠ R579) 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)
37% identity, 97% coverage: 13:679/686 of query aligns to 14:710/723 of 3zw9A
- active site: A64 (= A62), F69 (= F67), G79 (≠ P77), G103 (= G101), E106 (= E104), P125 (= P123), E126 (= E124), P133 (= P131), G134 (= G132), K252 (≠ A241), S413 (= S397), H434 (= H418), E446 (= E430), N484 (= N468)
- binding nicotinamide-adenine-dinucleotide: L305 (≠ V286), G306 (= G287), G308 (= G289), T309 (≠ S290), M310 (= M291), E329 (= E310), Q334 (≠ S315), A383 (= A367), V384 (= V368), F385 (= F369), E386 (= E370), N411 (= N395), S413 (= S397), H434 (= H418)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V23), A62 (= A60), G63 (= G61), A64 (= A62), I66 (≠ A64), G102 (= G100), G103 (= G101), E106 (= E104), E126 (= E124), P133 (= P131), Y159 (≠ V157)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
37% identity, 97% coverage: 13:679/686 of query aligns to 17:713/727 of 3zwaA
- active site: A67 (= A62), F72 (= F67), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), P136 (= P131), G137 (= G132), K255 (≠ A241), S416 (= S397), H437 (= H418), E449 (= E430), N487 (= N468)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V23), A65 (= A60), G66 (= G61), A67 (= A62), D68 (= D63), I69 (≠ A64), L104 (= L99), E109 (= E104), R124 (≠ T119), E129 (= E124), L132 (= L127), G137 (= G132), Y162 (≠ V157)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
37% identity, 97% coverage: 13:679/686 of query aligns to 16:712/725 of 5omoA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ A241), S415 (= S397), H436 (= H418), E448 (= E430), N486 (= N468)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P22), V26 (= V23), A28 (≠ V25), P31 (≠ H28), A64 (= A60), A66 (= A62), D67 (= D63), I68 (≠ A64), L103 (= L99), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), Y161 (≠ V157), F260 (= F247), K280 (≠ R267)
- binding 3-keto-decanoyl-coa: S415 (= S397), N486 (= N468), K519 (≠ A501), M520 (= M502), V525 (= V507), Y658 (= Y627)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
37% identity, 97% coverage: 13:679/686 of query aligns to 16:712/725 of 5mgbA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ A241), S415 (= S397), H436 (= H418), E448 (= E430), N486 (= N468)
- binding acetoacetyl-coenzyme a: P25 (= P22), V26 (= V23), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (≠ A64), G105 (= G101), E128 (= E124), Y161 (≠ V157)
- binding nicotinamide-adenine-dinucleotide: L307 (≠ V286), G308 (= G287), G310 (= G289), T311 (≠ S290), M312 (= M291), E331 (= E310), S332 (≠ T311), Q336 (≠ S315), V386 (= V368), F387 (= F369), E388 (= E370), N413 (= N395), S415 (= S397), H436 (= H418)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
37% identity, 97% coverage: 13:679/686 of query aligns to 16:712/725 of 3zwcA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ A241), S415 (= S397), H436 (= H418), E448 (= E430), N486 (= N468)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V23), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (≠ A64), G77 (≠ P73), L78 (≠ P74), L80 (= L76), V101 (≠ T97), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), F260 (= F247)
- binding nicotinamide-adenine-dinucleotide: G308 (= G287), G310 (= G289), T311 (≠ S290), M312 (= M291), E331 (= E310), Q336 (≠ S315), A385 (= A367), V386 (= V368), F387 (= F369), E388 (= E370), K393 (= K375), N413 (= N395), S415 (= S397), H436 (= H418)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
37% identity, 97% coverage: 13:679/686 of query aligns to 16:712/725 of 2x58A
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), P135 (= P131), G136 (= G132), K254 (≠ A241), S415 (= S397), H436 (= H418), E448 (= E430), N486 (= N468)
- binding adenosine-5'-diphosphate: G310 (= G289), T311 (≠ S290), M312 (= M291), E331 (= E310), S332 (≠ T311), Q336 (≠ S315), V386 (= V368), L392 (≠ V374)
- binding coenzyme a: V26 (= V23), A28 (≠ V25), A64 (= A60), A66 (= A62), D67 (= D63), I68 (≠ A64), E128 (= E124)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
37% identity, 97% coverage: 13:679/686 of query aligns to 16:710/723 of 6zibAAA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ A241), S413 (= S397), H434 (= H418), E446 (= E430), N484 (= N468)
- binding acetoacetyl-coenzyme a: P25 (= P22), V26 (= V23), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (≠ A64), G104 (= G100), G105 (= G101), E128 (= E124), Y161 (≠ V157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G289), T311 (≠ S290), M312 (= M291), E331 (= E310), S332 (≠ T311), Q336 (≠ S315), A383 (= A367), V384 (= V368), F385 (= F369), E386 (= E370), N411 (= N395), H434 (= H418)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
37% identity, 97% coverage: 13:679/686 of query aligns to 16:712/725 of 3zwbA
- active site: A66 (= A62), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), A128 (≠ E124), P135 (= P131), G136 (= G132), S415 (= S397), H436 (= H418), E448 (= E430), N486 (= N468)
- binding (2E)-Hexenoyl-CoA: P25 (= P22), V26 (= V23), A28 (≠ V25), A64 (= A60), G65 (= G61), A66 (= A62), D67 (= D63), I68 (≠ A64), V101 (≠ T97), L103 (= L99), G105 (= G101), E108 (= E104), G136 (= G132), Y161 (≠ V157), K280 (≠ R267)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
37% identity, 97% coverage: 13:679/686 of query aligns to 16:710/723 of 6zicAAA
- active site: A66 (= A62), F71 (= F67), G81 (≠ P77), G105 (= G101), E108 (= E104), P127 (= P123), E128 (= E124), G136 (= G132), K254 (≠ A241), S413 (= S397), H434 (= H418), E446 (= E430), N484 (= N468)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P22), V26 (= V23), A28 (≠ V25), A66 (= A62), D67 (= D63), I68 (≠ A64), G104 (= G100), G105 (= G101), E108 (= E104), E128 (= E124), Y161 (≠ V157)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G287), G310 (= G289), T311 (≠ S290), M312 (= M291), E331 (= E310), S332 (≠ T311), Q336 (≠ S315), A383 (= A367), V384 (= V368), F385 (= F369), E386 (= E370), L390 (≠ V374), K391 (= K375), N411 (= N395), S413 (= S397), H434 (= H418)
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
37% identity, 97% coverage: 13:679/686 of query aligns to 17:706/716 of 6z5oAAA
- active site: A67 (= A62), F72 (= F67), G82 (≠ P77), G106 (= G101), E109 (= E104), P128 (= P123), E129 (= E124), G137 (= G132), K255 (≠ A241), S409 (= S397), H430 (= H418), E442 (= E430), N480 (= N468)
- binding coenzyme a: P26 (= P22), V27 (= V23), A65 (= A60), D68 (= D63), I69 (≠ A64), P128 (= P123), Y162 (≠ V157), F277 (= F263), K281 (≠ R267)
- binding nicotinamide-adenine-dinucleotide: G309 (= G287), G311 (= G289), T312 (≠ S290), M313 (= M291), E332 (= E310), S333 (≠ T311), Q337 (≠ S315), A379 (= A367), V380 (= V368), F381 (= F369), E382 (= E370), K387 (= K375), N407 (= N395), S409 (= S397), H430 (= H418)
- binding nicotinamide: A67 (= A62), E109 (= E104), E129 (= E124), P136 (= P131), F261 (= F247)
6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha (see paper)
30% identity, 97% coverage: 9:676/686 of query aligns to 13:710/719 of 6tnmA
- active site: A68 (= A62), F73 (= F67), G116 (= G101), E119 (= E104), P138 (= P123), E139 (= E124), G147 (= G132), N271 (≠ A241), S429 (= S397), H450 (= H418), E462 (= E430), N500 (= N468)
- binding adenosine-5'-triphosphate: D343 (≠ E310), I344 (≠ T311), V400 (= V368), V401 (≠ F369), V406 (= V374), K584 (= K550)
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, 97% coverage: 9:676/686 of query aligns to 13:710/729 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 (= G289) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H418) active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
30% identity, 95% coverage: 7:656/686 of query aligns to 11:691/715 of 1wdlA
- active site: A69 (= A62), N89 (vs. gap), N93 (≠ P77), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S397), H451 (= H418), E463 (= E430), N501 (= N468)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G288), I324 (≠ S290), M325 (= M291), D344 (≠ E310), I345 (≠ T311), A400 (= A367), V401 (= V368), E403 (= E370), N428 (= N395), T429 (= T396), S430 (= S397)
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)
30% identity, 95% coverage: 7:656/686 of query aligns to 11:691/715 of P28793
- D297 (≠ E266) binding substrate
- M325 (= M291) binding NAD(+)
- D344 (≠ E310) binding NAD(+)
- VVE 401:403 (≠ VFE 368:370) binding NAD(+)
- K408 (= K375) binding NAD(+)
- S430 (= S397) binding NAD(+)
- N454 (≠ S421) binding NAD(+)
- N501 (= N468) binding substrate
- Y660 (≠ H625) binding substrate
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
30% identity, 95% coverage: 7:656/686 of query aligns to 11:683/707 of 1wdmA
- active site: A69 (= A62), N89 (vs. gap), N93 (≠ P77), G117 (= G101), E120 (= E104), P139 (= P123), E140 (= E124), P147 (= P131), G148 (= G132), S430 (= S397), H451 (= H418), E463 (= E430), N501 (= N468)
- binding acetyl coenzyme *a: K142 (≠ T126), D297 (≠ E266), M459 (= M426), N501 (= N468), P534 (≠ A501), Y652 (≠ H625), L658 (≠ R631)
- binding nicotinamide-adenine-dinucleotide: G321 (= G287), A322 (≠ G288), I324 (≠ S290), M325 (= M291), D344 (≠ E310), V401 (= V368), E403 (= E370), N428 (= N395), S430 (= S397), N454 (≠ S421)
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)
28% identity, 94% coverage: 13:658/686 of query aligns to 49:739/763 of P40939
- V282 (≠ A203) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (= I225) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ V262) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E430) 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
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
31% identity, 93% coverage: 11:649/686 of query aligns to 11:672/707 of 6yswA
- active site: A66 (= A62), I71 (vs. gap), A84 (= A68), Q88 (= Q72), G112 (= G101), E115 (= E104), P136 (= P123), E137 (= E124), G145 (= G132), D264 (≠ A241), S422 (= S397), H443 (= H418), E455 (= E430), N493 (= N468)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V23), A66 (= A62), D67 (= D63), I68 (vs. gap), P136 (= P123), E137 (= E124), L140 (= L127), T290 (≠ R267), K293 (≠ L270)
4b3iA Crystal structure of mycobacterium tuberculosis fatty acid beta- oxidation complex with coenzymea bound at the hydratase active sites (see paper)
30% identity, 92% coverage: 11:639/686 of query aligns to 24:693/731 of 4b3iA
- active site: G79 (≠ A62), E100 (= E81), R104 (vs. gap), G127 (= G101), E130 (= E104), P151 (= P123), E152 (= E124), G160 (= G132), S452 (= S397), H473 (= H418), E485 (= E430), S523 (≠ N468)
- binding adenosine-5'-diphosphate: Q640 (≠ R584), P641 (≠ R585), P642 (= P586), L643 (≠ F587), Q644 (≠ D588)
- binding coenzyme a: T38 (≠ V23), V40 (= V25), A77 (= A60), G79 (≠ A62), D80 (= D63), V81 (≠ A64), E152 (= E124), F315 (= F264), Q319 (≠ A268)
Query Sequence
>WP_034990821.1 NCBI__GCF_000745425.1:WP_034990821.1
MSECVHTSFDDGLAIITIDNPPVNVTSHAVREGLMAALDKIEAAGATRVILTGTGKSFVA
GADAKEFALPPQPPVLPEIVERIENFPVPVIAALNGTALGGGLELALACRLRLAAPQATL
GLPEVTLGVVPGAGGTQRLPRLIGLAPALSLIAEGRVIGAVEAERLGLIDGLMDDPVTAA
RSHPLPERPVTGALPAPALDPQAIETARREANRRNPRQDAPQKAIGLVEATCRLPLAQGL
ALERETFLALKTSDQASALRHVFFAERAALAQGKTGGAEIGKAVVVGGGSMGAAIAYALA
GTGIEVTVVETDTASRERARANVAKLYAESVKRGKMNAEAAAAEEATRLRFQSGYDALPA
ADLAIEAVFEDMDVKRQVFTALDAALPQSAILATNTSFLDVNRIGDGLSNPSRFLGLHFF
SPAHVMKLLEVVRGAQTSAATVTTALRLAARLKKIAVLAGVCDGFIGNRILTRYRQICDI
MLIEGALPWQVDAALRGFGMAMGPYEVQDLSGLDIAYANRKRLGWRTKPGFRYIPIADRI
VEETSRLGRKTGAGWYDYDNGKQTPSALIDSLVIGESARAGITRRPFDDDEIVRRAITAM
SEEGFHILEEGIAAKSADIDLVMIHGYAFPRWRGGPIHYAGRVGLPEILHRIEAYAAADP
LSWKVPDLLRRAVREGVDPDSFGEQP
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