SitesBLAST
Comparing WP_013256921.1 NCBI__GCF_000143965.1:WP_013256921.1 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
35% identity, 99% coverage: 7:706/709 of query aligns to 1:690/692 of 6iunB
- active site: A60 (= A66), F65 (≠ L71), E73 (= E79), H77 (= H88), G101 (= G112), E104 (= E115), E124 (= E135), G132 (= G143), K248 (= K266), S407 (= S425), H428 (= H446), E440 (= E458), N478 (≠ S496)
- binding nicotinamide-adenine-dinucleotide: G300 (= G317), T301 (≠ V318), M302 (= M319), E321 (≠ D338), T322 (≠ I339), Y365 (≠ L383), A377 (= A395), V378 (= V396), E380 (= E398), V384 (= V402), V388 (≠ I406), N405 (= N423), S407 (= S425)
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)
34% identity, 99% coverage: 8:708/709 of query aligns to 41:763/763 of P40939
- V282 (vs. gap) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (≠ L250) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ M287) to P: in LCHAD deficiency; dbSNP:rs137852772
- E510 (= E458) 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)
34% identity, 98% coverage: 11:707/709 of query aligns to 12:714/715 of 1wdlA
- active site: A69 (= A66), N89 (≠ V84), N93 (≠ H88), G117 (= G112), E120 (= E115), P139 (= P134), E140 (= E135), P147 (= P142), G148 (= G143), S430 (= S425), H451 (= H446), E463 (= E458), N501 (≠ S496)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G316), I324 (≠ V318), M325 (= M319), D344 (= D338), I345 (= I339), A400 (= A395), V401 (= V396), E403 (= E398), N428 (= N423), T429 (= T424), S430 (= S425)
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)
34% identity, 98% coverage: 11:707/709 of query aligns to 12:714/715 of P28793
- D297 (≠ T291) binding substrate
- M325 (= M319) binding NAD(+)
- D344 (= D338) binding NAD(+)
- VVE 401:403 (≠ VLE 396:398) binding NAD(+)
- K408 (= K403) binding NAD(+)
- S430 (= S425) binding NAD(+)
- N454 (= N449) binding NAD(+)
- N501 (≠ S496) binding substrate
- Y660 (= Y652) binding substrate
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
33% identity, 98% coverage: 11:707/709 of query aligns to 12:706/707 of 1wdmA
- active site: A69 (= A66), N89 (≠ V84), N93 (≠ H88), G117 (= G112), E120 (= E115), P139 (= P134), E140 (= E135), P147 (= P142), G148 (= G143), S430 (= S425), H451 (= H446), E463 (= E458), N501 (≠ S496)
- binding acetyl coenzyme *a: K142 (≠ S137), D297 (≠ T291), M459 (= M454), N501 (≠ S496), P534 (= P529), Y652 (= Y652), L658 (≠ P658)
- binding nicotinamide-adenine-dinucleotide: G321 (= G315), A322 (≠ G316), I324 (≠ V318), M325 (= M319), D344 (= D338), V401 (= V396), E403 (= E398), N428 (= N423), S430 (= S425), N454 (= N449)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
34% identity, 98% coverage: 14:708/709 of query aligns to 11:704/707 of 6yswA
- active site: A66 (= A66), I71 (≠ L71), A84 (≠ V84), Q88 (≠ H88), G112 (= G112), E115 (= E115), P136 (= P134), E137 (= E135), G145 (= G143), D264 (≠ K266), S422 (= S425), H443 (= H446), E455 (= E458), N493 (≠ S496)
- binding coenzyme a: E23 (vs. gap), M25 (≠ V26), A66 (= A66), D67 (= D67), I68 (= I68), P136 (= P134), E137 (= E135), L140 (= L138), T290 (≠ R292), K293 (≠ G295)
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)
32% identity, 98% coverage: 12:709/709 of query aligns to 7:711/723 of Q08426
- V40 (≠ W45) to G: in dbSNP:rs1062551
- I41 (≠ K46) to R: in dbSNP:rs1062552
- T75 (≠ V84) to I: in dbSNP:rs1062553
- K165 (≠ V176) 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 (≠ E182) 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 (≠ N290) to T: in dbSNP:rs2302819
- A325 (≠ L336) to G: in dbSNP:rs1062555
- K346 (= K361) 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 (≠ Q598) to T: in dbSNP:rs1042437
- T606 (≠ A606) 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
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, 98% coverage: 12:707/709 of query aligns to 13:714/729 of P21177
- G116 (= G112) 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 (= G317) mutation to A: 10-fold increase in KM for NADH.
- H450 (= H446) 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, 98% coverage: 12:707/709 of query aligns to 13:714/719 of 6tnmA
- active site: A68 (= A66), F73 (≠ L71), G116 (= G112), E119 (= E115), P138 (= P134), E139 (= E135), G147 (= G143), N271 (≠ K266), S429 (= S425), H450 (= H446), E462 (= E458), N500 (≠ S496)
- binding adenosine-5'-triphosphate: D343 (= D338), I344 (= I339), V400 (= V396), V401 (≠ L397), V406 (= V402), K584 (= K577)
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
32% identity, 94% coverage: 12:681/709 of query aligns to 12:683/723 of 6zibAAA
- active site: A66 (= A66), F71 (≠ L71), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), G136 (= G143), K254 (= K266), S413 (= S425), H434 (= H446), E446 (= E458), N484 (≠ S496)
- binding acetoacetyl-coenzyme a: P25 (= P25), V26 (= V26), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), G104 (= G111), G105 (= G112), E128 (= E135), Y161 (≠ P168)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G317), T311 (≠ V318), M312 (= M319), E331 (≠ D338), S332 (≠ I339), Q336 (≠ G347), A383 (= A395), V384 (= V396), F385 (≠ L397), E386 (= E398), N411 (= N423), H434 (= H446)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
32% identity, 94% coverage: 12:681/709 of query aligns to 12:683/723 of 6zicAAA
- active site: A66 (= A66), F71 (≠ L71), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), G136 (= G143), K254 (= K266), S413 (= S425), H434 (= H446), E446 (= E458), N484 (≠ S496)
- binding 3-hydroxybutanoyl-coenzyme a: P25 (= P25), V26 (= V26), A28 (≠ Q28), A66 (= A66), D67 (= D67), I68 (= I68), G104 (= G111), G105 (= G112), E108 (= E115), E128 (= E135), Y161 (≠ P168)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G315), G310 (= G317), T311 (≠ V318), M312 (= M319), E331 (≠ D338), S332 (≠ I339), Q336 (≠ G347), A383 (= A395), V384 (= V396), F385 (≠ L397), E386 (= E398), L390 (≠ V402), K391 (= K403), N411 (= N423), S413 (= S425), H434 (= H446)
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 13:679/716 of 6z5oAAA
- active site: A67 (= A66), F72 (≠ L71), G82 (≠ H88), G106 (= G112), E109 (= E115), P128 (= P134), E129 (= E135), G137 (= G143), K255 (= K266), S409 (= S425), H430 (= H446), E442 (= E458), N480 (≠ S496)
- binding coenzyme a: P26 (= P25), V27 (= V26), A65 (= A64), D68 (= D67), I69 (= I68), P128 (= P134), Y162 (≠ P168), F277 (= F288), K281 (≠ R292)
- binding nicotinamide-adenine-dinucleotide: G309 (= G315), G311 (= G317), T312 (≠ V318), M313 (= M319), E332 (≠ D338), S333 (≠ I339), Q337 (≠ G347), A379 (= A395), V380 (= V396), F381 (≠ L397), E382 (= E398), K387 (= K403), N407 (= N423), S409 (= S425), H430 (= H446)
- binding nicotinamide: A67 (= A66), E109 (= E115), E129 (= E135), P136 (= P142), F261 (= F272)
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2-methylbutanoyl-coa (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 10:683/723 of 3zw9A
- active site: A64 (= A66), F69 (≠ L71), G79 (≠ H88), G103 (= G112), E106 (= E115), P125 (= P134), E126 (= E135), P133 (= P142), G134 (= G143), K252 (= K266), S413 (= S425), H434 (= H446), E446 (= E458), N484 (≠ S496)
- binding nicotinamide-adenine-dinucleotide: L305 (= L314), G306 (= G315), G308 (= G317), T309 (≠ V318), M310 (= M319), E329 (≠ D338), Q334 (≠ G347), A383 (= A395), V384 (= V396), F385 (≠ L397), E386 (= E398), N411 (= N423), S413 (= S425), H434 (= H446)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (= V26), A62 (= A64), G63 (= G65), A64 (= A66), I66 (= I68), G102 (= G111), G103 (= G112), E106 (= E115), E126 (= E135), P133 (= P142), Y159 (≠ P168)
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
32% identity, 94% coverage: 12:681/709 of query aligns to 12:685/725 of 5omoA
- active site: A66 (= A66), F71 (≠ L71), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), P135 (= P142), G136 (= G143), K254 (= K266), S415 (= S425), H436 (= H446), E448 (= E458), N486 (≠ S496)
- binding (s)-3-hydroxydecanoyl-coa: P25 (= P25), V26 (= V26), A28 (≠ Q28), P31 (≠ D31), A64 (= A64), A66 (= A66), D67 (= D67), I68 (= I68), L103 (= L110), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), Y161 (≠ P168), F260 (= F272), K280 (≠ R292)
- binding 3-keto-decanoyl-coa: S415 (= S425), N486 (≠ S496), K519 (≠ P529), M520 (= M530), V525 (≠ L535), Y658 (≠ T654)
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 12:685/725 of 5mgbA
- active site: A66 (= A66), F71 (≠ L71), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), P135 (= P142), G136 (= G143), K254 (= K266), S415 (= S425), H436 (= H446), E448 (= E458), N486 (≠ S496)
- binding acetoacetyl-coenzyme a: P25 (= P25), V26 (= V26), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), G105 (= G112), E128 (= E135), Y161 (≠ P168)
- binding nicotinamide-adenine-dinucleotide: L307 (= L314), G308 (= G315), G310 (= G317), T311 (≠ V318), M312 (= M319), E331 (≠ D338), S332 (≠ I339), Q336 (≠ G347), V386 (= V396), F387 (≠ L397), E388 (= E398), N413 (= N423), S415 (= S425), H436 (= H446)
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 12:685/725 of 3zwcA
- active site: A66 (= A66), F71 (≠ L71), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), P135 (= P142), G136 (= G143), K254 (= K266), S415 (= S425), H436 (= H446), E448 (= E458), N486 (≠ S496)
- binding (s)-3-hydroxydecanoyl-coa: V26 (= V26), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), G77 (≠ V84), L78 (≠ M85), L80 (≠ G87), V101 (≠ N108), G104 (= G111), G105 (= G112), E108 (= E115), E128 (= E135), F260 (= F272)
- binding nicotinamide-adenine-dinucleotide: G308 (= G315), G310 (= G317), T311 (≠ V318), M312 (= M319), E331 (≠ D338), Q336 (≠ G347), A385 (= A395), V386 (= V396), F387 (≠ L397), E388 (= E398), K393 (= K403), N413 (= N423), S415 (= S425), H436 (= H446)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 12:685/725 of 2x58A
- active site: A66 (= A66), F71 (≠ L71), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), E128 (= E135), P135 (= P142), G136 (= G143), K254 (= K266), S415 (= S425), H436 (= H446), E448 (= E458), N486 (≠ S496)
- binding adenosine-5'-diphosphate: G310 (= G317), T311 (≠ V318), M312 (= M319), E331 (≠ D338), S332 (≠ I339), Q336 (≠ G347), V386 (= V396), L392 (≠ V402)
- binding coenzyme a: V26 (= V26), A28 (≠ Q28), A64 (= A64), A66 (= A66), D67 (= D67), I68 (= I68), E128 (= E135)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 13:686/727 of 3zwaA
- active site: A67 (= A66), F72 (≠ L71), G82 (≠ H88), G106 (= G112), E109 (= E115), P128 (= P134), E129 (= E135), P136 (= P142), G137 (= G143), K255 (= K266), S416 (= S425), H437 (= H446), E449 (= E458), N487 (≠ S496)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (= V26), A65 (= A64), G66 (= G65), A67 (= A66), D68 (= D67), I69 (= I68), L104 (= L110), E109 (= E115), R124 (≠ S130), E129 (= E135), L132 (= L138), G137 (= G143), Y162 (≠ P168)
3zwbA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 2trans-hexenoyl-coa (see paper)
32% identity, 94% coverage: 12:681/709 of query aligns to 12:685/725 of 3zwbA
- active site: A66 (= A66), G81 (≠ H88), G105 (= G112), E108 (= E115), P127 (= P134), A128 (≠ E135), P135 (= P142), G136 (= G143), S415 (= S425), H436 (= H446), E448 (= E458), N486 (≠ S496)
- binding (2E)-Hexenoyl-CoA: P25 (= P25), V26 (= V26), A28 (≠ Q28), A64 (= A64), G65 (= G65), A66 (= A66), D67 (= D67), I68 (= I68), V101 (≠ N108), L103 (= L110), G105 (= G112), E108 (= E115), G136 (= G143), Y161 (≠ P168), K280 (≠ R292)
7o4uA Structure of the alpha subunit of mycobacterium tuberculosis beta- oxidation trifunctional enzyme in complex with oxidized nicotinamide adenine dinucleotide (see paper)
34% identity, 96% coverage: 14:692/709 of query aligns to 11:705/711 of 7o4uA
Query Sequence
>WP_013256921.1 NCBI__GCF_000143965.1:WP_013256921.1
MKTDFKTVQVAIEDGVAVFTMNNPPVNQLSDYFIKDLVAAFEEAWKDDQVYAIVLTGEGK
NFVAGADITQLQKMKNRDEAFGLVMEGHKFYNAIELSPKPVIAAINGNCLGGGLELAMCC
HYRVAVKGVSLGLPEVSLGLLPGGGGTQRLPRIIGLPNAAQMMTTGKPIKAEVAFVRGLV
DEVCAPDKLLKKAFGAAKMFKARMYNQKVRTARNTFYRLPSFNEKLHFMNYIRAMVGAQS
KGYIAPGKILDCLDKGLSADFEADLKVEANGFADLVTSAVAKNLIGMFLNTRSAGRLPRI
KDLKPAKPMKVAQLGGGVMGCGIVHLLLANGFECVLWDINDAALAKGVESVKKTFAFMIK
KKKMKPADLDKLLAEKLTTTTKLEDLGDVDLVIEAVLENMKVKQEIWLTLEKTCRPDVIF
GTNTSALPITEMASVLKDPGRMIGLHFFNPAERMQLLEIICAQQTSDQTLATSVDFGRRI
KKVPIVVNDGPGFYVSRQLGGLMGGSVFLVADGVSGEAIEKAMMNFGMPMGPATLADLTG
IDINYHVNQTFARELGDRYTVHPLTEAIYNLGDYGRKTGRGYMDYTSGKPVPNPRLQQVV
ADYLKANNVAPKDMPEQEIIDAMLGLAINEAALMIEQGICDRPADMDLAMIYGTGFPPYR
GGILRYADTWGLKNVYETLVKLEGRYGKRFAPAKLIKDMAEKGETFYKE
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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