SitesBLAST
Comparing WP_012967492.1 NCBI__GCF_000025465.1:WP_012967492.1 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)
6yswA E. Coli anaerobic trifunctional enzyme subunit-alpha in complex with coenzyme a
77% identity, 99% coverage: 4:707/714 of query aligns to 1:703/707 of 6yswA
- active site: A66 (= A69), I71 (= I74), A84 (= A87), Q88 (= Q91), G112 (= G115), E115 (= E118), P136 (= P139), E137 (= E140), G145 (= G148), D264 (≠ A267), S422 (= S425), H443 (= H446), E455 (= E458), N493 (= N496)
- binding coenzyme a: E23 (= E26), M25 (= M28), A66 (= A69), D67 (= D70), I68 (= I71), P136 (= P139), E137 (= E140), L140 (= L143), T290 (= T293), K293 (= K296)
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)
41% identity, 96% coverage: 11:696/714 of query aligns to 45:750/763 of P40939
- V282 (≠ L228) to D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
- I305 (≠ L251) to N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
- L342 (≠ I288) 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)
37% identity, 97% coverage: 16:707/714 of query aligns to 17:714/715 of 1wdlA
- active site: A69 (= A69), N89 (vs. gap), N93 (≠ Q91), G117 (= G115), E120 (= E118), P139 (= P139), E140 (= E140), P147 (= P147), G148 (= G148), S430 (= S425), H451 (= H446), E463 (= E458), N501 (= N496)
- binding nicotinamide-adenine-dinucleotide: A322 (≠ G316), I324 (≠ L318), M325 (= M319), D344 (= D339), I345 (= I340), 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)
37% identity, 97% coverage: 16:707/714 of query aligns to 17:714/715 of P28793
- D297 (≠ S292) binding substrate
- M325 (= M319) binding NAD(+)
- D344 (= D339) binding NAD(+)
- VVE 401:403 (≠ VFE 396:398) binding NAD(+)
- K408 (= K403) binding NAD(+)
- S430 (= S425) binding NAD(+)
- N454 (≠ S449) binding NAD(+)
- N501 (= N496) binding substrate
- Y660 (≠ F652) binding substrate
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
36% identity, 97% coverage: 16:707/714 of query aligns to 17:706/707 of 1wdmA
- active site: A69 (= A69), N89 (vs. gap), N93 (≠ Q91), G117 (= G115), E120 (= E118), P139 (= P139), E140 (= E140), P147 (= P147), G148 (= G148), S430 (= S425), H451 (= H446), E463 (= E458), N501 (= N496)
- binding acetyl coenzyme *a: K142 (≠ Q142), D297 (≠ S292), M459 (= M454), N501 (= N496), P534 (= P529), Y652 (≠ F652), L658 (≠ P658)
- binding nicotinamide-adenine-dinucleotide: G321 (= G315), A322 (≠ G316), I324 (≠ L318), M325 (= M319), D344 (= D339), V401 (= V396), E403 (= E398), N428 (= N423), S430 (= S425), N454 (≠ S449)
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)
35% identity, 98% coverage: 9:708/714 of query aligns to 10:715/729 of P21177
- G116 (= G115) 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)
35% identity, 98% coverage: 9:708/714 of query aligns to 10:715/719 of 6tnmA
- active site: A68 (= A69), F73 (≠ I74), G116 (= G115), E119 (= E118), P138 (= P139), E139 (= E140), G147 (= G148), N271 (≠ A267), S429 (= S425), H450 (= H446), E462 (= E458), N500 (= N496)
- binding adenosine-5'-triphosphate: D343 (= D339), I344 (= I340), V400 (= V396), V401 (≠ F397), V406 (≠ L402), K584 (= K578)
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
33% identity, 97% coverage: 14:706/714 of query aligns to 8:690/692 of 6iunB
- active site: A60 (= A69), F65 (≠ I74), E73 (= E82), H77 (≠ Q91), G101 (= G115), E104 (= E118), E124 (= E140), G132 (= G148), K248 (≠ A267), S407 (= S425), H428 (= H446), E440 (= E458), N478 (= N496)
- binding nicotinamide-adenine-dinucleotide: G300 (= G317), T301 (≠ L318), M302 (= M319), E321 (≠ D339), T322 (≠ I340), Y365 (= Y383), A377 (= A395), V378 (= V396), E380 (= E398), V384 (≠ L402), V388 (≠ M406), N405 (= N423), S407 (= S425)
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: 13:697/714 of query aligns to 10:710/711 of 7o4uA
6z5oAAA Peroxisomal bifunctional enzyme (see paper)
34% identity, 95% coverage: 28:704/714 of query aligns to 27:704/716 of 6z5oAAA
- active site: A67 (= A69), F72 (≠ I74), G82 (≠ A87), G106 (= G115), E109 (= E118), P128 (= P139), E129 (= E140), G137 (= G148), K255 (≠ A267), S409 (= S425), H430 (= H446), E442 (= E458), N480 (= N496)
- binding coenzyme a: V27 (≠ M28), A65 (= A67), D68 (= D70), I69 (= I71), P128 (= P139), Y162 (≠ Q173), F277 (= F289), K281 (≠ T293)
- binding nicotinamide-adenine-dinucleotide: G309 (= G315), G311 (= G317), T312 (≠ L318), M313 (= M319), E332 (≠ D339), S333 (≠ I340), Q337 (≠ G344), A379 (= A395), V380 (= V396), F381 (= F397), E382 (= E398), K387 (= K403), N407 (= N423), S409 (= S425), H430 (= H446)
- binding nicotinamide: A67 (= A69), E109 (= E118), E129 (= E140), P136 (= P147), F261 (= F273)
Sites not aligning to the query:
5omoA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with with 3s-hydroxy-decanoyl-coa and 3-keto- decanoyl-coa
34% identity, 95% coverage: 28:704/714 of query aligns to 26:710/725 of 5omoA
- active site: A66 (= A69), F71 (≠ I74), G81 (≠ A87), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), P135 (= P147), G136 (= G148), K254 (≠ A267), S415 (= S425), H436 (= H446), E448 (= E458), N486 (= N496)
- binding (s)-3-hydroxydecanoyl-coa: V26 (≠ M28), A28 (≠ T30), P31 (≠ A33), A64 (= A67), A66 (= A69), D67 (= D70), I68 (= I71), L103 (= L113), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), Y161 (≠ Q173), F260 (= F273), K280 (≠ T293)
- binding 3-keto-decanoyl-coa: S415 (= S425), N486 (= N496), K519 (≠ P529), M520 (≠ V530), V525 (≠ L535), Y658 (≠ I654)
Sites not aligning to the query:
5mgbA Crystal structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and NAD (see paper)
34% identity, 95% coverage: 28:704/714 of query aligns to 26:710/725 of 5mgbA
- active site: A66 (= A69), F71 (≠ I74), G81 (≠ A87), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), P135 (= P147), G136 (= G148), K254 (≠ A267), S415 (= S425), H436 (= H446), E448 (= E458), N486 (= N496)
- binding acetoacetyl-coenzyme a: V26 (≠ M28), A64 (= A67), G65 (= G68), A66 (= A69), D67 (= D70), I68 (= I71), G105 (= G115), E128 (= E140), Y161 (≠ Q173)
- binding nicotinamide-adenine-dinucleotide: L307 (= L314), G308 (= G315), G310 (= G317), T311 (≠ L318), M312 (= M319), E331 (≠ D339), S332 (≠ I340), Q336 (≠ G344), V386 (= V396), F387 (= F397), E388 (= E398), N413 (= N423), S415 (= S425), H436 (= H446)
Sites not aligning to the query:
3zwcA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-decanoyl-coa (see paper)
34% identity, 95% coverage: 28:704/714 of query aligns to 26:710/725 of 3zwcA
- active site: A66 (= A69), F71 (≠ I74), G81 (≠ A87), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), P135 (= P147), G136 (= G148), K254 (≠ A267), S415 (= S425), H436 (= H446), E448 (= E458), N486 (= N496)
- binding (s)-3-hydroxydecanoyl-coa: V26 (≠ M28), A64 (= A67), G65 (= G68), A66 (= A69), D67 (= D70), I68 (= I71), G77 (≠ A83), L78 (≠ E84), L80 (= L86), V101 (≠ A111), G104 (= G114), G105 (= G115), E108 (= E118), E128 (= E140), F260 (= F273)
- binding nicotinamide-adenine-dinucleotide: G308 (= G315), G310 (= G317), T311 (≠ L318), M312 (= M319), E331 (≠ D339), Q336 (≠ G344), A385 (= A395), V386 (= V396), F387 (= F397), E388 (= E398), K393 (= K403), N413 (= N423), S415 (= S425), H436 (= H446)
2x58A The crystal structure of mfe1 liganded with coa (see paper)
34% identity, 95% coverage: 28:704/714 of query aligns to 26:710/725 of 2x58A
- active site: A66 (= A69), F71 (≠ I74), G81 (≠ A87), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), P135 (= P147), G136 (= G148), K254 (≠ A267), S415 (= S425), H436 (= H446), E448 (= E458), N486 (= N496)
- binding adenosine-5'-diphosphate: G310 (= G317), T311 (≠ L318), M312 (= M319), E331 (≠ D339), S332 (≠ I340), Q336 (≠ G344), V386 (= V396), L392 (= L402)
- binding coenzyme a: V26 (≠ M28), A28 (≠ T30), A64 (= A67), A66 (= A69), D67 (= D70), I68 (= I71), E128 (= E140)
3zwaA Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with 3s-hydroxy-hexanoyl-coa (see paper)
34% identity, 95% coverage: 28:704/714 of query aligns to 27:711/727 of 3zwaA
- active site: A67 (= A69), F72 (≠ I74), G82 (≠ A87), G106 (= G115), E109 (= E118), P128 (= P139), E129 (= E140), P136 (= P147), G137 (= G148), K255 (≠ A267), S416 (= S425), H437 (= H446), E449 (= E458), N487 (= N496)
- binding (S)-3-Hydroxyhexanoyl-CoA: V27 (≠ M28), A65 (= A67), G66 (= G68), A67 (= A69), D68 (= D70), I69 (= I71), L104 (= L113), E109 (= E118), R124 (= R135), E129 (= E140), L132 (= L143), G137 (= G148), Y162 (≠ Q173)
3zw9A Crystal structure of rat peroxisomal multifunctional enzyme type 1 (rpmfe1) complexed with (2s,3s)-3-hydroxy-2-methylbutanoyl-coa (see paper)
34% identity, 95% coverage: 28:704/714 of query aligns to 24:708/723 of 3zw9A
- active site: A64 (= A69), F69 (≠ I74), G79 (≠ A87), G103 (= G115), E106 (= E118), P125 (= P139), E126 (= E140), P133 (= P147), G134 (= G148), K252 (≠ A267), S413 (= S425), H434 (= H446), E446 (= E458), N484 (= N496)
- binding nicotinamide-adenine-dinucleotide: L305 (= L314), G306 (= G315), G308 (= G317), T309 (≠ L318), M310 (= M319), E329 (≠ D339), Q334 (≠ G344), A383 (= A395), V384 (= V396), F385 (= F397), E386 (= E398), N411 (= N423), S413 (= S425), H434 (= H446)
- binding (2s,3s)-3-hydroxy-2-methylbutanoyl-coa: V24 (≠ M28), A62 (= A67), G63 (= G68), A64 (= A69), I66 (= I71), G102 (= G114), G103 (= G115), E106 (= E118), E126 (= E140), P133 (= P147), Y159 (≠ Q173)
6zicAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with 3s-hydroxybutanoyl-coa and nadh'
34% identity, 95% coverage: 28:704/714 of query aligns to 26:708/723 of 6zicAAA
- active site: A66 (= A69), F71 (≠ I74), G81 (≠ A87), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), G136 (= G148), K254 (≠ A267), S413 (= S425), H434 (= H446), E446 (= E458), N484 (= N496)
- binding 3-hydroxybutanoyl-coenzyme a: V26 (≠ M28), A28 (≠ T30), A66 (= A69), D67 (= D70), I68 (= I71), G104 (= G114), G105 (= G115), E108 (= E118), E128 (= E140), Y161 (≠ Q173)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G308 (= G315), G310 (= G317), T311 (≠ L318), M312 (= M319), E331 (≠ D339), S332 (≠ I340), Q336 (≠ G344), A383 (= A395), V384 (= V396), F385 (= F397), E386 (= E398), L390 (= L402), K391 (= K403), N411 (= N423), S413 (= S425), H434 (= H446)
Sites not aligning to the query:
6zibAAA structure of rat peroxisomal multifunctional enzyme type-1 (rpmfe1) complexed with acetoacetyl-coa and nadh'
34% identity, 95% coverage: 28:704/714 of query aligns to 26:708/723 of 6zibAAA
- active site: A66 (= A69), F71 (≠ I74), G81 (≠ E84), G105 (= G115), E108 (= E118), P127 (= P139), E128 (= E140), G136 (= G148), K254 (≠ A267), S413 (= S425), H434 (= H446), E446 (= E458), N484 (= N496)
- binding acetoacetyl-coenzyme a: V26 (≠ M28), A64 (= A67), G65 (= G68), A66 (= A69), D67 (= D70), I68 (= I71), G104 (= G114), G105 (= G115), E128 (= E140), Y161 (≠ Q173)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G310 (= G317), T311 (≠ L318), M312 (= M319), E331 (≠ D339), S332 (≠ I340), Q336 (≠ G344), A383 (= A395), V384 (= V396), F385 (= F397), E386 (= E398), N411 (= N423), H434 (= H446)
Sites not aligning to the query:
8oqrA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-80
34% identity, 96% coverage: 13:697/714 of query aligns to 21:728/728 of 8oqrA
- binding 4-cyanobenzenesulfonic acid: G76 (= G68), G77 (≠ A69), T81 (≠ M73), M82 (≠ I74), M82 (≠ I74), A85 (≠ C77), D89 (vs. gap), T96 (≠ E82), L123 (= L113), G124 (= G114), P149 (= P139), E150 (= E140), S366 (≠ Q341), L367 (≠ P342), E368 (≠ R343), A420 (= A395), V421 (= V396), F422 (= F397)
8pf8A Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-72
34% identity, 96% coverage: 13:697/714 of query aligns to 21:728/729 of 8pf8A
- binding [2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boronic acid: G76 (= G68), F169 (≠ I159), N173 (≠ T163), S177 (≠ D166), I193 (≠ A182), F313 (= F290)
- binding bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]-bis(oxidanyl)boranuide: M39 (≠ L31), N40 (≠ K32), E41 (≠ A33), T81 (≠ M73), D92 (vs. gap), V93 (vs. gap)
- binding [(2~{R})-2,3-bis(oxidanyl)propoxy]-[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]borinic acid: M39 (≠ L31), G77 (≠ A69), D78 (= D70), M82 (≠ I74), V93 (vs. gap)
- binding (2~{R})-3-bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boranyloxypropane-1,2-diol: T152 (≠ Q142), R184 (≠ Q173), A311 (≠ I288), F312 (= F289), I673 (= I648)
Sites not aligning to the query:
Query Sequence
>WP_012967492.1 NCBI__GCF_000025465.1:WP_012967492.1
MDTVSAFKLEVRADKIAVITIDAPGEKMNTLKAEFGNQVRGLIRQVRDDKSVRGVVFISA
KADNFIAGADINMIARCRSAQEAEALARQGQQIMAEIHGLSIPVIAAIHGACLGGGLELA
LACHGRICSDDEKTRLGLPEVQLGLLPGSGGTQRLPRLIGVSTALDMMLTGRQLRARQAL
KAGLVDEVVPQAILLQAAVELALKGRPASRDMPVRERVLAGPLGRHLLFHFVGKQTQRKT
QGNYPAVKRILQVVENGLTHGCSSGYAEEARAFGELAMTPQSQALRSIFFASTDLKKDRG
AEAEPGPLTSIAVLGGGLMGGGIAYVTACKGGLPVRIKDIQPRGINHALKYSWELLNKQV
RQRRLRPSERDRQMAMISGATDYQGFAHRDVVIEAVFEDLALKQRMVSEVEQYCGPQTIF
ASNTSSLPIGDIAAQARRPGRVIGLHFFSPVEKMPLVEVIPHKGTDPQAIATVVQLAKRQ
GKTPIVVADKAGFYVNRILAPYINEAMRLLVEGEPVEEIDKALVKFGFPVGPIQLLDEVG
IDTGTKIIPVLERAFGERFSPPANIIDAILKDDRKGRKNNRGFYLYETKGRKSKKRPDPA
VYPLLGIDRPQSRLSAQQVAERCVMMMLNEAARCFDEQIIRSARDGDIGAVFGIGFPPFL
GGPFRYMDTIGAGEVAAILQRLAAQYGPRFTPCDTLLRMAEQGTTFWPADERLT
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