SitesBLAST
Comparing WP_038207304.1 NCBI__GCF_000745855.1:WP_038207304.1 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)
6wy8C Tcur3481-tcur3483 steroid acad (see paper)
33% identity, 93% coverage: 1:345/370 of query aligns to 1:334/364 of 6wy8C
Sites not aligning to the query:
6wy9B Tcur3481-tcur3483 steroid acad g363a variant (see paper)
35% identity, 83% coverage: 38:345/370 of query aligns to 36:331/361 of 6wy9B
Sites not aligning to the query:
6af6A Piga with fad and proline (see paper)
26% identity, 94% coverage: 1:348/370 of query aligns to 1:358/383 of 6af6A
- active site: A127 (= A124), T128 (≠ L125), A244 (= A233)
- binding flavin-adenine dinucleotide: N125 (≠ L122), A127 (= A124), T128 (≠ L125), G133 (= G130), S134 (≠ Q131), F158 (≠ V155), I159 (≠ V156), T160 (≠ A157), W211 (vs. gap)
- binding 1,4,7,10,13,16-hexaoxacyclooctadecane: L41 (≠ A42), K44 (≠ D45), K275 (≠ A264), F280 (= F269)
- binding proline: G133 (= G130), I136 (≠ F133), F237 (≠ L226), M241 (≠ V230)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
26% identity, 95% coverage: 5:356/370 of query aligns to 3:363/379 of 6fahD
- active site: L124 (≠ A124), T125 (≠ L125), G241 (≠ A233)
- binding flavin-adenine dinucleotide: F122 (≠ L122), L124 (≠ A124), T125 (≠ L125), R152 (= R152), F155 (≠ V155), T157 (≠ A157), E198 (≠ D196), R267 (= R259), Q269 (= Q261), F270 (≠ Y262), I274 (≠ L266), F277 (= F269), Q335 (= Q328), I336 (≠ M329), G339 (= G332), Y361 (≠ Q354)
Sites not aligning to the query:
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
29% identity, 70% coverage: 105:362/370 of query aligns to 109:374/383 of 1bucA
- active site: L128 (≠ A124), T129 (≠ L125), G246 (≠ A233), E367 (≠ F355)
- binding acetoacetyl-coenzyme a: F126 (≠ L122), G134 (= G130), T135 (≠ Q131), T162 (≠ A157), N182 (vs. gap), H183 (vs. gap), F236 (≠ A223), M240 (≠ T227), M241 (≠ L228), L243 (≠ V230), D244 (= D231), T317 (≠ R304), Y366 (≠ Q354), E367 (≠ F355), G368 (= G356)
- binding flavin-adenine dinucleotide: F126 (≠ L122), L128 (≠ A124), T129 (≠ L125), G134 (= G130), T135 (≠ Q131), F160 (≠ V155), T162 (≠ A157), Y366 (≠ Q354), T369 (≠ D357), E371 (≠ A359)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
29% identity, 70% coverage: 105:362/370 of query aligns to 109:374/383 of Q06319
- E367 (≠ F355) active site, Proton acceptor; mutation to Q: Loss of activity.
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
25% identity, 92% coverage: 5:345/370 of query aligns to 53:402/430 of P51174
- K318 (≠ E260) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ A264) modified: N6-acetyllysine; alternate; mutation to R: Reduces activity by 23%; reduces activity by 80% when associated with R-318.
Sites not aligning to the query:
- 42 modified: N6-acetyllysine; K→R: Reduces activity by 90% when associated with R-318 and R-322.
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
27% identity, 96% coverage: 1:356/370 of query aligns to 1:363/378 of 5ol2F
- active site: L124 (≠ A124), T125 (≠ L125), G241 (≠ A233)
- binding calcium ion: E29 (= E30), E33 (≠ D35), R35 (≠ G37)
- binding coenzyme a persulfide: L238 (≠ V230), R242 (≠ S234), E362 (≠ F355), G363 (= G356)
- binding flavin-adenine dinucleotide: F122 (≠ L122), L124 (≠ A124), T125 (≠ L125), P127 (≠ N127), T131 (≠ Q131), F155 (≠ V155), I156 (≠ V156), T157 (≠ A157), E198 (≠ S191), R267 (= R259), F270 (≠ Y262), L274 (= L266), F277 (= F269), Q335 (= Q328), L336 (≠ M329), G338 (= G331), G339 (= G332), Y361 (≠ Q354)
Sites not aligning to the query:
7szvA Crystal structure of acyl-coa dehydrogenase from mycobacterium marinum in complex with fda
27% identity, 80% coverage: 50:346/370 of query aligns to 46:347/372 of 7szvA
- binding dihydroflavine-adenine dinucleotide: L122 (≠ A124), T123 (≠ L125), F153 (≠ V155), I154 (≠ V156), T155 (≠ A157), K194 (≠ N195), R261 (= R259), S263 (≠ Q261), Y271 (≠ F269), I274 (≠ L272), Q329 (= Q328), V330 (≠ M329), G332 (= G331), G333 (= G332)
Sites not aligning to the query:
7w0jE Acyl-coa dehydrogenase, tfu_1647
26% identity, 89% coverage: 38:366/370 of query aligns to 39:377/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (≠ L125), W157 (≠ V155), R270 (= R259), Q272 (= Q261), F273 (≠ Y262), I277 (≠ L266), F280 (= F269), I283 (≠ L272), Q339 (= Q328), L340 (≠ M329), G343 (= G332), Y365 (≠ Q354), E366 (≠ F355), T368 (≠ D357), Q370 (≠ A359), I371 (≠ F360)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
26% identity, 89% coverage: 38:366/370 of query aligns to 38:376/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ Q131), T134 (≠ F133), R180 (vs. gap), R234 (≠ D224), L237 (≠ T227), R238 (≠ L228), L240 (≠ V230), D241 (= D231), R244 (≠ S234), E365 (≠ F355), G366 (= G356)
- binding flavin-adenine dinucleotide: Y123 (≠ L122), L125 (≠ A124), S126 (≠ L125), G131 (= G130), S132 (≠ Q131), W156 (≠ V155), I157 (≠ V156), T158 (≠ A157), I360 (≠ L350), T367 (≠ D357), Q369 (≠ A359)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
26% identity, 89% coverage: 38:366/370 of query aligns to 38:376/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ L122), L125 (≠ A124), S126 (≠ L125), G131 (= G130), S132 (≠ Q131), W156 (≠ V155), I157 (≠ V156), T158 (≠ A157), I360 (≠ L350), Y364 (≠ Q354), T367 (≠ D357), Q369 (≠ A359)
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
27% identity, 81% coverage: 41:341/370 of query aligns to 63:380/567 of 2uxwA
- active site: L148 (≠ A124), T149 (≠ L125), G272 (≠ A233)
- binding flavin-adenine dinucleotide: F146 (≠ L122), L148 (≠ A124), T149 (≠ L125), G154 (= G130), S155 (≠ Q131), W181 (≠ V155), I182 (≠ V156), S183 (≠ A157)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ M74), G107 (≠ A81), L110 (≠ E84), F146 (≠ L122), L269 (≠ V230)
Sites not aligning to the query:
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
27% identity, 81% coverage: 41:341/370 of query aligns to 63:380/554 of 3b96A
- active site: L148 (≠ A124), T149 (≠ L125), G272 (≠ A233)
- binding flavin-adenine dinucleotide: F146 (≠ L122), L148 (≠ A124), T149 (≠ L125), G154 (= G130), S155 (≠ Q131), W181 (≠ V155), I182 (≠ V156), S183 (≠ A157)
- binding tetradecanoyl-coa: V96 (≠ M74), G107 (≠ A81), F146 (≠ L122), L269 (≠ V230)
Sites not aligning to the query:
7s7gA Crystal structure analysis of human vlcad (see paper)
27% identity, 81% coverage: 41:341/370 of query aligns to 63:380/571 of 7s7gA
Sites not aligning to the query:
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
26% identity, 81% coverage: 41:341/370 of query aligns to 131:448/655 of P49748
- 214:223 (vs. 122:131, 20% identical) binding FAD
- WIS 249:251 (≠ VVA 155:157) binding FAD
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
- 458 F → L: in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding; dbSNP:rs118204017; F→T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.; F→V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.; F→Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
- 461:463 binding substrate
- 462 active site, Proton acceptor; E→D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.; E→Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
- 464:466 binding FAD
- 490 A → P: in ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates; dbSNP:rs759775666; mutation A->G,V,S,D,H: Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
- 502 L → P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- 534 E → K: in ACADVLD; uncertain significance; dbSNP:rs2230180
- 562 binding FAD
- 583 S → W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
25% identity, 94% coverage: 10:356/370 of query aligns to 13:363/381 of 8sgsA
- binding coenzyme a: S131 (≠ Q131), A133 (≠ F133), N177 (≠ P172), F231 (≠ A223), M235 (≠ T227), L238 (≠ V230), I312 (≠ M305), E362 (≠ F355), G363 (= G356)
- binding flavin-adenine dinucleotide: F122 (≠ L122), L124 (≠ A124), S125 (≠ L125), G130 (= G130), S131 (≠ Q131), W155 (≠ V155), T157 (≠ A157), R267 (= R259), F270 (≠ Y262), L274 (= L266), L277 (≠ F269), Q335 (= Q328), I336 (≠ M329), G338 (= G331), G339 (= G332), I357 (≠ L350), I360 (≠ L353), Y361 (≠ Q354)
Sites not aligning to the query:
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
25% identity, 94% coverage: 10:356/370 of query aligns to 19:369/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L122), L130 (≠ A124), S131 (≠ L125), G136 (= G130), S137 (≠ Q131), W161 (≠ V155), T163 (≠ A157), T214 (≠ A200), R273 (= R259), F276 (≠ Y262), L280 (= L266), L283 (≠ F269), V285 (= V271), Q341 (= Q328), I342 (≠ M329), G345 (= G332), I363 (≠ L350), Y367 (≠ Q354)
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
25% identity, 94% coverage: 10:356/370 of query aligns to 16:366/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (= M333), T347 (≠ E337), E348 (= E338)
- binding flavin-adenine dinucleotide: F125 (≠ L122), L127 (≠ A124), S128 (≠ L125), G133 (= G130), S134 (≠ Q131), W158 (≠ V155), T160 (≠ A157), R270 (= R259), F273 (≠ Y262), L280 (≠ F269), V282 (= V271), Q338 (= Q328), I339 (≠ M329), G342 (= G332), I360 (≠ L350), Y364 (≠ Q354)
Sites not aligning to the query:
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
29% identity, 96% coverage: 11:365/370 of query aligns to 14:371/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ Q131), L133 (≠ F133), K178 (vs. gap), F231 (≠ A222), M235 (≠ L226), L238 (= L228), N241 (≠ D231), R242 (≠ H232), Y362 (≠ Q354), T363 (≠ F355), G364 (= G356)
- binding flavin-adenine dinucleotide: L122 (= L122), A124 (= A124), T125 (≠ L125), G130 (= G130), S131 (≠ Q131), F155 (≠ V155), I156 (≠ V156), T157 (≠ A157), K200 (≠ Y192), N208 (≠ A200), L358 (= L350), T365 (≠ D357), Q367 (≠ H361), I368 (≠ L362)
Sites not aligning to the query:
Query Sequence
>WP_038207304.1 NCBI__GCF_000745855.1:WP_038207304.1
MDFDYSSDQQMLRDSAQRYLQQEYSYLQREKILRDGGFSRTAWQDFAGFGWLGAALPEDA
GGFGGGPVEAGILMEAFGRHAVLEPFLSTVIVGGLLLQQGLHGTRRSELLERMIGGELQL
ALAALENDVGQDFARIETQAKATAKGWTLRGRKAVVANGGIADKFFVSARTPEGLSLFLV
DRTAPGMKVRSYRSNDGQTAAELTLDGVDVAREDLVGPAGGAADLLTLAVDHASAAICAE
VVGSSAYLVETTCEYLKTREQYGAPLAKFQVLQHKLADMYVQVELARSMAHVAAAALAKP
APERMREVSAARVQAIKCARLAGREAVQMHGGMGMSEELDVSAHFKRLTLTTLQFGDEAF
HLARMAALSE
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