SitesBLAST
Comparing 14442 FitnessBrowser__Keio:14442 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)
6kgyB Hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
100% identity, 100% coverage: 1:441/441 of query aligns to 1:441/441 of 6kgyB
- active site: C43 (= C43), C48 (= C48), T51 (= T51), Y168 (= Y168), E172 (= E172), H426 (= H426), E431 (= E431)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), E33 (= E33), Q34 (= Q34), M38 (= M38), G41 (= G41), T42 (= T42), G47 (= G47), C48 (= C48), A99 (= A99), N126 (= N126), T127 (= T127), G128 (= G128), G291 (= G291), D292 (= D292), F299 (= F299), T300 (= T300), Y301 (= Y301), S303 (= S303), F333 (= F333)
6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
99% identity, 99% coverage: 5:441/441 of query aligns to 1:432/432 of 6kyyA
- active site: C39 (= C43), C44 (= C48), T47 (= T51), Y159 (= Y168), E163 (= E172), H417 (= H426), E422 (= E431)
- binding copper (ii) ion: C39 (= C43), C44 (= C48), H226 (= H235), H229 (= H238), T291 (= T300)
- binding flavin-adenine dinucleotide: F7 (= F11), G8 (= G12), E29 (= E33), Q30 (= Q34), M34 (= M38), T38 (= T42), C39 (= C43), C44 (= C48), K48 (= K52), A95 (= A99), N117 (= N126), T118 (= T127), G119 (= G128), I160 (= I169), R243 (= R252), D283 (= D292), F290 (= F299), T291 (= T300), S294 (= S303)
8ajjA Crystal structure of the disulfide reductase mera from staphylococcus aureus (see paper)
50% identity, 99% coverage: 4:439/441 of query aligns to 2:438/442 of 8ajjA
- binding flavin-adenine dinucleotide: G10 (= G12), E31 (= E33), Q32 (= Q34), M36 (= M38), G39 (= G41), T40 (= T42), C41 (= C43), C46 (= C48), K50 (= K52), A97 (= A99), N126 (= N126), T127 (= T127), G128 (= G128), I169 (= I169), N255 (≠ A255), G290 (= G291), D291 (= D292), Q297 (= Q298), F298 (= F299), T299 (= T300), Y300 (= Y301), S302 (= S303)
- binding histidine: D353 (= D354), Y354 (≠ I355)
Sites not aligning to the query:
8ajkB Crystal structure of a c43s variant from the disulfide reductase mera from staphylococcus aureus (see paper)
49% identity, 100% coverage: 1:439/441 of query aligns to 2:441/447 of 8ajkB
- binding flavin-adenine dinucleotide: G11 (= G10), G13 (= G12), E34 (= E33), Q35 (= Q34), M39 (= M38), G42 (= G41), T43 (= T42), G48 (= G47), C49 (= C48), K53 (= K52), K99 (≠ Q98), A100 (= A99), N129 (= N126), T130 (= T127), G131 (= G128), G293 (= G291), D294 (= D292), Q300 (= Q298), F301 (= F299), T302 (= T300), Y303 (= Y301), S305 (= S303)
P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
33% identity, 98% coverage: 4:433/441 of query aligns to 170:612/631 of P16171
- Y264 (≠ F83) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
- Y605 (≠ H426) mutation to F: 10-fold decrease in activity. 300-fold decrease in activity; when associated with F-264.; mutation to H: 2-fold decrease in activity.
D9J041 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Lysinibacillus sphaericus (Bacillus sphaericus) (see paper)
31% identity, 98% coverage: 2:433/441 of query aligns to 83:527/546 of D9J041
- C122 (= C43) modified: Disulfide link with 127, Redox-active
- C127 (= C48) modified: Disulfide link with 122, Redox-active
5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
31% identity, 98% coverage: 2:434/441 of query aligns to 2:447/454 of 5x1yB
- active site: A13 (≠ K13), V37 (≠ A37), C41 (= C43), C46 (= C48), S49 (≠ T51), A74 (vs. gap), G75 (≠ Q60), Y178 (= Y168), E182 (= E172), A318 (≠ L304), A437 (≠ F424), Y439 (≠ H426), E444 (= E431)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), I32 (= I32), E33 (= E33), R34 (≠ Q34), G39 (= G41), T40 (= T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), A114 (= A99), T138 (= T127), G139 (= G128), Y178 (= Y168), R266 (= R252), G305 (= G291), D306 (= D292), F313 (= F299), V314 (≠ T300), A317 (≠ S303)
3ladA Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 angstroms resolution. A comparison with the structure of glutathione reductase (see paper)
31% identity, 98% coverage: 2:435/441 of query aligns to 2:459/472 of 3ladA
- active site: L44 (≠ Y39), C48 (= C43), C53 (= C48), S56 (≠ T51), V190 (≠ Y168), E194 (= E172), F448 (= F424), H450 (= H426), E455 (= E431)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (≠ K13), E33 (= E33), K34 (vs. gap), G46 (= G41), T47 (= T42), C48 (= C43), G52 (= G47), C53 (= C48), H120 (≠ Q98), G121 (≠ A99), A149 (≠ N126), S150 (≠ T127), G151 (= G128), I191 (= I169), R278 (= R252), D318 (= D292), L325 (≠ F299), A326 (≠ T300)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
31% identity, 98% coverage: 2:435/441 of query aligns to 3:460/477 of P18925
- 34:49 (vs. 33:43, 31% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- D319 (= D292) binding
- A327 (≠ T300) binding
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
30% identity, 98% coverage: 2:435/441 of query aligns to 2:459/473 of 5u8wA
- active site: P13 (≠ K13), L44 (≠ Y39), C48 (= C43), C53 (= C48), S56 (≠ T51), G82 (vs. gap), V83 (vs. gap), V190 (≠ Y168), E194 (= E172), S330 (≠ L304), F448 (= F424), H450 (= H426), E455 (= E431)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), P13 (≠ K13), G14 (≠ A14), E33 (= E33), K34 (vs. gap), G46 (= G41), T47 (= T42), C48 (= C43), G52 (= G47), C53 (= C48), K57 (= K52), H120 (≠ Q98), G121 (≠ A99), A149 (≠ N126), S150 (≠ T127), G151 (= G128), S170 (= S148), G317 (= G291), D318 (= D292), M324 (≠ Q298), L325 (≠ F299), A326 (≠ T300), H327 (≠ Y301), Y357 (≠ F333), H450 (= H426), P451 (= P427)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ L164), G189 (= G167), V190 (≠ Y168), I191 (= I169), E194 (= E172), E210 (= E188), A211 (= A189), L212 (≠ A190), A275 (= A249), V276 (≠ S250), G277 (= G251), R278 (= R252), M324 (≠ Q298), L325 (≠ F299), V355 (≠ S331), Y357 (≠ F333)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
30% identity, 98% coverage: 2:435/441 of query aligns to 1:458/472 of 5u8vA
- active site: P12 (≠ K13), L43 (≠ Y39), C47 (= C43), C52 (= C48), S55 (≠ T51), G81 (vs. gap), V82 (vs. gap), V189 (≠ Y168), E193 (= E172), S329 (≠ L304), F447 (= F424), H449 (= H426), E454 (= E431)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (≠ K13), G13 (≠ A14), E32 (= E33), G45 (= G41), T46 (= T42), C47 (= C43), G51 (= G47), C52 (= C48), K56 (= K52), H119 (≠ Q98), G120 (≠ A99), A148 (≠ N126), S149 (≠ T127), G150 (= G128), S169 (= S148), I190 (= I169), R277 (= R252), G316 (= G291), D317 (= D292), M323 (≠ Q298), L324 (≠ F299), A325 (≠ T300), H326 (≠ Y301), H449 (= H426), P450 (= P427)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ L164), G186 (= G165), G188 (= G167), V189 (≠ Y168), I190 (= I169), L208 (= L187), E209 (= E188), A210 (= A189), V243 (= V222), V275 (≠ S250), G276 (= G251)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
30% identity, 98% coverage: 2:435/441 of query aligns to 5:462/477 of 5u8uD
- active site: P16 (≠ K13), L47 (≠ Y39), C51 (= C43), C56 (= C48), S59 (≠ T51), G85 (vs. gap), V86 (vs. gap), V193 (≠ Y168), E197 (= E172), S333 (≠ L304), F451 (= F424), H453 (= H426), E458 (= E431)
- binding flavin-adenine dinucleotide: I12 (= I9), G15 (= G12), P16 (≠ K13), G17 (≠ A14), E36 (= E33), K37 (vs. gap), G49 (= G41), T50 (= T42), C51 (= C43), G55 (= G47), C56 (= C48), K60 (= K52), H123 (≠ Q98), G124 (≠ A99), A152 (≠ N126), S153 (≠ T127), G154 (= G128), I194 (= I169), R281 (= R252), G320 (= G291), D321 (= D292), M327 (≠ Q298), L328 (≠ F299), A329 (≠ T300), H330 (≠ Y301), H453 (= H426), P454 (= P427)
Sites not aligning to the query:
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
29% identity, 98% coverage: 2:435/441 of query aligns to 3:460/475 of 6awaA
- active site: L45 (≠ Y39), C49 (= C43), C54 (= C48), S57 (≠ T51), V191 (≠ Y168), E195 (= E172), F449 (= F424), H451 (= H426), E456 (= E431)
- binding adenosine monophosphate: I187 (≠ L164), E211 (= E188), A212 (= A189), L213 (≠ A190), V245 (= V222), V277 (≠ S250)
- binding flavin-adenine dinucleotide: I10 (= I9), G13 (= G12), P14 (≠ K13), G15 (≠ A14), E34 (= E33), K35 (vs. gap), T48 (= T42), C49 (= C43), G53 (= G47), C54 (= C48), K58 (= K52), H121 (≠ Q98), G122 (≠ A99), S151 (≠ T127), G152 (= G128), I192 (= I169), R279 (= R252), G318 (= G291), D319 (= D292), M325 (≠ Q298), L326 (≠ F299), A327 (≠ T300), Y358 (≠ F333)
Sites not aligning to the query:
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
30% identity, 98% coverage: 2:435/441 of query aligns to 3:460/478 of P14218
- 34:49 (vs. 33:43, 31% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- G122 (≠ A99) binding
- D319 (= D292) binding
- A327 (≠ T300) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see 2 papers)
30% identity, 98% coverage: 5:434/441 of query aligns to 100:543/561 of P00392
- A110 (≠ G15) binding
- G130 (≠ S35) binding
- T135 (= T42) binding
- C136 (= C43) modified: Disulfide link with 141, Redox-active
- C141 (= C48) modified: Disulfide link with 136, Redox-active
- K145 (= K52) binding
- A211 (= A99) binding
- D403 (= D292) binding
- V411 (≠ T300) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 558 binding
- 559 binding
4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
30% identity, 98% coverage: 5:434/441 of query aligns to 5:448/466 of 4k8dA
- active site: G13 (≠ K13), I37 (≠ Y39), C41 (= C43), C46 (= C48), S49 (≠ T51), V75 (vs. gap), P76 (≠ Q60), V185 (≠ Y168), E189 (= E172), A320 (≠ L304), F438 (= F424), Y440 (≠ H426), E445 (= E431)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), A14 (= A14), E33 (= E33), R34 (≠ Q34), G39 (= G41), T40 (= T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), E115 (≠ Q98), A116 (= A99), T145 (= T127), G146 (= G128), R268 (= R252), G307 (= G291), D308 (= D292), F315 (= F299), V316 (≠ T300), Y317 (= Y301)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S183 (≠ G166), S184 (≠ G167), V185 (≠ Y168), V186 (≠ I169), E189 (= E172), R206 (≠ A189), N207 (≠ A190), R212 (= R196), T266 (≠ S250), G267 (= G251), Q314 (= Q298), F315 (= F299), V345 (≠ S331)
Sites not aligning to the query:
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
30% identity, 97% coverage: 5:431/441 of query aligns to 5:445/455 of 1ebdA
- active site: P13 (≠ K13), L37 (≠ Y39), C41 (= C43), C46 (= C48), S49 (≠ T51), N74 (vs. gap), V75 (vs. gap), Y180 (= Y168), E184 (= E172), S320 (≠ L304), H438 (≠ F424), H440 (= H426), E445 (= E431)
- binding flavin-adenine dinucleotide: G10 (= G10), G12 (= G12), P13 (≠ K13), V32 (≠ I32), E33 (= E33), K34 (≠ Q34), G39 (= G41), V40 (≠ T42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), E112 (≠ Q98), A113 (= A99), T141 (= T127), G142 (= G128), Y180 (= Y168), I181 (= I169), R268 (= R252), D308 (= D292), A314 (≠ Q298), L315 (≠ F299), A316 (≠ T300)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
30% identity, 97% coverage: 5:431/441 of query aligns to 11:451/470 of P11959
- 39:47 (vs. 33:43, 45% identical) binding
- K56 (= K52) binding
- D314 (= D292) binding
- A322 (≠ T300) binding
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
30% identity, 99% coverage: 1:435/441 of query aligns to 4:457/470 of 6uziC
- active site: C45 (= C43), C50 (= C48), S53 (≠ T51), V187 (≠ Y168), E191 (= E172), H448 (= H426), E453 (= E431)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (≠ K13), G17 (≠ A14), E36 (= E33), K37 (≠ Q34), G43 (= G41), T44 (= T42), C45 (= C43), G49 (= G47), C50 (= C48), S53 (≠ T51), K54 (= K52), V117 (≠ Q98), G118 (≠ A99), T147 (= T127), G148 (= G128), I188 (= I169), R276 (= R252), D316 (= D292), M322 (≠ Q298), L323 (≠ F299), A324 (≠ T300)
- binding zinc ion: H448 (= H426), E453 (= E431)
4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
30% identity, 98% coverage: 5:434/441 of query aligns to 6:449/467 of 4k7zA
- active site: G14 (≠ K13), I38 (≠ Y39), A42 (≠ C43), A47 (≠ C48), S50 (≠ T51), V76 (vs. gap), P77 (≠ Q60), V186 (≠ Y168), E190 (= E172), A321 (≠ L304), F439 (= F424), Y441 (≠ H426), E446 (= E431)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), A15 (= A14), E34 (= E33), R35 (≠ Q34), G40 (= G41), T41 (= T42), A42 (≠ C43), G46 (= G47), A47 (≠ C48), K51 (= K52), E116 (≠ Q98), A117 (= A99), T146 (= T127), G147 (= G128), R269 (= R252), G308 (= G291), D309 (= D292), Q315 (= Q298), F316 (= F299), V317 (≠ T300), Y318 (= Y301)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S184 (≠ G166), S185 (≠ G167), V186 (≠ Y168), V187 (≠ I169), E190 (= E172), R207 (≠ A189), N208 (≠ A190), R213 (= R196), T267 (≠ S250), G268 (= G251), R269 (= R252), Q315 (= Q298), F316 (= F299), V346 (≠ S331)
Sites not aligning to the query:
Query Sequence
>14442 FitnessBrowser__Keio:14442
MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQ
HTDFVRAIQRKNEVVNFLRNKNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHG
EKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANF
GSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQ
LAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKRLHTTADNIWAMGDVTGGLQFT
YISLDDYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL
PVAAIPRARVMNDTRGVLKAIVDNKTQRMLGASLLCVDSHEMINIVKMVMDAGLPYSILR
DQIFTHPSMSESLNDLFSLVK
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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