SitesBLAST
Comparing PP_5366 FitnessBrowser__Putida:PP_5366 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)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
56% identity, 98% coverage: 4:458/466 of query aligns to 1:458/465 of 3urhB
- active site: Y35 (≠ L38), C39 (= C42), C44 (= C47), S47 (= S50), V183 (= V184), E187 (= E188), H443 (= H443), H445 (= H445), E450 (= E450)
- binding flavin-adenine dinucleotide: I6 (= I9), G7 (= G10), G9 (= G12), P10 (= P13), G11 (= G14), E30 (= E33), K31 (≠ G34), G37 (= G40), T38 (= T41), C39 (= C42), G43 (= G46), C44 (= C47), K48 (= K51), T111 (≠ W114), G112 (= G115), A140 (= A143), T141 (= T144), G142 (= G145), I184 (= I185), R273 (= R274), G312 (= G312), D313 (= D313), M319 (= M319), L320 (= L320), A321 (= A321), H322 (= H322)
P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see 2 papers)
55% identity, 97% coverage: 5:457/466 of query aligns to 39:492/501 of P31023
- 67:76 (vs. 33:42, 70% identical) binding
- C76 (= C42) modified: Disulfide link with 81, Redox-active
- C81 (= C47) modified: Disulfide link with 76, Redox-active
- G149 (= G115) binding
- D348 (= D313) binding
- MLAH 354:357 (= MLAH 319:322) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
55% identity, 97% coverage: 5:457/466 of query aligns to 5:458/467 of 1dxlA
- active site: L38 (= L38), C42 (= C42), C47 (= C47), S50 (= S50), Y184 (≠ V184), E188 (= E188), H444 (= H443), H446 (= H445), E451 (= E450)
- binding flavin-adenine dinucleotide: I9 (= I9), P13 (= P13), G14 (= G14), E33 (= E33), K34 (≠ G34), R35 (= R35), G40 (= G40), T41 (= T41), C42 (= C42), G46 (= G46), C47 (= C47), K51 (= K51), Y114 (≠ W114), G115 (= G115), T144 (= T144), G145 (= G145), Y184 (≠ V184), I185 (= I185), R274 (= R274), D314 (= D313), M320 (= M319), L321 (= L320), A322 (= A321), H323 (= H322)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
54% identity, 97% coverage: 5:457/466 of query aligns to 43:499/509 of P09622
- 71:80 (vs. 33:42, 70% identical) binding
- K72 (≠ G34) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K51) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ D66) to T: in dbSNP:rs1130477
- G154 (= G115) binding
- TGS 183:185 (= TGS 144:146) binding
- 220:227 (vs. 181:188, 88% identical) binding
- E243 (= E204) binding
- V278 (= V238) binding
- G314 (= G273) binding
- D355 (= D313) binding
- MLAH 361:364 (= MLAH 319:322) binding
- E375 (= E333) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ E341) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D406) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to N: Does not affect dihydrolipoyl dehydrogenase activity.
- E466 (= E424) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F431) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to F: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
- D479 (= D437) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ L440) to G: in DLDD; reduced enzyme activity; dbSNP:rs397514650; mutation to A: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to M: Does not affect interaction with PDHX.
- H485 (= H443) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P446) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S449) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E450) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (= R453) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
Sites not aligning to the query:
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
54% identity, 97% coverage: 5:457/466 of query aligns to 6:462/472 of 1zmdA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V184), E190 (= E188), H448 (= H443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (≠ G34), N36 (≠ R35), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ W114), G117 (= G115), T146 (= T144), G147 (= G145), S166 (= S164), R278 (= R274), F281 (≠ Y277), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I180), G183 (= G181), G185 (= G183), V186 (= V184), I187 (= I185), E190 (= E188), E206 (= E204), F207 (≠ Y205), L208 (= L206), I276 (= I272), G277 (= G273), R278 (= R274), M324 (= M319), L325 (= L320), V355 (= V350), Y357 (= Y352)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
54% identity, 97% coverage: 5:457/466 of query aligns to 6:462/472 of 1zmcA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V184), E190 (= E188), H448 (= H443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (≠ G34), N36 (≠ R35), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ W114), G117 (= G115), T146 (= T144), G147 (= G145), S166 (= S164), I187 (= I185), F281 (≠ Y277), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding nicotinamide-adenine-dinucleotide: G183 (= G181), G185 (= G183), V205 (≠ I203), E206 (= E204), F207 (≠ Y205), L208 (= L206), K240 (= K237), V241 (= V238), I276 (= I272), G277 (= G273), R278 (= R274), R297 (= R293), M324 (= M319)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
53% identity, 97% coverage: 5:457/466 of query aligns to 16:472/482 of 6hg8B
- active site: C53 (= C42), C58 (= C47), S61 (= S50), V196 (= V184), E200 (= E188), H460 (= H445), E465 (= E450)
- binding flavin-adenine dinucleotide: I20 (= I9), G23 (= G12), P24 (= P13), G25 (= G14), E44 (= E33), K45 (≠ G34), N46 (≠ R35), G51 (= G40), T52 (= T41), C53 (= C42), G57 (= G46), C58 (= C47), K62 (= K51), Y126 (≠ W114), G127 (= G115), T156 (= T144), G157 (= G145), I197 (= I185), R288 (= R274), F291 (≠ Y277), G327 (= G312), D328 (= D313), M334 (= M319), L335 (= L320), A336 (= A321), H337 (= H322)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
53% identity, 99% coverage: 1:461/466 of query aligns to 4:464/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V184), E191 (= E188), H448 (= H445), E453 (= E450)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (= P13), G17 (= G14), E36 (= E33), K37 (≠ G34), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), S53 (= S50), K54 (= K51), V117 (≠ W114), G118 (= G115), T147 (= T144), G148 (= G145), I188 (= I185), R276 (= R274), D316 (= D313), M322 (= M319), L323 (= L320), A324 (= A321)
- binding zinc ion: H448 (= H445), E453 (= E450)
1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
52% identity, 98% coverage: 2:457/466 of query aligns to 4:469/478 of 1v59A
- active site: L40 (= L38), C44 (= C42), C49 (= C47), S52 (= S50), I193 (≠ V184), E197 (= E188), T349 (≠ G337), H455 (= H443), H457 (= H445), E462 (= E450)
- binding flavin-adenine dinucleotide: G14 (= G12), P15 (= P13), A16 (≠ G14), E35 (= E33), K36 (≠ G34), R37 (= R35), G42 (= G40), T43 (= T41), C44 (= C42), G48 (= G46), C49 (= C47), K53 (= K51), N117 (≠ W114), G118 (= G115), T153 (= T144), G154 (= G145), R285 (= R274), Y288 (= Y277), G324 (= G312), D325 (= D313), M331 (= M319), L332 (= L320), A333 (= A321), H334 (= H322), Y364 (= Y352)
- binding nicotinamide-adenine-dinucleotide: I189 (= I180), G190 (= G181), E213 (= E204), F214 (≠ Y205), K246 (= K237), V283 (≠ I272)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
52% identity, 98% coverage: 2:457/466 of query aligns to 4:469/478 of 1jehA
- active site: L40 (= L38), C44 (= C42), C49 (= C47), S52 (= S50), I193 (≠ V184), E197 (= E188), T349 (≠ G337), H455 (= H443), H457 (= H445), E462 (= E450)
- binding flavin-adenine dinucleotide: I11 (= I9), G14 (= G12), P15 (= P13), A16 (≠ G14), V34 (= V32), E35 (= E33), K36 (≠ G34), R37 (= R35), G42 (= G40), T43 (= T41), C44 (= C42), G48 (= G46), C49 (= C47), K53 (= K51), G118 (= G115), T153 (= T144), G154 (= G145), I194 (= I185), R285 (= R274), Y288 (= Y277), L292 (= L281), G324 (= G312), D325 (= D313), M331 (= M319), L332 (= L320), A333 (= A321), H334 (= H322)
P09624 Dihydrolipoyl dehydrogenase, mitochondrial; DLD; 2-oxoglutarate dehydrogenase complex component E3; OGDC-E3; OGDHC subunit E3; Alpha-ketoglutarate dehydrogenase complex subunit E3; alpha-KGDHC subunit E3; Dihydrolipoamide dehydrogenase; Dihydrolipoamide:NAD(+) oxidoreductase; Glycine decarboxylase complex subunit L; GDC subunit L; Lipoamide dehydrogenase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E3 component; PDC subunit E3; PDH complex subunit E3; EC 1.8.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
52% identity, 98% coverage: 2:457/466 of query aligns to 25:490/499 of P09624
- 56:65 (vs. 33:42, 70% identical) binding
- C65 (= C42) modified: Disulfide link with 70, Redox-active
- C70 (= C47) modified: Disulfide link with 65, Redox-active
- K74 (= K51) binding
- G139 (= G115) binding
- D346 (= D313) binding
- MLAH 352:355 (= MLAH 319:322) binding
- H478 (= H445) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
53% identity, 94% coverage: 18:457/466 of query aligns to 17:456/465 of 2qaeA
- active site: L37 (= L38), C41 (= C42), C46 (= C47), S49 (= S50), V184 (= V184), E188 (= E188), H442 (= H443), H444 (= H445), E449 (= E450)
- binding flavin-adenine dinucleotide: E32 (= E33), K33 (≠ G34), R34 (= R35), G39 (= G40), T40 (= T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), E114 (≠ W114), G115 (= G115), T144 (= T144), G145 (= G145), S164 (= S164), I185 (= I185), F274 (≠ Y277), G310 (= G312), D311 (= D313), M318 (= M319), L319 (= L320), A320 (= A321), H321 (= H322)
Sites not aligning to the query:
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
52% identity, 98% coverage: 2:460/466 of query aligns to 1:467/473 of 6aonA
- active site: P43 (≠ L38), C47 (= C42), C52 (= C47), S55 (= S50), V191 (= V184), E195 (= E188), H450 (= H443), H452 (= H445), E457 (= E450)
- binding calcium ion: A218 (≠ P211), A220 (≠ T213), Q222 (≠ T215)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), D32 (vs. gap), A33 (vs. gap), W34 (vs. gap), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), K119 (≠ W114), G120 (= G115), T151 (= T144), G152 (= G145), N171 (≠ S164), I192 (= I185), R280 (= R274), Y283 (= Y277), G319 (= G312), D320 (= D313), M326 (= M319), L327 (= L320), A328 (= A321), H329 (= H322)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
49% identity, 100% coverage: 2:466/466 of query aligns to 3:472/478 of P14218
- 34:49 (vs. 33:42, 44% identical) binding
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding
- G122 (= G115) binding
- D319 (= D313) binding
- A327 (= A321) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
49% identity, 100% coverage: 2:466/466 of query aligns to 1:470/472 of 5u8vA
- active site: P12 (= P13), L43 (= L38), C47 (= C42), C52 (= C47), S55 (= S50), G81 (vs. gap), V82 (≠ P77), V189 (= V184), E193 (= E188), S329 (≠ E325), F447 (≠ H443), H449 (= H445), E454 (= E450)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), E32 (= E33), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), H119 (≠ W114), G120 (= G115), A148 (= A143), S149 (≠ T144), G150 (= G145), S169 (= S164), I190 (= I185), R277 (= R274), G316 (= G312), D317 (= D313), M323 (= M319), L324 (= L320), A325 (= A321), H326 (= H322), H449 (= H445), P450 (= P446)
- binding nicotinamide-adenine-dinucleotide: I185 (= I180), G186 (= G181), G188 (= G183), V189 (= V184), I190 (= I185), L208 (≠ I203), E209 (= E204), A210 (≠ Y205), V243 (= V238), V275 (≠ I272), G276 (= G273)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
49% identity, 100% coverage: 2:466/466 of query aligns to 2:471/473 of 5u8wA
- active site: P13 (= P13), L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), G82 (vs. gap), V83 (≠ P77), V190 (= V184), E194 (= E188), S330 (≠ E325), F448 (≠ H443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), P13 (= P13), G14 (= G14), E33 (= E33), K34 (vs. gap), G46 (= G40), T47 (= T41), C48 (= C42), G52 (= G46), C53 (= C47), K57 (= K51), H120 (≠ W114), G121 (= G115), A149 (= A143), S150 (≠ T144), G151 (= G145), S170 (= S164), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322), Y357 (= Y352), H450 (= H445), P451 (= P446)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I180), G189 (= G183), V190 (= V184), I191 (= I185), E194 (= E188), E210 (= E204), A211 (≠ Y205), L212 (= L206), A275 (= A271), V276 (≠ I272), G277 (= G273), R278 (= R274), M324 (= M319), L325 (= L320), V355 (= V350), Y357 (= Y352)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
49% identity, 100% coverage: 2:466/466 of query aligns to 5:474/477 of 5u8uD
- active site: P16 (= P13), L47 (= L38), C51 (= C42), C56 (= C47), S59 (= S50), G85 (vs. gap), V86 (≠ P77), V193 (= V184), E197 (= E188), S333 (≠ E325), F451 (≠ H443), H453 (= H445), E458 (= E450)
- binding flavin-adenine dinucleotide: I12 (= I9), G15 (= G12), P16 (= P13), G17 (= G14), E36 (= E33), K37 (vs. gap), G49 (= G40), T50 (= T41), C51 (= C42), G55 (= G46), C56 (= C47), K60 (= K51), H123 (≠ W114), G124 (= G115), A152 (= A143), S153 (≠ T144), G154 (= G145), I194 (= I185), R281 (= R274), G320 (= G312), D321 (= D313), M327 (= M319), L328 (= L320), A329 (= A321), H330 (= H322), H453 (= H445), P454 (= P446)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
51% identity, 97% coverage: 4:457/466 of query aligns to 2:446/455 of 2yquB
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (≠ P77), V73 (≠ T78), V177 (= V184), E181 (= E188), S314 (≠ E325), H432 (= H443), H434 (= H445), E439 (= E450)
- binding carbonate ion: A310 (= A321), S314 (≠ E325), S423 (= S434), D426 (= D437)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (≠ G34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ W114), A111 (≠ G115), T137 (= T144), G138 (= G145), I178 (= I185), Y265 (= Y277), G301 (= G312), D302 (= D313), M308 (= M319), L309 (= L320), A310 (= A321), H311 (= H322)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
51% identity, 97% coverage: 4:457/466 of query aligns to 2:446/455 of 2yquA
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (≠ P77), V73 (≠ T78), V177 (= V184), E181 (= E188), S314 (≠ E325), H432 (= H443), H434 (= H445), E439 (= E450)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (≠ G34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ W114), A111 (≠ G115), T137 (= T144), G138 (= G145), S157 (= S164), I178 (= I185), Y265 (= Y277), G301 (= G312), D302 (= D313), M308 (= M319), L309 (= L320), A310 (= A321)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
51% identity, 97% coverage: 4:457/466 of query aligns to 2:446/452 of 2eq7A
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (≠ P77), V73 (≠ T78), V177 (= V184), E181 (= E188), S314 (≠ E325), H432 (= H443), H434 (= H445), E439 (= E450)
- binding flavin-adenine dinucleotide: G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (≠ G34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ W114), A111 (≠ G115), T137 (= T144), G138 (= G145), S157 (= S164), I178 (= I185), R262 (= R274), Y265 (= Y277), D302 (= D313), M308 (= M319), L309 (= L320), A310 (= A321), H311 (= H322), Y341 (= Y352)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G153), G174 (= G181), G176 (= G183), V177 (= V184), I178 (= I185), E197 (= E204), Y198 (= Y205), V231 (= V238), V260 (≠ I272), G261 (= G273), R262 (= R274), M308 (= M319), L309 (= L320), V339 (= V350)
Query Sequence
>PP_5366 FitnessBrowser__Putida:PP_5366
MKSYDVVIIGGGPGGYNAAIRAGQLGLSVACVEGRSTLGGTCLNVGCMPSKALLHASELY
EAASGDEFAHLGIEVKPTLNLAQMMKQKDESVTGLTKGIEYLFRKNKVEWIKGWGRLDGI
GKVVVKAEDGSETALQAKDIVIATGSEPTPLPGVTVDNQRIIDSTGALSLPQVPKHLVVI
GAGVIGLELGSVWRRLGSQVTVIEYLDRICPGTDTETAKTLQKALAKQGMVFKLGSKVTQ
ATAGADGVSLTLEPAAGGTAESLQADYVLVAIGRRPYTKGLNLESVGLEADKRGMLNNEH
HRTSVPGVWVIGDVTSGPMLAHKAEDEAVACIERIAGKPHEVNYNLIPGVIYTRPEMATV
GKTEEQLKAEGRAYKVGKFPFTANSRAKINHETEGFAKVIADAETDEVLGVHLVGPSVSE
MIGEFCVAMEFSASAEDIALTCHPHPTRSEALRQAAMNVDGMAMQI
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