SitesBLAST
Comparing WP_035236837.1 NCBI__GCF_000745975.1:WP_035236837.1 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)
Q72IB8 Proline dehydrogenase; PRODH; Proline oxidase; TtPRODH; EC 1.5.5.2 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see 2 papers)
38% identity, 88% coverage: 23:289/303 of query aligns to 33:294/307 of Q72IB8
2g37B Structure of thermus thermophilus l-proline dehydrogenase (see paper)
38% identity, 88% coverage: 23:289/303 of query aligns to 39:300/300 of 2g37B
- binding flavin-adenine dinucleotide: D139 (= D123), M140 (= M124), V167 (= V151), R190 (= R179), V192 (= V181), K193 (= K182), G194 (= G183), A195 (≠ V184), A231 (= A220), T232 (= T221), H233 (= H222), D234 (= D223), L260 (= L249), V263 (= V252), Y281 (= Y270)
Q9RW55 Proline dehydrogenase; PRODH; DrPRODH; Proline oxidase; EC 1.5.5.2 from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) (see paper)
34% identity, 93% coverage: 18:300/303 of query aligns to 27:308/310 of Q9RW55
- G63 (= G54) mutation to A: 140-fold decrease in catalytic efficiency for proline.
- E64 (= E55) mutation to A: 27-fold decrease in catalytic efficiency for proline.
- K98 (= K89) binding substrate
- M136 (= M124) binding FAD
- Q166 (= Q153) binding FAD
- RMVKGA 187:192 (≠ RLVKGV 179:184) binding FAD
- TH 229:230 (= TH 221:222) binding FAD
- RR 291:292 (= RR 283:284) binding substrate
- RIAE 292:295 (≠ RLKE 284:287) binding FAD
4h6qA Structure of oxidized deinococcus radiodurans proline dehydrogenase complexed with l-tetrahydrofuroic acid (see paper)
36% identity, 90% coverage: 18:289/303 of query aligns to 11:281/281 of 4h6qA
- binding flavin-adenine dinucleotide: D119 (= D123), M120 (= M124), Q150 (= Q153), R171 (= R179), V173 (= V181), K174 (= K182), G175 (= G183), A176 (≠ V184), A212 (= A220), T213 (= T221), H214 (= H222), M240 (= M248), L241 (= L249), I244 (≠ V252), R276 (= R284), E279 (= E287), P281 (= P289)
- binding tetrahydrofuran-2-carboxylic acid: K82 (= K89), Y262 (= Y270), R275 (= R283), R276 (= R284)
4h6rA Structure of reduced deinococcus radiodurans proline dehydrogenase (see paper)
36% identity, 90% coverage: 18:289/303 of query aligns to 2:272/272 of 4h6rA
- binding dihydroflavine-adenine dinucleotide: D110 (= D123), M111 (= M124), V139 (= V151), Q141 (= Q153), R162 (= R179), V164 (= V181), K165 (= K182), G166 (= G183), A167 (≠ V184), A203 (= A220), T204 (= T221), H205 (= H222), Q230 (= Q247), L232 (= L249), I235 (≠ V252), Y253 (= Y270), R267 (= R284), E270 (= E287), P272 (= P289)
5m42A Structure of thermus thermophilus l-proline dehydrogenase lacking alpha helices a, b and c (see paper)
37% identity, 81% coverage: 30:274/303 of query aligns to 3:242/242 of 5m42A
- binding flavin mononucleotide: D96 (= D123), M97 (= M124), V124 (= V151), Q126 (= Q153), R147 (= R179), V149 (= V181), K150 (= K182), G151 (= G183), A152 (≠ V184), A188 (= A220), T189 (= T221), H190 (= H222), L217 (= L249)
4nmaA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca in complex with l-tetrahydro-2-furoic acid (see paper)
26% identity, 93% coverage: 8:290/303 of query aligns to 80:410/977 of 4nmaA
- binding flavin-adenine dinucleotide: D226 (= D123), M227 (= M124), Q258 (= Q153), R285 (= R179), V287 (= V181), K288 (= K182), G289 (= G183), A290 (≠ V184), Y291 (= Y185), W292 (≠ V186), W309 (≠ Y193), T310 (≠ K194), I311 (≠ A195), K312 (≠ Y196), S315 (≠ I199), A338 (= A220), S339 (≠ T221), H340 (= H222), N341 (≠ D223), Q365 (= Q247), L367 (= L249), E407 (= E287)
- binding tetrahydrofuran-2-carboxylic acid: K185 (= K89), Y388 (= Y270), Y400 (= Y280), R403 (= R283), R404 (= R284)
Sites not aligning to the query:
4nmdA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca reduced with dithionite (see paper)
26% identity, 90% coverage: 18:290/303 of query aligns to 94:410/979 of 4nmdA
- binding dihydroflavine-adenine dinucleotide: D226 (= D123), M227 (= M124), V256 (= V151), Q258 (= Q153), R285 (= R179), V287 (= V181), K288 (= K182), G289 (= G183), A290 (≠ V184), W292 (≠ V186), W309 (≠ Y193), T310 (≠ K194), I311 (≠ A195), K312 (≠ Y196), S315 (≠ I199), A338 (= A220), S339 (≠ T221), H340 (= H222), N341 (≠ D223), Q365 (= Q247), V366 (≠ M248), L367 (= L249), Y388 (= Y270)
Sites not aligning to the query:
7na0A Structure of geobacter sulfurreducens proline utilization a (puta) variant a206w (see paper)
26% identity, 90% coverage: 18:290/303 of query aligns to 94:410/981 of 7na0A
- binding flavin-adenine dinucleotide: D226 (= D123), M227 (= M124), V256 (= V151), Q258 (= Q153), R285 (= R179), V287 (= V181), K288 (= K182), G289 (= G183), A290 (≠ V184), Y291 (= Y185), W292 (≠ V186), W309 (≠ Y193), T310 (≠ K194), I311 (≠ A195), K312 (≠ Y196), S315 (≠ I199), A338 (= A220), S339 (≠ T221), H340 (= H222), N341 (≠ D223), L367 (= L249), Y388 (= Y270), E407 (= E287)
Sites not aligning to the query:
4nmfA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
26% identity, 90% coverage: 18:290/303 of query aligns to 90:406/973 of 4nmfA
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K181 (= K89), Y287 (= Y185), Y384 (= Y270), Y396 (= Y280), R399 (= R283), R400 (= R284)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K181 (= K89), D222 (= D123), M223 (= M124), V252 (= V151), Q254 (= Q153), R281 (= R179), V283 (= V181), K284 (= K182), G285 (= G183), A286 (≠ V184), W288 (≠ V186), W305 (≠ Y193), T306 (≠ K194), I307 (≠ A195), K308 (≠ Y196), S311 (≠ I199), A334 (= A220), S335 (≠ T221), H336 (= H222), N337 (≠ D223), Q361 (= Q247), V362 (≠ M248), L363 (= L249), Y384 (= Y270), E403 (= E287)
Sites not aligning to the query:
4nmfB Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine and complexed with menadione bisulfite (see paper)
26% identity, 90% coverage: 18:290/303 of query aligns to 93:409/979 of 4nmfB
- binding (2R)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K89), Y290 (= Y185), Y387 (= Y270), Y399 (= Y280), R402 (= R283), R403 (= R284)
- binding (2S)-2-methyl-1,4-dioxo-1,2,3,4-tetrahydronaphthalene-2-sulfonic acid: K184 (= K89), L366 (= L249), Y399 (= Y280), R402 (= R283)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K184 (= K89), D225 (= D123), M226 (= M124), V255 (= V151), Q257 (= Q153), R284 (= R179), V286 (= V181), K287 (= K182), G288 (= G183), A289 (≠ V184), W291 (≠ V186), W308 (≠ Y193), T309 (≠ K194), I310 (≠ A195), K311 (≠ Y196), S314 (≠ I199), A337 (= A220), S338 (≠ T221), H339 (= H222), N340 (≠ D223), Q364 (= Q247), L366 (= L249), Y387 (= Y270), E406 (= E287)
Sites not aligning to the query:
4nmeA Crystal structure of proline utilization a (puta) from geobacter sulfurreducens pca inactivated by n-propargylglycine (see paper)
26% identity, 90% coverage: 18:290/303 of query aligns to 92:405/972 of 4nmeA
- binding N-propargylglycine-modified flavin adenine dinucleotide: K183 (= K89), D224 (= D123), M225 (= M124), V254 (= V151), Q256 (= Q153), R283 (= R179), V285 (= V181), K286 (= K182), G287 (= G183), A288 (≠ V184), W290 (≠ V186), W307 (≠ Y193), T308 (≠ K194), I309 (≠ A195), K310 (≠ Y196), S313 (≠ I199), A336 (= A220), S337 (≠ T221), H338 (= H222), N339 (≠ D223), Q363 (= Q247), L365 (= L249), Y383 (= Y270), E402 (= E287)
Sites not aligning to the query:
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
27% identity, 90% coverage: 16:288/303 of query aligns to 84:399/959 of 5ur2B
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K89), D215 (= D123), M216 (= M124), Q249 (= Q153), V278 (= V181), K279 (= K182), G280 (= G183), A281 (≠ V184), W283 (≠ V186), Y300 (vs. gap), T301 (≠ A192), N302 (≠ Y193), K303 (= K194), S306 (≠ K197), A329 (= A220), S330 (≠ T221), H331 (= H222), N332 (≠ D223), Q356 (= Q247), M357 (= M248), L358 (= L249), Y379 (= Y270), E398 (= E287)
Sites not aligning to the query:
4nmcA Crystal structure of oxidized proline utilization a (puta) from geobacter sulfurreducens pca complexed with zwittergent 3-12 (see paper)
25% identity, 91% coverage: 18:292/303 of query aligns to 83:400/941 of 4nmcA
- binding flavin-adenine dinucleotide: D215 (= D123), M216 (= M124), V245 (= V151), Q247 (= Q153), R274 (= R179), V276 (= V181), K277 (= K182), G278 (= G183), A279 (≠ V184), W281 (≠ V186), W298 (≠ Y193), T299 (≠ K194), I300 (≠ A195), K301 (≠ Y196), S304 (≠ I199), A327 (= A220), S328 (≠ T221), H329 (= H222), N330 (≠ D223), L356 (= L249), Y377 (= Y270)
Sites not aligning to the query:
9d7lA Bifunctional protein PutA (see paper)
26% identity, 89% coverage: 20:290/303 of query aligns to 52:355/380 of 9d7lA
- binding {[(3E)-4-{10-[(2S,3S,4R)-5-{[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-7,8-dimethyl-2,4-dioxo-2,3,4,10-tetrahydrobenzo[g]pteridin-5(1H)-yl}but-3-en-2-ylidene]amino}acetic acid (non-preferred name): K127 (= K89), D168 (= D123), A169 (≠ M124), V200 (= V151), Q202 (= Q153), R229 (= R179), V231 (= V181), K232 (= K182), G233 (= G183), A234 (≠ V184), Y235 (= Y185), W236 (≠ V186), F252 (≠ I191), T253 (≠ A192), R254 (≠ Y193), K255 (= K194), T258 (≠ K197), A281 (= A220), T282 (= T221), H283 (= H222), N284 (≠ D223), Q307 (= Q247), C308 (≠ M248), L309 (= L249), Y333 (= Y270), Y345 (= Y280), E352 (= E287)
Sites not aligning to the query:
- binding {[(3E)-4-{10-[(2S,3S,4R)-5-{[(R)-{[(R)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]oxy}-2,3,4-trihydroxypentyl]-7,8-dimethyl-2,4-dioxo-2,3,4,10-tetrahydrobenzo[g]pteridin-5(1H)-yl}but-3-en-2-ylidene]amino}acetic acid (non-preferred name): 358
9c8aA Minimal puta proline dehydrogenase domain (design #2) with the fad n5 modified with propanal resulting from inactivation with n- allylglycine(replicate #1) (see paper)
26% identity, 89% coverage: 20:290/303 of query aligns to 51:356/382 of 9c8aA
- binding flavin-adenine dinucleotide: D167 (= D123), A168 (≠ M124), Q201 (= Q153), R228 (= R179), V230 (= V181), K231 (= K182), G232 (= G183), A233 (≠ V184), Y234 (= Y185), W235 (≠ V186), F253 (≠ I191), T254 (≠ A192), R255 (≠ Y193), K256 (= K194), T259 (≠ K197), A282 (= A220), T283 (= T221), H284 (= H222), N285 (≠ D223), C309 (≠ M248), L310 (= L249), E353 (= E287)
- binding dihydroflavine-adenine dinucleotide: D167 (= D123), A168 (≠ M124), V199 (= V151), Q201 (= Q153), R228 (= R179), V230 (= V181), K231 (= K182), G232 (= G183), A233 (≠ V184), Y234 (= Y185), W235 (≠ V186), F253 (≠ I191), T254 (≠ A192), R255 (≠ Y193), K256 (= K194), T259 (≠ K197), A282 (= A220), T283 (= T221), H284 (= H222), N285 (≠ D223), Q308 (= Q247), C309 (≠ M248), L310 (= L249), E353 (= E287)
Sites not aligning to the query:
8w0kB Minimal puta proline dehydrogenase domain (design #2) complexed with 1-hydroxyethane-1-sulfonate (see paper)
26% identity, 89% coverage: 22:290/303 of query aligns to 54:357/383 of 8w0kB
- binding flavin-adenine dinucleotide: D168 (= D123), A169 (≠ M124), V200 (= V151), Q202 (= Q153), R229 (= R179), V231 (= V181), K232 (= K182), G233 (= G183), A234 (≠ V184), Y235 (= Y185), W236 (≠ V186), F254 (≠ I191), T255 (≠ A192), R256 (≠ Y193), K257 (= K194), T260 (≠ K197), A283 (= A220), T284 (= T221), H285 (= H222), N286 (≠ D223), C310 (≠ M248), L311 (= L249), E354 (= E287)
- binding (1R)-1-hydroxyethane-1-sulfonic acid: K127 (= K89), A234 (≠ V184), Y335 (= Y270), Y347 (= Y280), R350 (= R283), R351 (= R284)
Sites not aligning to the query:
8dkoB Minimal puta proline dehydrogenase domain (design #1) complexed with s-(-)-tetrahydro-2-furoic acid (see paper)
26% identity, 89% coverage: 21:290/303 of query aligns to 58:362/393 of 8dkoB
- binding flavin-adenine dinucleotide: D173 (= D123), A174 (≠ M124), V205 (= V151), Q207 (= Q153), R234 (= R179), V236 (= V181), K237 (= K182), G238 (= G183), A239 (≠ V184), Y240 (= Y185), W241 (≠ V186), F259 (≠ I191), T260 (≠ A192), R261 (≠ Y193), K262 (= K194), T265 (≠ K197), A288 (= A220), T289 (= T221), H290 (= H222), N291 (≠ D223), C315 (≠ M248), L316 (= L249), E359 (= E287)
- binding tetrahydrofuran-2-carboxylic acid: K132 (= K89), D173 (= D123), Y340 (= Y270), R355 (= R283), R356 (= R284)
Sites not aligning to the query:
8w0kA Minimal puta proline dehydrogenase domain (design #2) complexed with 1-hydroxyethane-1-sulfonate (see paper)
26% identity, 89% coverage: 22:290/303 of query aligns to 51:354/380 of 8w0kA
- binding flavin-adenine dinucleotide: D165 (= D123), A166 (≠ M124), V197 (= V151), Q199 (= Q153), R226 (= R179), V228 (= V181), K229 (= K182), G230 (= G183), A231 (≠ V184), Y232 (= Y185), W233 (≠ V186), F251 (≠ I191), T252 (≠ A192), R253 (≠ Y193), K254 (= K194), T257 (≠ K197), A280 (= A220), T281 (= T221), H282 (= H222), N283 (≠ D223), C307 (≠ M248), L308 (= L249), E351 (= E287)
- binding (1R)-1-hydroxyethane-1-sulfonic acid: K124 (= K89), A231 (≠ V184), Y332 (= Y270), Y344 (= Y280), R347 (= R283), R348 (= R284)
Sites not aligning to the query:
8uq1A Minimal puta proline dehydrogenase domain (design #2) complexed with (allylthio)acetic acid (see paper)
26% identity, 88% coverage: 23:290/303 of query aligns to 64:366/393 of 8uq1A
- binding flavin-adenine dinucleotide: D177 (= D123), A178 (≠ M124), V209 (= V151), Q211 (= Q153), R238 (= R179), V240 (= V181), K241 (= K182), G242 (= G183), A243 (≠ V184), Y244 (= Y185), W245 (≠ V186), F263 (≠ I191), T264 (≠ A192), R265 (≠ Y193), K266 (= K194), T269 (≠ K197), A292 (= A220), T293 (= T221), H294 (= H222), N295 (≠ D223), Q318 (= Q247), C319 (≠ M248), L320 (= L249), E363 (= E287)
- binding (Allylthio)acetic acid: K136 (= K89), D177 (= D123), A243 (≠ V184), Y244 (= Y185), L320 (= L249), Y344 (= Y270), Y356 (= Y280), R359 (= R283), R360 (= R284)
Sites not aligning to the query:
Query Sequence
>WP_035236837.1 NCBI__GCF_000745975.1:WP_035236837.1
MFHKIISQALPYFPPKLIWQFSKSYIAGTTTQDAINASKALNRENVMVTLDILGEFIKTM
SQAAKNRDDYLALIRTIEAAAINGNYSLKPSMFGLLIDKKTCFEYMRELTAEAASHGNFV
RIDMEDSPCVDDSIDIFRRLKQEFPRNIGLVLQAYLKRTSGDLESMLDLRRDDADLNFRL
VKGVYVEPAAIAYKAYKDINAHYLEDLEFMFKNNVYAAIATHDTPLIQGALDLIDQYQVP
KEKYEFQMLYGVTPKKRRELVQNGHRMRVYVPFGEQWFGYSTRRLKENPAMVRHILKALV
DKG
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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