SitesBLAST
Comparing WP_089214372.1 NCBI__GCF_900188185.1:WP_089214372.1 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)
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
54% identity, 94% coverage: 3:456/483 of query aligns to 17:473/486 of 3ju8A
- active site: N147 (= N131), K170 (= K154), E245 (= E229), C279 (= C263), E377 (= E360), P455 (= P438)
- binding nicotinamide-adenine-dinucleotide: G144 (= G128), Y146 (= Y130), N147 (= N131), L152 (= L136), K170 (= K154), S172 (= S156), F220 (= F204), T221 (= T205), G222 (= G206), S223 (= S207), T226 (= T210), E245 (= E229), M246 (= M230), G247 (= G231), C279 (= C263), E377 (= E360), F379 (= F362), F444 (= F427)
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
51% identity, 93% coverage: 7:456/483 of query aligns to 22:473/488 of 5u0mA
- active site: N148 (= N131), K171 (= K154), E246 (= E229), C280 (= C263), E377 (= E360), P455 (= P438)
- binding nicotinamide-adenine-dinucleotide: F144 (≠ L127), Y147 (= Y130), N148 (= N131), K171 (= K154), S173 (= S156), E174 (= E157), G207 (= G190), T222 (= T205), G223 (= G206), S224 (= S207), V227 (≠ T210), E246 (= E229), M247 (= M230), G248 (= G231), C280 (= C263), E377 (= E360), F379 (= F362)
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
51% identity, 93% coverage: 7:456/483 of query aligns to 22:473/488 of 5u0lA
- active site: N148 (= N131), K171 (= K154), E246 (= E229), C280 (= C263), E377 (= E360), P455 (= P438)
- binding decanal: K107 (= K89), H152 (= H135), L153 (= L136), G156 (= G139), H157 (= H140), S456 (= S439), A457 (= A440)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
33% identity, 83% coverage: 37:435/483 of query aligns to 557:956/983 of 3hazA
- active site: N652 (= N131), K675 (= K154), E752 (= E229), C786 (= C263), E878 (= E360)
- binding nicotinamide-adenine-dinucleotide: I648 (≠ L127), S649 (≠ G128), P650 (= P129), W651 (≠ Y130), N652 (= N131), I657 (≠ L136), K675 (= K154), P676 (= P155), A677 (≠ S156), G708 (≠ P187), G711 (= G190), A712 (≠ K191), T726 (= T205), G727 (= G206), S728 (= S207), V731 (≠ T210), I735 (≠ L214), E752 (= E229), T753 (≠ M230), C786 (= C263), E878 (= E360), F880 (= F362), F948 (= F427)
Sites not aligning to the query:
- active site: 960
- binding flavin-adenine dinucleotide: 272, 273, 306, 333, 335, 336, 337, 338, 339, 340, 358, 359, 360, 361, 364, 387, 388, 389, 390, 435, 460, 461
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
29% identity, 90% coverage: 2:437/483 of query aligns to 32:466/497 of P17202
- D96 (≠ E71) binding K(+)
- SPW 156:158 (≠ GPY 128:130) binding NAD(+)
- Y160 (≠ F132) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G139) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (= KPSE 154:157) binding NAD(+)
- L186 (≠ K158) binding K(+)
- SSAT 236:239 (≠ SART 207:210) binding NAD(+)
- V251 (≠ G223) binding in other chain
- L258 (≠ M230) binding NAD(+)
- W285 (≠ L257) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E360) binding NAD(+)
- A441 (≠ V411) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ A421) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F427) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (≠ G431) binding K(+)
Sites not aligning to the query:
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
28% identity, 88% coverage: 14:437/483 of query aligns to 44:471/498 of 4pxnA
- active site: N161 (= N131), K184 (= K154), E262 (= E229), C296 (= C263), E392 (= E360)
- binding nicotinamide-adenine-dinucleotide: I157 (≠ L127), T158 (≠ G128), A159 (≠ P129), F160 (≠ Y130), N161 (= N131), K184 (= K154), T221 (≠ P187), G224 (= G190), Q225 (≠ K191), F238 (= F204), T239 (= T205), G240 (= G206), S241 (= S207), A244 (≠ T210), V248 (≠ L214), E262 (= E229), L263 (≠ M230), S264 (≠ G231), C296 (= C263), E392 (= E360), F394 (= F362), F461 (= F427)
Sites not aligning to the query:
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
30% identity, 88% coverage: 23:446/483 of query aligns to 42:469/489 of 4o6rA
- active site: N150 (= N131), K173 (= K154), E248 (= E229), C282 (= C263), E383 (= E360), E460 (≠ P438)
- binding adenosine monophosphate: I146 (≠ L127), V147 (≠ G128), K173 (= K154), G206 (= G186), G210 (= G190), Q211 (≠ K191), F224 (= F204), G226 (= G206), S227 (= S207), T230 (= T210), R233 (= R216)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
29% identity, 90% coverage: 14:449/483 of query aligns to 37:470/490 of 5ekcE
- active site: N154 (= N131), K177 (= K154), E252 (= E229), C286 (= C263), E381 (= E360), E459 (≠ P438)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (≠ L127), T151 (≠ G128), P152 (= P129), W153 (≠ Y130), K177 (= K154), S180 (≠ E157), G210 (= G186), G214 (= G190), F228 (= F204), G230 (= G206), E231 (≠ S207), T234 (= T210), N331 (≠ D308), R333 (≠ E310), Q334 (≠ A311)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
29% identity, 90% coverage: 14:449/483 of query aligns to 30:463/482 of 5ek6A
- active site: N147 (= N131), K170 (= K154), E245 (= E229), C279 (= C263), E374 (= E360), E452 (≠ P438)
- binding 2-methylpropanal: I152 (≠ L136), K155 (≠ G139), T222 (= T205), E245 (= E229), F441 (= F427)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (≠ L127), T144 (≠ G128), W146 (≠ Y130), N147 (= N131), I152 (≠ L136), K170 (= K154), A172 (≠ S156), S173 (≠ E157), P202 (vs. gap), G203 (= G186), G207 (= G190), F221 (= F204), T222 (= T205), G223 (= G206), E224 (≠ S207), T227 (= T210), I231 (≠ F218), E245 (= E229), L246 (≠ M230), C279 (= C263), E374 (= E360)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
29% identity, 90% coverage: 14:449/483 of query aligns to 30:463/482 of 4h73A
- active site: N147 (= N131), K170 (= K154), E245 (= E229), C279 (= C263), E374 (= E360), E452 (≠ P438)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (≠ L127), T144 (≠ G128), P145 (= P129), W146 (≠ Y130), K170 (= K154), A172 (≠ S156), S173 (≠ E157), G203 (= G186), G207 (= G190), F221 (= F204), G223 (= G206), E224 (≠ S207), T227 (= T210)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
32% identity, 86% coverage: 21:435/483 of query aligns to 520:947/973 of 6bsnA
- active site: N643 (= N131), E743 (= E229), A777 (≠ C263)
- binding proline: M630 (≠ H118), W642 (≠ Y130), F644 (= F132), G718 (= G206), R776 (= R262), S778 (≠ T264), F871 (= F362), I930 (≠ N419), G931 (= G420), A932 (= A421), F939 (= F427)
Sites not aligning to the query:
- active site: 951
- binding dihydroflavine-adenine dinucleotide: 269, 270, 303, 330, 332, 333, 334, 335, 336, 337, 355, 356, 357, 358, 361, 384, 385, 386, 387, 432, 457, 458
- binding proline: 958, 959, 961
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
29% identity, 90% coverage: 2:437/483 of query aligns to 30:464/495 of 4v37A
- active site: N157 (= N131), K180 (= K154), E255 (= E229), A289 (≠ C263), E388 (= E360)
- binding 3-aminopropan-1-ol: C448 (≠ A421), W454 (≠ F427)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ L127), S154 (≠ G128), P155 (= P129), W156 (≠ Y130), N157 (= N131), M162 (≠ L136), K180 (= K154), S182 (= S156), E183 (= E157), G213 (= G186), G217 (= G190), A218 (≠ K191), T232 (= T205), G233 (= G206), S234 (= S207), T237 (= T210), E255 (= E229), L256 (≠ M230), A289 (≠ C263), E388 (= E360), F390 (= F362)
Sites not aligning to the query:
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
30% identity, 88% coverage: 23:445/483 of query aligns to 55:478/491 of 5gtlA
- active site: N165 (= N131), K188 (= K154), E263 (= E229), C297 (= C263), E394 (= E360), E471 (≠ P438)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (≠ L127), P163 (= P129), K188 (= K154), A190 (≠ S156), E191 (= E157), Q192 (≠ K158), G221 (= G186), G225 (= G190), G241 (= G206), S242 (= S207), T245 (= T210), L264 (≠ M230), C297 (= C263), E394 (= E360), F396 (= F362)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
30% identity, 88% coverage: 23:445/483 of query aligns to 55:478/491 of 5gtkA
- active site: N165 (= N131), K188 (= K154), E263 (= E229), C297 (= C263), E394 (= E360), E471 (≠ P438)
- binding nicotinamide-adenine-dinucleotide: I161 (≠ L127), I162 (≠ G128), P163 (= P129), W164 (≠ Y130), K188 (= K154), E191 (= E157), G221 (= G186), G225 (= G190), A226 (≠ K191), F239 (= F204), G241 (= G206), S242 (= S207), T245 (= T210), Y248 (≠ A213), L264 (≠ M230), C297 (= C263), Q344 (≠ A311), R347 (≠ G314), E394 (= E360), F396 (= F362)
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
29% identity, 89% coverage: 4:434/483 of query aligns to 19:451/475 of Q59931
- R103 (≠ S85) binding substrate
- S151 (≠ G128) binding NADP(+)
- K177 (= K154) binding NADP(+)
- T180 (≠ E157) binding NADP(+)
- D215 (≠ K191) binding NADP(+)
- 230:251 (vs. 206:230, 28% identical) binding NADP(+)
- E377 (≠ L361) binding NADP(+)
- R437 (≠ G420) binding substrate
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
30% identity, 94% coverage: 7:462/483 of query aligns to 30:491/494 of 4pz2B
- active site: N159 (= N131), K182 (= K154), E258 (= E229), C292 (= C263), E392 (= E360), D469 (≠ P438)
- binding nicotinamide-adenine-dinucleotide: I155 (≠ L127), I156 (≠ G128), P157 (= P129), W158 (≠ Y130), N159 (= N131), M164 (≠ L136), K182 (= K154), A184 (≠ S156), E185 (= E157), G215 (= G186), G219 (= G190), F233 (= F204), T234 (= T205), G235 (= G206), S236 (= S207), V239 (≠ T210), E258 (= E229), L259 (≠ M230), C292 (= C263), E392 (= E360), F394 (= F362)
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
29% identity, 89% coverage: 4:434/483 of query aligns to 18:450/474 of 2esdA
- active site: N153 (= N131), K176 (= K154), A249 (≠ E229), C283 (= C263), E376 (≠ L361)
- binding glyceraldehyde-3-phosphate: R102 (≠ S85), Y154 (≠ F132), R282 (= R262), C283 (= C263), T284 (= T264), Q435 (≠ N419), R436 (≠ G420)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ Y130), K176 (= K154), P178 (≠ S156), T179 (≠ E157), G209 (= G186), G213 (= G190), D214 (≠ K191), F227 (= F204), S230 (= S207), I233 (≠ T210), K328 (≠ E310), S329 (≠ A311), Y332 (≠ G314)
Sites not aligning to the query:
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
29% identity, 89% coverage: 7:434/483 of query aligns to 25:457/486 of 4pxlA
- active site: N154 (= N131), K177 (= K154), E253 (= E229), C287 (= C263), E384 (= E360)
- binding nicotinamide-adenine-dinucleotide: I150 (≠ L127), V151 (≠ G128), P152 (= P129), W153 (≠ Y130), K177 (= K154), E180 (= E157), G210 (= G186), G214 (= G190), A215 (≠ K191), F228 (= F204), G230 (= G206), S231 (= S207), V234 (≠ T210), E253 (= E229), G255 (= G231), C287 (= C263), Q334 (≠ A311), K337 (≠ G314), E384 (= E360), F386 (= F362)
Sites not aligning to the query:
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
27% identity, 90% coverage: 14:446/483 of query aligns to 30:472/483 of 4npiA
- active site: N152 (= N131), K175 (= K154), E251 (= E229), C285 (= C263), E387 (= E360), E464 (≠ P438)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (vs. gap), L157 (= L136), W160 (≠ G139), E251 (= E229), C285 (= C263), Y445 (≠ N419), R447 (≠ A421), F453 (= F427)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ L127), S149 (≠ G128), P150 (= P129), W151 (≠ Y130), K175 (= K154), E178 (= E157), G208 (= G186), G213 (= G190), E214 (≠ K191), F227 (= F204), G229 (= G206), E230 (≠ S207), T233 (= T210), G253 (= G231), C285 (= C263), K335 (≠ G314), E387 (= E360), F389 (= F362)
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
27% identity, 90% coverage: 14:446/483 of query aligns to 30:472/483 of 4i2rA
- active site: N152 (= N131), K175 (= K154), E251 (= E229), C285 (= C263), E387 (= E360), E464 (≠ P438)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (vs. gap), L157 (= L136), C285 (= C263), Y445 (≠ N419), R447 (≠ A421), F453 (= F427)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ L127), S149 (≠ G128), W151 (≠ Y130), N152 (= N131), K175 (= K154), E178 (= E157), G208 (= G186), F227 (= F204), T228 (= T205), G229 (= G206), E230 (≠ S207), T233 (= T210), E251 (= E229), L252 (≠ M230), G253 (= G231), C285 (= C263), E387 (= E360), F389 (= F362)
Query Sequence
>WP_089214372.1 NCBI__GCF_900188185.1:WP_089214372.1
MSEELISHEPATGAELWRGGISDVDAEVAAARQAWPGWAAKPLAYRAETLRRFADRVKAD
AESFADLIARETGKPLWEARTEVESVAAKVDISVKAYAERTPNRRIEGAMGLRHAVRHKP
HGALAVLGPYNFPAHLPNGHIVPALLAGNSVIFKPSEKTPAVGAKLAQLFHSAGVPEEVL
RLVIGGPDQGKALAGHDGIDGLLFTGSARTGVALNRQFADRPGKILALEMGGNNPIVVWD
TPDIRTAAMLVVQSAFLSAGQRCTNARRLIVRQTVAEALIDEVRNLTNRLIVDHPHADPA
PYMGPVIDNEAADGLTESFLILMSNGGQVIRHMTRPIADRPFLTPGIIDVTAMPERPDIE
LFGPLLQLVRVDSFEAAIAEANNTAFGLSAALIGGTPQLYDQFWANARAGVINWNRPTNG
ASSAAPFGGIGLSGNHRPSAFYAADYCAYPVASSESDALRASIGVGLRESDHDAPKLVRK
GFL
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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