SitesBLAST
Comparing WP_089214372.1 NCBI__GCF_900188185.1:WP_089214372.1 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)
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