SitesBLAST
Comparing PP_3602 FitnessBrowser__Putida:PP_3602 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
44% identity, 94% coverage: 26:520/526 of query aligns to 9:502/504 of 1eyyA
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
25% identity, 73% coverage: 22:407/526 of query aligns to 24:403/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 157:160) binding
- K162 (≠ D171) active site, Charge relay system
- KPSE 176:179 (≠ KAHS 185:188) binding
- G209 (= G222) binding
- GTST 230:233 (≠ SLKG 241:244) binding
- E252 (= E264) active site, Proton acceptor
- C286 (= C301) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E391) binding
Sites not aligning to the query:
- 464 active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
25% identity, 73% coverage: 22:407/526 of query aligns to 23:402/489 of 4cazA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E386 (= E391)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (≠ F156), G149 (= G157), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G222), G212 (= G224), F226 (= F238), T227 (= T239), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248), E251 (= E264), L252 (≠ M265), C285 (= C301), E386 (= E391), F388 (= F393)
Sites not aligning to the query:
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
25% identity, 73% coverage: 22:407/526 of query aligns to 23:402/489 of 2woxA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E386 (= E391)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F156), G149 (= G157), W151 (≠ S159), N152 (= N160), K175 (= K185), S177 (≠ H187), E178 (≠ S188), G208 (= G222), G212 (= G224), F226 (= F238), T227 (= T239), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248), E251 (= E264), L252 (≠ M265), C285 (= C301), E386 (= E391), F388 (= F393)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
25% identity, 73% coverage: 22:407/526 of query aligns to 23:402/489 of 2wmeA
- active site: N152 (= N160), K175 (= K185), E251 (= E264), C285 (= C301), E386 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G157), W151 (≠ S159), K175 (= K185), S177 (≠ H187), E178 (≠ S188), G208 (= G222), G212 (= G224), F226 (= F238), G228 (= G240), G229 (≠ S241), T232 (≠ G244), V236 (≠ L248)
Sites not aligning to the query:
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
30% identity, 57% coverage: 4:302/526 of query aligns to 1:280/486 of 3ju8A
- active site: N147 (= N160), K170 (= K185), E245 (= E264), C279 (= C301)
- binding nicotinamide-adenine-dinucleotide: G144 (= G157), Y146 (≠ S159), N147 (= N160), L152 (≠ F165), K170 (= K185), S172 (≠ H187), F220 (= F238), T221 (= T239), G222 (= G240), S223 (= S241), T226 (≠ G244), E245 (= E264), M246 (= M265), G247 (≠ S266), C279 (= C301)
Sites not aligning to the query:
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)
27% identity, 58% coverage: 7:312/526 of query aligns to 6:295/475 of Q59931
- R103 (= R106) binding
- S151 (≠ G157) binding
- K177 (= K185) binding
- T180 (≠ S188) binding
- D215 (≠ E225) binding
- 230:251 (vs. 240:265, 31% identical) binding
Sites not aligning to the query:
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
26% identity, 76% coverage: 9:407/526 of query aligns to 9:401/489 of 6wsbA
- active site: N152 (= N160), E250 (= E264), C284 (= C301)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F156), G149 (= G157), A150 (= A158), W151 (≠ S159), N152 (= N160), K175 (= K185), E178 (≠ S188), G208 (= G221), G211 (= G224), A212 (≠ E225), F225 (= F238), T226 (= T239), G227 (= G240), G228 (≠ S241), T231 (≠ G244), V235 (≠ L248), E250 (= E264), L251 (≠ M265), G252 (≠ S266), C284 (= C301), E385 (= E391), F387 (= F393)
Sites not aligning to the query:
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
27% identity, 58% coverage: 7:312/526 of query aligns to 5:294/474 of 2esdA
- active site: N153 (= N160), K176 (= K185), A249 (≠ E264), C283 (= C301)
- binding glyceraldehyde-3-phosphate: R102 (= R106), Y154 (≠ F161), R282 (≠ F300), C283 (= C301), T284 (= T302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (≠ S159), K176 (= K185), P178 (≠ H187), T179 (≠ S188), G209 (= G222), G213 (= G224), D214 (≠ E225), F227 (= F238), S230 (= S241), I233 (≠ G244)
Sites not aligning to the query:
1qi1B Ternary complex of an NADP dependent aldehyde dehydrogenase (see paper)
28% identity, 52% coverage: 7:277/526 of query aligns to 5:262/474 of 1qi1B
- active site: N153 (= N160), K176 (= K185), E249 (= E264)
- binding sn-glycerol-3-phosphate: Y154 (≠ F161)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P151 (≠ A158), F152 (≠ S159), N153 (= N160), L158 (≠ T167), K176 (= K185), P178 (≠ H187), T179 (≠ S188), G209 (= G222), G213 (= G224), G229 (= G240), S230 (= S241), I233 (≠ G244), E249 (= E264), L250 (≠ M265)
Sites not aligning to the query:
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
30% identity, 48% coverage: 3:254/526 of query aligns to 2:244/485 of 4u3wA
Sites not aligning to the query:
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
26% identity, 71% coverage: 36:407/526 of query aligns to 34:394/480 of 3rhhD
- active site: N155 (= N160), K178 (= K185), E251 (= E264), C285 (= C301), E378 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ F156), P153 (≠ A158), F154 (≠ S159), K178 (= K185), P179 (≠ A186), A180 (≠ H187), T181 (≠ S188), G211 (= G222), G215 (= G224), D216 (≠ E225), F229 (= F238), G231 (= G240), G232 (≠ S241), T235 (≠ G244)
Sites not aligning to the query:
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
26% identity, 76% coverage: 9:408/526 of query aligns to 20:411/491 of 5gtlA
- active site: N165 (= N160), K188 (= K185), E263 (= E264), C297 (= C301), E394 (= E391)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (vs. gap), P163 (vs. gap), K188 (= K185), A190 (≠ S188), E191 (≠ G189), Q192 (≠ H190), G221 (= G220), G225 (= G224), G241 (= G240), S242 (= S241), T245 (≠ G244), L264 (≠ M265), C297 (= C301), E394 (= E391), F396 (= F393)
Sites not aligning to the query:
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
26% identity, 76% coverage: 9:408/526 of query aligns to 20:411/491 of 5gtkA
- active site: N165 (= N160), K188 (= K185), E263 (= E264), C297 (= C301), E394 (= E391)
- binding nicotinamide-adenine-dinucleotide: I161 (vs. gap), I162 (vs. gap), P163 (vs. gap), W164 (≠ S159), K188 (= K185), E191 (≠ G189), G221 (= G220), G225 (= G224), A226 (≠ E225), F239 (= F238), G241 (= G240), S242 (= S241), T245 (≠ G244), Y248 (≠ A247), L264 (≠ M265), C297 (= C301), Q344 (≠ G355), R347 (≠ H358), E394 (= E391), F396 (= F393)
Sites not aligning to the query:
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
26% identity, 81% coverage: 9:432/526 of query aligns to 6:423/474 of P77674
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
27% identity, 61% coverage: 4:322/526 of query aligns to 1:301/476 of 4f3xA
- active site: N150 (= N160), K173 (= K185), E247 (= E264), C281 (= C301)
- binding nicotinamide-adenine-dinucleotide: I146 (≠ F156), A147 (≠ G157), P148 (≠ A158), W149 (≠ S159), K173 (= K185), E176 (≠ S188), G205 (= G222), G209 (= G224), I213 (≠ V228), I223 (≠ F238), G225 (= G240), D226 (≠ S241), T229 (≠ G244), G249 (≠ S266), C281 (= C301)
Sites not aligning to the query:
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
26% identity, 81% coverage: 9:432/526 of query aligns to 6:423/474 of 1wndA
Sites not aligning to the query:
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
26% identity, 81% coverage: 9:432/526 of query aligns to 6:423/474 of 1wnbB
- active site: N149 (= N160), K172 (= K185), E246 (= E264), C280 (= C301), E378 (= E391)
- binding betaine aldehyde: D279 (≠ F300)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ F156), A146 (≠ G157), W148 (≠ S159), K172 (= K185), G204 (= G222), G208 (= G224), D209 (≠ E225), T223 (= T239), G224 (= G240), S225 (= S241), T228 (≠ G244), H231 (≠ A247), G248 (≠ S266), E378 (= E391)
Sites not aligning to the query:
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
26% identity, 81% coverage: 9:432/526 of query aligns to 6:423/474 of 1wnbA
- active site: N149 (= N160), K172 (= K185), E246 (= E264), C280 (= C301), E378 (= E391)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (≠ F156), A146 (≠ G157), W148 (≠ S159), K172 (= K185), G204 (= G222), G208 (= G224), D209 (≠ E225), G224 (= G240), S225 (= S241), T228 (≠ G244), H231 (≠ A247), G248 (≠ S266), F380 (= F393)
Sites not aligning to the query:
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
24% identity, 76% coverage: 9:406/526 of query aligns to 425:819/902 of P28037
- IPW 571:573 (≠ GAS 157:159) binding
- KPAQ 597:600 (≠ KAHS 185:188) binding
- GSLVGQ 630:635 (≠ G--VGE 222:225) binding
- GS 650:651 (= GS 240:241) binding
- E673 (= E264) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (≠ EM 264:265) binding
- C707 (= C301) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (vs. gap) binding
- ESF 804:806 (≠ EVF 391:393) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
Query Sequence
>PP_3602 FitnessBrowser__Putida:PP_3602
MPEILGHNFIAGQRSAAGPQRLQSLDASTGEALPYSFAQATEAEVDKAAKAAAAAFADFR
QLAPARRAEFLDAIAAELDELDDAFVAIVCRETALPAARIQGERGRTSGQMRLFAQVLRR
GDFLGARIDLALPERQPLPRVDLRQMRIGVGPVAVFGASNFPLAFSTAGGDTAAALAAGC
PVVFKAHSGHMATADLVACAIVRAAERTGMPKGVFNMVFGGGVGEWLVKHPAIQAVGFTG
SLKGGDALCRMAAERPQPIPVFAEMSSINPVIILPGALAKRGEAIARELAGSVCMGAGQF
CTNPGLVIGLQSPQYSQLLADLGQYLDQQAGQTMLNAGGLHSYVGGLEHLHAHAGIEHVA
GQVQEGNQARAQLFKADARLLVESDPLLQEEVFGPTTVAVEVQDNDQLRDALLGLRGQLT
ATLIGEAEDFDAFAWLVPLLEEKVGRILVNGYPTGVEVCDAMVHGGPYPATSDARGTSVG
TLAIDRFLRPVCYQNYPQTLLPEALRDGNPLGLRRLVNGQWSDGAI
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