SitesBLAST
Comparing HSERO_RS00735 FitnessBrowser__HerbieS:HSERO_RS00735 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
44% identity, 95% coverage: 20:522/529 of query aligns to 2:502/504 of 1eyyA
Q84LK3 Betaine aldehyde dehydrogenase 2; OsBADH2; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
27% identity, 62% coverage: 126:452/529 of query aligns to 120:448/503 of Q84LK3
- N162 (= N162) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2-fold for Bet-ald and 8-fold for GAB-ald).
- W170 (≠ G172) mutation to A: Slightly reduced affinity for NAD, 4-fold enhanced affinity for betaine aldehyde (Bet-ald), but 2-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and reduced catalytic efficiency (2.5-fold for Bet-ald and 6-fold for GAB-ald).; mutation to F: Slightly reduced affinity for NAD, 5-fold enhanced affinity for betaine aldehyde (Bet-ald), but 3-fold reduction in gamma-4-aminobutyraldehyde (GAB-ald) affinity and 1.5-fold increase in catalytic efficiency towards gamma-aminobutyraldehyde (GAB-ald).
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
26% identity, 79% coverage: 10:425/529 of query aligns to 8:413/477 of 2opxA
- active site: N151 (= N162), K174 (= K187), E249 (= E266), C283 (= C303), E381 (= E393)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ R108), F152 (= F163), N284 (≠ T304), F312 (vs. gap), G313 (vs. gap), R318 (vs. gap), D320 (vs. gap), I321 (vs. gap), A322 (vs. gap), Y362 (≠ L375)
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
29% identity, 56% coverage: 45:340/529 of query aligns to 48:324/481 of 3jz4A
- active site: N156 (= N162), K179 (= K187), E254 (= E266), C288 (= C303)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A160), W155 (≠ S161), K179 (= K187), A181 (≠ H189), S182 (= S190), A212 (vs. gap), G216 (= G226), G232 (= G242), S233 (= S243), I236 (≠ G246), C288 (= C303)
Sites not aligning to the query:
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
26% identity, 79% coverage: 10:425/529 of query aligns to 8:413/477 of 2impA
- active site: N151 (= N162), K174 (= K187), E249 (= E266), C283 (= C303), E381 (= E393)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (≠ F158), L148 (≠ G159), P149 (≠ A160), W150 (≠ S161), K174 (= K187), E177 (= E197), F178 (≠ L198), G207 (= G222), G211 (= G226), Q212 (≠ A227), S228 (= S243), A231 (≠ G246), K234 (≠ A249), R334 (≠ H344)
Sites not aligning to the query:
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
26% identity, 79% coverage: 10:425/529 of query aligns to 8:413/477 of 2iluA
- active site: N151 (= N162), K174 (= K187), E249 (= E266), C283 (= C303), E381 (= E393)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (≠ F158), L148 (≠ G159), P149 (≠ A160), W150 (≠ S161), K174 (= K187), S176 (= S196), E177 (= E197), R206 (vs. gap), G207 (= G222), G211 (= G226), Q212 (≠ A227), S228 (= S243), A231 (≠ G246), K234 (≠ A249), I235 (≠ L250), N328 (= N338), R334 (≠ H344), F383 (= F395)
Sites not aligning to the query:
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
29% identity, 56% coverage: 45:340/529 of query aligns to 49:325/482 of P25526
Sites not aligning to the query:
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
26% identity, 79% coverage: 10:425/529 of query aligns to 10:415/479 of P25553
- L150 (≠ G159) binding
- R161 (≠ G172) binding
- K-------PSE 176:179 (≠ KAHSGHLVTSE 187:197) binding
- F180 (≠ L198) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ A227) binding
- S230 (= S243) binding
- E251 (= E266) binding
- N286 (≠ T304) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ H344) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 443 binding
- 449 binding
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
22% identity, 77% coverage: 23:427/529 of query aligns to 25:425/487 of Q9H2A2
- R109 (= R108) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N162) mutation to A: Complete loss of activity.
Sites not aligning to the query:
- 451 R→A: Complete loss of activity.
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
30% identity, 39% coverage: 49:255/529 of query aligns to 47:243/485 of 4u3wA
Sites not aligning to the query:
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
27% identity, 53% coverage: 151:431/529 of query aligns to 641:918/983 of 3hazA
- active site: N652 (= N162), K675 (= K187), E752 (= E266), C786 (= C303), E878 (= E393)
- binding nicotinamide-adenine-dinucleotide: I648 (≠ F158), S649 (≠ G159), P650 (≠ A160), W651 (≠ S161), N652 (= N162), I657 (≠ F167), K675 (= K187), P676 (vs. gap), A677 (= A188), G708 (vs. gap), G711 (= G226), A712 (= A227), T726 (= T241), G727 (= G242), S728 (= S243), V731 (≠ G246), I735 (≠ L250), E752 (= E266), T753 (≠ M267), C786 (= C303), E878 (= E393), F880 (= F395)
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
- binding nicotinamide-adenine-dinucleotide: 948
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
25% identity, 73% coverage: 27:411/529 of query aligns to 16:403/489 of 6wsbA
- active site: N152 (= N162), E250 (= E266), C284 (= C303)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F158), G149 (= G159), A150 (= A160), W151 (≠ S161), N152 (= N162), K175 (= K187), E178 (≠ S190), G208 (vs. gap), G211 (= G226), A212 (= A227), F225 (= F240), T226 (= T241), G227 (= G242), G228 (≠ S243), T231 (≠ G246), V235 (≠ L250), E250 (= E266), L251 (≠ M267), G252 (≠ S268), C284 (= C303), E385 (= E393), F387 (= F395)
Sites not aligning to the query:
5kj5B Crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase n169d in complex with NAD+ (see paper)
24% identity, 79% coverage: 9:426/529 of query aligns to 6:421/484 of 5kj5B
- active site: D153 (≠ N162), K176 (= K187), E252 (= E266), C286 (= C303), E388 (= E393)
- binding nicotinamide-adenine-dinucleotide: I149 (≠ F158), S150 (≠ G159), P151 (≠ A160), W152 (≠ S161), D153 (≠ N162), L158 (≠ F167), K176 (= K187), G209 (vs. gap), K210 (vs. gap), G214 (= G226), F228 (= F240), T229 (= T241), G230 (= G242), E231 (≠ S243), T234 (≠ G246), E252 (= E266), L253 (≠ M267), C286 (= C303), E388 (= E393), F390 (= F395)
Sites not aligning to the query:
5kllA Crystal structure of 2-hydroxymuconate-6-semialdehyde derived tautomeric intermediate in 2-aminomuconate 6-semialdehyde dehydrogenase n169d (see paper)
24% identity, 79% coverage: 9:426/529 of query aligns to 5:420/483 of 5kllA
- active site: D152 (≠ N162), K175 (= K187), E251 (= E266), C285 (= C303), E387 (= E393)
- binding (3~{E},5~{E})-6-oxidanyl-2-oxidanylidene-hexa-3,5-dienoic acid: R103 (= R108), D152 (≠ N162), L157 (≠ F167), W160 (≠ G172), C285 (= C303)
Sites not aligning to the query:
P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Homo sapiens (Human) (see paper)
23% identity, 71% coverage: 39:416/529 of query aligns to 4:357/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
24% identity, 70% coverage: 45:414/529 of query aligns to 42:404/489 of 4o6rA
- active site: N150 (= N162), K173 (= K187), E248 (= E266), C282 (= C303), E383 (= E393)
- binding adenosine monophosphate: I146 (≠ F158), V147 (≠ G159), K173 (= K187), G206 (= G222), G210 (= G226), Q211 (≠ A227), F224 (= F240), G226 (= G242), S227 (= S243), T230 (≠ G246), R233 (≠ A249)
Sites not aligning to the query:
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 32% coverage: 162:330/529 of query aligns to 147:305/476 of 4yweA
Sites not aligning to the query:
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
27% identity, 53% coverage: 151:431/529 of query aligns to 632:909/973 of 6bsnA
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: 630, 930, 931, 932, 939, 958, 959, 961
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
27% identity, 51% coverage: 42:310/529 of query aligns to 53:305/505 of 4neaA
- active site: N166 (= N162), K189 (= K187), E264 (= E266), C298 (= C303)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A160), K189 (= K187), E192 (≠ S190), G222 (= G222), G226 (= G226), G242 (= G242), G243 (≠ S243), T246 (≠ G246), H249 (≠ A249), I250 (≠ L250), C298 (= C303)
Sites not aligning to the query:
6mvtA Structure of a bacterial aldh16 complexed with nadh (see paper)
26% identity, 62% coverage: 126:453/529 of query aligns to 127:429/751 of 6mvtA
- active site: N151 (= N162), E247 (= E266), C281 (= C303)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (= V155), I148 (≠ A156), K174 (= K187), E177 (≠ S190), G207 (≠ R224), G210 (≠ A227), E211 (≠ Q228), F223 (= F240), S226 (= S243), V229 (≠ G246), D327 (≠ N346), R331 (≠ Q354)
Sites not aligning to the query:
Query Sequence
>HSERO_RS00735 FitnessBrowser__HerbieS:HSERO_RS00735
VSFNILGHNYIGGQRSGQGDVALHSVDATTGALFETPFLTATDKEVAAAVHAAEQAYPLY
RATTSEQRAQFLEAIADEIDALGDDFLAAVARETALPATPRLAGERARTSGQMRLFAKVV
RRGDFYGARIDTALPQRQPLPRPDIRQYKIGVGPVAVFGASNFPLAFSVAGGDTAAALAA
GCPVVFKAHSGHLVTSELVADAIERAVKKTGMPAGTFNMIYGDRVGAQLVKSAGIQAVGF
TGSLRGGRALCDMAAARPQPIPVFAEMSSINPIILMPEALKLRGDAIAKDLAGSVTVGVG
QLCTSPGLLLGVRSPELTSFIEKLSAAFGGTNPATMLNSGGLTHYNGGVARLTQLPGVKV
IATGGTSYTQAVPHLFKADAALLFSKEAPLEEEVFGPSTVIVELESREQLLDFAAKMNGQ
LTATLQAEIGDLQGNQDLIAILEQKAGRLLLNGFPTGVEVCDAMVHGGPYPATSDARGTS
VGSLAIERFLRPVCYQNYPDAMLPAALQNANPLGLMRLVDGEQTRATVG
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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