SitesBLAST
Comparing AZOBR_RS32475 AZOBR_RS32475 aldehyde Dehydrogenase 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)
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
38% identity, 95% coverage: 17:467/475 of query aligns to 2:449/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P123), I107 (≠ S124), H133 (≠ S150), P134 (= P151), T185 (= T203), G186 (= G204), G187 (≠ S205), R190 (≠ N208), V204 (= V222), C238 (= C256), E328 (= E346), L407 (≠ M426)
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
38% identity, 95% coverage: 17:467/475 of query aligns to 2:449/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (= K83), P106 (= P123), T108 (= T125), N109 (= N126), A131 (= A148), P132 (= P149), H133 (≠ S150), P134 (= P151), R169 (≠ K187), G189 (≠ D207), R190 (≠ N208), I237 (≠ S255), C238 (= C256), S239 (= S257), T391 (= T409), G394 (= G413), T405 (≠ L424), L407 (≠ M426)
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
38% identity, 95% coverage: 17:467/475 of query aligns to 2:449/449 of 8cejA
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
38% identity, 91% coverage: 24:457/475 of query aligns to 20:453/455 of 5j7iC
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
38% identity, 91% coverage: 24:457/475 of query aligns to 21:454/456 of 5j7iB
7bvpA Adhe spirosome in extended conformation (see paper)
38% identity, 90% coverage: 20:447/475 of query aligns to 11:440/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P123), T113 (≠ S124), H139 (≠ S150), G194 (= G204), G195 (≠ S205), M198 (≠ N208), V212 (= V222), G213 (= G223), A214 (= A224), C246 (= C256), E335 (= E346), L337 (= L348), H367 (= H378), T418 (≠ S425), L419 (≠ M426)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 487, 489, 519, 547, 550, 597, 598, 601, 610, 619, 646, 737
- binding zinc ion: 653, 657, 723, 737
6tqmA Escherichia coli adhe structure in its compact conformation (see paper)
38% identity, 90% coverage: 20:447/475 of query aligns to 11:440/869 of 6tqmA
Sites not aligning to the query:
- binding fe (iii) ion: 653, 657, 723, 737
- 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: 487, 490, 545, 547, 550, 597, 603, 608, 646, 727
P0A9Q7 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli (strain K12) (see 8 papers)
38% identity, 90% coverage: 20:447/475 of query aligns to 11:440/891 of P0A9Q7
- IVPTTN 110:115 (≠ VTPSTN 121:126) binding
- G195 (≠ S205) binding
- G213 (= G223) binding
- A267 (≠ E277) mutation to T: Shows aerobic growth ability on ethanol. Shows 5-6 fold increase in acetaldehyde dehydrogenase activity, but does not affect ethanol dehydrogenase activity. Shows decreased thermal enzyme stability and increased sensitivity to MCO damage. Shows increased protein stability and resistance to MCO; when associated with K-568.
- E335 (= E346) binding
- K358 (= K369) modified: N6-acetyllysine
- L419 (≠ M426) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 446:449 mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.
- 487 binding
- 519 binding
- 546:550 binding
- 568 E→K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- 610 binding
- 619 binding
- 653 binding
- 657 binding
- 670 mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- 723 binding
- 737 binding
P0A9Q8 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli O157:H7 (see paper)
38% identity, 90% coverage: 20:447/475 of query aligns to 11:440/891 of P0A9Q8
Sites not aligning to the query:
- 487 binding
- 519 binding
- 546:550 binding
- 597:598 binding
- 638 binding
- 653 binding
- 657 binding
- 723 binding
- 737 binding
Q9XDN1 Propanal dehydrogenase (CoA-propanoylating); Coenzyme-A-acylating propionaldehyde dehydrogenase; Propanediol utilization protein PduP; EC 1.2.1.87 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
29% identity, 78% coverage: 60:429/475 of query aligns to 77:440/464 of Q9XDN1
Sites not aligning to the query:
- 1:10 mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:14 mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:18 Targets protein to the BMC
- 2:18 mutation Missing: No longer interacts with PduA.
- 7 E→A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- 10 I→A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- 14 L→A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
4c3sA Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
29% identity, 84% coverage: 25:425/475 of query aligns to 15:407/435 of 4c3sA
- active site: T110 (= T125), A208 (≠ V222), C242 (= C256)
- binding nicotinamide-adenine-dinucleotide: I106 (≠ V121), T107 (= T122), P108 (= P123), C109 (≠ S124), H135 (≠ S150), L171 (≠ K187), T189 (= T203), G190 (= G204), G191 (≠ S205), V194 (≠ N208), A208 (≠ V222), G209 (= G223), C242 (= C256), E330 (≠ K347), M332 (≠ S349), H360 (= H378), T405 (= T423), I406 (≠ L424)
5jfmB Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
30% identity, 77% coverage: 60:425/475 of query aligns to 64:424/452 of 5jfmB
- active site: T126 (= T125), A224 (≠ V222), C258 (= C256)
- binding coenzyme a: I122 (≠ V121), P124 (= P123), T125 (≠ S124), T126 (= T125), N127 (= N126), P150 (= P149), H151 (≠ S150), S186 (≠ I185), I187 (≠ T186), T190 (= T190), T205 (= T203), G206 (= G204), G207 (≠ S205), T308 (≠ R304)
5jflA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound NAD+ (see paper)
30% identity, 77% coverage: 60:425/475 of query aligns to 52:412/440 of 5jflA
- active site: T114 (= T125), A212 (≠ V222), C246 (= C256)
- binding nicotinamide-adenine-dinucleotide: I110 (≠ V121), T111 (= T122), P112 (= P123), T113 (≠ S124), T114 (= T125), H139 (≠ S150), I175 (≠ T186), T193 (= T203), G194 (= G204), I198 (≠ N208), A212 (≠ V222), G213 (= G223), A214 (= A224), C246 (= C256), E335 (≠ K347), H365 (= H378), F409 (= F422), T410 (= T423), I411 (≠ L424)
5jfmA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
30% identity, 77% coverage: 60:425/475 of query aligns to 51:411/439 of 5jfmA
- active site: T113 (= T125), A211 (≠ V222), C245 (= C256)
- binding propionyl Coenzyme A: I109 (≠ V121), T110 (= T122), T113 (= T125), N114 (= N126), S136 (≠ A148), P137 (= P149), H138 (≠ S150), I174 (≠ T186), T192 (= T203), G193 (= G204), G194 (≠ S205), P244 (≠ S255), C245 (= C256)
6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
30% identity, 77% coverage: 60:425/475 of query aligns to 53:413/441 of 6gvsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (= P123), T114 (≠ S124), H140 (≠ S150), R176 (≠ K187), T194 (= T203), G195 (= G204), G196 (≠ S205), L199 (≠ N208), A213 (≠ V222), G214 (= G223), A215 (= A224), C247 (= C256), E336 (≠ K347), H366 (= H378), I412 (≠ L424)
5dbvA Structure of a c269a mutant of propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
29% identity, 84% coverage: 25:425/475 of query aligns to 14:403/431 of 5dbvA
- active site: T109 (= T125), G208 (= G223), A241 (≠ C256)
- binding coenzyme a: I105 (≠ V121), C108 (≠ S124), N132 (≠ A148), P133 (= P149), H134 (≠ S150), G189 (= G204), G190 (≠ S205), V193 (≠ N208), A241 (≠ C256), K245 (≠ N260), R290 (= R304), E326 (≠ K347), M328 (≠ S349)
3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
25% identity, 85% coverage: 4:405/475 of query aligns to 30:433/480 of 3rhhD
- active site: N155 (≠ T125), K178 (≠ A148), E251 (≠ V222), C285 (= C256), E378 (≠ H341)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (≠ V121), P153 (= P123), F154 (≠ S124), K178 (≠ A148), P179 (= P149), A180 (≠ S150), T181 (≠ P151), G211 (≠ T186), G215 (≠ T190), D216 (≠ Q191), F229 (≠ V202), G231 (= G204), G232 (≠ S205), T235 (≠ N208)
Sites not aligning to the query:
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
27% identity, 33% coverage: 113:268/475 of query aligns to 145:302/492 of 7w5nA
Sites not aligning to the query:
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
29% identity, 37% coverage: 106:283/475 of query aligns to 137:315/481 of 3jz4A
- active site: N156 (≠ T125), K179 (≠ A148), E254 (vs. gap), C288 (= C256)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P123), W155 (≠ S124), K179 (≠ A148), A181 (≠ S150), S182 (≠ P151), A212 (vs. gap), G216 (≠ T186), G232 (= G204), S233 (= S205), I236 (≠ N208), C288 (= C256)
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, 37% coverage: 106:283/475 of query aligns to 138:316/482 of P25526
Sites not aligning to the query:
Query Sequence
>AZOBR_RS32475 AZOBR_RS32475 aldehyde Dehydrogenase
MDNIMLDRTPASADQEAIAALVARARTAQRAFADATQERVDDAVAALAWAIYEPGRARAL
AELAVADTGLGNVADKIVKNQRKTFGTLRDLMRVRTVGVIEEDTAKGIVKIAKPLGVVGA
VTPSTNPAATPVNKAMMAVKGRNAIIIAPSPMGSAATGRTVELMRAELARIGAPEDLVQM
IPTPITKGLTQALMEAVDLVVVTGSQDNVRRAYSSGTPAIGVGAGNVPVIVDESADLAEA
ARKIGASKTFDNSTSCSSENALVVLDSVYDATIAALEEAGAHLCTPEERERVQSRLWENG
KLNRKLIAKDPAILAEAFELAPKAREARFFLVEETGVGKAHPFSGEKLSLVLAVYRVPDF
DAAVDQVRKILDHQGRGHSCGIHTRDEAHAKRLADELDVVRVLVNFAHTFGNGGGFDSGL
NFTLSMGCGSWQKNSISENLSWKHFVNITHLVRPIPEDKPSEEALFGPFWSRHGR
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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