SitesBLAST
Comparing WP_012967296.1 NCBI__GCF_000025465.1:WP_012967296.1 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)
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)
86% identity, 100% coverage: 1:461/461 of query aligns to 1:464/464 of Q9XDN1
- 1:10 (vs. 1:10, 90% identical) mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:14 (vs. 1:14, 93% identical) mutation Missing: Much less protein associates with BMCs, no effect on enzyme activity.
- 1:18 (vs. 1:18, 89% identical) Targets protein to the BMC
- 2:18 (vs. 2:18, 88% identical) mutation Missing: No longer interacts with PduA.
- E7 (= E7) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- I10 (= I10) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
- L14 (= L14) mutation to A: Substantially decreased protein levels in BMCs, no change in enzyme activity.
5jfmB Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
50% identity, 94% coverage: 28:461/461 of query aligns to 16:452/452 of 5jfmB
- active site: T126 (= T136), A224 (= A234), C258 (= C268)
- binding coenzyme a: I122 (≠ V132), P124 (= P134), T125 (≠ S135), T126 (= T136), N127 (= N137), P150 (= P160), H151 (= H161), S186 (≠ T196), I187 (≠ F197), T190 (= T200), T205 (= T215), G206 (= G216), G207 (= G217), T308 (≠ K316)
5jfmA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
50% identity, 94% coverage: 28:461/461 of query aligns to 3:439/439 of 5jfmA
- active site: T113 (= T136), A211 (= A234), C245 (= C268)
- binding propionyl Coenzyme A: I109 (≠ V132), T110 (≠ A133), T113 (= T136), N114 (= N137), S136 (= S159), P137 (= P160), H138 (= H161), I174 (≠ F197), T192 (= T215), G193 (= G216), G194 (= G217), P244 (= P267), C245 (= C268)
5jflA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound NAD+ (see paper)
50% identity, 94% coverage: 28:461/461 of query aligns to 4:440/440 of 5jflA
- active site: T114 (= T136), A212 (= A234), C246 (= C268)
- binding nicotinamide-adenine-dinucleotide: I110 (≠ V132), T111 (≠ A133), P112 (= P134), T113 (≠ S135), T114 (= T136), H139 (= H161), I175 (≠ F197), T193 (= T215), G194 (= G216), I198 (= I220), A212 (= A234), G213 (= G235), A214 (= A236), C246 (= C268), E335 (= E356), H365 (= H386), F409 (= F430), T410 (= T431), I411 (= I432)
6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+ (see paper)
49% identity, 94% coverage: 28:461/461 of query aligns to 5:441/441 of 6gvsA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P113 (= P134), T114 (≠ S135), H140 (= H161), R176 (≠ F197), T194 (= T215), G195 (= G216), G196 (= G217), L199 (≠ I220), A213 (= A234), G214 (= G235), A215 (= A236), C247 (= C268), E336 (= E356), H366 (= H386), I412 (= I432)
4c3sA Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
46% identity, 94% coverage: 29:461/461 of query aligns to 3:435/435 of 4c3sA
- active site: T110 (= T136), A208 (= A234), C242 (= C268)
- binding nicotinamide-adenine-dinucleotide: I106 (≠ V132), T107 (≠ A133), P108 (= P134), C109 (≠ S135), H135 (= H161), L171 (≠ F197), T189 (= T215), G190 (= G216), G191 (= G217), V194 (≠ I220), A208 (= A234), G209 (= G235), C242 (= C268), E330 (= E356), M332 (≠ L358), H360 (= H386), T405 (= T431), I406 (= I432)
5dbvA Structure of a c269a mutant of propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
45% identity, 94% coverage: 29:461/461 of query aligns to 2:431/431 of 5dbvA
- active site: T109 (= T136), G208 (= G235), A241 (≠ C268)
- binding coenzyme a: I105 (≠ V132), C108 (≠ S135), N132 (≠ S159), P133 (= P160), H134 (= H161), G189 (= G216), G190 (= G217), V193 (≠ I220), A241 (≠ C268), K245 (= K272), R290 (≠ K316), E326 (= E356), M328 (≠ L358)
5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
32% identity, 79% coverage: 59:421/461 of query aligns to 39:408/455 of 5j7iC
5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
32% identity, 79% coverage: 59:421/461 of query aligns to 40:409/456 of 5j7iB
8uhwB The structure of the clostridium thermocellum adhe spirosome
33% identity, 76% coverage: 72:423/461 of query aligns to 45:402/859 of 8uhwB
Sites not aligning to the query:
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)
32% identity, 76% coverage: 72:421/461 of query aligns to 47:406/891 of P0A9Q7
- IVPTTN 110:115 (≠ VAPSTN 132:137) binding NAD(+)
- G195 (= G217) binding NAD(+)
- G213 (= G235) binding NAD(+)
- A267 (≠ Q289) 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 (= E356) binding NAD(+)
- K358 (≠ R379) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 419 binding NAD(+)
- 446:449 mutation Missing: Can form dimers, but does not assemble into long filaments. Strongly affects ALDH activity, but not ADH activity.
- 487 binding NAD(+)
- 519 binding NAD(+)
- 546:550 binding NAD(+)
- 568 E→K: Partially restores protein stability and resistance to MCO damage; when associated with T-267.
- 610 binding NAD(+)
- 619 binding NAD(+)
- 653 binding Fe cation
- 657 binding Fe cation
- 670 mutation F->A,E,V: Disrupts spirosome formation. Affects the forward activity of ALDH.
- 723 binding Fe cation
- 737 binding Fe cation
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)
32% identity, 76% coverage: 72:421/461 of query aligns to 47:406/891 of P0A9Q8
Sites not aligning to the query:
- 487 binding NAD(+)
- 519 binding NAD(+)
- 546:550 binding NAD(+)
- 597:598 binding NAD(+)
- 638 binding NAD(+)
- 653 binding Fe cation
- 657 binding Fe cation
- 723 binding Fe cation
- 737 binding Fe cation
7bvpA Adhe spirosome in extended conformation (see paper)
32% identity, 76% coverage: 72:421/461 of query aligns to 47:406/869 of 7bvpA
- binding nicotinamide-adenine-dinucleotide: P112 (= P134), T113 (≠ S135), H139 (= H161), G194 (= G216), G195 (= G217), M198 (≠ I220), V212 (≠ A234), G213 (= G235), A214 (= A236), C246 (= C268), E335 (= E356), L337 (= L358), H367 (= H386)
Sites not aligning to the query:
- binding nicotinamide-adenine-dinucleotide: 418, 419, 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)
32% identity, 76% coverage: 72:421/461 of query aligns to 47:406/869 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
8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH (see paper)
30% identity, 81% coverage: 59:431/461 of query aligns to 28:405/449 of 8cekA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P106 (= P134), I107 (≠ S135), H133 (= H161), P134 (= P162), T185 (= T215), G186 (= G216), G187 (= G217), R190 (≠ I220), V204 (≠ A234), C238 (= C268), E328 (= E356)
Sites not aligning to the query:
8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
30% identity, 81% coverage: 59:431/461 of query aligns to 28:405/449 of 8cejC
- binding Mesaconyl Coenzme A: K66 (= K93), P106 (= P134), T108 (= T136), N109 (= N137), A131 (≠ S159), P132 (= P160), H133 (= H161), P134 (= P162), R169 (≠ F197), G189 (= G219), R190 (≠ I220), I237 (≠ P267), C238 (= C268), S239 (≠ I269), T391 (≠ Y417), G394 (≠ I420), T405 (= T431)
Sites not aligning to the query:
8cejA Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
30% identity, 81% coverage: 59:431/461 of query aligns to 28:405/449 of 8cejA
Sites not aligning to the query:
P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; Long-chain fatty aldehyde dehydrogenase; Medium-chain fatty aldehyde dehydrogenase; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7; EC 1.2.1.48 from Homo sapiens (Human) (see paper)
25% identity, 72% coverage: 125:454/461 of query aligns to 104:430/468 of P43353
Sites not aligning to the query:
- 463 modified: S-palmitoyl cysteine
- 465 modified: S-geranylgeranyl cysteine
J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
23% identity, 80% coverage: 86:455/461 of query aligns to 82:444/479 of J3QMK6
Sites not aligning to the query:
- 462:463 RR→AA: Reduces membrane localization.
7uyyA The crystal structure of the pseudomonas aeruginosa aldehyde dehydrogenase encoded by the pa4189 gene in complex with nadh (see paper)
26% identity, 63% coverage: 109:397/461 of query aligns to 142:443/496 of 7uyyA
- binding 1,4-dihydronicotinamide adenine dinucleotide: V165 (= V132), L166 (≠ A133), P167 (= P134), W168 (≠ S135), K192 (≠ S159), G225 (≠ A193), G229 (≠ T200), F243 (≠ I214), G245 (= G216), S246 (≠ G217), T249 (≠ I220), L252 (≠ M223), F253 (≠ G224), Y256 (≠ S227), C269 (≠ A234), G270 (= G235), C303 (= C268), H350 (≠ E300), K353 (≠ T303), F400 (≠ L358)
Query Sequence
>WP_012967296.1 NCBI__GCF_000025465.1:WP_012967296.1
MNTAELETLIRTILSEKLAPAPVSQEQQGIFRDVGSAIDAAHQAFLRYQQCPLKTRSAII
SALRETLAPELVTLAEESATETGMGNKEDKYLKNKAALENTPGIEDLTTSALTGDGGMVL
FEYSPFGVIGAVAPSTNPTETIINNSISMLAAGNSVYFSPHPGAKKVSLTLIARIEEIAY
RCSGIRNLVVTVAEPTFEATQQMMAHPLIAVLAITGGPGIVAMGMKSGKKVIGAGAGNPP
CIVDETADLVKAAEDIISGAAFDYNLPCIAEKSLIVVASVADRLIQQMQDFDALLLSPQE
TDTLRAVCLPDGAANKKLVGKSPAELLAAAGLAVPSRPPRLLIAEVQANDPWVTCEQLMP
VLPIVRVADFDSALALALRVEEGLHHTAIMHSQNVSRLNLAARTLQTSIFVKNGPSYAGI
GVGGEGFTTFTIATPTGEGTTSARTFARLRRCVLTNGFSIR
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