SitesBLAST
Comparing SMa1488 FitnessBrowser__Smeli:SMa1488 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 19 hits to proteins with known functional sites (download)
8gy3C Cryo-em structure of membrane-bound aldehyde dehydrogenase from gluconobacter oxydans
28% identity, 91% coverage: 64:743/747 of query aligns to 20:724/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (≠ G82), G39 (= G83), Q40 (= Q84), H41 (≠ G85), V42 (≠ I86), A45 (= A89), G79 (= G126), G80 (= G127), S81 (= S128), S83 (= S130), V84 (= V131), G374 (≠ F415), F375 (= F416), L379 (≠ F420), L499 (≠ W533), R500 (= R534), V624 (= V643), D625 (≠ N644), Q632 (= Q651), T687 (≠ G706), G688 (= G707), L689 (≠ I708), G690 (= G709), E691 (= E710)
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
26% identity, 51% coverage: 209:591/747 of query aligns to 7:401/748 of 5y6qC
Sites not aligning to the query:
- active site: 715, 716
- binding pterin cytosine dinucleotide: 461, 462, 463, 464, 468, 500, 502, 503, 504, 505, 638, 640, 641, 648, 711, 713, 714, 715
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
37% identity, 19% coverage: 598:738/747 of query aligns to 598:746/761 of 1rm6A
- active site: E718 (= E710), G719 (≠ P711)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): L646 (≠ V643), N647 (= N644), V651 (≠ I648), Q654 (= Q651), K714 (vs. gap), E715 (vs. gap), A716 (vs. gap), S717 (vs. gap), E718 (= E710)
Sites not aligning to the query:
- active site: 206, 241, 318, 322, 350
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 235, 236, 237, 238, 350, 473, 474, 475, 476, 513, 514, 515, 517, 518
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
37% identity, 19% coverage: 598:738/747 of query aligns to 606:754/769 of O33819
- VGKALN 650:655 (≠ PGSIVN 639:644) binding
- KEAS 722:725 (vs. gap) binding
Sites not aligning to the query:
- 214 binding
- 244:245 binding
- 522:526 binding
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
25% identity, 48% coverage: 207:566/747 of query aligns to 12:403/786 of 1t3qB
Sites not aligning to the query:
- active site: 743, 744
- binding pterin cytosine dinucleotide: 506, 507, 508, 510, 513, 545, 547, 549, 550, 666, 670, 674, 675, 678, 739, 740, 741, 742
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
27% identity, 48% coverage: 206:564/747 of query aligns to 15:380/732 of P77489
Sites not aligning to the query:
- 440 mutation R->H,K: Decrease in catalytic efficiency.
- 468:470 binding
- 511:512 binding
- 615:621 binding
- 625 binding
- 688:691 binding
- 692 E→Q: Loss of activity.
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
27% identity, 48% coverage: 206:564/747 of query aligns to 15:380/731 of 5g5gC
Sites not aligning to the query:
- active site: 692, 693
- binding pterin cytosine dinucleotide: 468, 469, 470, 507, 509, 511, 512, 617, 618, 621, 625, 688, 690, 691, 692
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 48% coverage: 205:564/747 of query aligns to 3:380/420 of 3hrdE
- active site: Q207 (= Q385), L242 (≠ F420), R318 (≠ S501), H322 (≠ E505), R350 (= R534)
- binding calcium ion: T206 (≠ N384), N208 (≠ A386), D212 (≠ F390), K241 (≠ H419), L242 (≠ F420), D243 (≠ L421)
- binding pterin cytosine dinucleotide: G237 (≠ F415), F238 (= F416), R350 (= R534)
- binding selenium atom: F238 (= F416), A348 (≠ F532), F349 (≠ W533), R350 (= R534)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 48% coverage: 205:564/747 of query aligns to 3:380/420 of 3hrdA
- active site: Q207 (= Q385), L242 (≠ F420), R318 (≠ S501), H322 (≠ E505), R350 (= R534)
- binding pterin cytosine dinucleotide: G236 (= G414), G237 (≠ F415), F238 (= F416), R350 (= R534)
- binding magnesium ion: T206 (≠ N384), N208 (≠ A386), D212 (≠ F390), K241 (≠ H419), L242 (≠ F420), D243 (≠ L421), T305 (= T488), Y308 (≠ W491), A309 (≠ F492), S346 (≠ I530)
- binding nicotinic acid: A314 (≠ D497), R318 (≠ S501), F352 (≠ V536)
- binding selenium atom: F238 (= F416), G239 (= G417), A348 (≠ F532), F349 (≠ W533), R350 (= R534)
Q0QLF2 Nicotinate dehydrogenase large molybdopterin subunit; NDH; Nicotinic acid hydroxylase large molybdopterin subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see 2 papers)
23% identity, 48% coverage: 205:564/747 of query aligns to 4:381/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
28% identity, 18% coverage: 608:738/747 of query aligns to 561:696/701 of 4zohA
Sites not aligning to the query:
- active site: 186, 219, 298, 300, 304, 332
- binding pterin cytosine dinucleotide: 213, 214, 215, 332, 442, 443, 444, 446, 482, 484, 486, 487
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
32% identity, 17% coverage: 613:742/747 of query aligns to 183:321/330 of 3hrdB
- active site: E289 (= E710), P290 (= P711)
- binding pterin cytosine dinucleotide: I215 (≠ V643), N216 (= N644), M219 (≠ I647), V220 (≠ I648), Q223 (= Q651), K285 (vs. gap), G286 (= G707), V287 (≠ I708), G288 (= G709), E289 (= E710)
Sites not aligning to the query:
Q0QLF1 Nicotinate dehydrogenase medium molybdopterin subunit; NDH; Nicotinic acid hydroxylase medium molybdopterin subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see paper)
32% identity, 17% coverage: 613:742/747 of query aligns to 183:321/330 of Q0QLF1
- 211:223 (vs. 639:651, 31% identical) binding
- AKGVGE 284:289 (≠ --GIGE 707:710) binding
Sites not aligning to the query:
- 45:49 binding
- 85:90 binding
O54754 Aldehyde oxidase 1; Azaheterocycle hydroxylase 1; Retinal oxidase; EC 1.2.3.1; EC 1.17.3.- from Mus musculus (Mouse) (see paper)
25% identity, 36% coverage: 209:479/747 of query aligns to 579:864/1333 of O54754
- V806 (≠ L421) mutation to E: Decreases substrate affinity and activity on benzaldehyde, phthalazine and acetaldehyde, while increases affinity for more hydrophobic aldehydes like retinal. Abolishes catalytic activity; when associated with R-884.
Sites not aligning to the query:
- 884 M→R: Abolishes catalytic activity on phthalazine and acetaldehyde. Decreases catalytic efficiency on benzaldehyde and retinal. Abolishes catalytic activity; when associated with E-806.
- 1265 E→Q: Abolishes catalytic activity.
Q8GUQ8 Xanthine dehydrogenase 1; AtXDH1; EC 1.17.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
24% identity, 55% coverage: 209:617/747 of query aligns to 598:1040/1361 of Q8GUQ8
- E831 (vs. gap) mutation to A: Loss of activity.
- R909 (≠ E505) mutation to A: Decreases activity 12-fold.
Sites not aligning to the query:
- 364 W→A: Decreases activity 8-fold.
- 421 Y→A: Decreases activity 4-fold.
- 1297 E→A: Decreases activity 40-fold.
Q7G9P4 Abscisic-aldehyde oxidase; Aldehyde oxidase 3; AO-3; AtAO-3; AtAO4; Indole-3-acetaldehyde oxidase; IAA oxidase; EC 1.2.3.14; EC 1.2.3.7 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 20% coverage: 333:479/747 of query aligns to 716:862/1332 of Q7G9P4
- LQRPVK 821:826 (≠ VARPVK 438:443) mutation to WDLDQ: In aao3-3; wilty phenotype in rosette leaves, reduced ABA levels, reduced dormancy, abnormal water loss and abnormal response to water deficit.
1dgjA Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774 (see paper)
28% identity, 19% coverage: 595:736/747 of query aligns to 751:895/906 of 1dgjA
- active site: E869 (= E710), M870 (≠ P711)
- binding molybdenum (iv)oxide: E869 (= E710)
- binding pterin cytosine dinucleotide: C799 (≠ V643), N800 (= N644), V803 (≠ I647), V804 (≠ I648), Q807 (= Q651), S865 (vs. gap), G866 (= G707), V867 (≠ I708), G868 (= G709), E869 (= E710)
Sites not aligning to the query:
- active site: 391, 427, 503, 507, 535
- binding molybdenum (iv)oxide: 424, 535, 698
- binding fe2/s2 (inorganic) cluster: 38, 39, 40, 41, 43, 44, 45, 46, 48, 58, 60, 100, 101, 103, 137, 139
- binding pterin cytosine dinucleotide: 99, 139, 423, 424, 535, 652, 655, 656, 657, 658, 697, 698, 700, 702, 703
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
22% identity, 39% coverage: 195:486/747 of query aligns to 525:838/1291 of 6a7xB
Sites not aligning to the query:
- active site: 851, 855, 883, 1231, 1232
- binding bicarbonate ion: 880, 881, 885, 886, 889
- binding flavin-adenine dinucleotide: 44, 227, 228, 229, 230, 231, 232, 233, 234, 307, 312, 317, 320, 321, 323, 324, 330, 373, 374
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 111, 113, 145, 147
- binding nicotinamide-adenine-dinucleotide: 327, 363, 364, 428, 430, 431, 471, 478
- binding uric acid: 851, 885, 980, 981, 1049, 1050, 1232
2e1qA Crystal structure of human xanthine oxidoreductase mutant, glu803val (see paper)
26% identity, 27% coverage: 278:479/747 of query aligns to 644:835/1307 of 2e1qA
- active site: Q742 (= Q385), V777 (≠ F420)
- binding bicarbonate ion: R814 (= R458), H815 (≠ P459)
- binding calcium ion: E715 (≠ V359), H716 (= H360), Y718 (≠ Q362), T741 (≠ N384), T747 (≠ F390), S780 (≠ Q423), T781 (= T424), S784 (≠ P427), T811 (≠ D455), G812 (≠ T456)
- binding fe2/s2 (inorganic) cluster: L719 (= L363)
- binding hydroxy(dioxo)molybdenum: F773 (= F416), G774 (= G417)
Sites not aligning to the query:
- active site: 855, 859, 887, 1235, 1236
- binding bicarbonate ion: 852, 886, 889, 890, 893
- binding flavin-adenine dinucleotide: 43, 44, 230, 231, 232, 233, 234, 235, 236, 237, 238, 311, 312, 316, 320, 321, 324, 325, 327, 328, 333, 334, 377, 378
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 110, 111, 112, 114, 146, 148
- binding hydroxy(dioxo)molybdenum: 887, 1053, 1054, 1236
Query Sequence
>SMa1488 FitnessBrowser__Smeli:SMa1488
MNDMTPVTSEITASEIGKPFKLPRRGFLGASLGALVLGVTLPAGRARAQAAAAAITPGTR
ISAFLEILPNETVLFRSAFIEGGQGIFTAMAQIVGEELDVDPMQFVVEGAPPGPDYLLTG
GGRFTGGSMSVRMSYDAMRKLGASARHMLIQAAAVRLRVPVSELSTEPGRVVHGASGRTL
PYGEIADAAAGLPLPTNVVLRDRADFRWIGKPVARLDVRDKSTGKARYAIDLKVDRMLHA
AVQHSPRLGGEPGALQNEADVRGMPGVHSIHSLPGTVAVVADSWWRARMAAEALQVTWTE
PTRGTAHVMPADFSTEAHMAMLKATPGEGVAYETVGNAATALGDAARVVEATYDAPYLVH
GQLEPPSALARWNDDGSLDLWVPNQAPEMFQAEAAKVAGIAPEKVTIHSPMLGGFFGRHF
LYQTANPFPQAILLAKAVARPVKLIWSREEEFLRDTLRPMGAVRFRAGLDAEGLPVALEA
VAVGEGPTGRWFGRQPDKVDSSSVEGIAGKVYAIPNRHIGQVHVDDPAIIGFWRSVGHSM
NDFFYETFFDEMADAGQQDPYELRRRLLADSPRHRTLLEAVAELSGGWRRGPFIADDGTR
RARGVAMASPFGSEVATIAEVSLRSGEVVVHDVWVAIDPGSIVNPAIIEAQVNSAVALGL
SSALLEEVVYVDGMPQARNYDGYPILTPDRMPRVHVRIVESGAPMGGIGEPGLPGVPPAI
ANAVSVLAGRRVRSLPLSKHDFKGVDG
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