SitesBLAST
Comparing AO356_26900 FitnessBrowser__pseudo5_N2C3_1:AO356_26900 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)
8gy3C Cryo-em structure of membrane-bound aldehyde dehydrogenase from gluconobacter oxydans
28% identity, 92% coverage: 62:747/747 of query aligns to 8:721/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (≠ F92), G39 (= G93), Q40 (= Q94), H41 (≠ G95), V42 (= V96), A45 (≠ G99), G79 (= G137), G80 (= G138), S81 (= S139), S83 (≠ T141), V84 (≠ I142), G374 (= G421), F375 (= F422), L379 (≠ P428), L499 (≠ W543), R500 (= R544), V624 (= V649), D625 (≠ N650), Q632 (= Q657), T687 (= T713), G688 (= G714), L689 (≠ M715), G690 (= G716), E691 (= E717)
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
23% identity, 49% coverage: 219:581/747 of query aligns to 7:381/748 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
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 48% coverage: 214:575/747 of query aligns to 2:381/420 of 3hrdE
- active site: Q207 (= Q391), L242 (≠ V433), R318 (≠ T514), H322 (≠ G518), R350 (= R544)
- binding calcium ion: T206 (= T390), N208 (≠ F392), D212 (= D396), K241 (≠ R425), L242 (≠ V433), D243 (≠ V434)
- binding pterin cytosine dinucleotide: G237 (= G421), F238 (= F422), R350 (= R544)
- binding selenium atom: F238 (= F422), A348 (vs. gap), F349 (≠ W543), R350 (= R544)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
23% identity, 48% coverage: 214:575/747 of query aligns to 2:381/420 of 3hrdA
- active site: Q207 (= Q391), L242 (≠ V433), R318 (≠ T514), H322 (≠ G518), R350 (= R544)
- binding pterin cytosine dinucleotide: G236 (= G420), G237 (= G421), F238 (= F422), R350 (= R544)
- binding magnesium ion: T206 (= T390), N208 (≠ F392), D212 (= D396), K241 (≠ R425), L242 (≠ V433), D243 (≠ V434), T305 (≠ S496), Y308 (≠ R506), A309 (≠ V507), S346 (≠ L541)
- binding nicotinic acid: A314 (vs. gap), R318 (≠ T514), F352 (≠ V546)
- binding selenium atom: F238 (= F422), G239 (= G423), A348 (vs. gap), F349 (≠ W543), R350 (= R544)
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: 214:575/747 of query aligns to 3:382/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
3zyvB Crystal structure of the mouse liver aldehyde oxidase 3 (maox3) (see paper)
26% identity, 49% coverage: 210:574/747 of query aligns to 523:891/1262 of 3zyvB
Sites not aligning to the query:
- active site: 1207, 1208
- binding flavin-adenine dinucleotide: 227, 229, 230, 231, 232, 233, 234, 267, 303, 304, 312, 313, 316, 317, 319, 325, 326, 366, 392, 393
- binding fe2/s2 (inorganic) cluster: 39, 41, 42, 44, 46, 49, 69, 71, 111, 112, 114, 146, 148
G3X982 Aldehyde oxidase 3; Aldehyde oxidase homolog 1; Azaheterocycle hydroxylase 3; EC 1.2.3.1; EC 1.17.3.- from Mus musculus (Mouse) (see paper)
27% identity, 49% coverage: 210:574/747 of query aligns to 576:947/1335 of G3X982
- A802 (≠ G421) binding
- A807 (≠ R425) mutation to V: No effect on kinetic constants with smaller substrates like benzaldehyde or phthalazine. Decreases substrate affinity and slightly increases catalytic efficiency for bulkier substrates like phenanthridine.
- Y885 (vs. gap) mutation to M: Slightly decreases substrate affinity but no effect on activity with smaller substrates like benzaldehyde or phthalazine. Increases catalytic efficiency with bulkier substrates like phenanthridine or more charged substrates like N1-methylnicotinamide.
- K889 (≠ G518) mutation to H: No effect on substrate affinity but decreases catalytic efficiency for smaller substrates like benzaldehyde or phthalazine. Increases substrate affinity and activity for bulkier substrates like phenanthridine.
Sites not aligning to the query:
- 47 binding
- 52 binding
- 55 binding
- 77 binding
- 116 binding
- 117 binding
- 120 binding
- 152 binding
- 154 binding
- 264:271 binding
- 354 binding
- 358 binding
- 367 binding
- 411 binding
- 1043 binding
- 1199 binding
- 1266 E→Q: Loss of activity with different N-heterocyclic compounds as substrates. 60% reduction of activity with benzaldehyde.
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
25% identity, 54% coverage: 219:618/747 of query aligns to 3:438/761 of 1rm6A
Sites not aligning to the query:
- active site: 718, 719
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): 473, 474, 475, 476, 513, 514, 515, 517, 518, 646, 647, 651, 654, 714, 715, 716, 717, 718
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
25% identity, 54% coverage: 219:618/747 of query aligns to 11:446/769 of O33819
Sites not aligning to the query:
- 522:526 binding
- 650:655 binding
- 722:725 binding
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
24% identity, 49% coverage: 211:575/747 of query aligns to 9:381/732 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)
24% identity, 49% coverage: 211:575/747 of query aligns to 9:381/731 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
7dqxD Crystal structure of xanthine dehydrogenase family protein
23% identity, 46% coverage: 219:560/747 of query aligns to 6:379/770 of 7dqxD
Sites not aligning to the query:
- binding pterin cytosine dinucleotide: 491, 492, 493, 494, 498, 530, 531, 532, 533, 534, 535, 536, 658, 659, 662, 725, 726, 727, 728
O54754 Aldehyde oxidase 1; Azaheterocycle hydroxylase 1; Retinal oxidase; EC 1.2.3.1; EC 1.17.3.- from Mus musculus (Mouse) (see paper)
29% identity, 27% coverage: 291:489/747 of query aligns to 671:864/1333 of O54754
- V806 (≠ G426) 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.
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
27% identity, 15% coverage: 632:746/747 of query aligns to 577:697/701 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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
25% identity, 38% coverage: 291:575/747 of query aligns to 635:906/1290 of 4uhxA
Sites not aligning to the query:
- active site: 1223, 1224
- binding flavin-adenine dinucleotide: 43, 44, 229, 230, 231, 232, 233, 234, 235, 236, 237, 310, 311, 319, 320, 323, 324, 326, 329, 332, 333, 377, 404
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 111, 112, 114, 146, 148
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: 540, 542, 543, 1014, 1015, 1018, 1019, 1020, 1079
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: 540, 542, 543, 1014, 1015, 1018, 1019, 1020
8emtB Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
24% identity, 49% coverage: 219:583/747 of query aligns to 488:848/1221 of 8emtB
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 210, 211, 213, 214, 216, 217, 218, 291, 292, 300, 304, 305, 307, 314
- binding fe2/s2 (inorganic) cluster: 38, 39, 40, 42, 44, 45, 47, 69, 109, 112, 144, 146
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
24% identity, 48% coverage: 211:566/747 of query aligns to 538:907/1291 of 2e3tA
- active site: Q740 (= Q391), E775 (≠ G426), R853 (≠ T514), H857 (≠ G518), R885 (= R544)
- binding bicarbonate ion: R812 (= R468), H813 (≠ P469), I850 (= I511), T882 (≠ L541), A883 (≠ W542), F887 (≠ V546), G888 (= G547), Q891 (≠ H550)
- binding calcium ion: E713 (≠ A365), H714 (= H366), Y716 (≠ P368), T809 (≠ K463), G810 (= G464), G840 (= G504), T843 (≠ V507), E844 (≠ K508), S847 (vs. gap), S880 (≠ V540), N881 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L717 (≠ M369)
- binding uric acid: E775 (≠ G426), R853 (≠ T514), F887 (≠ V546)
Sites not aligning to the query:
- active site: 1233, 1234
- binding flavin-adenine dinucleotide: 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 318, 319, 322, 323, 325, 326, 331, 332, 375, 376
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 113, 145, 147
- binding uric acid: 982, 983, 1051, 1052, 1234
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
24% identity, 48% coverage: 211:566/747 of query aligns to 536:905/1286 of 4yswA
- active site: Q738 (= Q391), E773 (≠ G426), R851 (≠ T514), H855 (≠ G518), R883 (= R544)
- binding bicarbonate ion: R810 (= R468), H811 (≠ P469), I848 (= I511), T880 (≠ L541), A881 (≠ W542), F882 (≠ W543), F885 (≠ V546), G886 (= G547), Q889 (≠ H550)
- binding calcium ion: G838 (= G504), T841 (≠ V507), E842 (≠ K508), S845 (vs. gap), S878 (≠ V540), N879 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M369)
- binding uric acid: E773 (≠ G426), R851 (≠ T514), F885 (≠ V546)
Sites not aligning to the query:
- active site: 1231, 1232
- binding flavin-adenine dinucleotide: 44, 226, 227, 228, 229, 230, 231, 232, 233, 234, 307, 308, 312, 316, 317, 320, 321, 323, 324, 329, 330, 373, 374, 399
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 110, 111, 113, 145, 147
- binding 1,4-dihydronicotinamide adenine dinucleotide: 233, 326, 327, 328, 363, 364, 400, 401, 428, 430, 431, 471, 478, 1196
- binding uric acid: 980, 981, 1050, 1232
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
24% identity, 48% coverage: 211:566/747 of query aligns to 538:907/1295 of 6a7xA
- active site: Q740 (= Q391), E775 (≠ G426), R853 (≠ T514), H857 (≠ G518), R885 (= R544)
- binding bicarbonate ion: R812 (= R468), H813 (≠ P469), I850 (= I511), A883 (≠ W542), F884 (≠ W543), F887 (≠ V546), G888 (= G547), Q891 (≠ H550)
- binding uric acid: E775 (≠ G426), R853 (≠ T514), F887 (≠ V546)
Sites not aligning to the query:
- active site: 1233, 1234
- binding flavin-adenine dinucleotide: 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 314, 319, 322, 323, 325, 326, 332, 376
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 109, 110, 111, 113, 145, 147
- binding nicotinamide-adenine-dinucleotide: 329, 365, 366, 432, 433, 473, 480
- binding uric acid: 982, 983, 1052, 1234
P22985 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 48% coverage: 211:566/747 of query aligns to 565:934/1331 of P22985
Sites not aligning to the query:
- 43 binding
- 48 binding
- 51 binding
- 73 binding
- 112 binding
- 115 binding
- 147 binding
- 149 binding
- 256:263 binding
- 335:336 WF→AL: Converts the enzyme to the oxidase form that utilizes molecular oxygen as electron acceptor. Interferes with normal conversion to the dehydrogenase form by reducing agents.
- 346:350 binding
- 359 binding
- 403 binding
- 535 C→A: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with R-992. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with R-992 and S-1316.
- 992 C→R: Slows the conversion from the dehydrogenase form to the oxidase form; when associated with A-535. Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and S-1316.
- 1316 C→S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992.
Query Sequence
>AO356_26900 FitnessBrowser__pseudo5_N2C3_1:AO356_26900
MLNEIFPNELPRALQHMLERDEADGPAALPRRSFLKIVGIGGLALGAFPHLALAQEANGA
VAAPLKPTQQPSAFVQIAPNGEVTVTINRLEFGQGVQTGLPMILAEELDADWSLVRSRNG
SNDAAYMDPAFGIHLTGGSNTIKNSYTQYRELGARARAMLLSAAAARWNVDVASLSTQAG
MVLGPAGRKASYGELAQAAMAMPVPEQITLKDPKDFRIIGQATTRIDAKAKSSGQQDFGI
DMHLPGQLTAVVARPPVFGARIAALDDSAARATKGVKAVLRVPLDGGAEGVAVVADSYWQ
AKLARDALKVEWNASAVEKLDSEKQLAQYRELASQPGPLHFDADMTPLATAPHRLEAEFL
FPYLAHAPMEPLNCTVQLAGKNGAQLWVGTQFPGGDAAAAAKVLDLKPEQIQVNVQTAGG
GFGRRGVPTNDFVVLACEVAKAARTAGVDAPIRTLWSREDDIKGGYYRPMHLHRARIGFD
DSGKVLAWDHALVGQSIITGTVFGGRVKNGIDPTATEGLRDPYPLPMRLTVHHPKLNVPV
LWWRSVGSTHTAFVMETLIDEIARTTKQDPVAYRMKLFGDQSPRHRAALQLAVDKSEYGK
RQLPAGRAWGVAVHESFSSVVAYVVEASVQDGRPVLHNVTAGVHCNLAVNPRSVEAQVQG
AALMGLSMCLPGGAITLKDGVVQQSNFADFSVPRITDMPEFAVHIVPSAEPPTGMGEPGL
PALAPAFANAVASLTGKPMRELPFKLA
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