SitesBLAST
Comparing 5209812 FitnessBrowser__PV4:5209812 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, 94% coverage: 37:741/747 of query aligns to 6:718/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (= M69), G39 (= G70), Q40 (= Q71), H41 (≠ G72), V42 (≠ I73), A45 (≠ G76), G79 (≠ D109), G80 (= G110), S81 (= S111), S83 (= S113), V84 (≠ I114), G374 (= G402), F375 (= F403), L379 (≠ S407), L499 (≠ M516), R500 (= R517), V624 (= V647), D625 (≠ N648), Q632 (= Q655), T687 (≠ A710), G688 (= G711), L689 (≠ V712), G690 (= G713), E691 (= E714)
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
36% identity, 17% coverage: 614:741/747 of query aligns to 179:316/330 of 3hrdB
- active site: E289 (= E714), P290 (= P715)
- binding pterin cytosine dinucleotide: I215 (≠ V647), N216 (= N648), M219 (≠ R651), V220 (= V652), Q223 (= Q655), K285 (vs. gap), G286 (= G711), V287 (= V712), G288 (= G713), E289 (= E714)
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)
36% identity, 17% coverage: 614:741/747 of query aligns to 179:316/330 of Q0QLF1
- 211:223 (vs. 643:655, 38% identical) binding
- AKGVGE 284:289 (≠ --GVGE 711:714) binding
Sites not aligning to the query:
- 45:49 binding
- 85:90 binding
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
33% identity, 20% coverage: 590:742/747 of query aligns to 591:743/748 of 5y6qC
Sites not aligning to the query:
- active site: 204, 239, 310, 316, 344
- binding pterin cytosine dinucleotide: 233, 234, 235, 461, 462, 463, 464, 468, 500, 502, 503, 504, 505
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
34% identity, 19% coverage: 603:742/747 of query aligns to 604:746/761 of 1rm6A
- active site: E718 (≠ V717), G719 (≠ P718)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): L646 (≠ V647), N647 (= N648), V651 (= V652), Q654 (= Q655), K714 (≠ G713), E715 (= E714), A716 (≠ P715), S717 (≠ G716), E718 (≠ V717)
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)
34% identity, 19% coverage: 603:742/747 of query aligns to 612:754/769 of O33819
Sites not aligning to the query:
- 214 binding
- 244:245 binding
- 522:526 binding
3zyvB Crystal structure of the mouse liver aldehyde oxidase 3 (maox3) (see paper)
29% identity, 30% coverage: 223:448/747 of query aligns to 557:795/1262 of 3zyvB
Sites not aligning to the query:
- active site: 829, 833, 861, 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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
25% identity, 35% coverage: 197:461/747 of query aligns to 546:824/1290 of 4uhxA
Sites not aligning to the query:
- active site: 843, 847, 875, 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)
25% identity, 35% coverage: 197:461/747 of query aligns to 489:753/1221 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
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
29% identity, 15% coverage: 631:742/747 of query aligns to 601:720/731 of 5g5gC
Sites not aligning to the query:
- active site: 211, 246, 316, 322, 350
- binding pterin cytosine dinucleotide: 240, 241, 242, 350, 468, 469, 470, 507, 509, 511, 512
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
29% identity, 15% coverage: 631:742/747 of query aligns to 601:720/732 of P77489
- 615:621 (vs. 645:651, 29% identical) binding
- Q625 (= Q655) binding
- KGVG 688:691 (≠ -GVG 711:713) binding
- E692 (= E714) mutation to Q: Loss of activity.
Sites not aligning to the query:
- 241:242 binding
- 440 mutation R->H,K: Decrease in catalytic efficiency.
- 468:470 binding
- 511:512 binding
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)
25% identity, 58% coverage: 223:655/747 of query aligns to 610:1057/1335 of G3X982
- A802 (≠ G402) binding
- A807 (vs. gap) 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 (≠ F490) 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 (≠ P494) 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.
- L1043 (≠ I641) binding
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
- 1199 binding
- 1266 E→Q: Loss of activity with different N-heterocyclic compounds as substrates. 60% reduction of activity with benzaldehyde.
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
26% identity, 34% coverage: 198:448/747 of query aligns to 552:819/1291 of 2e3tA
Sites not aligning to the query:
- active site: 853, 857, 885, 1233, 1234
- binding bicarbonate ion: 850, 882, 883, 887, 888, 891
- binding calcium ion: 840, 843, 844, 847, 880, 881
- 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: 853, 887, 982, 983, 1051, 1052, 1234
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
26% identity, 34% coverage: 198:448/747 of query aligns to 550:817/1286 of 4yswA
Sites not aligning to the query:
- active site: 851, 855, 883, 1231, 1232
- binding bicarbonate ion: 848, 880, 881, 882, 885, 886, 889
- binding calcium ion: 838, 841, 842, 845, 878, 879
- 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: 851, 885, 980, 981, 1050, 1232
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
26% identity, 34% coverage: 198:448/747 of query aligns to 550:817/1291 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
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
26% identity, 34% coverage: 198:448/747 of query aligns to 552:819/1295 of 6a7xA
Sites not aligning to the query:
- active site: 853, 857, 885, 1233, 1234
- binding bicarbonate ion: 850, 883, 884, 887, 888, 891
- 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: 853, 887, 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)
26% identity, 34% coverage: 198:448/747 of query aligns to 579:846/1331 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.
8emtA Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
26% identity, 35% coverage: 197:461/747 of query aligns to 505:786/1254 of 8emtA
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 215, 216, 217, 218, 219, 221, 222, 223, 296, 297, 306, 309, 310, 312, 319
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 45, 46, 49, 69, 71, 111, 112, 114, 146, 148
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
31% identity, 17% coverage: 615:741/747 of query aligns to 562:695/701 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
O54754 Aldehyde oxidase 1; Azaheterocycle hydroxylase 1; Retinal oxidase; EC 1.2.3.1; EC 1.17.3.- from Mus musculus (Mouse) (see paper)
27% identity, 32% coverage: 209:448/747 of query aligns to 594:850/1333 of O54754
- V806 (≠ S407) 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.
Query Sequence
>5209812 FitnessBrowser__PV4:5209812
MSQFSAVQNFSRRDVLKLFGAAGGGLALGASGLAWSPMALAQNGEARLNLFIAIGEDDRV
YLTCHRSEMGQGIRTGIPQVLADELGADWDKVVVVQGLADKRYGSQNTDGSRSIRKGFDK
MREMGAMARTMLEQAAAERLKVPVAELSTADNKVTHSASGRSLSFGELAMAAAKLPLPEV
TGLKLKSAKAFTHIGKGHTIVDMEAILDGSAEYGYDIHLENMLYASIVRPPVLGSKVDKL
DDKAARAVAGVVDVIPLPGHQGAPSFQPLGGVAVLATNSWSAAQGRKALKVSWSDSPNDG
HDSSAYLAQLKRAVQKSGKPVRQLGEQSQSWPADKTIEAVYSVPYLAHAMMEPPAAAASV
TDKTAEIWASTQTPQSAQGTVAAALGLQAEQVTVHVTLLGGGFGRKSKPDFCVEAALLSQ
KTGRPVKVCWSREDELQNGYLHAISAQYFKARVGDKAVEAILQRTGFPSISSTFAEGVDE
PSASELDLGFVDVPLAIDSLRCESVKASAHTRIGWMRSVCNIQHGFGIGVFVDELANKRG
LDTYTMWRELLGKDRQETFSDQQFNYGNYGETLERHPVDTARYKGVISAVEQEVKQMAKP
EAGQGWGFAVHRSFTAYVAAASLVEVTQDKQLKVLKTVIAIDAGTLVNPDRVASQLEGAV
MFGLSIALMGRISFKDGRVEQSNFHDYPLLRMSQCPEIETILVPSMAPPAGVGEPGVPPI
APSIVNAIYAASGTRIRDLPLSDHFKI
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