SitesBLAST
Comparing Pf6N2E2_1204 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1204 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: 60:745/745 of query aligns to 7:721/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (≠ F91), G39 (= G92), Q40 (= Q93), H41 (≠ G94), V42 (= V95), A45 (≠ G98), G79 (= G136), G80 (= G137), S81 (= S138), S83 (= S140), V84 (≠ I141), G374 (= G419), F375 (= F420), L379 (≠ P426), L499 (≠ W541), R500 (= R542), V624 (= V647), D625 (≠ N648), Q632 (= Q655), T687 (= T711), G688 (= G712), L689 (≠ M713), G690 (= G714), E691 (= E715)
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
23% identity, 51% coverage: 218:599/745 of query aligns to 7:410/748 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)
24% identity, 48% coverage: 213:573/745 of query aligns to 2:381/420 of 3hrdE
- active site: Q207 (= Q389), L242 (≠ V431), R318 (≠ T512), H322 (≠ G516), R350 (= R542)
- binding calcium ion: T206 (= T388), N208 (≠ F390), D212 (= D394), K241 (≠ R423), L242 (≠ V431), D243 (≠ V432)
- binding pterin cytosine dinucleotide: G237 (= G419), F238 (= F420), R350 (= R542)
- binding selenium atom: F238 (= F420), A348 (vs. gap), F349 (≠ W541), R350 (= R542)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
24% identity, 48% coverage: 213:573/745 of query aligns to 2:381/420 of 3hrdA
- active site: Q207 (= Q389), L242 (≠ V431), R318 (≠ T512), H322 (≠ G516), R350 (= R542)
- binding pterin cytosine dinucleotide: G236 (= G418), G237 (= G419), F238 (= F420), R350 (= R542)
- binding magnesium ion: T206 (= T388), N208 (≠ F390), D212 (= D394), K241 (≠ R423), L242 (≠ V431), D243 (≠ V432), T305 (≠ S494), Y308 (≠ R504), A309 (≠ V505), S346 (≠ L539)
- binding nicotinic acid: A314 (vs. gap), R318 (≠ T512), F352 (≠ V544)
- binding selenium atom: F238 (= F420), G239 (= G421), A348 (vs. gap), F349 (≠ W541), R350 (= R542)
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)
24% identity, 48% coverage: 213:573/745 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
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: 209:572/745 of query aligns to 576:947/1335 of G3X982
- A802 (≠ G419) binding
- A807 (≠ R423) 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 (≠ G516) 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)
26% identity, 48% coverage: 218:572/745 of query aligns to 3:380/761 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)
27% identity, 39% coverage: 218:509/745 of query aligns to 11:334/769 of O33819
Sites not aligning to the query:
- 522:526 binding
- 650:655 binding
- 722:725 binding
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
24% identity, 49% coverage: 210:573/745 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
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
24% identity, 49% coverage: 210:573/745 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.
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
25% identity, 48% coverage: 210:564/745 of query aligns to 538:907/1291 of 2e3tA
- active site: Q740 (= Q389), E775 (≠ G424), R853 (≠ T512), H857 (≠ G516), R885 (= R542)
- binding bicarbonate ion: R812 (= R466), H813 (≠ P467), I850 (= I509), T882 (≠ L539), A883 (≠ W540), F887 (≠ V544), G888 (= G545), Q891 (≠ H548)
- binding calcium ion: E713 (≠ A364), H714 (= H365), Y716 (≠ P367), T809 (≠ K461), G810 (= G462), G840 (= G502), T843 (≠ V505), E844 (≠ K506), S847 (vs. gap), S880 (≠ V538), N881 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L717 (≠ M368)
- binding uric acid: E775 (≠ G424), R853 (≠ T512), F887 (≠ V544)
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
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
25% identity, 48% coverage: 210:564/745 of query aligns to 536:905/1291 of 6a7xB
- active site: Q738 (= Q389), E773 (≠ G424), R851 (≠ T512), H855 (≠ G516), R883 (= R542)
- binding bicarbonate ion: R810 (= R466), H811 (≠ P467), T880 (≠ L539), A881 (≠ W540), F885 (≠ V544), G886 (= G545), Q889 (≠ H548)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M368)
- binding uric acid: E773 (≠ G424), R851 (≠ T512), F885 (≠ V544)
Sites not aligning to the query:
- active site: 1231, 1232
- 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: 980, 981, 1049, 1050, 1232
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
25% identity, 48% coverage: 210:564/745 of query aligns to 538:907/1295 of 6a7xA
- active site: Q740 (= Q389), E775 (≠ G424), R853 (≠ T512), H857 (≠ G516), R885 (= R542)
- binding bicarbonate ion: R812 (= R466), H813 (≠ P467), I850 (= I509), A883 (≠ W540), F884 (≠ W541), F887 (≠ V544), G888 (= G545), Q891 (≠ H548)
- binding uric acid: E775 (≠ G424), R853 (≠ T512), F887 (≠ V544)
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
Q8GUQ8 Xanthine dehydrogenase 1; AtXDH1; EC 1.17.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
24% identity, 38% coverage: 202:487/745 of query aligns to 577:889/1361 of Q8GUQ8
- E831 (≠ P426) mutation to A: Loss of activity.
Sites not aligning to the query:
- 364 W→A: Decreases activity 8-fold.
- 421 Y→A: Decreases activity 4-fold.
- 909 R→A: Decreases activity 12-fold.
- 1297 E→A: Decreases activity 40-fold.
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
25% identity, 48% coverage: 210:564/745 of query aligns to 536:905/1286 of 4yswA
- active site: Q738 (= Q389), E773 (≠ G424), R851 (≠ T512), H855 (≠ G516), R883 (= R542)
- binding bicarbonate ion: R810 (= R466), H811 (≠ P467), I848 (= I509), T880 (≠ L539), A881 (≠ W540), F882 (≠ W541), F885 (≠ V544), G886 (= G545), Q889 (≠ H548)
- binding calcium ion: G838 (= G502), T841 (≠ V505), E842 (≠ K506), S845 (vs. gap), S878 (≠ V538), N879 (vs. gap)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M368)
- binding uric acid: E773 (≠ G424), R851 (≠ T512), F885 (≠ V544)
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
P22985 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Rattus norvegicus (Rat) (see 2 papers)
25% identity, 48% coverage: 210:564/745 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.
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
23% identity, 48% coverage: 218:574/745 of query aligns to 14:403/786 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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
24% identity, 49% coverage: 218:585/745 of query aligns to 545:921/1290 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: 218:585/745 of query aligns to 488:852/1221 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
P47989 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Homo sapiens (Human) (see 4 papers)
27% identity, 37% coverage: 291:564/745 of query aligns to 670:935/1333 of P47989
- I703 (≠ E322) to V: in dbSNP:rs17011368
- L763 (= L384) to F: in a breast cancer sample; somatic mutation
- R791 (≠ N412) to G: in a breast cancer sample; somatic mutation; dbSNP:rs775646772
- T910 (≠ L539) to M: in dbSNP:rs669884
Sites not aligning to the query:
- 133 E → K: in dbSNP:rs45447191
- 172 G → R: in dbSNP:rs45523133
- 235 T → M: in dbSNP:rs45469499
- 257:264 binding
- 337 binding
- 347:351 binding
- 360 binding
- 395 K → M: in dbSNP:rs34929837
- 422 binding
- 509 modified: Disulfide link with 1318, In oxidase form
- 536 modified: Disulfide link with 993, In oxidase form
- 555 P → S: in dbSNP:rs45577338
- 584 D → A: in dbSNP:rs45491693
- 607 R → Q: in dbSNP:rs45442092
- 617 K → N: in dbSNP:rs45442398
- 623 T → I: in dbSNP:rs45448694
- 646 I → V: in dbSNP:rs17323225
- 993 modified: Disulfide link with 536, In oxidase form
- 1091 V → L: in dbSNP:rs45619033
- 1109 N → T: in dbSNP:rs45547640
- 1150 P → R: in dbSNP:rs1042036
- 1176 R → C: in dbSNP:rs45624433
- 1296 R → W: in dbSNP:rs45564939
- 1318 modified: Disulfide link with 509, In oxidase form
Query Sequence
>Pf6N2E2_1204 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1204
MLNEIFPNERPRALQLLLERDEADSPATLPRRSFLKIVGIGGLALGAFPHLALAQETNGA
AVPLKPSQQPSAFVQIAPSGEVTVTINRLEFGQGVQTGLPMILAEELDADWSLVRSRNGN
SDAAYMDPNFGIHLTGGSNSIKNSYTQYRELGARARAMLLSAAAARWNVDVASLSTQAGM
VLGPAGRKASYGELAEAAMAMPVPEQITLKDPKDFRIIGQATTRIDAKAKSSGQQDFGID
MHLPGQLTAVVARPPVFGARIASLDDSAARATKGVKAVLRVPLDGGAEGVAVVADSYWQA
KLARDALKVEWDASAVEKVDSEKQLAQYRELANQPGPLHFDADMTPLASAPHQLDAEFVF
PYLAHAPMEPLNCTVQLAGDGAQLWVGTQFPGGDGAAAAKVLGLKPEQIQVNVQTAGGGF
GRRGVPTNDFVVLACEVAKAARTAGVNAPIRTLWSREDDIKGGYYRPMHLHRARIGFDDS
GKVLAWDHALVGQSIITGTVFGGRVKNGIDPTATEGLRNPYPLPMRLTVHHPKLNVPVLW
WRSVGSTHTAFVMETLIDEIARTTKQDPVAYRMKLFGDQSPRHREALQLAVDKSEYGKRQ
LPAGHAWGVAVHESFSSVVAYVVEASVQDGRPVLHNVTAGVHCNLAVNPRSVEAQVQGAA
LMGLSMCLPGGAITLKDGVVQQSNFADFSVPRITDMPTFAVHIVPSAEPPTGMGEPGLPA
LAPAFANAVASLTGKPLRELPFKLA
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