SitesBLAST
Comparing Pf1N1B4_4584 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4584 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
31% identity, 94% coverage: 46:722/722 of query aligns to 15:723/732 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 (= G116), G80 (= G117), S81 (= S118), S83 (= S120), V84 (≠ T121), G374 (= G397), F375 (= F398), L379 (≠ A402), L499 (= L519), R500 (= R520), V624 (= V623), D625 (≠ N624), Q632 (= Q631), T687 (≠ G686), G688 (= G687), L689 (≠ I688), G690 (= G689), E691 (= E690)
5y6qC Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
24% identity, 49% coverage: 199:550/722 of query aligns to 7:374/748 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)
31% identity, 25% coverage: 534:717/722 of query aligns to 553:745/761 of 1rm6A
- active site: E718 (= E690), G719 (≠ V691)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): L646 (≠ V623), N647 (= N624), V651 (≠ I628), Q654 (= Q631), K714 (vs. gap), E715 (vs. gap), A716 (vs. gap), S717 (vs. gap), E718 (= E690)
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)
31% identity, 25% coverage: 534:717/722 of query aligns to 561:753/769 of O33819
- VGKALN 650:655 (≠ CGIAVN 619:624) 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)
20% identity, 49% coverage: 197:551/722 of query aligns to 12:402/786 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
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
28% identity, 19% coverage: 580:719/722 of query aligns to 588:721/731 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)
28% identity, 19% coverage: 580:719/722 of query aligns to 588:721/732 of P77489
- 615:621 (vs. 621:627, 29% identical) binding
- Q625 (= Q631) binding
- KGVG 688:691 (≠ GGIG 686:689) binding
- E692 (= E690) 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
3hrdB Crystal structure of nicotinate dehydrogenase (see paper)
29% identity, 17% coverage: 593:717/722 of query aligns to 183:316/330 of 3hrdB
- active site: E289 (= E690), P290 (≠ V691)
- binding pterin cytosine dinucleotide: I215 (≠ V623), N216 (= N624), M219 (≠ S627), V220 (≠ I628), Q223 (= Q631), K285 (vs. gap), G286 (= G687), V287 (≠ I688), G288 (= G689), E289 (= E690)
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)
29% identity, 17% coverage: 593:717/722 of query aligns to 183:316/330 of Q0QLF1
- 211:223 (vs. 619:631, 23% identical) binding
- AKGVGE 284:289 (≠ --GIGE 687:690) 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)
23% identity, 50% coverage: 199:557/722 of query aligns to 579:953/1333 of O54754
- V806 (≠ A402) 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.
- M884 (= M478) mutation to R: Abolishes catalytic activity on phthalazine and acetaldehyde. Decreases catalytic efficiency on benzaldehyde and retinal. Abolishes catalytic activity; when associated with E-806.
Sites not aligning to the query:
- 1265 E→Q: Abolishes catalytic activity.
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
24% identity, 49% coverage: 199:550/722 of query aligns to 545:905/1290 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
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
24% identity, 20% coverage: 317:460/722 of query aligns to 688:833/1291 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
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
24% identity, 20% coverage: 317:460/722 of query aligns to 686:831/1291 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
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
24% identity, 20% coverage: 317:460/722 of query aligns to 686:831/1286 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
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
24% identity, 20% coverage: 317:460/722 of query aligns to 688:833/1295 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)
24% identity, 20% coverage: 317:460/722 of query aligns to 715:860/1331 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.
2e1qA Crystal structure of human xanthine oxidoreductase mutant, glu803val (see paper)
23% identity, 20% coverage: 317:460/722 of query aligns to 690:835/1307 of 2e1qA
- active site: Q742 (= Q367), V777 (≠ A402)
- binding bicarbonate ion: R814 (= R439), H815 (≠ S440)
- binding calcium ion: E715 (≠ A342), H716 (= H343), Y718 (≠ P345), T741 (= T366), T747 (≠ D372), S780 (≠ T405), T781 (≠ S406), S784 (≠ V409), T811 (≠ R434), G812 (= G435)
- binding fe2/s2 (inorganic) cluster: L719 (≠ M346)
- binding hydroxy(dioxo)molybdenum: F773 (= F398), G774 (= G399)
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
2ckjA Human milk xanthine oxidoreductase
23% identity, 20% coverage: 317:460/722 of query aligns to 659:804/1264 of 2ckjA
Sites not aligning to the query:
- active site: 824, 828, 856, 1204, 1205
- binding flavin-adenine dinucleotide: 228, 230, 231, 232, 233, 234, 308, 309, 317, 318, 321, 322, 324, 325, 331, 375
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 71, 111, 112, 114, 146, 147, 148
P47989 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Homo sapiens (Human) (see 4 papers)
23% identity, 20% coverage: 317:460/722 of query aligns to 716:861/1333 of P47989
- L763 (≠ I362) to F: in a breast cancer sample; somatic mutation
- R791 (≠ H390) to G: in a breast cancer sample; somatic mutation; dbSNP:rs775646772
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
- 703 I → V: in dbSNP:rs17011368
- 910 T → M: in dbSNP:rs669884
- 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
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
23% identity, 37% coverage: 199:463/722 of query aligns to 16:331/804 of 1zxiB
Sites not aligning to the query:
- active site: 347, 353, 382, 383, 758, 759
- binding copper (ii) ion: 383, 384, 758
- binding cu(i)-s-mo(vi)(=o)oh cluster: 380, 381, 382, 383, 563, 564, 758
- binding pterin cytosine dinucleotide: 382, 523, 524, 525, 527, 530, 562, 563, 565, 567, 568, 681, 685, 689, 690, 693, 754, 755, 756, 758
Query Sequence
>Pf1N1B4_4584 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4584
MNRINPVSRRGFLKGSAVLGGGLVVAFVIPGANRFAHGAENQGNVFAPNAFLRIGNDNSI
TVLLGHSEMGQGIWTGLTMLIAEELDADWSKIRVEHAPASAADYGLPAFGGIQITGGSTS
TWMEFDRYRQAGAAARLMLIEAAAKRFDVAPSQIRTESGVVMAGDKRATYGELADDAGKL
PVPDPASIKFKEAKDWKIIGKPTKRLDTPEKITGQAKFGMDVQFDGLMTAMVARPPVFGG
SVKSFEGAEALAVPGVHKVVQVPTGVAVIADHYWAAKLGRDALKVEWDLGPNAGLDSQKL
LESFRKLAATPGTSASQAGDATATLGKAAKTIEAEYSVPYLAHAPMEPLNCTVKISKDKC
EIWTGTQFQTLDQMIAGKITGLKPEQVEIHTQFLGGGFGRRANPTSDFVSEAVYVAKAAG
GPVKTVWAREDDIRGGYYRSAFLHQARIGLGADGMPMAWKHVLVGQSILTGTSFAATMVK
DGIDKTSVEGVADSPYLEGLANHQVELHSPQTGISVLWLRSVGHTHTAFVMESLIDELAD
AAGKDPVEYRRALLKAHPRHLGVLNLAVEKANWKAPLPDGHALGVAVHESFGSYVAQVAE
VSQDNLAIRVHRVVCAVDCGIAVNPQSIAAQMESGITFGLSFTLHSKLTFKDGQVEQSNY
HDYQVLRLNEMPVVEVHIVPSSDKPGGIGEVGVPPVAPAVANAVFALTGQRLRELPLQLS
GV
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