SitesBLAST
Comparing RR42_RS09125 FitnessBrowser__Cup4G11:RR42_RS09125 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
29% identity, 94% coverage: 46:755/755 of query aligns to 18:721/732 of 8gy3C
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): M38 (= M66), G39 (= G67), Q40 (= Q68), H41 (≠ G69), V42 (= V70), A45 (≠ G73), G79 (= G141), G80 (= G142), S81 (= S143), S83 (= S145), V84 (≠ L146), G374 (≠ A428), F375 (= F429), L379 (= L433), L499 (≠ W548), R500 (= R549), V624 (= V658), D625 (≠ N659), Q632 (= Q666), T687 (≠ Q721), G688 (= G722), L689 (≠ V723), G690 (= G724), E691 (= E725)
8emtB Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
26% identity, 47% coverage: 223:579/755 of query aligns to 488:836/1221 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
8emtA Cryo-em analysis of the human aldehyde oxidase from liver (see paper)
25% identity, 48% coverage: 219:579/755 of query aligns to 500:869/1254 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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
27% identity, 47% coverage: 223:579/755 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
Q06278 Aldehyde oxidase; Aldehyde oxidase 1; Azaheterocycle hydroxylase; EC 1.2.3.1; EC 1.17.3.- from Homo sapiens (Human) (see 3 papers)
26% identity, 47% coverage: 223:579/755 of query aligns to 580:951/1338 of Q06278
- R802 (≠ L424) to C: decreases homodimerization but nearly no effect on kinetic parameters; dbSNP:rs41309768
- AF 806:807 (= AF 428:429) binding
- R921 (= R549) to H: increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM; dbSNP:rs56199635
Sites not aligning to the query:
- 44 binding ; C→W: Disrupts protein stability.
- 49 binding
- 52 binding
- 74 binding
- 113 binding
- 114 binding
- 117 binding
- 149 binding
- 151 binding ; binding
- 264:271 binding
- 345 binding
- 354 binding
- 358 binding
- 367 binding
- 411 binding
- 1047 binding
- 1088:1091 binding
- 1135 N → S: increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate; dbSNP:rs55754655
- 1203 binding
- 1268 binding
- 1269 G→R: No effect on dimerization. Loss of oxidase activity.
- 1271 S → L: no effect on dimerization; no effect on oxidase activity; dbSNP:rs141786030
- 1297 H → R: increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate; dbSNP:rs3731722
7orcB Human aldehyde oxidase in complex with raloxifene (see paper)
26% identity, 47% coverage: 223:579/755 of query aligns to 543:914/1299 of 7orcB
Sites not aligning to the query:
- binding flavin-adenine dinucleotide: 43, 44, 228, 229, 230, 231, 232, 233, 234, 235, 236, 309, 310, 318, 319, 322, 323, 326, 328, 331, 332, 376, 403
- binding fe2/s2 (inorganic) cluster: 40, 41, 42, 44, 46, 47, 49, 69, 71, 111, 112, 114, 146, 148
- binding raloxifene: 417, 418, 419, 449, 451, 506, 507
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)
25% identity, 53% coverage: 218:618/755 of query aligns to 3:420/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
25% identity, 53% coverage: 218:618/755 of query aligns to 2:419/420 of 3hrdE
- active site: Q207 (= Q398), L242 (= L433), R318 (= R505), H322 (≠ P510), R350 (= R549)
- binding calcium ion: T206 (= T397), N208 (≠ L399), D212 (≠ A403), K241 (≠ R432), L242 (= L433), D243 (≠ E434)
- binding pterin cytosine dinucleotide: G237 (≠ A428), F238 (= F429), R350 (= R549)
- binding selenium atom: F238 (= F429), A348 (≠ F547), F349 (≠ W548), R350 (= R549)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
25% identity, 53% coverage: 218:618/755 of query aligns to 2:419/420 of 3hrdA
- active site: Q207 (= Q398), L242 (= L433), R318 (= R505), H322 (≠ P510), R350 (= R549)
- binding pterin cytosine dinucleotide: G236 (= G427), G237 (≠ A428), F238 (= F429), R350 (= R549)
- binding magnesium ion: T206 (= T397), N208 (≠ L399), D212 (≠ A403), K241 (≠ R432), L242 (= L433), D243 (≠ E434), T305 (= T492), Y308 (≠ S495), A309 (≠ Q496), S346 (vs. gap)
- binding nicotinic acid: A314 (= A501), R318 (= R505), F352 (≠ V551)
- binding selenium atom: F238 (= F429), G239 (= G430), A348 (≠ F547), F349 (≠ W548), R350 (= R549)
O54754 Aldehyde oxidase 1; Azaheterocycle hydroxylase 1; Retinal oxidase; EC 1.2.3.1; EC 1.17.3.- from Mus musculus (Mouse) (see paper)
24% identity, 48% coverage: 223:586/755 of query aligns to 579:953/1333 of O54754
- V806 (≠ L433) 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 (≠ L507) 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.
P47989 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Homo sapiens (Human) (see 4 papers)
25% identity, 48% coverage: 209:572/755 of query aligns to 555:936/1333 of P47989
- P555 (= P209) to S: in dbSNP:rs45577338
- D584 (≠ A233) to A: in dbSNP:rs45491693
- R607 (≠ S255) to Q: in dbSNP:rs45442092
- K617 (≠ T265) to N: in dbSNP:rs45442398
- T623 (≠ G271) to I: in dbSNP:rs45448694
- I646 (≠ V296) to V: in dbSNP:rs17323225
- I703 (≠ S341) to V: in dbSNP:rs17011368
- L763 (≠ V393) to F: in a breast cancer sample; somatic mutation
- R791 (≠ Q421) to G: in a breast cancer sample; somatic mutation; dbSNP:rs775646772
- T910 (≠ V545) 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
- 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
2ckjA Human milk xanthine oxidoreductase
24% identity, 49% coverage: 202:572/755 of query aligns to 493:879/1264 of 2ckjA
Sites not aligning to the query:
- active site: 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
5g5gC Escherichia coli periplasmic aldehyde oxidase (see paper)
27% identity, 51% coverage: 219:604/755 of query aligns to 14:416/731 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
2e1qA Crystal structure of human xanthine oxidoreductase mutant, glu803val (see paper)
25% identity, 48% coverage: 209:572/755 of query aligns to 529:910/1307 of 2e1qA
- active site: Q742 (= Q398), V777 (≠ L433), R855 (= R505), H859 (≠ A522), R887 (= R549)
- binding bicarbonate ion: R814 (= R469), H815 (≠ P470), I852 (≠ M502), F886 (= F547), F889 (≠ V551), G890 (= G552), Q893 (≠ H555)
- binding calcium ion: E715 (≠ A373), H716 (= H374), Y718 (≠ A376), T741 (= T397), T747 (≠ A403), S780 (≠ V435), T781 (≠ D436), S784 (= S439), T811 (≠ D466), G812 (≠ F467)
- binding fe2/s2 (inorganic) cluster: L719 (≠ V377)
- binding hydroxy(dioxo)molybdenum: F773 (= F429), G774 (= G430), R887 (= R549)
Sites not aligning to the query:
- active site: 1235, 1236
- 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: 1053, 1054, 1236
P77489 Aldehyde oxidoreductase molybdenum-binding subunit PaoC; EC 1.2.99.6 from Escherichia coli (strain K12) (see 2 papers)
27% identity, 51% coverage: 219:604/755 of query aligns to 14:416/732 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.
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: 209:572/755 of query aligns to 554:935/1331 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.
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
25% identity, 48% coverage: 209:572/755 of query aligns to 527:908/1295 of 6a7xA
- active site: Q740 (= Q398), E775 (≠ R432), R853 (= R505), H857 (≠ A522), R885 (= R549)
- binding bicarbonate ion: R812 (= R469), H813 (≠ P470), I850 (≠ M502), A883 (≠ G546), F884 (= F547), F887 (≠ V551), G888 (= G552), Q891 (≠ H555)
- binding uric acid: E775 (≠ R432), R853 (= R505), F887 (≠ V551)
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
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
25% identity, 48% coverage: 209:572/755 of query aligns to 527:908/1291 of 2e3tA
- active site: Q740 (= Q398), E775 (≠ R432), R853 (= R505), H857 (≠ A522), R885 (= R549)
- binding bicarbonate ion: R812 (= R469), H813 (≠ P470), I850 (≠ M502), T882 (≠ V545), A883 (≠ G546), F887 (≠ V551), G888 (= G552), Q891 (≠ H555)
- binding calcium ion: E713 (≠ A373), H714 (= H374), Y716 (≠ A376), T809 (≠ D466), G810 (≠ F467), G840 (≠ T492), T843 (≠ S495), E844 (≠ Q496), S847 (≠ V499), S880 (≠ V543), N881 (≠ P544)
- binding fe2/s2 (inorganic) cluster: L717 (≠ V377)
- binding uric acid: E775 (≠ R432), R853 (= R505), F887 (≠ V551)
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: 209:572/755 of query aligns to 525:906/1291 of 6a7xB
- active site: Q738 (= Q398), E773 (≠ R432), R851 (= R505), H855 (≠ A522), R883 (= R549)
- binding bicarbonate ion: R810 (= R469), H811 (≠ P470), T880 (≠ V545), A881 (≠ G546), F885 (≠ V551), G886 (= G552), Q889 (≠ H555)
- binding fe2/s2 (inorganic) cluster: L715 (≠ V377)
- binding uric acid: E773 (≠ R432), R851 (= R505), F885 (≠ V551)
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
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
25% identity, 48% coverage: 209:572/755 of query aligns to 525:906/1286 of 4yswA
- active site: Q738 (= Q398), E773 (≠ R432), R851 (= R505), H855 (≠ A522), R883 (= R549)
- binding bicarbonate ion: R810 (= R469), H811 (≠ P470), I848 (≠ M502), T880 (≠ V545), A881 (≠ G546), F882 (= F547), F885 (≠ V551), G886 (= G552), Q889 (≠ H555)
- binding calcium ion: G838 (≠ T492), T841 (≠ S495), E842 (≠ Q496), S845 (≠ V499), S878 (≠ V543), N879 (≠ P544)
- binding fe2/s2 (inorganic) cluster: L715 (≠ V377)
- binding uric acid: E773 (≠ R432), R851 (= R505), F885 (≠ V551)
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
Query Sequence
>RR42_RS09125 FitnessBrowser__Cup4G11:RR42_RS09125
MKRRAFLVAGIGGAGALLVGWSVLPPRQRLATSQPLPAVGTQVGLNGWVKVAADNTVTIM
MCRSEMGQGVHTGLAMVLADELDANWAQVKVEHAPVDKIYNNLEVVVEDLPFRADDDGVA
RHLAAWLTRKLMREIGEMVTGGSSSLNDLWNPMREAGASARAMLIGAAAARWNVPAGACR
AQDGKVLHPSGKTATFGELAAQAGQLPLPAKVALKTPSEFKLIGKDIRRIEAASKIDGTA
RFGIDVLPEGLLYASVTMCPTLGGTVASFDGAVAAAMPGIVKVLAVDAYNGGTGGVAVIA
DNAYRAMKALDAVKIVWNPGAAASLSSPEVSRRLAQALDASDGHAYYRHGDVDAALKSAA
KPVSAEYSAPYLAHGAVEPINCTVQVRDGAARVWVSTQLPGLARRAVSKVLGIDADKVDV
QPQLIGGAFGRRLEVDFISQAAAIARAGGGRPVQTIWSRVQDTTHDFYRPACLSRFKAGL
DGAGNLVAWHNTSASQAVVPAMLARLLGLPGLGIDKTTTEGAFDRPYEWPNARVGHVIVD
LPVPVGFWRSVGHSHQAFFTESFIDELAAAAGKDPVAFRAGLLARHPRHLAVLHMAADKA
GWAKPLGKTADGAARARGVALHEAYGSIVAQVAEVSVAPDKTVRVHRVVCAIDCGLPVNP
NLIRQQMESAIIFGLSAALFEEITIVDGQVHQKTFGDFPVIFMNNCPAIETYIMPSQDHP
QGVGEPGTPPIAPAVANALFALTGQRLRALPLKLA
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