SitesBLAST
Comparing 3610338 FitnessBrowser__Dino:3610338 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
34% identity, 82% coverage: 1:802/983 of query aligns to 9:786/786 of 1t3qB
- active site: Q224 (= Q214), A259 (≠ Q250), E336 (≠ Y327), V343 (vs. gap), R371 (= R360), E743 (= E758), S744 (≠ G759)
- binding pterin cytosine dinucleotide: G254 (≠ S245), F255 (= F246), R371 (= R360), S506 (≠ Q504), G507 (= G505), Q508 (= Q506), H510 (= H508), T513 (≠ V511), Y545 (= Y547), S547 (= S549), G549 (≠ F551), A550 (= A552), C666 (= C681), I670 (≠ L685), I674 (≠ M689), V675 (= V690), Q678 (= Q693), K739 (= K754), G740 (= G755), M741 (≠ V756), G742 (= G757)
1ffvB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava (see paper)
32% identity, 81% coverage: 5:804/983 of query aligns to 11:796/797 of 1ffvB
- active site: Q231 (= Q214), V266 (≠ Q250), P343 (≠ Y327), I349 (≠ L333), R378 (≠ N359), C379 (≠ R360), E751 (= E758), S752 (≠ G759)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G260 (= G244), G261 (≠ S245), F262 (= F246), G263 (= G247), A376 (vs. gap), R378 (≠ N359), C379 (≠ R360), Q516 (= Q504), G517 (= G505), Q518 (= Q506), H520 (= H508), T523 (≠ V511), Y556 (= Y547), G557 (≠ S548), S558 (= S549), S560 (≠ F551), T561 (≠ A552), C674 (= C681), I678 (≠ L685), I683 (≠ V690), Q686 (= Q693), K747 (= K754), G748 (= G755), V749 (= V756), A750 (≠ G757), E751 (= E758)
1ffuB Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
32% identity, 81% coverage: 5:804/983 of query aligns to 11:796/797 of 1ffuB
- active site: Q231 (= Q214), V266 (≠ Q250), P343 (≠ Y327), I349 (≠ L333), R378 (≠ N359), C379 (≠ R360), E751 (= E758), S752 (≠ G759)
- binding cytidine-5'-diphosphate: Q518 (= Q506), H520 (= H508), T523 (≠ V511), S558 (= S549), S560 (≠ F551), T561 (≠ A552), C674 (= C681), T676 (= T683), I678 (≠ L685), I683 (≠ V690), K747 (= K754), G748 (= G755), V749 (= V756), A750 (≠ G757)
P19913 Carbon monoxide dehydrogenase large chain; CO dehydrogenase subunit L; CO-DH L; EC 1.2.5.3 from Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava) (see paper)
31% identity, 80% coverage: 14:804/983 of query aligns to 26:802/803 of P19913
- R384 (≠ N359) modified: 4-hydroxyarginine
7dqxD Crystal structure of xanthine dehydrogenase family protein
32% identity, 76% coverage: 8:758/983 of query aligns to 8:728/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G244), S248 (= S245), F249 (= F246), R363 (= R360), V491 (≠ Q504), G492 (= G505), Q493 (= Q506), G494 (= G507), V498 (= V511), S530 (≠ N546), W531 (≠ Y547), S532 (= S548), S533 (= S549), R534 (= R550), S535 (≠ F551), T536 (≠ A552), T658 (≠ M689), T659 (≠ V690), Q662 (= Q693), G725 (= G755), L726 (≠ V756), G727 (= G757), E728 (= E758)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
30% identity, 78% coverage: 12:777/983 of query aligns to 21:776/803 of 1n60B
- active site: Q234 (= Q214), V269 (≠ Q250), P346 (≠ Y327), I352 (≠ L333), R381 (≠ N359), C382 (≠ R360), E757 (= E758), S758 (≠ G759)
- binding pterin cytosine dinucleotide: G264 (≠ S245), F265 (= F246), R381 (≠ N359), Q522 (= Q504), G523 (= G505), Q524 (= Q506), H526 (= H508), T529 (≠ V511), T561 (≠ N546), Y562 (= Y547), G563 (≠ S548), S564 (= S549), S566 (≠ F551), T567 (≠ A552), C680 (= C681), I684 (≠ L685), I688 (≠ M689), I689 (≠ V690), Q692 (= Q693), K753 (= K754), G754 (= G755), V755 (= V756), E757 (= E758)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F246), G266 (= G247), Y562 (= Y547), G563 (≠ S548), E757 (= E758)
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
30% identity, 78% coverage: 12:777/983 of query aligns to 22:777/804 of 1n62B
- active site: Q235 (= Q214), V270 (≠ Q250), P347 (≠ Y327), I353 (≠ L333), R382 (≠ N359), C383 (≠ R360), E758 (= E758), S759 (≠ G759)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G247), V379 (≠ L358), A380 (vs. gap), R382 (≠ N359), C383 (≠ R360), F385 (= F362), Y563 (= Y547), G564 (≠ S548), E758 (= E758)
- binding pterin cytosine dinucleotide: G265 (≠ S245), F266 (= F246), R382 (≠ N359), Q523 (= Q504), G524 (= G505), Q525 (= Q506), H527 (= H508), T530 (≠ V511), T562 (≠ N546), Y563 (= Y547), G564 (≠ S548), S565 (= S549), S567 (≠ F551), T568 (≠ A552), C681 (= C681), I685 (≠ L685), I689 (≠ M689), I690 (≠ V690), Q693 (= Q693), K754 (= K754), G755 (= G755), V756 (= V756), G757 (= G757), E758 (= E758)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
30% identity, 78% coverage: 12:777/983 of query aligns to 22:777/804 of 1n5wB
- active site: Q235 (= Q214), V270 (≠ Q250), P347 (≠ Y327), I353 (≠ L333), R382 (≠ N359), C383 (≠ R360), E758 (= E758), S759 (≠ G759)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G247), A380 (vs. gap), R382 (≠ N359), C383 (≠ R360), Y563 (= Y547), G564 (≠ S548), E758 (= E758)
- binding pterin cytosine dinucleotide: G265 (≠ S245), F266 (= F246), R382 (≠ N359), Q523 (= Q504), G524 (= G505), Q525 (= Q506), H527 (= H508), T530 (≠ V511), T562 (≠ N546), Y563 (= Y547), S565 (= S549), S567 (≠ F551), T568 (≠ A552), C681 (= C681), I685 (≠ L685), I689 (≠ M689), I690 (≠ V690), Q693 (= Q693), K754 (= K754), G755 (= G755), V756 (= V756), E758 (= E758)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
30% identity, 78% coverage: 12:777/983 of query aligns to 22:777/804 of 1zxiB
- active site: Q235 (= Q214), V270 (≠ Q250), P347 (≠ Y327), I353 (≠ L333), R382 (≠ N359), C383 (≠ R360), E758 (= E758), S759 (≠ G759)
- binding copper (ii) ion: C383 (≠ R360), S384 (≠ G361), E758 (= E758)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F246), G267 (= G247), A380 (vs. gap), Y381 (vs. gap), R382 (≠ N359), C383 (≠ R360), Y563 (= Y547), G564 (≠ S548), E758 (= E758)
- binding pterin cytosine dinucleotide: G265 (≠ S245), F266 (= F246), R382 (≠ N359), Q523 (= Q504), G524 (= G505), Q525 (= Q506), H527 (= H508), T530 (≠ V511), T562 (≠ N546), Y563 (= Y547), S565 (= S549), S567 (≠ F551), T568 (≠ A552), C681 (= C681), I685 (≠ L685), I689 (≠ M689), I690 (≠ V690), Q693 (= Q693), K754 (= K754), G755 (= G755), V756 (= V756), E758 (= E758)
P19919 Carbon monoxide dehydrogenase large chain; CO dehydrogenase subunit L; CO-DH L; EC 1.2.5.3 from Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) (Oligotropha carboxidovorans) (see 2 papers)
30% identity, 78% coverage: 12:777/983 of query aligns to 27:782/809 of P19919
- C388 (≠ R360) binding
- E763 (= E758) binding
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
30% identity, 78% coverage: 12:777/983 of query aligns to 23:778/805 of 1n63B
- active site: Q236 (= Q214), V271 (≠ Q250), P348 (≠ Y327), I354 (≠ L333), R383 (≠ N359), C384 (≠ R360), E759 (= E758), S760 (≠ G759)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G247), A381 (vs. gap), R383 (≠ N359), C384 (≠ R360), Y564 (= Y547), G565 (≠ S548), E759 (= E758)
- binding pterin cytosine dinucleotide: G266 (≠ S245), F267 (= F246), R383 (≠ N359), Q524 (= Q504), G525 (= G505), Q526 (= Q506), H528 (= H508), T531 (≠ V511), T563 (≠ N546), Y564 (= Y547), S566 (= S549), S568 (≠ F551), T569 (≠ A552), C682 (= C681), I686 (≠ L685), I690 (≠ M689), I691 (≠ V690), Q694 (= Q693), K755 (= K754), G756 (= G755), V757 (= V756), E759 (= E758)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
29% identity, 79% coverage: 19:798/983 of query aligns to 16:754/761 of 1rm6A
- active site: Q206 (= Q214), T241 (≠ Q250), Y318 (= Y327), L322 (vs. gap), R350 (= R360), E718 (= E758), G719 (= G759)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G244), G236 (≠ S245), F237 (= F246), G238 (= G247), R350 (= R360), I473 (≠ Q504), G474 (= G505), Q475 (= Q506), G476 (= G507), Y513 (= Y547), S514 (= S548), S515 (= S549), V517 (≠ F551), T518 (≠ A552), L646 (= L685), N647 (≠ H686), V651 (= V690), Q654 (= Q693), K714 (= K754), E715 (≠ G755), A716 (≠ V756), S717 (≠ G757), E718 (= E758)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
29% identity, 79% coverage: 19:798/983 of query aligns to 24:762/769 of O33819
4zohA Crystal structure of glyceraldehyde oxidoreductase (see paper)
29% identity, 78% coverage: 12:776/983 of query aligns to 9:686/701 of 4zohA
- active site: Q186 (≠ F217), I219 (≠ Q250), V298 (vs. gap), S300 (vs. gap), M304 (vs. gap), R332 (= R360), E668 (= E758), A669 (≠ G759)
- binding pterin cytosine dinucleotide: G213 (= G244), A214 (≠ S245), F215 (= F246), R332 (= R360), H442 (≠ Q504), G443 (= G505), Q444 (= Q506), D446 (≠ H508), W482 (≠ Y547), S484 (= S549), T486 (≠ F551), V487 (≠ A552), I594 (≠ L685), N595 (≠ H686), L598 (≠ M689), Q602 (= Q693), K664 (= K754), G665 (= G755), I666 (≠ V756), G667 (= G757), E668 (= E758)
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)
31% identity, 39% coverage: 6:389/983 of query aligns to 8:380/425 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)
31% identity, 39% coverage: 6:389/983 of query aligns to 7:379/420 of 3hrdE
- active site: Q207 (= Q214), L242 (≠ I248), R318 (= R328), H322 (≠ N332), R350 (= R360)
- binding calcium ion: T206 (≠ N212), N208 (≠ G215), D212 (≠ I219), K241 (vs. gap), L242 (≠ I248), D243 (≠ K249)
- binding pterin cytosine dinucleotide: G237 (≠ S245), F238 (= F246), R350 (= R360)
- binding selenium atom: F238 (= F246), A348 (≠ L358), F349 (≠ N359), R350 (= R360)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
31% identity, 39% coverage: 6:389/983 of query aligns to 7:379/420 of 3hrdA
- active site: Q207 (= Q214), L242 (≠ I248), R318 (= R328), H322 (≠ N332), R350 (= R360)
- binding pterin cytosine dinucleotide: G236 (= G244), G237 (≠ S245), F238 (= F246), R350 (= R360)
- binding magnesium ion: T206 (≠ N212), N208 (≠ G215), D212 (≠ I219), K241 (vs. gap), L242 (≠ I248), D243 (≠ K249), T305 (≠ V314), Y308 (= Y317), A309 (≠ L318), S346 (≠ T356)
- binding nicotinic acid: A314 (= A324), R318 (= R328), F352 (= F362)
- binding selenium atom: F238 (= F246), G239 (= G247), A348 (≠ L358), F349 (≠ N359), R350 (= R360)
Q8GUQ8 Xanthine dehydrogenase 1; AtXDH1; EC 1.17.1.4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
24% identity, 80% coverage: 19:805/983 of query aligns to 611:1349/1361 of Q8GUQ8
- E831 (≠ Q250) mutation to A: Loss of activity.
- R909 (= R328) mutation to A: Decreases activity 12-fold.
- E1297 (= E758) mutation to A: Decreases activity 40-fold.
Sites not aligning to the query:
- 364 W→A: Decreases activity 8-fold.
- 421 Y→A: Decreases activity 4-fold.
Q06278 Aldehyde oxidase; Aldehyde oxidase 1; Azaheterocycle hydroxylase; EC 1.2.3.1; EC 1.17.3.- from Homo sapiens (Human) (see 3 papers)
23% identity, 82% coverage: 2:803/983 of query aligns to 576:1320/1338 of Q06278
- R802 (≠ D241) to C: decreases homodimerization but nearly no effect on kinetic parameters; dbSNP:rs41309768
- AF 806:807 (≠ SF 245:246) binding
- R921 (= R360) 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
- M1047 (≠ Q504) binding
- GSVV 1088:1091 (≠ -SRF 549:551) binding
- N1135 (= N597) to 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
- Q1203 (= Q693) binding
- L1268 (≠ V756) binding
- G1269 (= G757) mutation to R: No effect on dimerization. Loss of oxidase activity.
- S1271 (≠ G759) to L: no effect on dimerization; no effect on oxidase activity; dbSNP:rs141786030
- H1297 (vs. gap) to 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
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
4uhxA Human aldehyde oxidase in complex with phthalazine and thioridazine (see paper)
23% identity, 82% coverage: 2:803/983 of query aligns to 541:1274/1290 of 4uhxA
- active site: Q732 (= Q214), V767 (vs. gap), M843 (≠ G331), K847 (vs. gap), R875 (= R360), G1223 (= G757), E1224 (= E758)
- binding 10-{2-[(2S)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: E542 (≠ K3), D543 (= D4), S1014 (≠ A517), R1015 (≠ E518), R1018 (≠ G521), M1019 (≠ L522), P1020 (≠ E523), W1079 (≠ F587)
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: E542 (≠ K3), D543 (= D4), S1014 (≠ A517), R1015 (≠ E518), R1018 (≠ G521), M1019 (≠ L522), P1020 (≠ E523)
Sites not aligning to the query:
- 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
- binding 10-{2-[(2R)-1-methylpiperidin-2-yl]ethyl}-2-(methylsulfanyl)-10H-phenothiazine: 540
Query Sequence
>3610338 FitnessBrowser__Dino:3610338
MPKDGLHQTMLRVEDAPLLTGRGQFFDDLPTPHGTLQAAILRSPYAHARITDISADAARR
LAGVHAVLTGEDYASVASPLMVGVKLPIECWPIARDKVRYVGEPVAVVLADDRYLAEDAL
DLIEVSYDTLAPVIDPLKALADDAPVLHDEMGGNLGADRRFSYGDPDSAFAEADHVVEIS
VRYPRNSCTPIETYGVLTRWNPHTRSYDVTSNFQGPFSIHPVVARALNVPGNRLRLRTPE
DSGGSFGIKQGVFPYIALLSACARLADRPVKWVEDRLEHLTASVSATNRAITLRAAVTAK
GRVTALDYDQVEDVGAYLRAPEPATLYRMHGNLCGAYDIANLRVRNRIVMTNKTPTGLNR
GFGGPQIYFALERLMQRIAIELGLDPVNVARDNLIPKGAFPYRTASGATYDSGDYQNAFD
TALKDGRYDALCQKRDAARAEGRLYGIGLAVAVEPSVSNMGYLSTALTPAERAKAGPKNG
AQSCATIAIDPVGSITVQIDSVPQGQGHKTVAASIVAERFGLEPGAITVVAAMDTGKDAW
SIAAGNYSSRFAAASAGAVRIAADRLRERIAAIAASQLNARPEDIEFENGKVFIASNPGA
ALVFARVASTGHWAPGTLPDGIAAPMRETAIWTAPELTAPTDEDGINSSLCHAFIFDFCG
VEIDPVTHEARVDHYVTMHDCGTILHEGMVEGQIRGAFAQAVGAALYEEYVYDDDGAFLA
GTLADYPVPTVHEIPDLEILHTCTPSPLTPLGAKGVGEGNCMSTPVCIANAVADALAPAR
GNVDVTLPLSPARIASYLPDEPTAPEGIAQPRPSSGKGLSGQGEARVGAAPQEIWDLLMD
ADQLAAIIPGAHGVKRLSPTRFLADVTLGVGPVKGRYRVQVGLSDLDAPKSATLTGKAGG
ALGTGEGSGRVTLTPDGSGGTVIGYSYEAAVGGKVASVGGRLLDGAAKIVIGQFFAALGR
RAGDAPQPDGMIARIRGWIGGTR
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