SitesBLAST
Comparing SM_b20132 SM_b20132 dehydrogenase 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)
1rm6A Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
34% identity, 97% coverage: 19:766/772 of query aligns to 3:757/761 of 1rm6A
- active site: Q206 (= Q229), T241 (≠ Q264), Y318 (≠ G342), L322 (= L346), R350 (= R373), E718 (= E727), G719 (≠ D728)
- binding (molybdopterin-cytosine dinucleotide-s,s)-dioxo-aqua-molybdenum(v): G235 (= G258), G236 (= G259), F237 (= F260), G238 (= G261), R350 (= R373), I473 (≠ L495), G474 (= G496), Q475 (≠ T497), G476 (= G498), Y513 (≠ F535), S514 (≠ A536), S515 (= S537), V517 (≠ T539), T518 (= T540), L646 (≠ I652), N647 (≠ H653), V651 (≠ A657), Q654 (= Q660), K714 (= K723), E715 (≠ G724), A716 (≠ V725), S717 (≠ G726), E718 (= E727)
O33819 4-hydroxybenzoyl-CoA reductase subunit alpha; 4-HBCR subunit alpha; EC 1.1.7.1 from Thauera aromatica (see paper)
34% identity, 97% coverage: 19:766/772 of query aligns to 11:765/769 of O33819
1t3qB Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
32% identity, 97% coverage: 19:766/772 of query aligns to 14:785/786 of 1t3qB
- active site: Q224 (= Q229), A259 (≠ Q264), E336 (vs. gap), V343 (≠ A345), R371 (= R373), E743 (= E727), S744 (≠ D728)
- binding pterin cytosine dinucleotide: G254 (= G259), F255 (= F260), R371 (= R373), S506 (≠ L495), G507 (= G496), Q508 (≠ T497), H510 (≠ A499), T513 (≠ A502), Y545 (≠ F535), S547 (= S537), G549 (≠ T539), A550 (≠ T540), C666 (≠ I648), I670 (= I652), I674 (≠ A656), V675 (≠ A657), Q678 (= Q660), K739 (= K723), G740 (= G724), M741 (≠ V725), G742 (= G726)
7dqxD Crystal structure of xanthine dehydrogenase family protein
30% identity, 96% coverage: 19:761/772 of query aligns to 6:764/770 of 7dqxD
- binding pterin cytosine dinucleotide: G247 (= G258), S248 (≠ G259), F249 (= F260), R363 (= R373), V491 (≠ L495), G492 (= G496), Q493 (≠ T497), G494 (= G498), V498 (≠ A502), S530 (≠ A534), W531 (≠ F535), S532 (≠ A536), S533 (= S537), R534 (≠ H538), S535 (≠ T539), T536 (= T540), T658 (≠ A656), T659 (≠ A657), Q662 (= Q660), G725 (= G724), L726 (≠ V725), G727 (= G726), E728 (= E727)
3hrdE Crystal structure of nicotinate dehydrogenase (see paper)
40% identity, 52% coverage: 14:411/772 of query aligns to 2:388/420 of 3hrdE
- active site: Q207 (= Q229), L242 (≠ Q264), R318 (≠ V341), H322 (≠ A345), R350 (= R373)
- binding calcium ion: T206 (= T228), N208 (≠ S230), D212 (≠ V234), K241 (= K263), L242 (≠ Q264), D243 (= D265)
- binding pterin cytosine dinucleotide: G237 (= G259), F238 (= F260), R350 (= R373)
- binding selenium atom: F238 (= F260), A348 (= A371), F349 (= F372), R350 (= R373)
3hrdA Crystal structure of nicotinate dehydrogenase (see paper)
40% identity, 52% coverage: 14:411/772 of query aligns to 2:388/420 of 3hrdA
- active site: Q207 (= Q229), L242 (≠ Q264), R318 (≠ V341), H322 (≠ A345), R350 (= R373)
- binding pterin cytosine dinucleotide: G236 (= G258), G237 (= G259), F238 (= F260), R350 (= R373)
- binding magnesium ion: T206 (= T228), N208 (≠ S230), D212 (≠ V234), K241 (= K263), L242 (≠ Q264), D243 (= D265), T305 (≠ S328), Y308 (= Y331), A309 (≠ G332), S346 (≠ A369)
- binding nicotinic acid: A314 (≠ G337), R318 (≠ V341), F352 (≠ Y375)
- binding selenium atom: F238 (= F260), G239 (= G261), A348 (= A371), F349 (= F372), R350 (= R373)
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)
39% identity, 52% coverage: 14:411/772 of query aligns to 3:389/425 of Q0QLF2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:425 modified: mature protein, Nicotinate dehydrogenase large molybdopterin subunit
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)
29% identity, 94% coverage: 19:744/772 of query aligns to 21:780/809 of P19919
- C388 (vs. gap) binding
- E763 (= E727) binding
1n62B Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 16:775/804 of 1n62B
- active site: Q235 (= Q229), V270 (≠ Q264), P347 (= P336), I353 (≠ V341), R382 (= R373), C383 (vs. gap), E758 (= E727), S759 (≠ D728)
- binding cu(i)-s-mo(iv)(=o)o-nbic cluster: G267 (= G261), V379 (vs. gap), A380 (= A371), R382 (= R373), C383 (vs. gap), F385 (≠ Y375), Y563 (≠ F535), G564 (≠ A536), E758 (= E727)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R373), Q523 (≠ L495), G524 (= G496), Q525 (≠ T497), H527 (≠ A499), T530 (≠ A502), T562 (≠ A534), Y563 (≠ F535), G564 (≠ A536), S565 (= S537), S567 (≠ T539), T568 (= T540), C681 (≠ I648), I685 (= I652), I689 (≠ A656), I690 (≠ A657), Q693 (= Q660), K754 (= K723), G755 (= G724), V756 (= V725), G757 (= G726), E758 (= E727)
1n5wB Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 16:775/804 of 1n5wB
- active site: Q235 (= Q229), V270 (≠ Q264), P347 (= P336), I353 (≠ V341), R382 (= R373), C383 (vs. gap), E758 (= E727), S759 (≠ D728)
- binding cu(i)-s-mo(vi)(=o)oh cluster: G267 (= G261), A380 (= A371), R382 (= R373), C383 (vs. gap), Y563 (≠ F535), G564 (≠ A536), E758 (= E727)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R373), Q523 (≠ L495), G524 (= G496), Q525 (≠ T497), H527 (≠ A499), T530 (≠ A502), T562 (≠ A534), Y563 (≠ F535), S565 (= S537), S567 (≠ T539), T568 (= T540), C681 (≠ I648), I685 (= I652), I689 (≠ A656), I690 (≠ A657), Q693 (= Q660), K754 (= K723), G755 (= G724), V756 (= V725), E758 (= E727)
1n60B Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide- inactivated form (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 15:774/803 of 1n60B
- active site: Q234 (= Q229), V269 (≠ Q264), P346 (= P336), I352 (≠ V341), R381 (= R373), C382 (vs. gap), E757 (= E727), S758 (≠ D728)
- binding pterin cytosine dinucleotide: G264 (= G259), F265 (= F260), R381 (= R373), Q522 (≠ L495), G523 (= G496), Q524 (≠ T497), H526 (≠ A499), T529 (≠ A502), T561 (≠ A534), Y562 (≠ F535), G563 (≠ A536), S564 (= S537), S566 (≠ T539), T567 (= T540), C680 (≠ I648), I684 (= I652), I688 (≠ A656), I689 (≠ A657), Q692 (= Q660), K753 (= K723), G754 (= G724), V755 (= V725), E757 (= E727)
- binding mo(vi)(=o)(oh)2 cluster: F265 (= F260), G266 (= G261), Y562 (≠ F535), G563 (≠ A536), E757 (= E727)
1zxiB Reconstituted co dehydrogenase from oligotropha carboxidovorans (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 16:775/804 of 1zxiB
- active site: Q235 (= Q229), V270 (≠ Q264), P347 (= P336), I353 (≠ V341), R382 (= R373), C383 (vs. gap), E758 (= E727), S759 (≠ D728)
- binding copper (ii) ion: C383 (vs. gap), S384 (≠ G374), E758 (= E727)
- binding cu(i)-s-mo(vi)(=o)oh cluster: F266 (= F260), G267 (= G261), A380 (= A371), Y381 (≠ F372), R382 (= R373), C383 (vs. gap), Y563 (≠ F535), G564 (≠ A536), E758 (= E727)
- binding pterin cytosine dinucleotide: G265 (= G259), F266 (= F260), R382 (= R373), Q523 (≠ L495), G524 (= G496), Q525 (≠ T497), H527 (≠ A499), T530 (≠ A502), T562 (≠ A534), Y563 (≠ F535), S565 (= S537), S567 (≠ T539), T568 (= T540), C681 (≠ I648), I685 (= I652), I689 (≠ A656), I690 (≠ A657), Q693 (= Q660), K754 (= K723), G755 (= G724), V756 (= V725), E758 (= E727)
1n63B Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state (see paper)
29% identity, 94% coverage: 19:744/772 of query aligns to 17:776/805 of 1n63B
- active site: Q236 (= Q229), V271 (≠ Q264), P348 (= P336), I354 (≠ V341), R383 (= R373), C384 (vs. gap), E759 (= E727), S760 (≠ D728)
- binding cu(i)-s-mo(iv)(=o)oh cluster: G268 (= G261), A381 (= A371), R383 (= R373), C384 (vs. gap), Y564 (≠ F535), G565 (≠ A536), E759 (= E727)
- binding pterin cytosine dinucleotide: G266 (= G259), F267 (= F260), R383 (= R373), Q524 (≠ L495), G525 (= G496), Q526 (≠ T497), H528 (≠ A499), T531 (≠ A502), T563 (≠ A534), Y564 (≠ F535), S566 (= S537), S568 (≠ T539), T569 (= T540), C682 (≠ I648), I686 (= I652), I690 (≠ A656), I691 (≠ A657), Q694 (= Q660), K755 (= K723), G756 (= G724), V757 (= V725), E759 (= E727)
6a7xA Rat xanthine oxidoreductase, d428a variant, NAD bound form
28% identity, 98% coverage: 4:762/772 of query aligns to 533:1276/1295 of 6a7xA
- active site: Q740 (= Q229), E775 (≠ Q264), R853 (≠ V341), H857 (≠ A345), R885 (= R373), G1233 (= G726), E1234 (= E727)
- binding bicarbonate ion: R812 (= R300), H813 (= H301), I850 (≠ V338), A883 (= A371), F884 (= F372), F887 (≠ Y375), G888 (= G376), Q891 (= Q379)
- binding uric acid: E775 (≠ Q264), R853 (≠ V341), F887 (≠ Y375), F982 (≠ A466), T983 (≠ Y467), A1052 (= A536), E1234 (= E727)
Sites not aligning to the query:
- 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
P47989 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Homo sapiens (Human) (see 4 papers)
28% identity, 99% coverage: 4:766/772 of query aligns to 561:1313/1333 of P47989
- D584 (≠ L29) to A: in dbSNP:rs45491693
- R607 (≠ K51) to Q: in dbSNP:rs45442092
- K617 (≠ R61) to N: in dbSNP:rs45442398
- T623 (= T67) to I: in dbSNP:rs45448694
- I646 (≠ S98) to V: in dbSNP:rs17323225
- I703 (= I161) to V: in dbSNP:rs17011368
- L763 (≠ M224) to F: in a breast cancer sample; somatic mutation
- R791 (≠ I252) to G: in a breast cancer sample; somatic mutation; dbSNP:rs775646772
- T910 (≠ G370) to M: in dbSNP:rs669884
- C993 (≠ T449) modified: Disulfide link with 536, In oxidase form
- V1091 (≠ A547) to L: in dbSNP:rs45619033
- N1109 (≠ E569) to T: in dbSNP:rs45547640
- P1150 (= P603) to R: in dbSNP:rs1042036
- R1176 (≠ Q641) to C: in dbSNP:rs45624433
- R1296 (vs. gap) to W: in dbSNP:rs45564939
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
- 1318 modified: Disulfide link with 509, In oxidase form
6a7xB Rat xanthine oxidoreductase, d428a variant, NAD bound form
28% identity, 98% coverage: 4:762/772 of query aligns to 531:1278/1291 of 6a7xB
- active site: Q738 (= Q229), E773 (≠ Q264), R851 (≠ V341), H855 (≠ A345), R883 (= R373), G1231 (= G726), E1232 (= E727)
- binding bicarbonate ion: R810 (= R300), H811 (= H301), T880 (≠ G370), A881 (= A371), F885 (≠ Y375), G886 (= G376), Q889 (= Q379)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M207)
- binding uric acid: E773 (≠ Q264), R851 (≠ V341), F885 (≠ Y375), F980 (≠ A466), T981 (≠ Y467), A1049 (≠ F535), A1050 (= A536), E1232 (= E727)
Sites not aligning to the query:
- 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
2ckjA Human milk xanthine oxidoreductase
28% identity, 99% coverage: 4:766/772 of query aligns to 504:1256/1264 of 2ckjA
Sites not aligning to the query:
- 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
2e3tA Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l) (see paper)
28% identity, 98% coverage: 4:762/772 of query aligns to 533:1280/1291 of 2e3tA
- active site: Q740 (= Q229), E775 (≠ Q264), R853 (≠ V341), H857 (≠ A345), R885 (= R373), G1233 (= G726), E1234 (= E727)
- binding bicarbonate ion: R812 (= R300), H813 (= H301), I850 (≠ V338), T882 (≠ G370), A883 (= A371), F887 (≠ Y375), G888 (= G376), Q891 (= Q379)
- binding calcium ion: E713 (≠ T203), H714 (≠ P204), Y716 (= Y206), T809 (≠ G297), G810 (≠ R298), G840 (≠ S328), T843 (≠ Y331), E844 (≠ G332), S847 (≠ G335), S880 (≠ I368), N881 (≠ A369)
- binding fe2/s2 (inorganic) cluster: L717 (≠ M207)
- binding uric acid: E775 (≠ Q264), R853 (≠ V341), F887 (≠ Y375), F982 (≠ A466), T983 (≠ Y467), A1051 (≠ F535), A1052 (= A536), E1234 (= E727)
Sites not aligning to the query:
- 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
P22985 Xanthine dehydrogenase/oxidase; EC 1.17.1.4; EC 1.17.3.2 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 98% coverage: 4:762/772 of query aligns to 560:1307/1331 of P22985
- C992 (≠ T449) mutation to 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.
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.
- 1316 C→S: Abolishes conversion from the dehydrogenase form to the oxidase form; when associated with A-535 and R-992.
4yswA Structure of rat xanthine oxidoreductase, c-terminal deletion protein variant, nadh bound form (see paper)
28% identity, 98% coverage: 4:762/772 of query aligns to 531:1278/1286 of 4yswA
- active site: Q738 (= Q229), E773 (≠ Q264), R851 (≠ V341), H855 (≠ A345), R883 (= R373), G1231 (= G726), E1232 (= E727)
- binding bicarbonate ion: R810 (= R300), H811 (= H301), I848 (≠ V338), T880 (≠ G370), A881 (= A371), F882 (= F372), F885 (≠ Y375), G886 (= G376), Q889 (= Q379)
- binding calcium ion: G838 (≠ S328), T841 (≠ Y331), E842 (≠ G332), S845 (≠ G335), S878 (≠ I368), N879 (≠ A369)
- binding fe2/s2 (inorganic) cluster: L715 (≠ M207)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S1196 (= S690)
- binding uric acid: E773 (≠ Q264), R851 (≠ V341), F885 (≠ Y375), F980 (≠ A466), T981 (≠ Y467), A1050 (= A536), E1232 (= E727)
Sites not aligning to the query:
- 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
Query Sequence
>SM_b20132 SM_b20132 dehydrogenase
MNTYERIDRDLSDRDFTVVGKSVKRSDTLEKVTGTARYAGDVALPGMLHAKMKRSNIAHA
RIRSIDTSKALALKGVKAVLTHEDVPRVLHAGSPHPRSASVTKDQYILDDRVRYWGEGVA
AVAAVSEEIAERAVALIEVEYEPLPGLFTIEAASVPGAPPIHENGLDRNQVLPPVFVTRG
DVDRGFAEADLILEREYDLGRPTPAYMEPNVCVSQWDGNGKLTMWTSTQSAFMVRGTLAE
VLGVPLNKVRVIVDHMGGGFGAKQDLFQNEFLCALLARQTGRPVKMEFSRKETFLGGRSR
HPGKIWLKQGFTKDGRIVAREARVTFNSGAYGSHGPGVTNVGTAALTSLYRCENVRLEGR
CIYTNSPIAGAFRGYGVVQTYYALDLMMDEAAEKLGFDPAEFKLMNAVREGDIAPSGHPI
VGHGLGDCIRRVMEETNWHELRRREKPETVKRRGIGIGCEMHGSSAYPGIKEQGNAIVKM
NEDGTVTLITGTAGLGTGAHTALSQIVAEELGVPFEAVSVVQGDTDIVPWDIGAFASHTT
YLGGRAAQLAAADVRRQVLEHAAPMLKAEPENLAIRDGFVVVTNGSNRSIRLSEAVGPQR
GMPAVQLVGVGTYMPTKSYSFAAHFAEVEVDTETGEVAVLQVVPVHEIGRVIHPIAAAGQ
IEGGIQQGIGHTLSEDYVIDLTDGRSLNPSFVDYKMPLSMDMPSIRTIILETAPDPGGPY
GAKGVGEDPIIAIGPAIANAIYDAIGVRFHHYPITPEQVLNALKSKANETRQ
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