SitesBLAST
Comparing SM_b20396 FitnessBrowser__Smeli:SM_b20396 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 13 hits to proteins with known functional sites (download)
P77324 Aldehyde oxidoreductase FAD-binding subunit PaoB; EC 1.2.99.6 from Escherichia coli (strain K12) (see paper)
52% identity, 99% coverage: 1:323/327 of query aligns to 1:313/318 of P77324
- 26:34 (vs. 26:34, 67% identical) binding
- T108 (= T108) binding
- C119 (= C119) binding
- C129 (= C129) binding
- C138 (= C138) binding
- C157 (= C157) binding
- D164 (= D164) binding
- I213 (= I212) binding
- K230 (= K230) binding
5g5gB Escherichia coli periplasmic aldehyde oxidase (see paper)
52% identity, 99% coverage: 1:323/327 of query aligns to 1:313/316 of 5g5gB
- binding flavin-adenine dinucleotide: K26 (= K26), F27 (≠ L27), I28 (≠ L28), A29 (≠ G29), G30 (= G30), G31 (= G31), T32 (= T32), N33 (= N33), L34 (= L34), G98 (= G98), A99 (= A99), L103 (≠ I103), A107 (= A107), T108 (= T108), A110 (= A110), G111 (= G111), N112 (= N112), L114 (≠ M114), Q115 (= Q115), R118 (= R118), P162 (= P162), S163 (= S163), D164 (= D164), L212 (= L211), I213 (= I212), K230 (= K230), Y237 (= Y237), A238 (= A238), F239 (= F239)
- binding iron/sulfur cluster: C119 (= C119), F122 (= F122), C129 (= C129), N130 (= N130), K131 (= K131), C138 (= C138), A139 (≠ D139), A140 (= A140), H148 (= H148), C157 (= C157), I158 (= I158), A159 (= A159)
5y6qB Crystal structure of an aldehyde oxidase from methylobacillus sp. Ky4400 (see paper)
44% identity, 99% coverage: 1:325/327 of query aligns to 1:330/330 of 5y6qB
- binding flavin-adenine dinucleotide: Q25 (≠ K26), I26 (≠ L27), L27 (= L28), A28 (≠ G29), G29 (= G30), G30 (= G31), T31 (= T32), T32 (≠ N33), Q33 (≠ L34), I50 (≠ V51), M74 (≠ N75), A97 (≠ G98), A98 (= A99), I102 (= I103), A106 (= A107), T107 (= T108), G110 (= G111), N111 (= N112), R113 (≠ M114), Q114 (= Q115), R115 (= R116), G164 (≠ S163), D165 (= D164), I213 (≠ L211), I214 (= I212), K232 (= K230), Y239 (= Y237), E240 (≠ A238), F241 (= F239)
- binding iron/sulfur cluster: C118 (= C119), Y121 (≠ F122), C130 (= C129), N131 (= N130), K132 (= K131), C139 (= C138), A140 (≠ D139), A141 (= A140), H149 (= H148), S157 (= S156), C158 (= C157), I159 (= I158), A160 (= A159)
O33820 4-hydroxybenzoyl-CoA reductase subunit beta; 4-HBCR subunit beta; EC 1.1.7.1 from Thauera aromatica (see paper)
37% identity, 82% coverage: 1:269/327 of query aligns to 4:263/324 of O33820
- 29:36 (vs. 26:34, 56% identical) binding
- T111 (= T108) binding
- N115 (= N112) binding
- Q118 (= Q115) binding
- D162 (= D164) binding
- K224 (= K230) binding
1rm6B Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica (see paper)
37% identity, 82% coverage: 1:269/327 of query aligns to 4:263/323 of 1rm6B
- binding flavin-adenine dinucleotide: P29 (≠ K26), L30 (= L27), G31 (= G29), A32 (≠ G30), G33 (= G31), T34 (= T32), D35 (≠ N33), L36 (= L34), L53 (≠ V51), V101 (≠ G98), A102 (= A99), H106 (≠ I103), A110 (= A107), T111 (= T108), G113 (≠ A110), G114 (= G111), N115 (= N112), C117 (≠ M114), Q118 (= Q115), H160 (≠ P162), G161 (≠ S163), D162 (= D164), L206 (= L211), L207 (≠ I212), K224 (= K230), V231 (≠ Y237), D232 (≠ A238), F233 (= F239), P234 (≠ A240)
- binding iron/sulfur cluster: C122 (= C119), F124 (= F122), C138 (= C138), L139 (≠ D139), K140 (≠ A140), C146 (≠ M147), H147 (= H148), V148 (≠ A149), C155 (= C157), Y156 (≠ I158), A157 (= A159)
1n5wC Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form (see paper)
29% identity, 95% coverage: 3:313/327 of query aligns to 5:271/287 of 1n5wC
- binding flavin-adenine dinucleotide: H35 (≠ T32), I101 (≠ G98), A102 (= A99), I106 (= I103), N115 (= N112), N123 (≠ S163), D124 (= D164), K185 (≠ S226), G191 (≠ R232), D192 (= D233), Y193 (≠ R234)
P19920 Carbon monoxide dehydrogenase medium chain; CO dehydrogenase subunit M; CO-DH M; EC 1.2.5.3 from Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) (Oligotropha carboxidovorans) (see 2 papers)
29% identity, 95% coverage: 3:313/327 of query aligns to 5:271/288 of P19920
4zohB Crystal structure of glyceraldehyde oxidoreductase (see paper)
27% identity, 97% coverage: 4:321/327 of query aligns to 6:273/274 of 4zohB
- active site: Y256 (≠ N306)
- binding flavin-adenine dinucleotide: R28 (≠ K26), P29 (≠ L27), L30 (= L28), A31 (≠ G29), G32 (= G30), G33 (= G31), H34 (≠ T32), S35 (≠ N33), L36 (= L34), I53 (≠ V51), H77 (≠ N75), I95 (≠ G98), G96 (≠ A99), V100 (≠ I103), G104 (≠ A107), T105 (= T108), G107 (≠ A110), G108 (= G111), S109 (≠ N112), S111 (≠ M114), H112 (≠ Q115), A117 (= A136), D118 (= D164), L155 (= L206), L160 (= L211), V161 (≠ I212), K178 (= K230), G184 (≠ S236), D185 (≠ A238), F186 (= F239)
7dqxE Crystal structure of xanthine dehydrogenase family protein
25% identity, 85% coverage: 3:279/327 of query aligns to 5:234/293 of 7dqxE
- binding flavin-adenine dinucleotide: K29 (= K26), I30 (≠ L27), I31 (≠ L28), A32 (≠ G29), G33 (= G30), G34 (= G31), Q35 (≠ T32), S36 (≠ N33), L37 (= L34), H78 (≠ N75), I101 (≠ G98), A102 (= A99), I106 (= I103), G110 (≠ A107), T111 (= T108), G113 (≠ A110), G114 (= G111), S115 (≠ N112), A117 (= A136), A122 (≠ P162), A123 (≠ S163), E124 (≠ D164), L166 (= L211), I167 (= I212), Y193 (= Y237)
1ffuC Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor (see paper)
27% identity, 80% coverage: 4:266/327 of query aligns to 6:220/287 of 1ffuC
- binding flavin-adenine dinucleotide: K29 (= K26), L30 (= L27), L31 (= L28), A32 (≠ G29), G33 (= G30), G34 (= G31), H35 (≠ T32), S36 (≠ N33), L37 (= L34), I54 (≠ V51), I101 (≠ G98), A102 (= A99), V106 (≠ I103), G110 (≠ A107), T111 (= T108), G114 (= G111), D115 (≠ N112), A117 (≠ M114), H118 (= H125), N123 (= N130), D124 (≠ K131), L161 (= L206), V166 (≠ L211), M167 (≠ I212), K185 (≠ S226), G191 (≠ R232), D192 (= D233), W193 (≠ R234)
1t3qC Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86 (see paper)
24% identity, 85% coverage: 3:281/327 of query aligns to 5:232/285 of 1t3qC
- binding flavin-adenine dinucleotide: I29 (≠ L27), I30 (≠ L28), A31 (≠ G29), G32 (= G30), G33 (= G31), Q34 (≠ T32), S35 (≠ N33), L36 (= L34), L53 (≠ V51), H77 (≠ N75), V100 (≠ G98), A101 (= A99), V105 (≠ I103), G109 (≠ A107), T110 (= T108), G112 (≠ A110), G113 (= G111), S114 (≠ N112), A116 (≠ M147), H117 (= H148), A122 (= A153), E123 (≠ D164), L160 (= L206), V165 (≠ L211), L166 (≠ I212), Y190 (≠ F239)
Q0QLF4 Nicotinate dehydrogenase FAD-subunit; NDH; Nicotinic acid hydroxylase FAD-subunit; NAH; EC 1.17.1.5 from Eubacterium barkeri (Clostridium barkeri) (see paper)
25% identity, 100% coverage: 1:327/327 of query aligns to 1:293/296 of Q0QLF4
- 29:36 (vs. 27:34, 50% identical) binding
- G101 (≠ A99) binding
- TIGGN 110:114 (≠ TVAGN 108:112) binding
- D123 (= D164) binding
- R160 (≠ E203) binding
- M169 (≠ I212) binding
- K187 (= K230) binding
3hrdG Crystal structure of nicotinate dehydrogenase (see paper)
25% identity, 88% coverage: 1:289/327 of query aligns to 1:247/292 of 3hrdG
- binding flavin-adenine dinucleotide: I29 (≠ L27), I30 (≠ L28), A31 (≠ G29), G32 (= G30), G33 (= G31), T34 (= T32), D35 (≠ N33), L36 (= L34), I53 (≠ V51), F77 (≠ N75), V100 (≠ G98), G101 (≠ A99), I105 (= I103), G109 (≠ A107), T110 (= T108), G112 (≠ A110), G113 (= G111), N114 (= N112), S116 (= S154), T117 (≠ D155), G122 (≠ S163), D123 (= D164), R160 (≠ E203), L163 (= L206), I168 (≠ L211), M169 (≠ I212), K187 (= K230)
Query Sequence
>SM_b20396 FitnessBrowser__Smeli:SM_b20396
MKSFAYARAADLEAAVKLLSKTPNAKLLGGGTNLVDLMRENIEQPDALVDVTGLPLDRIE
ERPDGGLVIGATVRNTAVAGHPVVRDRYPLLAQAIVFGASGQIRNMATVAGNLMQRTRCL
YFYDHAARCNKRAPGAGCDAIGGFNRMHAILGASDSCIATHPSDMCVALAALDAKVNVIG
PSGARTIAFEEFHRLPEDTPDIETDLQPGELITGIEIPPLGFARRSLYRKVRDRASYAFA
LVSVAAALEVDSGKVRNVRLALGGVAHKPWRATEAERVLAGANAGAESFRQAAEAELAPA
RGLAHNEFKIELAKRTIVGVLGELAGG
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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