SitesBLAST
Comparing CCNA_00092 FitnessBrowser__Caulo:CCNA_00092 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)
4bmsF Short chain alcohol dehydrogenase from ralstonia sp. Dsm 6428 in complex with NADPH
41% identity, 85% coverage: 4:256/296 of query aligns to 3:247/249 of 4bmsF
- active site: S137 (= S141), H147 (≠ P151), Y150 (= Y154), K154 (= K158), Q195 (≠ P199)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G14), N15 (≠ C16), S16 (= S17), I18 (= I19), R38 (≠ E42), R39 (≠ K43), A59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), S88 (≠ A89), G89 (= G90), V110 (≠ L112), S137 (= S141), Y150 (= Y154), K154 (= K158), G181 (= G185), I183 (= I187), T185 (= T189), I187 (= I191)
6ihhA Crystal structure of rasadh f12 from ralstonia.Sp in complex with NADPH and a6o
41% identity, 85% coverage: 4:256/296 of query aligns to 3:247/249 of 6ihhA
- binding (2R,3S)-2-ethyl-2-[(2E)-2-(6-methoxy-3,4-dihydro-2H-naphthalen-1-ylidene)ethyl]-3-oxidanyl-cyclopentan-1-one: S137 (= S141), H147 (≠ P151), Y150 (= Y154), L188 (≠ F192), L246 (≠ I255)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G14), N15 (≠ C16), S16 (= S17), G17 (= G18), I18 (= I19), R38 (≠ E42), R39 (≠ K43), D60 (= D61), V61 (= V62), N87 (= N88), S88 (≠ A89), G89 (= G90), V110 (≠ L112), T135 (= T139), S137 (= S141), Y150 (= Y154), K154 (= K158), P180 (= P184), G181 (= G185), A182 (≠ L186), I183 (= I187), T185 (= T189), S187 (≠ I191)
F1SWA0 Zerumbone synthase; EC 1.1.1.326 from Zingiber zerumbet (Shampoo ginger) (Amomum zerumbet) (see paper)
34% identity, 87% coverage: 4:261/296 of query aligns to 2:262/267 of F1SWA0
- S142 (= S141) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- S144 (≠ A143) mutation to A: Increased oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- Y155 (= Y154) mutation to A: Strong reduction in oxidoreductase activity toward 8-hydroxy-alpha-humulene and borneol.
- K159 (= K158) mutation to A: Abolishes all oxidoreductase activity.
5itvA Crystal structure of bacillus subtilis bacc dihydroanticapsin 7- dehydrogenase in complex with nadh (see paper)
35% identity, 86% coverage: 1:256/296 of query aligns to 1:253/255 of 5itvA
- active site: G18 (= G18), S141 (= S141), Y154 (= Y154), K158 (= K158)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), S17 (= S17), G18 (= G18), I19 (= I19), D38 (= D38), I39 (≠ L39), T61 (≠ C60), I63 (≠ V62), N89 (= N88), G91 (= G90), T139 (= T139), S141 (= S141), Y154 (= Y154), K158 (= K158), P184 (= P184), G185 (= G185), I186 (≠ L186), I187 (= I187)
4nbuB Crystal structure of fabg from bacillus sp (see paper)
37% identity, 85% coverage: 4:255/296 of query aligns to 4:242/244 of 4nbuB
- active site: G18 (= G18), N111 (≠ L113), S139 (= S141), Q149 (≠ P151), Y152 (= Y154), K156 (= K158)
- binding acetoacetyl-coenzyme a: D93 (≠ P95), K98 (≠ E100), S139 (= S141), N146 (≠ G148), V147 (≠ F149), Q149 (≠ P151), Y152 (= Y154), F184 (≠ L186), M189 (≠ I191), K200 (≠ Q205)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), N17 (≠ S17), G18 (= G18), I19 (= I19), D38 (= D38), F39 (≠ L39), V59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (≠ H91), T137 (= T139), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), F184 (≠ L186), T185 (≠ I187), T187 (= T189), M189 (≠ I191)
Q9C826 Xanthoxin dehydrogenase; Protein ABSCISIC ACID DEFICIENT 2; Protein GLUCOSE INSENSITIVE 1; Protein IMPAIRED SUCROSE INDUCTION 4; Protein SALOBRENO 3; Protein SALT RESISTANT 1; Protein SUGAR INSENSITIVE 4; Short-chain alcohol dehydrogenase ABA2; Short-chain dehydrogenase reductase 1; AtSDR1; Xanthoxin oxidase; EC 1.1.1.288 from Arabidopsis thaliana (Mouse-ear cress) (see 3 papers)
37% identity, 87% coverage: 4:261/296 of query aligns to 17:280/285 of Q9C826
- G28 (= G15) mutation to R: In aba2-12/sre1-2; reduced absicic acid synthesis.
- A45 (= A32) mutation to V: In aba2-4/sis4-2; reduced absicic acid synthesis.
- R145 (≠ P126) mutation to C: In gin1-2; reduced absicic acid synthesis.
- G162 (≠ A143) mutation to R: In aba2-3/sis4-1; reduced absicic acid synthesis.
- S176 (≠ A157) mutation to F: In aba2-13/san3-1; reduced absicic acid synthesis.
- A236 (≠ P215) mutation to V: In isi4; reduced absicic acid synthesis.
- S264 (≠ T245) mutation to N: In aba2-1; reduced absicic acid synthesis.
6zzsD Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and 3-oxovalerate (see paper)
36% identity, 86% coverage: 1:256/296 of query aligns to 1:259/261 of 6zzsD
- active site: G18 (= G18), S143 (= S141), Y156 (= Y154)
- binding nicotinamide-adenine-dinucleotide: G14 (= G14), S17 (= S17), I19 (= I19), D38 (= D38), M39 (≠ L39), D64 (= D61), V65 (= V62), N91 (= N88), A92 (= A89), G93 (= G90), M141 (≠ T139), A142 (= A140), S143 (= S141), Y156 (= Y154), K160 (= K158), P186 (= P184), G187 (= G185), V189 (≠ I187), T191 (= T189), L193 (≠ I191)
- binding 3-oxidanylidenepentanoic acid: Q95 (≠ G92), S143 (= S141), N145 (≠ A143), K153 (≠ P151), Y156 (= Y154), Q197 (≠ E201)
6zzqA Crystal structure of (r)-3-hydroxybutyrate dehydrogenase from acinetobacter baumannii complexed with NAD+ and acetoacetate (see paper)
36% identity, 85% coverage: 5:256/296 of query aligns to 4:258/260 of 6zzqA
- active site: G17 (= G18), S142 (= S141), Y155 (= Y154)
- binding acetoacetic acid: Q94 (≠ G92), S142 (= S141), K152 (≠ P151), Y155 (= Y154), Q196 (≠ E201)
- binding nicotinamide-adenine-dinucleotide: G13 (= G14), S16 (= S17), G17 (= G18), I18 (= I19), D37 (= D38), M38 (≠ L39), D63 (= D61), V64 (= V62), N90 (= N88), A91 (= A89), G92 (= G90), M140 (≠ T139), A141 (= A140), S142 (= S141), Y155 (= Y154), K159 (= K158), Y187 (≠ L186), V188 (≠ I187), T190 (= T189)
6zyzA Structure of the borneol dehydrogenases of salvia rosmarinus with NAD+ (see paper)
35% identity, 86% coverage: 4:257/296 of query aligns to 2:248/259 of 6zyzA
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S15 (= S17), G16 (= G18), I17 (= I19), D36 (= D38), I37 (≠ L39), Q38 (= Q40), C58 (= C60), D59 (= D61), V60 (= V62), N86 (= N88), A87 (= A89), V90 (≠ G92), I110 (≠ L112), T137 (= T139), Y152 (= Y154), K156 (= K158), V185 (≠ A194)
- binding (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol: P93 (= P95), N94 (≠ A96), S95 (= S97), D98 (≠ E100)
7djsD Crystal structure of isopiperitenol dehydrogenase from pseudomonas aeruginosa complexed with NAD
38% identity, 85% coverage: 5:256/296 of query aligns to 3:249/251 of 7djsD
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), G16 (= G18), I17 (= I19), D36 (= D38), L37 (= L39), C61 (= C60), D62 (= D61), V63 (= V62), N89 (= N88), A90 (= A89), T140 (= T139), S142 (= S141), Y155 (= Y154), K159 (= K158), A186 (≠ G185), V187 (≠ L186)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
36% identity, 84% coverage: 8:256/296 of query aligns to 3:248/250 of 2cfcA
- active site: G13 (= G18), S142 (= S141), Y155 (= Y154), K159 (= K158)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ G148), R152 (≠ P151), Y155 (= Y154), W195 (≠ A194), R196 (≠ S195)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), S12 (= S17), G13 (= G18), N14 (≠ I19), D33 (= D38), L34 (= L39), A59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I140 (≠ T139), P185 (= P184), G186 (= G185), M187 (≠ L186), I188 (= I187), T190 (= T189), P191 (≠ S190), M192 (≠ I191), T193 (≠ F192)
P9WGT1 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase; NADH-dependent 3alpha, 20beta-hydroxysteroid dehydrogenase; EC 1.1.1.53 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 87% coverage: 1:258/296 of query aligns to 1:241/260 of P9WGT1
- I6 (≠ N6) mutation to T: Maximal improvement in solubility; when associated with M-47 and K-69.
- RGM 17:19 (≠ SGI 17:19) binding
- D38 (= D38) binding
- V47 (≠ L47) mutation to M: Maximal improvement in solubility; when associated with T-6 and K-69.
- DV 61:62 (= DV 61:62) binding
- T69 (≠ A69) mutation to K: Maximal improvement in solubility; when associated with T-6 and M-47.
- N88 (= N88) binding
- S140 (= S141) mutation to A: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- Y153 (= Y154) binding ; mutation to F: Complete loss of both oxidation of androsterone and reduction of progesterone; when associated with T6; M-47 and K-69.
- K157 (= K158) binding
- 183:191 (vs. 184:195, 33% identical) binding
2hsdA The refined three-dimensional structure of 3alpha,20beta- hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases (see paper)
36% identity, 86% coverage: 5:259/296 of query aligns to 3:245/253 of 2hsdA
- active site: G16 (= G18), S138 (= S141), Y151 (= Y154), K155 (= K158)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), R15 (≠ S17), G16 (= G18), L17 (≠ I19), D36 (= D38), V37 (≠ L39), L58 (≠ C60), V60 (= V62), N86 (= N88), A87 (= A89), S138 (= S141), Y151 (= Y154), K155 (= K158), P181 (= P184), G182 (= G185), T184 (≠ I187)
1hdcA Mechanism of inhibition of 3alpha,20beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor (see paper)
36% identity, 86% coverage: 5:259/296 of query aligns to 3:245/253 of 1hdcA
- active site: G16 (= G18), S138 (= S141), Y151 (= Y154), K155 (= K158)
- binding carbenoxolone: S90 (≠ G93), T91 (= T94), G92 (≠ P95), L147 (≠ G150), Y151 (= Y154), M183 (≠ L186), M188 (≠ I191), T189 (≠ F192), T192 (≠ M196)
1nfqA Rv2002 gene product from mycobacterium tuberculosis (see paper)
34% identity, 86% coverage: 3:258/296 of query aligns to 2:240/244 of 1nfqA
- active site: G17 (= G18), S139 (= S141), Y152 (= Y154), K156 (= K158)
- binding Androsterone: L91 (≠ G92), E141 (≠ A143), C149 (≠ P151), Y152 (= Y154), V193 (≠ L198), I197 (≠ V202), F198 (≠ A203)
- binding 1,4-dihydronicotinamide adenine dinucleotide: R16 (≠ S17), G17 (= G18), M18 (≠ I19), D37 (= D38), L39 (≠ Q40), L59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), I137 (≠ T139), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), V185 (≠ I187), T187 (= T189), P188 (≠ S190), M189 (≠ I191), T190 (≠ S195)
1nffA Crystal structure of rv2002 gene product from mycobacterium tuberculosis (see paper)
34% identity, 86% coverage: 3:258/296 of query aligns to 2:240/244 of 1nffA
- active site: G17 (= G18), S139 (= S141), Y152 (= Y154), K156 (= K158)
- binding nicotinamide-adenine-dinucleotide: G13 (= G14), R16 (≠ S17), G17 (= G18), M18 (≠ I19), D37 (= D38), I38 (≠ L39), L39 (≠ Q40), L59 (≠ C60), D60 (= D61), V61 (= V62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (≠ H91), I137 (≠ T139), S139 (= S141), Y152 (= Y154), K156 (= K158), P182 (= P184), V185 (≠ I187), T187 (= T189), P188 (≠ S190), M189 (≠ I191), T190 (≠ S195)
Q94KL8 Secoisolariciresinol dehydrogenase; EC 1.1.1.331 from Podophyllum peltatum (American mandrake) (see 2 papers)
36% identity, 86% coverage: 3:256/296 of query aligns to 12:263/278 of Q94KL8
- GGAGGI 23:28 (≠ GGCSGI 14:19) binding
- D47 (= D38) binding
- V73 (= V62) binding
- N99 (= N88) binding
- S104 (≠ G92) binding
- S153 (= S141) mutation to A: Strongly reduces enzyme activity.
- S164 (≠ P151) binding
- Y167 (= Y154) active site, Proton donor/acceptor; mutation to A: Abolishes enzyme activity.
- K171 (= K158) binding ; mutation to A: Abolishes enzyme activity.
2bgmA X-ray structure of ternary-secoisolariciresinol dehydrogenase (see paper)
36% identity, 86% coverage: 3:256/296 of query aligns to 2:253/267 of 2bgmA
- active site: S143 (= S141), Y157 (= Y154), K161 (= K158)
- binding matairesinol: L93 (≠ H91), S94 (≠ G92), I144 (= I142), G152 (= G150), V153 (vs. gap), S154 (≠ P151), Y157 (= Y154), Y188 (≠ G185), I189 (≠ L186)
- binding nicotinamide-adenine-dinucleotide (acidic form): G13 (= G14), G16 (≠ S17), I18 (= I19), D37 (= D38), I38 (≠ L39), C61 (= C60), D62 (= D61), V63 (= V62), N89 (= N88), V90 (≠ A89), G91 (= G90), T141 (= T139), S143 (= S141), Y157 (= Y154), K161 (= K158), V190 (≠ I187)
2bglA X-ray structure of binary-secoisolariciresinol dehydrogenase (see paper)
36% identity, 86% coverage: 3:256/296 of query aligns to 2:253/267 of 2bglA
- active site: S143 (= S141), Y157 (= Y154), K161 (= K158)
- binding nicotinamide-adenine-dinucleotide (acidic form): G16 (≠ S17), G17 (= G18), I18 (= I19), D37 (= D38), I38 (≠ L39), V63 (= V62), N89 (= N88), G91 (= G90), T141 (= T139), A142 (= A140), S143 (= S141), Y157 (= Y154), K161 (= K158), V190 (≠ I187)
6zt2A 17beta-hydroxysteroid dehydrogenase type 14 variant s205 in complex with 3-chloro-2,6-difluorophenol
36% identity, 79% coverage: 24:258/296 of query aligns to 22:248/252 of 6zt2A
- binding beta-D-glucopyranose: W184 (≠ A188), T185 (= T189), P186 (≠ S190), E189 (≠ R200)
- binding nicotinamide-adenine-dinucleotide: D36 (= D38), K37 (≠ L39), D58 (= D61), V59 (= V62), N85 (= N88), L109 (= L112), S137 (= S141), Y150 (= Y154), K154 (= K158), P180 (= P184), G181 (= G185), N182 (≠ L186), I183 (= I187), T185 (= T189), L187 (≠ I191)
- binding 3-chloranyl-2,6-bis(fluoranyl)phenol: H89 (≠ G92), S137 (= S141), Y150 (= Y154), N182 (≠ L186), W188 (≠ F192)
Sites not aligning to the query:
Query Sequence
>CCNA_00092 FitnessBrowser__Caulo:CCNA_00092
MVGRLNGKVAVITGGCSGIGLGTVELFVAEGACVVAADLQDEKGRMLEQRFPDQVRFARC
DVTADDDLAKTMALAESSFGGLDILFNNAGHGGTPASVPELTAEAWDKTFALLVRGPAMG
MTHALPLMQKRGGGSIINTASIAGLQAGFGPLAYSSAKAAVIHMSRCAAAELSPQKIRVN
AICPGLIATSIFGASMGLPREVADQMAAQIASIGPKIQPIPKSGLPEDIAAAALYLASDD
SRFVTGTHIVVDGGITVGPRSAWDINTPSPILAAMGITPEQAEQMRAQLLAAGGTG
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