SitesBLAST
Comparing CCNA_01345 FitnessBrowser__Caulo:CCNA_01345 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)
1vl8B Crystal structure of gluconate 5-dehydrogenase (tm0441) from thermotoga maritima at 2.07 a resolution
40% identity, 97% coverage: 8:258/260 of query aligns to 1:250/252 of 1vl8B
- active site: G17 (= G24), S143 (= S150), I154 (≠ T164), Y157 (= Y167), K161 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G20), R16 (= R23), G17 (= G24), L18 (= L25), S37 (≠ A44), R38 (= R45), C63 (≠ A69), D64 (= D70), V65 (≠ L71), A91 (≠ N97), A92 (= A98), G93 (= G99), I94 (≠ A100), V114 (≠ L120), I141 (≠ V148), S143 (= S150), Y157 (= Y167), K161 (= K171), P187 (= P197), G188 (= G198), Y190 (≠ F200), T192 (≠ S202), M194 (= M204), T195 (= T205)
4za2D Crystal structure of pectobacterium carotovorum 2-keto-3-deoxy-d- gluconate dehydrogenase complexed with NAD+ (see paper)
38% identity, 95% coverage: 9:256/260 of query aligns to 6:243/247 of 4za2D
- binding nicotinamide-adenine-dinucleotide: G17 (= G20), D19 (≠ S22), L22 (= L25), I42 (≠ Q47), D65 (= D70), M66 (≠ L71), N92 (= N97), A93 (= A98), G94 (= G99), L115 (= L120), I143 (≠ V148), S145 (= S150), Y158 (= Y167), K162 (= K171), G189 (= G198), M191 (≠ F200), T193 (≠ S202), N195 (≠ M204)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
40% identity, 96% coverage: 11:259/260 of query aligns to 3:247/247 of 4jroC
- active site: G16 (= G24), S142 (= S150), Q152 (≠ T164), Y155 (= Y167), K159 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G20), S14 (= S22), R15 (= R23), G16 (= G24), I17 (≠ L25), N35 (≠ V43), Y36 (≠ A44), N37 (≠ R45), G38 (≠ K46), S39 (≠ Q47), N63 (≠ D70), V64 (≠ L71), N90 (= N97), A91 (= A98), I93 (≠ A100), I113 (≠ L120), S142 (= S150), Y155 (= Y167), K159 (= K171), P185 (= P197), I188 (≠ F200), T190 (≠ S202)
2b4qA Pseudomonas aeruginosa rhlg/NADP active-site complex (see paper)
38% identity, 98% coverage: 5:259/260 of query aligns to 1:256/256 of 2b4qA
- active site: G20 (= G24), S148 (= S150), V149 (≠ I151), Y162 (= Y167), K166 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G16 (= G20), S18 (= S22), R19 (= R23), I21 (≠ L25), A40 (= A44), R41 (= R45), D42 (= D51), D65 (= D70), L66 (= L71), S67 (≠ G72), N92 (= N97), A93 (= A98), G94 (= G99), I146 (≠ V148), G147 (≠ A149), S148 (= S150), Y162 (= Y167), K166 (= K171), P192 (= P197), G193 (= G198), R194 (≠ Y199), F195 (= F200), S197 (= S202), M199 (= M204)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
40% identity, 97% coverage: 6:257/260 of query aligns to 4:252/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G20), S20 (= S22), K21 (≠ R23), G22 (= G24), I23 (≠ L25), A43 (= A44), S44 (≠ R45), S45 (≠ K46), G68 (≠ A69), D69 (= D70), V70 (≠ L71), N96 (= N97), S97 (≠ A98), G98 (= G99), Y100 (≠ A101), I144 (≠ V148), S146 (= S150), Y159 (= Y167), K163 (= K171), P189 (= P197), G190 (= G198), M191 (≠ Y199), I192 (≠ F200), T194 (≠ S202), G196 (≠ M204), T197 (= T205)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S150), Y159 (= Y167), M191 (≠ Y199), I202 (≠ Q211)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
39% identity, 96% coverage: 11:260/260 of query aligns to 4:247/247 of P73574
- A14 (≠ G21) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ H158) mutation to F: 2.7-fold increase in activity on acetoacetyl-CoA.; mutation to V: 5.7-fold increase in activity on acetoacetyl-CoA.
- K160 (= K171) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ Y199) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ H212) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
5u9pB Crystal structure of a gluconate 5-dehydrogenase from burkholderia cenocepacia j2315 in complex with NADP and tartrate
36% identity, 96% coverage: 9:258/260 of query aligns to 12:258/261 of 5u9pB
- active site: G27 (= G24), S152 (= S150), Y165 (= Y167), K169 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G23 (= G20), R26 (= R23), G27 (= G24), I28 (≠ L25), R48 (= R45), D73 (= D70), V74 (≠ L71), N100 (= N97), A101 (= A98), I150 (≠ V148), Y165 (= Y167), K169 (= K171), P195 (= P197), F198 (= F200), T200 (≠ S202), L202 (≠ M204), N203 (≠ T205)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
37% identity, 94% coverage: 14:257/260 of query aligns to 5:244/246 of 3osuA
Q9BTZ2 Dehydrogenase/reductase SDR family member 4; NADPH-dependent carbonyl reductase; CR; NADPH-dependent retinol dehydrogenase/reductase; NRDR; humNRDR; Peroxisomal short-chain alcohol dehydrogenase; PSCD; SCAD-SRL; Short chain dehydrogenase/reductase family 25C member 2; Protein SDR25C2; Short-chain dehydrogenase/reductase family member 4; EC 1.1.1.184 from Homo sapiens (Human) (see 2 papers)
37% identity, 98% coverage: 2:256/260 of query aligns to 21:273/278 of Q9BTZ2
- S176 (≠ Q161) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to F: Decreased reduction activity for benzil, isatin and retinal and increased activity for 5beta-Pregnane-3,20-dione and 5beta-Dihydrotestosterone. No change of stereoselectivity in 3-ketosteroids reduction and no change in 3beta-hydroxysteroid oxidation. Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with L-179. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with L-179. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with L-179. Loss of cold catalytic inactivation; when associated with L-179 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with L-179 and N-195.
- F179 (≠ T164) Responsible for the stereoselective reduction of 3-ketosteroids into 3beta-hydroxysteroids and benzil into R-benzoin; mutation to L: Decreased reduction activity for isatin and increased activity for 5beta-Pregnane-3,20-dione, 5beta-Dihydrotestosterone, benzil and retinal; when associated with F-176. Change in stereoselective activity by the reduction of 5beta-Pregnane-3,20-dione predominantly to the 3alpha-hydroxysteroid; when associated with F-176. Switch from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176. Loss of cold catalytic inactivation; when associated with F-176 and N-195. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and N-195.
- T195 (≠ A180) mutation to N: Loss of cold catalytic inactivation. Loss of cold catalytic inactivation; when associated with F-176 and L-179. Switch in stereoselective activity from 3beta-hydroxysteroid to 3alpha-hydroxysteroid oxidation; when associated with F-176 and L-179. Increased reduction activity for renital and oxidation activity for retinol; when associated with F-176 and L-179.
3o03A Quaternary complex structure of gluconate 5-dehydrogenase from streptococcus suis type 2 (see paper)
35% identity, 96% coverage: 9:257/260 of query aligns to 7:246/254 of 3o03A
- active site: G22 (= G24), S147 (= S150), V157 (≠ T164), Y160 (= Y167), K164 (= K171)
- binding calcium ion: S147 (= S150), M148 (≠ I151), P190 (= P197)
- binding D-gluconic acid: I99 (≠ A101), R101 (≠ G103), S147 (= S150), M149 (≠ H159), R154 (vs. gap), Y160 (= Y167)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G20), Y21 (≠ R23), G22 (= G24), I23 (≠ L25), D42 (≠ A44), I43 (≠ R45), L47 (≠ E49), D68 (= D70), V69 (≠ L71), N95 (= N97), A96 (= A98), G97 (= G99), I145 (≠ V148), Y160 (= Y167), K164 (= K171), P190 (= P197)
3o4rA Crystal structure of human dehydrogenase/reductase (sdr family) member 4 (dhrs4)
37% identity, 95% coverage: 11:256/260 of query aligns to 6:249/254 of 3o4rA
- active site: G19 (= G24), S145 (= S150), F155 (≠ T164), Y158 (= Y167), K162 (= K171), K203 (≠ Q211)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A15 (≠ G20), T17 (≠ S22), D18 (≠ R23), G19 (= G24), I20 (≠ L25), S39 (≠ A44), R40 (= R45), K41 (= K46), N44 (≠ E49), H65 (≠ D70), V66 (≠ L71), N92 (= N97), A94 (≠ G99), S145 (= S150), Y158 (= Y167), K162 (= K171), P188 (= P197), G189 (= G198), L190 (≠ Y199), I191 (≠ F200), T193 (≠ S202), F195 (≠ M204), S196 (≠ T205)
4dmmB 3-oxoacyl-[acyl-carrier-protein] reductase from synechococcus elongatus pcc 7942 in complex with NADP
41% identity, 96% coverage: 11:259/260 of query aligns to 3:239/240 of 4dmmB
- active site: G16 (= G24), S142 (= S150), Q152 (≠ T164), Y155 (= Y167), K159 (= K171)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G20), S14 (= S22), R15 (= R23), G16 (= G24), I17 (≠ L25), A37 (= A44), S38 (≠ R45), S39 (≠ K46), A62 (= A69), D63 (= D70), V64 (≠ L71), N90 (= N97), A91 (= A98), L113 (= L120), I140 (≠ V148), S142 (= S150), Y155 (= Y167), K159 (= K171), P185 (= P197), G186 (= G198), I188 (≠ F200), T190 (≠ S202), M192 (= M204)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
37% identity, 94% coverage: 14:257/260 of query aligns to 2:237/239 of 3sj7A
- active site: G12 (= G24), S138 (= S150), Q148 (≠ T164), Y151 (= Y167), K155 (= K171)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G20), S10 (= S22), R11 (= R23), I13 (≠ L25), N31 (vs. gap), Y32 (≠ V43), A33 (= A44), G34 (≠ R45), S35 (≠ K46), A58 (= A69), N59 (≠ D70), V60 (≠ L71), N86 (= N97), A87 (= A98), T109 (≠ L120), S138 (= S150), Y151 (= Y167), K155 (= K171), P181 (= P197), G182 (= G198)
Q9KJF1 (2S)-[(R)-hydroxy(phenyl)methyl]succinyl-CoA dehydrogenase subunit BbsD; (S,R)-2-(alpha-hydroxybenzyl)succinyl-CoA dehydrogenase subunit BbsD; EC 1.1.1.429 from Thauera aromatica (see 2 papers)
36% identity, 96% coverage: 11:260/260 of query aligns to 3:246/248 of Q9KJF1
- S15 (≠ R23) binding
- D36 (≠ A44) binding
- D62 (= D70) binding
- I63 (≠ L71) binding
- N89 (= N97) binding
- Y153 (= Y167) binding
- K157 (= K171) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
36% identity, 96% coverage: 11:260/260 of query aligns to 2:245/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G20), M16 (≠ L25), D35 (≠ A44), I36 (≠ R45), I62 (≠ L71), N88 (= N97), G90 (= G99), I138 (≠ V148), S140 (= S150), Y152 (= Y167), K156 (= K171), I185 (≠ F200)
6ixmC Crystal structure of the ketone reductase chkred20 from the genome of chryseobacterium sp. Ca49 complexed with NAD (see paper)
34% identity, 96% coverage: 11:260/260 of query aligns to 3:248/248 of 6ixmC
- active site: G16 (= G24), S142 (= S150), Y155 (= Y167), K159 (= K171)
- binding nicotinamide-adenine-dinucleotide: G12 (= G20), S15 (≠ R23), G16 (= G24), I17 (≠ L25), D36 (≠ A44), I37 (≠ R45), A61 (= A69), D62 (= D70), T63 (≠ L71), N89 (= N97), A90 (= A98), M140 (≠ V148), S142 (= S150), Y155 (= Y167), K159 (= K171), P185 (= P197), A186 (≠ G198), Y187 (= Y199), I188 (≠ F200), L192 (≠ M204)
3lqfA Crystal structure of the short-chain dehydrogenase galactitol- dehydrogenase (gatdh) of rhodobacter sphaeroides in complex with NAD and erythritol (see paper)
39% identity, 98% coverage: 6:259/260 of query aligns to 4:253/254 of 3lqfA
- active site: G22 (= G24), S144 (= S150), Y159 (= Y167), K163 (= K171)
- binding meso-erythritol: N151 (≠ H158), Y159 (= Y167), Y191 (= Y199), T197 (= T205), M200 (= M206)
- binding nicotinamide-adenine-dinucleotide: G18 (= G20), S21 (≠ R23), G22 (= G24), I23 (≠ L25), D42 (≠ A44), R43 (= R45), D66 (= D70), V67 (≠ L71), S92 (≠ N97), L142 (≠ V148), S144 (= S150), K163 (= K171), P189 (= P197), V192 (≠ F200), T194 (≠ S202), M196 (= M204), T197 (= T205)
2wsbA Crystal structure of the short-chain dehydrogenase galactitol-dehydrogenase (gatdh) of rhodobacter sphaeroides in complex with NAD (see paper)
39% identity, 98% coverage: 6:259/260 of query aligns to 4:253/254 of 2wsbA
- active site: G22 (= G24), S144 (= S150), Y159 (= Y167), K163 (= K171)
- binding nicotinamide-adenine-dinucleotide: G18 (= G20), S21 (≠ R23), G22 (= G24), I23 (≠ L25), D42 (≠ A44), R43 (= R45), D66 (= D70), V67 (≠ L71), S92 (≠ N97), A93 (= A98), L142 (≠ V148), S144 (= S150), Y159 (= Y167), K163 (= K171), P189 (= P197), V192 (≠ F200), T194 (≠ S202), M196 (= M204), T197 (= T205)
- binding n-propanol: S144 (= S150), M145 (≠ I151), N151 (≠ H158), N151 (≠ H158), Y159 (= Y167), Y159 (= Y167), Y191 (= Y199)
2wdzA Crystal structure of the short chain dehydrogenase galactitol-dehydrogenase (gatdh) of rhodobacter sphaeroides in complex with NAD+ and 1,2-pentandiol (see paper)
39% identity, 98% coverage: 6:259/260 of query aligns to 4:253/254 of 2wdzA
- active site: G22 (= G24), S144 (= S150), Y159 (= Y167), K163 (= K171)
- binding (2S)-pentane-1,2-diol: A45 (≠ Q47), D49 (= D51), R62 (≠ G66), S146 (≠ E152), Y159 (= Y167)
- binding nicotinamide-adenine-dinucleotide: G18 (= G20), S21 (≠ R23), G22 (= G24), I23 (≠ L25), D42 (≠ A44), R43 (= R45), A65 (= A69), D66 (= D70), V67 (≠ L71), S92 (≠ N97), A93 (= A98), L142 (≠ V148), S144 (= S150), Y159 (= Y167), K163 (= K171), P189 (= P197), V192 (≠ F200), T194 (≠ S202), M196 (= M204), T197 (= T205)
C0KTJ6 Galactitol 2-dehydrogenase (L-tagatose-forming); Galactitol dehydrogenase; GDH; GatDH; Galactitol:NAD(+) 5-oxidoreductase; EC 1.1.1.406 from Cereibacter sphaeroides (Rhodobacter sphaeroides) (see paper)
39% identity, 98% coverage: 6:259/260 of query aligns to 4:253/254 of C0KTJ6
Sites not aligning to the query:
Query Sequence
>CCNA_01345 FitnessBrowser__Caulo:CCNA_01345
MSSPLHKLFDLTGRVAIVTGGSRGLGLQIARALAEYGAAVALVARKQGELDAAVAALTAE
GRTAVGLVADLGQAGSAQDLTARVLERFGRIDILVNNAGAAWGAPAEDYPLEGWNKVMDL
NVTGLFLLTQAVAREAFLKQGKGAVVNVASIEGLQGHHHSQLGTIAYNTAKGAVINMTRA
LAAEWGPRNIRVNAVAPGYFPSKMTMTTLGQHGDDMLRQTPLGKLGGDTDLMGPALLLAS
DAGGHITGQIIVVDGGMTII
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