SitesBLAST
Comparing BPHYT_RS16120 FitnessBrowser__BFirm:BPHYT_RS16120 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)
6pejA Structure of sorbitol dehydrogenase from sinorhizobium meliloti 1021 bound to sorbitol
60% identity, 99% coverage: 4:260/260 of query aligns to 3:257/257 of 6pejA
4nbuB Crystal structure of fabg from bacillus sp (see paper)
42% identity, 99% coverage: 3:259/260 of query aligns to 3:244/244 of 4nbuB
- active site: G18 (= G18), N111 (= N114), S139 (= S143), Q149 (≠ V153), Y152 (= Y156), K156 (= K160)
- binding acetoacetyl-coenzyme a: D93 (≠ M96), K98 (≠ E101), S139 (= S143), N146 (≠ E150), V147 (≠ A151), Q149 (≠ V153), Y152 (= Y156), F184 (≠ V188), M189 (= M193), K200 (= K212)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), N17 (≠ S17), G18 (= G18), I19 (= I19), D38 (= D38), F39 (≠ V39), V59 (≠ A62), D60 (= D63), V61 (= V64), N87 (= N90), A88 (= A91), G89 (≠ A92), I90 (≠ L93), T137 (≠ M141), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), F184 (≠ V188), T185 (≠ V189), T187 (= T191), M189 (= M193)
Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
37% identity, 96% coverage: 8:256/260 of query aligns to 3:252/256 of Q48436
- 6:33 (vs. 11:38, 39% identical) binding
- D59 (= D63) binding
- K156 (= K160) binding
1gegE Cryatal structure analysis of meso-2,3-butanediol dehydrogenase (see paper)
37% identity, 96% coverage: 8:256/260 of query aligns to 3:252/256 of 1gegE
- active site: G13 (= G18), S139 (= S143), Y152 (= Y156), K156 (= K160), V197 (≠ F201)
- binding alpha-D-glucopyranose: R63 (= R67), D64 (= D68), F67 (≠ Q71), E123 (≠ Q127)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), Q12 (≠ S17), I14 (= I19), D33 (= D38), Y34 (≠ V39), V58 (≠ A62), D59 (= D63), V60 (= V64), N86 (= N90), A87 (= A91), I109 (≠ V113), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), V185 (= V189), T187 (= T191), M189 (= M193)
3wyeA Crystal structure of chimeric engineered (2s,3s)-butanediol dehydrogenase complexed with NAD+
38% identity, 96% coverage: 8:256/260 of query aligns to 2:251/255 of 3wyeA
- active site: G12 (= G18), S138 (= S143), Y151 (= Y156), K155 (= K160), L196 (≠ F201)
- binding nicotinamide-adenine-dinucleotide: G8 (= G14), Q11 (≠ S17), G12 (= G18), I13 (= I19), D32 (= D38), Y33 (≠ V39), V57 (≠ A62), D58 (= D63), V59 (= V64), N85 (= N90), A86 (= A91), S138 (= S143), Y151 (= Y156), K155 (= K160), P181 (= P186), G182 (= G187), V184 (= V189), T186 (= T191), M188 (= M193), W189 (= W194)
7do7A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NAD and l-rhamnose bound-form) (see paper)
37% identity, 98% coverage: 5:260/260 of query aligns to 3:254/256 of 7do7A
- active site: G16 (= G18), S146 (= S143), Y159 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), R15 (≠ S17), G16 (= G18), I17 (= I19), S37 (≠ V39), D66 (= D63), A67 (≠ V64), N93 (= N90), A94 (= A91), G95 (≠ A92), I96 (≠ L93), V144 (≠ M141), S145 (= S142), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (= G187), I192 (≠ V189), T194 (= T191), I196 (≠ M193)
- binding beta-L-rhamnopyranose: F99 (≠ M96), S146 (= S143), S148 (≠ A145), Q156 (≠ V153), Y159 (= Y156), N197 (≠ W194), D235 (≠ A241), M236 (≠ D242), R238 (≠ D244)
7b81A Crystal structure of azotobacter vinelandii l-rhamnose 1-dehydrogenase (NAD bound-form) (see paper)
37% identity, 98% coverage: 5:260/260 of query aligns to 3:254/256 of 7b81A
- active site: G16 (= G18), S146 (= S143), Y159 (= Y156)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), S14 (≠ A16), R15 (≠ S17), I17 (= I19), D66 (= D63), A67 (≠ V64), N93 (= N90), A94 (= A91), G95 (≠ A92), I96 (≠ L93), T116 (≠ V113), V144 (≠ M141), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (= G187), I192 (≠ V189), T194 (= T191), I196 (≠ M193)
Q5P5I4 (S)-1-Phenylethanol dehydrogenase; EC 1.1.1.311 from Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) (see 2 papers)
39% identity, 98% coverage: 1:256/260 of query aligns to 1:245/249 of Q5P5I4
- M1 (= M1) modified: Initiator methionine, Removed
- NGI 17:19 (≠ SGI 17:19) binding
- D38 (= D38) binding
- CDV 61:63 (≠ ADV 62:64) binding
- N89 (= N90) binding
- Y93 (≠ F94) binding
- K158 (= K160) binding
- PSLV 184:187 (≠ PGVV 186:189) binding
- T191 (≠ M193) binding
2ewmB Crystal structure of the (s)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain ebn1 (see paper)
40% identity, 97% coverage: 4:256/260 of query aligns to 2:243/247 of 2ewmB
- active site: G16 (= G18), S139 (= S143), Y149 (≠ V153), Y152 (= Y156), K156 (= K160)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), N15 (≠ S17), G16 (= G18), I17 (= I19), D36 (= D38), L37 (≠ V39), C59 (≠ A62), D60 (= D63), V61 (= V64), N87 (= N90), S139 (= S143), Y152 (= Y156), K156 (= K160), P182 (= P186), S183 (≠ G187), L184 (≠ V188), V185 (= V189), T189 (≠ M193)
7do6A Crystal structure of azotobacter vinelandii l-rhamnose 1- dehydrogenase(NADP bound-form) (see paper)
36% identity, 98% coverage: 5:260/260 of query aligns to 3:245/247 of 7do6A
- active site: G16 (= G18), S146 (= S143), Y159 (= Y156)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ A16), R15 (≠ S17), G16 (= G18), I17 (= I19), H36 (≠ D38), S37 (≠ V39), G42 (≠ S44), D66 (= D63), A67 (≠ V64), N93 (= N90), A94 (= A91), G95 (≠ A92), I96 (≠ L93), T116 (≠ V113), S146 (= S143), Y159 (= Y156), K163 (= K160), I192 (≠ V189)
Q9ZNN8 L-2,3-butanediol dehydrogenase; L-BDH; (S,S)-butanediol dehydrogenase; Diacetyl reductase [(S)-acetoin forming]; EC 1.1.1.76; EC 1.1.1.304 from Corynebacterium glutamicum (Brevibacterium saccharolyticum) (see paper)
35% identity, 96% coverage: 8:256/260 of query aligns to 3:254/258 of Q9ZNN8
- QGI 12:14 (≠ SGI 17:19) binding
- D33 (= D38) binding
- Q37 (≠ P41) binding
- DV 61:62 (= DV 63:64) binding
- N88 (= N90) binding
- I142 (≠ Q144) mutation to Q: Loss of L-BD oxidizing activity, and does not gain the ability to use meso-BD as substrate; when associated with N-148.; mutation to Q: Loss of L-BD oxidizing activity. Does not gain the ability to use meso-BD as substrate.
- F148 (≠ E150) mutation to N: Loss of L-BD oxidizing activity, and does not gain the ability to use meso-BD as substrate; when associated with Q-142.; mutation to N: Loss of L-BD oxidizing activity. Does not gain the ability to use meso-BD as substrate.
- Y154 (= Y156) binding
- K158 (= K160) binding
- PGIVGT 184:189 (≠ PGVVDT 186:191) binding
3a28C Crystal structure of l-2,3-butanediol dehydrogenase (see paper)
35% identity, 96% coverage: 8:256/260 of query aligns to 2:253/257 of 3a28C
- active site: G12 (= G18), S140 (= S143), Y153 (= Y156), K157 (= K160), L198 (≠ F201)
- binding nicotinamide-adenine-dinucleotide: G8 (= G14), Q11 (≠ S17), I13 (= I19), D32 (= D38), L33 (≠ V39), Q36 (≠ P41), L59 (≠ A62), D60 (= D63), V61 (= V64), N87 (= N90), S140 (= S143), Y153 (= Y156), K157 (= K160), P183 (= P186), V186 (= V189), T188 (= T191), M190 (= M193), W191 (= W194)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
37% identity, 98% coverage: 5:259/260 of query aligns to 3:247/247 of 4jroC
- active site: G16 (= G18), S142 (= S143), Q152 (≠ V153), Y155 (= Y156), K159 (= K160)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), S14 (≠ A16), R15 (≠ S17), G16 (= G18), I17 (= I19), N35 (≠ V37), Y36 (≠ D38), N37 (≠ V39), G38 (≠ K40), S39 (≠ P41), N63 (≠ D63), V64 (= V64), N90 (= N90), A91 (= A91), I93 (≠ L93), I113 (≠ V113), S142 (= S143), Y155 (= Y156), K159 (= K160), P185 (= P186), I188 (≠ V189), T190 (= T191)
4za2D Crystal structure of pectobacterium carotovorum 2-keto-3-deoxy-d- gluconate dehydrogenase complexed with NAD+ (see paper)
36% identity, 98% coverage: 5:260/260 of query aligns to 8:246/247 of 4za2D
- binding nicotinamide-adenine-dinucleotide: G17 (= G14), D19 (≠ A16), L22 (≠ I19), I42 (vs. gap), D65 (= D63), M66 (≠ V64), N92 (= N90), A93 (= A91), G94 (≠ A92), L115 (≠ V113), I143 (≠ M141), S145 (= S143), Y158 (= Y156), K162 (= K160), G189 (= G187), M191 (≠ V189), T193 (= T191), N195 (≠ P208)
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, 97% coverage: 5:256/260 of query aligns to 3:242/248 of Q9KJF1
- S15 (= S17) binding
- D36 (= D38) binding
- D62 (= D63) binding
- I63 (≠ V64) binding
- N89 (= N90) binding
- Y153 (= Y156) binding
- K157 (= K160) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
8cxaA Crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from mycobacterium smegmatis with bound NAD
37% identity, 97% coverage: 4:256/260 of query aligns to 2:247/251 of 8cxaA
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), Q15 (≠ S17), G16 (= G18), I17 (= I19), D36 (= D38), V63 (= V64), N89 (= N90), A91 (= A92), S94 (≠ D95), I142 (≠ M141), S143 (= S142), S144 (= S143), Y157 (= Y156), K161 (= K160), P187 (= P186), H188 (≠ G187), I190 (≠ V189), I194 (≠ M193)
7pcsB Structure of the heterotetrameric sdr family member bbscd (see paper)
36% identity, 97% coverage: 5:256/260 of query aligns to 2:241/247 of 7pcsB
- binding nicotinamide-adenine-dinucleotide: G11 (= G14), M16 (≠ I19), D35 (= D38), I36 (≠ V39), I62 (≠ V64), N88 (= N90), G90 (≠ A92), I138 (≠ M141), S140 (= S143), Y152 (= Y156), K156 (= K160), I185 (≠ V189)
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
33% identity, 100% coverage: 1:260/260 of query aligns to 1:245/245 of 5t5qC
- active site: G18 (= G18), S140 (= S143), N150 (≠ V153), Y153 (= Y156), K157 (= K160)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ A16), G17 (≠ S17), G18 (= G18), I19 (= I19), D38 (= D38), L39 (≠ V39), D63 (= D63), A64 (≠ V64), S90 (≠ N90), I113 (≠ V113), Y153 (= Y156), K157 (= K160), P182 (= P186), I185 (≠ V189), T187 (= T191), M189 (= M193)
7v0hG Crystal structure of putative glucose 1-dehydrogenase from burkholderia cenocepacia in complex with NADP and a potential reaction product
36% identity, 98% coverage: 3:256/260 of query aligns to 7:251/253 of 7v0hG
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G14), S20 (≠ A16), K21 (≠ S17), G22 (= G18), I23 (= I19), A43 (≠ K40), S44 (≠ P41), S45 (≠ A42), G68 (≠ A62), D69 (= D63), V70 (= V64), N96 (= N90), S97 (≠ A91), G98 (≠ A92), Y100 (≠ F94), I144 (≠ M141), S146 (= S143), Y159 (= Y156), K163 (= K160), P189 (= P186), G190 (= G187), M191 (≠ V188), I192 (≠ V189), T194 (= T191), G196 (≠ M193), T197 (≠ W194)
- binding (2R)-2-(hydroxymethyl)pentanedioic acid: S146 (= S143), Y159 (= Y156), M191 (≠ V188), I202 (≠ A199)
5ojiA Crystal structure of the dehydrogenase/reductase sdr family member 4 (dhrs4) from caenorhabditis elegans (see paper)
36% identity, 97% coverage: 4:256/260 of query aligns to 7:255/260 of 5ojiA
- active site: G21 (= G18), S148 (= S143), Y161 (= Y156), K165 (= K160)
- binding isatin: S148 (= S143), S150 (≠ A145), Y161 (= Y156), V193 (= V188), S199 (≠ W194), L202 (≠ V197)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: A17 (≠ G14), T19 (≠ A16), I22 (= I19), S41 (vs. gap), R42 (≠ V37), N43 (≠ D38), N46 (≠ P41), I69 (≠ V64), N95 (= N90), H96 (≠ A91), G97 (≠ A92), N146 (≠ M141), S148 (= S143), Y161 (= Y156), K165 (= K160), G192 (= G187), I194 (≠ V189), T196 (= T191), M198 (= M193)
Query Sequence
>BPHYT_RS16120 FitnessBrowser__BFirm:BPHYT_RS16120
MAARLQDKVAILTGAASGIGEAVARRYLDEGARCVLVDVKPADSFGDSLRATYGDRVLTV
SADVTRRDDIQRIVASTLERFGQIDILFNNAALFDMRPILEESWDVFDRLFAVNVKGMFF
LMQAVAQKMVEQGCGGKIINMSSQAGRRGEALVSHYCATKAAVLSYTQSAALALAPHKIN
VNGIAPGVVDTPMWNEVDALFARYENRPLGEKKRLVGEAVPLGRMGVPDDLTGAALFLAS
ADADYITAQTLNVDGGNWMS
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