SitesBLAST
Comparing GFF3731 FitnessBrowser__psRCH2:GFF3731 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)
6aa8E Crystal structure of (s)-3-hydroxybutyryl-coenzymea dehydrogenase from clostridium acetobutylicum complexed with NAD+ (see paper)
41% identity, 55% coverage: 3:282/508 of query aligns to 1:279/281 of 6aa8E
- active site: S116 (= S118), H137 (= H139), E149 (= E151), N187 (= N189)
- binding nicotinamide-adenine-dinucleotide: I6 (≠ V8), G9 (= G11), T10 (≠ A12), M11 (= M13), R29 (≠ H31), D30 (= D32), I31 (≠ S33), A86 (= A88), A87 (≠ I89), E89 (= E91), K94 (= K96), N114 (= N116), S116 (= S118)
4kugA Crystal structure of 3-hydroxybutylryl-coa dehydrogenase with NAD from clostridium butyricum
38% identity, 55% coverage: 2:282/508 of query aligns to 1:280/282 of 4kugA
- active site: S117 (= S118), H138 (= H139), E150 (= E151), N188 (= N189)
- binding nicotinamide-adenine-dinucleotide: G10 (= G11), T11 (≠ A12), M12 (= M13), R30 (≠ H31), D31 (= D32), A87 (= A88), A88 (≠ I89), E90 (= E91), N115 (= N116), S117 (= S118), H138 (= H139)
4kuhA Crystal structure of 3-hydroxybutylryl-coa dehydrogenase with acetoacetyl-coa from clostridium butyricum
38% identity, 55% coverage: 2:282/508 of query aligns to 1:280/280 of 4kuhA
4pzeA Crystal structure of (s)-3-hydroxybutyryl-coa dehydrogenase paah1 in complex with acetoacetyl-coa (see paper)
38% identity, 55% coverage: 5:282/508 of query aligns to 5:281/283 of 4pzeA
4pzdA Crystal structure of (s)-3-hydroxybutyryl-coa dehydrogenase paah1 in complex with NAD+ (see paper)
38% identity, 55% coverage: 5:282/508 of query aligns to 5:281/283 of 4pzdA
- active site: S118 (= S118), H139 (= H139), E151 (= E151), N189 (= N189)
- binding nicotinamide-adenine-dinucleotide: G11 (= G11), T12 (≠ A12), M13 (= M13), D32 (= D32), A88 (= A88), A89 (≠ I89), T90 (≠ V90), E91 (= E91), I99 (≠ L99), N116 (= N116), S118 (= S118), N142 (= N142)
P00348 Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial; HCDH; L-3-hydroxyacyl CoA dehydrogenase; Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase; Short-chain 3-hydroxyacyl-CoA dehydrogenase; EC 1.1.1.35 from Sus scrofa (Pig) (see paper)
39% identity, 56% coverage: 1:283/508 of query aligns to 26:314/314 of P00348
- GGGLMG 34:39 (≠ GAGAMG 9:14) binding
- D57 (= D32) binding
- E122 (= E91) binding
- K127 (= K96) binding
- S149 (= S118) binding
1f17A L-3-hydroxyacyl-coa dehydrogenase complexed with nadh (see paper)
38% identity, 56% coverage: 1:283/508 of query aligns to 3:291/293 of 1f17A
- active site: S126 (= S118), H147 (= H139), E159 (= E151), N197 (= N189)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G13 (= G11), L14 (≠ A12), M15 (= M13), D34 (= D32), Q35 (≠ S33), A96 (= A88), I97 (= I89), E99 (= E91), K104 (= K96), N124 (= N116), S126 (= S118), H147 (= H139)
1f12A L-3-hydroxyacyl-coa dehydrogenase complexed with 3-hydroxybutyryl-coa (see paper)
38% identity, 56% coverage: 1:283/508 of query aligns to 3:291/293 of 1f12A
- active site: S126 (= S118), H147 (= H139), E159 (= E151), N197 (= N189)
- binding 3-hydroxybutanoyl-coenzyme a: K57 (≠ G56), S126 (= S118), H147 (= H139), F149 (= F141), N150 (= N142), M155 (= M147), N197 (= N189), L200 (≠ G192), P232 (≠ R224), M233 (= M225), L238 (= L230)
1f0yA L-3-hydroxyacyl-coa dehydrogenase complexed with acetoacetyl-coa and NAD+ (see paper)
38% identity, 56% coverage: 1:283/508 of query aligns to 3:291/291 of 1f0yA
- active site: S126 (= S118), H147 (= H139), E159 (= E151), N197 (= N189)
- binding acetoacetyl-coenzyme a: S50 (≠ L48), K57 (≠ G56), S126 (= S118), H147 (= H139), F149 (= F141), N150 (= N142), P151 (= P143), P153 (= P145), V154 (≠ L146), N197 (= N189), P232 (≠ R224), M233 (= M225), L238 (= L230)
- binding nicotinamide-adenine-dinucleotide: G13 (= G11), L14 (≠ A12), M15 (= M13), D34 (= D32), Q35 (≠ S33), A96 (= A88), I97 (= I89), E99 (= E91), K104 (= K96), N124 (= N116), S126 (= S118), H147 (= H139), N150 (= N142), V242 (≠ T234), T246 (≠ I238), K282 (= K274)
Q16836 Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial; HCDH; Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase; Short-chain 3-hydroxyacyl-CoA dehydrogenase; EC 1.1.1.35 from Homo sapiens (Human) (see 7 papers)
38% identity, 56% coverage: 1:283/508 of query aligns to 26:314/314 of Q16836
- GGGLMG 34:39 (≠ GAGAMG 9:14) binding
- A40 (≠ R15) to T: in HADH deficiency; dbSNP:rs137853101
- D57 (= D32) binding ; to E: in HADH deficiency; dbSNP:rs137853102; to G: found in a patient with Reye-like syndrome. Does not affect 3-hydroxyacyl-CoA dehydrogenase activity. Increases KM value for NADH. Does not affect dimerization
- S73 (≠ L48) binding
- K80 (≠ G56) binding
- L86 (vs. gap) to P: in dbSNP:rs4956145
- E122 (= E91) binding
- K127 (= K96) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- S149 (= S118) binding ; binding
- Q152 (≠ S121) to H: in dbSNP:rs1051519
- N173 (= N142) binding
- Y226 (= Y195) to H: found in a patient with Reye-like syndrome; loss of 3-hydroxyacyl-CoA dehydrogenase activity. Does not affect dimerization; dbSNP:rs146036912
- P258 (= P227) to L: in HHF4; loss of 3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137853103
- K305 (= K274) binding
P9WNP7 3-hydroxybutyryl-CoA dehydrogenase; Beta-hydroxybutyryl-CoA dehydrogenase; BHBD; EC 1.1.1.157 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
38% identity, 55% coverage: 2:282/508 of query aligns to 5:286/286 of P9WNP7
- S122 (= S118) mutation to A: Loss of fatty acyl dehydrogenase activity.
6iunB Crystal structure of enoyl-coa hydratase (ech) from ralstonia eutropha h16 in complex with NAD
32% identity, 59% coverage: 2:302/508 of query aligns to 291:586/692 of 6iunB
- active site: S407 (= S118), H428 (= H139), E440 (= E151), N478 (= N189)
- binding nicotinamide-adenine-dinucleotide: G300 (= G11), T301 (≠ A12), M302 (= M13), E321 (≠ D32), T322 (≠ S33), Y365 (≠ L76), A377 (= A88), V378 (≠ I89), E380 (= E91), V384 (≠ I95), V388 (≠ L99), N405 (= N116), S407 (= S118)
Sites not aligning to the query:
1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
33% identity, 57% coverage: 22:310/508 of query aligns to 334:621/715 of 1wdlA
- active site: S430 (= S118), H451 (= H139), E463 (= E151), N501 (= N189)
- binding nicotinamide-adenine-dinucleotide: D344 (= D32), I345 (≠ S33), A400 (= A88), V401 (≠ I89), E403 (= E91), N428 (= N116), T429 (= T117), S430 (= S118)
Sites not aligning to the query:
- active site: 69, 89, 93, 117, 120, 139, 140, 147, 148
- binding nicotinamide-adenine-dinucleotide: 322, 324, 325
P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
33% identity, 57% coverage: 22:310/508 of query aligns to 334:621/715 of P28793
- D344 (= D32) binding
- VVE 401:403 (≠ IVE 89:91) binding
- K408 (= K96) binding
- S430 (= S118) binding
- N454 (= N142) binding
- N501 (= N189) binding
Sites not aligning to the query:
- 297 binding
- 325 binding
- 660 binding
Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
32% identity, 63% coverage: 5:324/508 of query aligns to 300:631/723 of Q08426
- A325 (≠ L30) to G: in dbSNP:rs1062555
- K346 (≠ R51) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
- K584 (≠ N284) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
- K598 (≠ P297) to T: in dbSNP:rs1042437
- T606 (≠ P303) to P: in dbSNP:rs1042438
Sites not aligning to the query:
- 3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
- 40 V → G: in dbSNP:rs1062551
- 41 I → R: in dbSNP:rs1062552
- 75 T → I: in dbSNP:rs1062553
- 165 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
- 171 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.
- 274 A → T: in dbSNP:rs2302819
1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
35% identity, 52% coverage: 22:283/508 of query aligns to 334:593/707 of 1wdmA
- active site: S430 (= S118), H451 (= H139), E463 (= E151), N501 (= N189)
- binding acetyl coenzyme *a: M459 (= M147), N501 (= N189), P534 (≠ R224)
- binding nicotinamide-adenine-dinucleotide: D344 (= D32), V401 (≠ I89), E403 (= E91), N428 (= N116), S430 (= S118), N454 (= N142)
Sites not aligning to the query:
- active site: 69, 89, 93, 117, 120, 139, 140, 147, 148
- binding acetyl coenzyme *a: 142, 297, 652, 658
- binding nicotinamide-adenine-dinucleotide: 321, 322, 324, 325
P21177 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Escherichia coli (strain K12) (see 2 papers)
32% identity, 52% coverage: 22:287/508 of query aligns to 333:597/729 of P21177
- H450 (= H139) active site, For 3-hydroxyacyl-CoA dehydrogenase activity; mutation H->A,Q: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity.
Sites not aligning to the query:
- 116 G→F: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected.
- 322 G→A: 10-fold increase in KM for NADH.
8oqrA Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-80
32% identity, 56% coverage: 2:287/508 of query aligns to 334:621/728 of 8oqrA
Sites not aligning to the query:
- binding 4-cyanobenzenesulfonic acid: 76, 77, 81, 82, 82, 85, 89, 96, 123, 124, 149, 150
8oqsB Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-83
32% identity, 56% coverage: 2:287/508 of query aligns to 340:627/735 of 8oqsB
- binding 4-phenylbenzenesulfonic acid: S456 (= S118), T457 (≠ S119), M485 (= M147), P486 (≠ K148), G523 (= G185), S527 (≠ N189), N535 (≠ T197), P560 (≠ R224), M575 (≠ S239), I578 (≠ V242), I578 (≠ V242)
Sites not aligning to the query:
- binding 4-phenylbenzenesulfonic acid: 7, 10, 11, 16, 17, 45, 50, 82, 83, 84, 87, 87, 88, 88, 91, 95, 98, 99, 102, 102, 134, 156, 159, 302, 302, 319, 682, 683, 686
8pf8A Structure of mycobacterium tuberculosis beta-oxidation trifunctional enzyme in complex with fragment-m-72
32% identity, 56% coverage: 2:287/508 of query aligns to 334:621/729 of 8pf8A
Sites not aligning to the query:
- binding [2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boronic acid: 76, 169, 173, 177, 193, 313
- binding bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]-bis(oxidanyl)boranuide: 5, 39, 40, 41, 81, 92, 93
- binding [(2~{R})-2,3-bis(oxidanyl)propoxy]-[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]borinic acid: 39, 77, 78, 82, 93
- binding (2~{R})-3-bis[2-methyl-5-(trifluoromethyl)pyrazol-3-yl]boranyloxypropane-1,2-diol: 152, 184, 311, 312, 673
Query Sequence
>GFF3731 FitnessBrowser__psRCH2:GFF3731
MFERIGVVGAGAMGRGIAQLFAGAGKQVWLHDSRSESISDALRFNRELLERGVAKGRLSV
AELDATLARMQAAPALADLSGCDLVIEAIVENLEIKQALFVELEALLAEDAVLATNTSSL
SVTRIAAACRLPGRVAGFHFFNPVPLMKLVEVVRGERSDPQVIQRLVKLAEDAGHFPAIT
PDTPGFLVNHAGRAYSTEAQRILAEGIADAEQIDRILRDGPGFRMGPFELFDLTGLDISH
AVMESVYQQFYQDPRYTPSYQAAQRVAAGLLGRKTGQGYYRYENGQQIRTPEPQFSPVRI
ERPFWLDSQDPALRSQLAALLQAAGAQLESGEVPSARAICLITPLGEDASSMIARLGLPA
ERSVALDQFCDFDRRRVLMRQPALAAAIEAQARQALGSDGVPVEVINDSPGFVSQRVVAS
IVNLGCEIAQKGIADPQTLDRAVTLALGYPKGPLGFAEHYGAARILAILQAMQGCYGGEA
RYRPSPWLRRRVQLSLPLTAADQPAALR
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