SitesBLAST
Comparing WP_161793854.1 NCBI__GCF_000877395.1:WP_161793854.1 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)
7tzpG Crystal structure of putataive short-chain dehydrogenase/reductase (fabg) from klebsiella pneumoniae subsp. Pneumoniae ntuh-k2044 in complex with nadh (see paper)
38% identity, 47% coverage: 244:475/494 of query aligns to 4:236/247 of 7tzpG
- binding 1,4-dihydronicotinamide adenine dinucleotide: G15 (= G255), R18 (= R258), G19 (= G259), I20 (= I260), D39 (≠ A279), R40 (= R280), C63 (= C301), I65 (≠ V303), N91 (= N329), G93 (= G331), I94 (= I333), V114 (= V353), Y155 (= Y395), K159 (= K399), I188 (≠ V428), T190 (= T430), T193 (≠ Q433)
3sj7A Structure of beta-ketoacetyl-coa reductase (fabg) from staphylococcus aureus complex with NADPH (see paper)
33% identity, 46% coverage: 249:475/494 of query aligns to 2:228/239 of 3sj7A
- active site: G12 (= G259), S138 (= S382), Q148 (≠ W392), Y151 (= Y395), K155 (= K399)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G255), S10 (= S257), R11 (= R258), I13 (= I260), N31 (≠ L277), Y32 (≠ A278), A33 (= A279), G34 (≠ R280), S35 (= S281), A58 (≠ C301), N59 (≠ D302), V60 (= V303), N86 (= N329), A87 (= A330), T109 (≠ V353), S138 (= S382), Y151 (= Y395), K155 (= K399), P181 (= P425), G182 (= G426)
3osuA Crystal structure of the 3-oxoacyl-acyl carrier protein reductase, fabg, from staphylococcus aureus
32% identity, 46% coverage: 249:475/494 of query aligns to 5:235/246 of 3osuA
5t2uA Short chain dehydrogenase/reductase family protein (see paper)
39% identity, 50% coverage: 244:489/494 of query aligns to 2:241/241 of 5t2uA
- active site: G17 (= G259), T135 (≠ S382), T145 (≠ W392), Y148 (= Y395), K152 (= K399)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G255), G17 (= G259), R38 (= R280), D39 (≠ S281), R42 (≠ A284), D60 (= D302), L61 (≠ V303), N83 (= N329), A84 (= A330), Y87 (≠ D334), I133 (= I380), T135 (≠ S382), Y148 (= Y395), K152 (= K399), P178 (= P425), P180 (≠ T427), T181 (≠ V428), T183 (= T430), T185 (≠ M432), T186 (≠ Q433)
4jroC Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (fabg) from listeria monocytogenes in complex with NADP+
32% identity, 48% coverage: 244:480/494 of query aligns to 1:241/247 of 4jroC
- active site: G16 (= G259), S142 (= S382), Q152 (≠ W392), Y155 (= Y395), K159 (= K399)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G255), S14 (= S257), R15 (= R258), G16 (= G259), I17 (= I260), N35 (vs. gap), Y36 (vs. gap), N37 (vs. gap), G38 (vs. gap), S39 (≠ A278), N63 (≠ D302), V64 (= V303), N90 (= N329), A91 (= A330), I93 (≠ L332), I113 (≠ V353), S142 (= S382), Y155 (= Y395), K159 (= K399), P185 (= P425), I188 (≠ V428), T190 (= T430)
P0AEK2 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 47% coverage: 244:475/494 of query aligns to 1:232/244 of P0AEK2
- GASR 12:15 (= GASR 255:258) binding NADP(+)
- T37 (≠ R280) binding NADP(+)
- NV 59:60 (≠ DV 302:303) binding NADP(+)
- N86 (= N329) binding NADP(+)
- Y151 (= Y395) mutation to F: Defect in the affinity for NADPH.
- YAAAK 151:155 (≠ YCATK 395:399) binding NADP(+)
- A154 (≠ T398) mutation to T: Decreases in the thermolability of the reductase; when associated with K-233.
- K155 (= K399) mutation to A: Defect in the affinity for NADPH.
- I184 (≠ V428) binding NADP(+)
Sites not aligning to the query:
- 233 E→K: Decreases in the thermolability of the reductase; when associated with T-154.
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
33% identity, 47% coverage: 244:475/494 of query aligns to 4:235/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G255), S17 (= S257), R18 (= R258), I20 (= I260), T40 (≠ R280), N62 (≠ D302), V63 (= V303), N89 (= N329), A90 (= A330), I92 (≠ L332), V139 (≠ I380), S141 (= S382), Y154 (= Y395), K158 (= K399), P184 (= P425), G185 (= G426), I187 (≠ V428), T189 (= T430), M191 (= M432)
4i08A Crystal structure of beta-ketoacyl-acyl carrier protein reductase (fabg) from vibrio cholerae in complex with NADPH (see paper)
34% identity, 47% coverage: 244:475/494 of query aligns to 4:231/243 of 4i08A
- active site: G19 (= G259), N113 (= N354), S141 (= S382), Q151 (≠ W392), Y154 (= Y395), K158 (= K399)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G15 (= G255), S17 (= S257), R18 (= R258), I20 (= I260), T40 (≠ R280), N62 (≠ D302), V63 (= V303), N89 (= N329), A90 (= A330), G140 (≠ S381), S141 (= S382), Y154 (= Y395), K158 (= K399), P184 (= P425), G185 (= G426), T189 (= T430)
1q7bA The structure of betaketoacyl-[acp] reductase from e. Coli in complex with NADP+ (see paper)
33% identity, 47% coverage: 245:475/494 of query aligns to 1:231/243 of 1q7bA
- active site: G15 (= G259), E101 (≠ D343), S137 (= S382), Q147 (≠ W392), Y150 (= Y395), K154 (= K399)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G255), S13 (= S257), R14 (= R258), T36 (≠ R280), N58 (≠ D302), V59 (= V303), N85 (= N329), A86 (= A330), G87 (= G331), I88 (≠ L332), S137 (= S382), Y150 (= Y395), K154 (= K399), P180 (= P425), G181 (= G426), I183 (≠ V428)
Sites not aligning to the query:
P0A2C9 3-oxoacyl-[acyl-carrier-protein] reductase FabG; 3-ketoacyl-acyl carrier protein reductase; Beta-Ketoacyl-acyl carrier protein reductase; Beta-ketoacyl-ACP reductase; EC 1.1.1.100 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
33% identity, 47% coverage: 244:475/494 of query aligns to 1:232/244 of P0A2C9
- M125 (= M369) mutation to I: Loss of the temperature-sensitive phenotype; when associated with T-223.
- A223 (≠ T466) mutation to T: Loss of the temperature-sensitive phenotype; when associated with I-125.
- S224 (≠ T467) mutation to F: Distorts the local conformation and prevent stacking around Phe-221. The S224F mutation would additionally disrupt the hydrogen bond formed between Ser-224 and Glu-226.
6d9yB Crystal structure of a short chain dehydrogenase/reductase sdr from burkholderia phymatum with partially occupied NAD
35% identity, 48% coverage: 244:480/494 of query aligns to 5:244/251 of 6d9yB
- active site: G20 (= G259), S145 (= S382), Y158 (= Y395)
- binding nicotinamide-adenine-dinucleotide: G16 (= G255), R19 (= R258), G20 (= G259), D40 (vs. gap), L41 (vs. gap), V64 (≠ C301), D65 (= D302), Q66 (≠ V303), A93 (= A330), S145 (= S382), Y158 (= Y395), K162 (= K399), P188 (= P425), A189 (≠ G426), A190 (≠ T427), A191 (≠ V428), T193 (= T430)
1q7cA The structure of betaketoacyl-[acp] reductase y151f mutant in complex with NADPH fragment (see paper)
33% identity, 47% coverage: 245:475/494 of query aligns to 1:231/243 of 1q7cA
- active site: G15 (= G259), S137 (= S382), Q147 (≠ W392), F150 (≠ Y395), K154 (= K399)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G11 (= G255), S13 (= S257), R14 (= R258), A35 (= A279), T36 (≠ R280), L57 (≠ C301), N58 (≠ D302), V59 (= V303), G87 (= G331), I88 (≠ L332)
3pk0B Crystal structure of short-chain dehydrogenase/reductase sdr from mycobacterium smegmatis (see paper)
37% identity, 48% coverage: 241:475/494 of query aligns to 3:242/262 of 3pk0B
7krmC Putative fabg bound to nadh from acinetobacter baumannii
35% identity, 47% coverage: 244:475/494 of query aligns to 1:232/244 of 7krmC
- active site: G18 (= G259), S140 (= S382), Y155 (= Y395)
- binding nicotinamide-adenine-dinucleotide: G12 (= G255), S15 (vs. gap), G18 (= G259), I19 (= I260), D38 (≠ A279), L39 (≠ R280), A60 (≠ C301), N61 (≠ D302), V62 (= V303), N88 (= N329), V111 (= V353), S140 (= S382), Y155 (= Y395), K159 (= K399), I188 (≠ V428), T190 (= T430)
7emgB Carbonyl reductase variant 4 (r123c/l209p/f183y/v61k) from serratia marcescens complexed with NADP+ (see paper)
34% identity, 46% coverage: 246:470/494 of query aligns to 2:226/243 of 7emgB
4nbuB Crystal structure of fabg from bacillus sp (see paper)
34% identity, 47% coverage: 246:475/494 of query aligns to 5:233/244 of 4nbuB
- active site: G18 (= G259), N111 (= N354), S139 (= S382), Q149 (≠ W392), Y152 (= Y395), K156 (= K399)
- binding acetoacetyl-coenzyme a: D93 (≠ P335), K98 (≠ D341), S139 (= S382), N146 (≠ L389), V147 (≠ E390), Q149 (≠ W392), Y152 (= Y395), F184 (≠ T427), M189 (= M432), K200 (≠ P443)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G255), N17 (≠ R258), G18 (= G259), I19 (= I260), D38 (≠ A279), F39 (≠ R280), V59 (≠ C301), D60 (= D302), V61 (= V303), N87 (= N329), A88 (= A330), G89 (= G331), I90 (≠ L332), T137 (≠ I380), S139 (= S382), Y152 (= Y395), K156 (= K399), P182 (= P425), F184 (≠ T427), T185 (≠ V428), T187 (= T430), M189 (= M432)
P73574 3-oxoacyl-[acyl-carrier-protein] reductase; 3-ketoacyl-acyl carrier protein reductase; EC 1.1.1.100 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
37% identity, 46% coverage: 246:473/494 of query aligns to 4:232/247 of P73574
- A14 (= A256) mutation to G: 4.2-fold increase in activity on acetoacetyl-CoA.
- P151 (≠ E390) 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 (= K399) mutation to A: Almost no activity on acetoacetyl-CoA.
- F188 (≠ T427) mutation to Y: 3.3-fold increase in activity on acetoacetyl-CoA.
- N198 (≠ R437) mutation to R: 3.5-fold increase in activity on acetoacetyl-CoA.
5t5qC Crystal structure of short-chain dehydrogenase/reductase sdr:glucose/ribitol dehydrogenase from brucella melitensis
34% identity, 47% coverage: 244:475/494 of query aligns to 3:233/245 of 5t5qC
- active site: G18 (= G259), S140 (= S382), N150 (≠ W392), Y153 (= Y395), K157 (= K399)
- binding nicotinamide-adenine-dinucleotide: N16 (≠ S257), G17 (≠ R258), G18 (= G259), I19 (= I260), D38 (≠ A279), L39 (≠ R280), D63 (= D302), A64 (≠ V303), S90 (≠ N329), I113 (≠ V353), Y153 (= Y395), K157 (= K399), P182 (= P425), I185 (≠ V428), T187 (= T430), M189 (= M432)
6t77A Crystal structure of klebsiella pneumoniae fabg(NADPH-dependent) NADP- complex at 1.75 a resolution (see paper)
32% identity, 47% coverage: 244:475/494 of query aligns to 1:232/244 of 6t77A
- active site: G16 (= G259), S138 (= S382), Y151 (= Y395)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G255), S14 (= S257), R15 (= R258), T37 (≠ R280), L58 (≠ C301), N59 (≠ D302), V60 (= V303), A87 (= A330), G88 (= G331), I89 (≠ L332)
C1DMX5 L-rhamnose 1-dehydrogenase (NAD(P)(+)); RhaDH; AvLRA1; EC 1.1.1.378 from Azotobacter vinelandii (strain DJ / ATCC BAA-1303) (see paper)
38% identity, 49% coverage: 244:485/494 of query aligns to 1:250/256 of C1DMX5
- G12 (= G255) binding NADP(+)
- S14 (= S257) binding NADP(+)
- R15 (= R258) binding NADP(+); mutation to T: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+).
- I17 (= I260) binding NADP(+)
- S37 (≠ R280) binding NADP(+); mutation to H: Increases specificity toward NAD(+). Shows a strong decrease in catalytic efficiency with NADP(+) and an increase in catalytic efficiency with NAD(+).
- D66 (= D302) binding NADP(+)
- A67 (≠ V303) binding NADP(+)
- N93 (= N329) binding NADP(+)
- F99 (≠ I336) mutation F->A,Y: Shows a strong decrease in catalytic efficiency with L-rhamnose, L-lyxose and L-mannose.
- S146 (= S382) binding beta-L-rhamnose
- S148 (≠ A384) binding beta-L-rhamnose
- Q156 (≠ W392) binding beta-L-rhamnose; mutation to A: Almost loss of activity with L-rhamnose as substrate.
- Y159 (= Y395) binding beta-L-rhamnose; binding NADP(+)
- K163 (= K399) binding NADP(+)
- T191 (= T427) binding beta-L-rhamnose; mutation to F: Retains 4% of wild-type activity with L-rhamnose as substrate.
- I192 (≠ V428) binding NADP(+)
- I196 (≠ M432) mutation to A: Shows a strong decrease in catalytic efficiency with L-rhamnose as substrate, but does not affect catalytic efficiency with L-lyxose and L-mannose.
- N197 (≠ Q433) binding beta-L-rhamnose
- D200 (vs. gap) mutation to A: Retains 16% of wild-type activity with L-rhamnose as substrate.; mutation to H: Retains 22% of wild-type activity with L-rhamnose as substrate.
Query Sequence
>WP_161793854.1 NCBI__GCF_000877395.1:WP_161793854.1
MMKTTMAACIALACAAPALAEPTEWTLDLGHAHIGWEIDHMNMANTVGRFNSFDGTFLID
EAEPANSRITFTIDASSIDSNHTGRDDHLRNPDYLNVEAHPQIDFVSTEVQMLTPTTGKL
RGDLTMLGVTAPVELDFEMVNRRTYPDFIPNYDEVEVVGFHATGEIARLDHGMDFIAFVG
SPTGFVVTLDARFDLVRCDGVPETNVPCHWGRVAELGAAAGNRTTDIGTGRRPVHPHLTI
GKTMDLEGKTVIVTGASRGIGEASARHLASLGANVVLAARSGDAVTKIAVEIGPNAIGVA
CDVSDWDQAAATVAQAVDTFGAVDLLVNNAGLIDPIARIEDADPGAWGRVVDVNVKGAFH
MLRAVVPPMIAGGSGLIVNISSGAATSALEGWSHYCATKAALLSLTRCAHKELAPKGVNV
IGLSPGTVATDMQRSIRDSGINPVSQLAWERHIPAEWVARAIAWLTTDAARAFDGADFSL
KTDEGREAVGLPTA
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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