SitesBLAST
Comparing WP_011777725.1 NCBI__GCF_000015305.1:WP_011777725.1 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)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 83% coverage: 27:291/318 of query aligns to 22:289/304 of 1wwkA
- active site: S96 (≠ N100), R230 (= R232), D254 (= D256), E259 (= E261), H278 (= H280)
- binding nicotinamide-adenine-dinucleotide: V100 (= V104), G146 (= G154), F147 (≠ Y155), G148 (= G156), R149 (≠ N157), I150 (= I158), Y168 (vs. gap), D169 (vs. gap), P170 (vs. gap), V201 (≠ L203), P202 (= P204), T207 (= T209), T228 (= T230), S229 (= S231), D254 (= D256), H278 (= H280), G280 (≠ T282)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
41% identity, 86% coverage: 20:291/318 of query aligns to 15:288/526 of 3dc2A
Sites not aligning to the query:
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
41% identity, 86% coverage: 20:291/318 of query aligns to 16:289/525 of 3ddnB
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
33% identity, 92% coverage: 24:314/318 of query aligns to 20:326/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A76), T102 (≠ V104), G155 (= G154), G157 (= G156), R158 (≠ N157), T159 (≠ I158), D178 (≠ S177), P179 (vs. gap), Y180 (vs. gap), H210 (= H202), C211 (≠ L203), N212 (≠ P204), A238 (≠ T230), R240 (= R232), H289 (= H280), A291 (≠ T282), W292 (= W283)
- binding : V25 (= V29), A26 (≠ R30), F27 (= F31), C28 (= C32), E35 (≠ T39), H37 (≠ Y41)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
33% identity, 92% coverage: 24:314/318 of query aligns to 20:326/330 of 4lcjA
- active site: A98 (≠ N100), R240 (= R232), D264 (= D256), E269 (= E261), H289 (= H280)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ W51), H51 (= H52), I72 (≠ L74), G73 (= G75), S74 (≠ A76), G75 (= G77), R240 (= R232), H289 (= H280), W292 (= W283)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A76), T102 (≠ V104), I154 (≠ V153), G155 (= G154), G157 (= G156), R158 (≠ N157), T159 (≠ I158), D178 (≠ S177), Y180 (vs. gap), H210 (= H202), C211 (≠ L203), N212 (≠ P204), N214 (≠ T206), N217 (≠ T209), A238 (≠ T230), A239 (≠ S231), R240 (= R232), H289 (= H280), W292 (= W283)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
33% identity, 92% coverage: 24:315/318 of query aligns to 52:359/445 of P56545
- IGFGRT 186:191 (≠ VGYGNI 153:158) binding NAD(+)
- D210 (≠ S177) binding NAD(+)
- 243:249 (vs. 203:209, 14% identical) binding NAD(+)
- AAR 270:272 (≠ TSR 230:232) binding NAD(+)
- D296 (= D256) binding NAD(+)
- HTAW 321:324 (≠ HVTW 280:283) binding NAD(+)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 21:327/331 of 1hl3A
- active site: S99 (≠ N100), R241 (= R232), D265 (= D256), E270 (= E261), H290 (= H280)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V104), G158 (= G156), R159 (≠ N157), V160 (≠ I158), D179 (≠ S177), Y181 (vs. gap), H211 (= H202), C212 (≠ L203), G213 (≠ P204), N218 (≠ T209), T239 (= T230), A240 (≠ S231), R241 (= R232), D265 (= D256), H290 (= H280)
- binding : V26 (= V29), A27 (≠ R30), F28 (= F31), C29 (= C32), E36 (≠ T39), H38 (≠ Y41), E39 (≠ R42)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 21:327/331 of 1hkuA
- active site: S99 (≠ N100), R241 (= R232), D265 (= D256), E270 (= E261), H290 (= H280)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ A76), T103 (≠ V104), G156 (= G154), G158 (= G156), R159 (≠ N157), V160 (≠ I158), Y178 (≠ T176), D179 (≠ S177), P180 (vs. gap), Y181 (vs. gap), C212 (≠ L203), N218 (≠ T209), T239 (= T230), A240 (≠ S231), R241 (= R232), H290 (= H280), W293 (= W283)
Sites not aligning to the query:
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 21:327/332 of 6v89A
6cdfA Human ctbp1 (28-378) (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 22:328/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V104), G157 (= G154), R160 (≠ N157), V161 (≠ I158), Y179 (≠ T176), D180 (≠ S177), P181 (vs. gap), Y182 (vs. gap), H212 (= H202), C213 (≠ L203), N219 (≠ T209), T240 (= T230), A241 (≠ S231), R242 (= R232), H291 (= H280), W294 (= W283)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 21:327/328 of 4u6sA
- active site: S99 (≠ N100), R241 (= R232), D265 (= D256), E270 (= E261), H290 (= H280)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V104), G156 (= G154), G158 (= G156), R159 (≠ N157), V160 (≠ I158), Y178 (≠ T176), D179 (≠ S177), P180 (vs. gap), Y181 (vs. gap), H211 (= H202), C212 (≠ L203), G213 (≠ P204), N218 (≠ T209), T239 (= T230), A240 (≠ S231), R241 (= R232), H290 (= H280), W293 (= W283)
- binding 3-phenylpyruvic acid: Y51 (≠ W51), H52 (= H52), I73 (≠ L74), G74 (= G75), S75 (≠ A76), G76 (= G77), R241 (= R232), W293 (= W283), M302 (≠ Y292)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 21:327/328 of 4u6qA
- active site: S99 (≠ N100), R241 (= R232), D265 (= D256), E270 (= E261), H290 (= H280)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ W51), I73 (≠ L74), G74 (= G75), S75 (≠ A76), G76 (= G77), R241 (= R232), H290 (= H280), W293 (= W283), M302 (≠ Y292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ A76), T103 (≠ V104), G156 (= G154), R159 (≠ N157), V160 (≠ I158), Y178 (≠ T176), D179 (≠ S177), P180 (vs. gap), Y181 (vs. gap), H211 (= H202), C212 (≠ L203), G213 (≠ P204), N218 (≠ T209), T239 (= T230), A240 (≠ S231), R241 (= R232), H290 (= H280), W293 (= W283)
4lceA Ctbp1 in complex with substrate mtob (see paper)
32% identity, 92% coverage: 24:314/318 of query aligns to 20:326/327 of 4lceA
- active site: S98 (≠ N100), R240 (= R232), D264 (= D256), E269 (= E261), H289 (= H280)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ K73), G73 (= G75), S74 (≠ A76), G75 (= G77), R240 (= R232), H289 (= H280), W292 (= W283)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ A76), T102 (≠ V104), G155 (= G154), G157 (= G156), R158 (≠ N157), V159 (≠ I158), Y177 (≠ T176), D178 (≠ S177), P179 (vs. gap), Y180 (vs. gap), H210 (= H202), C211 (≠ L203), N214 (≠ T206), N217 (≠ T209), T238 (= T230), A239 (≠ S231), R240 (= R232), W292 (= W283)
Q9Z2F5 C-terminal-binding protein 1; CtBP1; 50 kDa BFA-dependent ADP-ribosylation substrate; BARS-50; C-terminal-binding protein 3; CtBP3; EC 1.1.1.- from Rattus norvegicus (Rat) (see 3 papers)
32% identity, 92% coverage: 24:314/318 of query aligns to 35:341/430 of Q9Z2F5
- A41 (≠ R30) mutation to E: Strongly reduces interaction with E1A.
- V55 (≠ L44) mutation to R: Strongly reduces interaction with E1A.
- S89 (≠ A76) binding NAD(+)
- IGLGRV 169:174 (≠ VGYGNI 153:158) binding NAD(+)
- G172 (= G156) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ S177) binding NAD(+)
- 226:232 (vs. 203:209, 14% identical) binding NAD(+)
- TAR 253:255 (≠ TSR 230:232) binding NAD(+)
- D279 (= D256) binding NAD(+)
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
32% identity, 92% coverage: 24:314/318 of query aligns to 46:352/440 of Q13363
- A52 (≠ R30) mutation to E: Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3.
- V66 (≠ L44) mutation to R: Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3.
- C134 (≠ L110) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ A114) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R117) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (= RR 117:118) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ T126) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ G139) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (vs. gap) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G154) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G156) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-186.; mutation to V: Strongly reduces E1A binding; when associated with V-181 and A-204.
- G186 (≠ A159) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ S177) mutation to A: Strongly reduces E1A binding; when associated with V-181 and V-183.; mutation to L: Reduced proteolytic processing mediated by CAPN3.
- R266 (= R232) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D256) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E261) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H280) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295.
Sites not aligning to the query:
- 375:376 Cleavage; by CAPN1
- 387:388 Cleavage; by CAPN1
- 409:410 Cleavage; by CAPN1 and CAPN3
- 422 modified: Phosphoserine; by HIPK2; S→A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance.
- 428 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
31% identity, 80% coverage: 43:297/318 of query aligns to 39:311/334 of 3kb6B
- active site: S97 (≠ N100), R231 (= R232), D255 (= D256), E260 (= E261), H294 (= H280)
- binding lactic acid: F49 (≠ H52), S72 (≠ G75), V73 (≠ A76), G74 (= G77), Y96 (≠ A99), R231 (= R232), H294 (= H280)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A76), Y96 (≠ A99), V101 (= V104), G150 (= G156), R151 (≠ N157), I152 (= I158), D171 (= D172), V172 (= V173), P203 (= P204), T229 (= T230), A230 (≠ S231), R231 (= R232), H294 (= H280), A296 (≠ T282), Y297 (≠ W283)
7arzA Ternary complex of NAD-dependent formate dehydrogenase from physcomitrium patens
31% identity, 95% coverage: 2:302/318 of query aligns to 14:337/361 of 7arzA
- binding azide ion: T77 (≠ L54), P79 (= P56), F80 (vs. gap), L99 (≠ V71), V100 (≠ H72), T101 (≠ K73), G103 (= G75), V104 (≠ A76), R267 (= R232), H315 (= H280)
- binding nicotinamide-adenine-dinucleotide: V104 (≠ A76), N128 (= N100), V132 (= V104), G182 (= G156), R183 (≠ N157), I184 (= I158), D204 (≠ T178), R205 (= R179), T238 (≠ L203), P239 (= P204), Q243 (≠ A208), N265 (≠ T230), A266 (≠ S231), R267 (= R232), D291 (= D256), H315 (= H280), S317 (≠ T282), G318 (≠ W283)
Sites not aligning to the query:
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 81% coverage: 57:315/318 of query aligns to 57:323/334 of 5aovA
- active site: L100 (≠ N100), R241 (= R232), D265 (= D256), E270 (= E261), H288 (= H280)
- binding glyoxylic acid: Y74 (≠ L74), A75 (≠ G75), V76 (≠ A76), G77 (= G77), R241 (= R232), H288 (= H280)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A76), T104 (≠ V104), F158 (≠ Y155), G159 (= G156), R160 (≠ N157), I161 (= I158), S180 (= S177), R181 (vs. gap), A211 (≠ H202), V212 (≠ L203), P213 (= P204), T218 (= T209), I239 (≠ T230), A240 (≠ S231), R241 (= R232), H288 (= H280), G290 (≠ T282)
Sites not aligning to the query:
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
31% identity, 89% coverage: 36:317/318 of query aligns to 37:320/533 of O43175
- T78 (≠ A76) binding NAD(+)
- R135 (≠ S134) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ NI 157:158) binding NAD(+)
- D175 (vs. gap) binding NAD(+)
- T207 (≠ L203) binding NAD(+)
- CAR 234:236 (≠ TSR 230:232) binding NAD(+)
- D260 (= D256) binding NAD(+)
- V261 (= V257) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HVTW 280:283) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
36% identity, 78% coverage: 52:300/318 of query aligns to 55:315/332 of 4xkjA
- active site: S102 (≠ N100), R234 (= R232), D258 (= D256), E263 (= E261), H295 (= H280)
- binding nicotinamide-adenine-dinucleotide: Y101 (≠ A99), V106 (= V104), G152 (= G154), G154 (= G156), R155 (≠ N157), I156 (= I158), D175 (≠ S177), I176 (≠ T178), R179 (vs. gap), H204 (= H202), V205 (≠ L203), P206 (= P204), T211 (= T209), A232 (≠ T230), R234 (= R232), H295 (= H280), G297 (≠ T282), F298 (≠ W283)
Query Sequence
>WP_011777725.1 NCBI__GCF_000015305.1:WP_011777725.1
MRVLAHFVPGGPDSKVIEFLAPCRDWLDVRFCAEDDDDTFYRELADAEVIWHVLRPLSGE
DLARAPRLRLVHKLGAGVNTIDVDAATARGVAVANMPGANAESVAEGTLLLMLAALRRLP
VLDRATREGRGWPSDPTLGETVRDIGGCTVGLVGYGNIAKQVERILVAMGADVIHTSTRD
DGSAGWRSLPDLLSACDIVSLHLPLTDATAGLLGRDALARMKSDAVLVNTSRGPIVDEEA
LADALRTGKLAAAGLDVFAVEPVPADNPLLRLPNVVLTPHVTWYTADTMRRYLEFAVDNC
ERLRDGRNLVNVVNDVAG
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