SitesBLAST
Comparing Ac3H11_4531 FitnessBrowser__acidovorax_3H11:Ac3H11_4531 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
Q88H32 Ornithine cyclodeaminase; OCD; EC 4.3.1.12 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
65% identity, 95% coverage: 9:345/353 of query aligns to 2:338/350 of Q88H32
- R45 (= R52) binding
- K69 (= K76) binding
- T84 (= T91) binding
- R112 (= R119) binding ; binding
- AQ 139:140 (= AQ 146:147) binding
- D161 (= D168) binding
- T202 (= T208) binding
- VGGD 225:228 (= VGGD 231:234) binding
- D228 (= D234) binding
- K232 (= K238) binding
- S293 (= S299) binding
- V294 (= V300) binding
- K331 (= K336) binding
1x7dA Crystal structure analysis of ornithine cyclodeaminase complexed with NAD and ornithine to 1.6 angstroms (see paper)
65% identity, 95% coverage: 9:345/353 of query aligns to 1:337/340 of 1x7dA
- active site: E55 (= E63), D227 (= D234)
- binding nicotinamide-adenine-dinucleotide: T83 (= T91), R111 (= R119), T112 (= T120), G137 (= G145), A138 (= A146), Q139 (= Q147), D160 (= D168), T161 (= T169), V200 (= V207), T201 (= T208), A202 (= A209), I209 (= I216), V224 (= V231), G225 (= G232), D227 (= D234), K231 (= K238), S292 (= S299), V293 (= V300), G294 (= G301)
- binding L-ornithine: R44 (= R52), V53 (= V61), E55 (= E63), M57 (= M65), K68 (= K76), V70 (= V78), N71 (= N79), G72 (= G80), R111 (= R119), D227 (= D234), V293 (= V300)
1u7hA Structure and a proposed mechanism for ornithine cyclodeaminase from pseudomonas putida (see paper)
65% identity, 95% coverage: 9:345/353 of query aligns to 1:337/341 of 1u7hA
- active site: E55 (= E63), D227 (= D234)
- binding nicotinamide-adenine-dinucleotide: T83 (= T91), R111 (= R119), T112 (= T120), G137 (= G145), A138 (= A146), Q139 (= Q147), D160 (= D168), T161 (= T169), V200 (= V207), T201 (= T208), A202 (= A209), I209 (= I216), V224 (= V231), G225 (= G232), D227 (= D234), K231 (= K238), S292 (= S299), V293 (= V300), G294 (= G301)
O28608 Alanine dehydrogenase; AlaDH; EC 1.4.1.1 from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) (see paper)
33% identity, 72% coverage: 75:328/353 of query aligns to 64:319/322 of O28608
1omoA Alanine dehydrogenase dimer w/bound NAD (archaeal) (see paper)
33% identity, 72% coverage: 75:328/353 of query aligns to 64:319/320 of 1omoA
- active site: D219 (= D234)
- binding nicotinamide-adenine-dinucleotide: T109 (= T120), G134 (= G145), T135 (≠ A146), Q136 (= Q147), Y156 (≠ F167), D157 (= D168), V158 (≠ T169), R159 (≠ D170), T195 (= T208), P196 (≠ A209), G217 (= G232), D219 (= D234), K223 (= K238), S290 (= S299), T291 (≠ V300), G292 (= G301)
Sites not aligning to the query:
5gzlA Cyclodeaminase_pa
35% identity, 90% coverage: 6:323/353 of query aligns to 4:329/357 of 5gzlA
- binding lysine: G55 (≠ A46), E57 (≠ D48), I65 (≠ V61), E67 (= E63), D240 (= D234), R267 (≠ I261), E268 (= E262)
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ G80), T97 (= T91), I98 (≠ V92), T126 (= T120), G151 (= G145), A152 (= A146), Q153 (= Q147), D174 (= D168), T175 (= T169), H179 (≠ A173), A212 (≠ V207), T213 (= T208), S214 (≠ A209), V222 (≠ L217), V237 (= V231), G238 (= G232), A239 (≠ G233), D240 (= D234), K244 (= K238), S305 (= S299), T306 (≠ V300), G307 (= G301)
5gziA Cyclodeaminase_pa
35% identity, 90% coverage: 6:323/353 of query aligns to 4:329/354 of 5gziA
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ G80), T97 (= T91), R125 (= R119), T126 (= T120), G151 (= G145), A152 (= A146), Q153 (= Q147), D174 (= D168), T175 (= T169), H179 (≠ A173), A212 (≠ V207), T213 (= T208), S214 (≠ A209), V215 (≠ D210), V237 (= V231), G238 (= G232), A239 (≠ G233), S305 (= S299), T306 (≠ V300), G307 (= G301)
- binding (2S)-piperidine-2-carboxylic acid: R53 (= R43), K81 (= K76), R125 (= R119), A239 (≠ G233), T306 (≠ V300), G307 (= G301)
5yu4A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
35% identity, 90% coverage: 7:323/353 of query aligns to 1:325/344 of 5yu4A
- binding 2,4-diaminobutyric acid: E63 (= E63), K77 (= K76), R121 (= R119), T302 (≠ V300), G303 (= G301)
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ G80), T93 (= T91), I94 (≠ V92), R121 (= R119), T122 (= T120), G147 (= G145), A148 (= A146), Q149 (= Q147), D170 (= D168), T171 (= T169), H175 (≠ A173), A208 (≠ V207), T209 (= T208), S210 (≠ A209), V211 (≠ D210), V218 (≠ L217), V233 (= V231), A235 (≠ G233), S301 (= S299), T302 (≠ V300), G303 (= G301)
5yu3A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
35% identity, 90% coverage: 7:323/353 of query aligns to 1:325/344 of 5yu3A
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ G80), T93 (= T91), I94 (≠ V92), T122 (= T120), G147 (= G145), A148 (= A146), Q149 (= Q147), D170 (= D168), T171 (= T169), A208 (≠ V207), T209 (= T208), S210 (≠ A209), V211 (≠ D210), V233 (= V231), A235 (≠ G233), S301 (= S299), T302 (≠ V300), G303 (= G301)
- binding proline: M65 (= M65), K77 (= K76), R121 (= R119)
6t3eB Structure of thermococcus litoralis delta(1)-pyrroline-2-carboxylate reductase in complex with nadh and l-proline (see paper)
32% identity, 78% coverage: 53:328/353 of query aligns to 42:325/325 of 6t3eB
- binding 1,4-dihydronicotinamide adenine dinucleotide: S82 (≠ T91), T111 (= T120), G136 (= G145), V137 (≠ A146), Q138 (= Q147), D159 (= D168), I160 (≠ T169), A199 (= A209), T200 (≠ D210), T201 (≠ K211), A202 (≠ T212), V206 (≠ I216), V221 (= V231), G222 (= G232), W223 (≠ G233), S296 (= S299), V297 (= V300), G298 (= G301)
- binding proline: M54 (= M65), K67 (= K76), R110 (= R119)
Sites not aligning to the query:
4bv9A Crystal structure of the NADPH form of mouse mu-crystallin. (see paper)
33% identity, 66% coverage: 85:316/353 of query aligns to 76:300/303 of 4bv9A
- active site: S220 (≠ D234)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S82 (≠ T91), H83 (≠ V92), T111 (= T120), G134 (= G143), G136 (= G145), V137 (≠ A146), Q138 (= Q147), N159 (≠ D168), R160 (≠ T169), T161 (≠ D170), V195 (= V207), T196 (= T208), M197 (≠ A209), A198 (≠ T212), V217 (= V231), G218 (= G232), S283 (= S299), L284 (≠ V300), G285 (= G301)
- binding pyruvic acid: R110 (= R119)
Sites not aligning to the query:
4bvaA Crystal structure of the NADPH-t3 form of mouse mu-crystallin. (see paper)
33% identity, 62% coverage: 97:316/353 of query aligns to 87:299/303 of 4bvaA
- active site: S219 (≠ D234)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T106 (= T116), R109 (= R119), T110 (= T120), G135 (= G145), V136 (≠ A146), Q137 (= Q147), N158 (≠ D168), R159 (≠ T169), T160 (≠ D170), N163 (≠ A173), V194 (= V207), T195 (= T208), M196 (≠ A209), A197 (≠ T212), V216 (= V231), S282 (= S299), L283 (≠ V300), G284 (= G301)
- binding 3,5,3'triiodothyronine: S219 (≠ D234), R220 (≠ C235), W223 (≠ K238), E247 (= E262)
Sites not aligning to the query:
Q14894 Ketimine reductase mu-crystallin; NADP-regulated thyroid-hormone-binding protein; EC 1.5.1.25 from Homo sapiens (Human) (see paper)
31% identity, 65% coverage: 89:316/353 of query aligns to 89:309/314 of Q14894
2i99A Crystal structure of human mu_crystallin at 2.6 angstrom (see paper)
31% identity, 65% coverage: 89:316/353 of query aligns to 88:308/312 of 2i99A
- active site: S228 (≠ D234)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: S90 (≠ T91), H91 (≠ V92), R118 (= R119), T119 (= T120), G142 (= G143), A143 (≠ N144), G144 (= G145), V145 (≠ A146), Q146 (= Q147), N167 (≠ D168), R168 (≠ T169), T169 (≠ D170), V203 (= V207), T204 (= T208), L205 (≠ A209), A206 (≠ T212), V225 (= V231), G226 (= G232), S291 (= S299), L292 (≠ V300), G293 (= G301)
Sites not aligning to the query:
6rqaB Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
29% identity, 70% coverage: 82:328/353 of query aligns to 75:322/322 of 6rqaB
- binding Tb-Xo4: N76 (≠ K83)
- binding nicotinamide-adenine-dinucleotide: T113 (= T120), G138 (= G145), Q140 (= Q147), P162 (≠ T169), H163 (≠ D170), I199 (≠ V207), T200 (= T208), S201 (≠ A209), S202 (≠ T212), M221 (≠ V231), G222 (= G232), D224 (= D234), K228 (= K238), G293 (≠ S299), T294 (≠ V300), G295 (= G301)
Sites not aligning to the query:
6rqaA Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
29% identity, 70% coverage: 82:328/353 of query aligns to 75:322/322 of 6rqaA
- binding nicotinamide-adenine-dinucleotide: H85 (≠ V92), T113 (= T120), G138 (= G145), H139 (≠ A146), Q140 (= Q147), N161 (≠ D168), P162 (≠ T169), H163 (≠ D170), M166 (≠ A173), I199 (≠ V207), T200 (= T208), S201 (≠ A209), S202 (≠ T212), M221 (≠ V231), G222 (= G232), D224 (= D234), K228 (= K238), G293 (≠ S299)
A1B8Z0 Iminosuccinate reductase; EC 1.4.1.- from Paracoccus denitrificans (strain Pd 1222) (see paper)
29% identity, 70% coverage: 82:328/353 of query aligns to 73:320/320 of A1B8Z0
Q9FLY0 Protein SAR DEFICIENT 4; Ornithine cyclodeaminase-like protein; AtOCD from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 66% coverage: 76:307/353 of query aligns to 71:311/325 of Q9FLY0
- G89 (≠ A94) mutation to E: In sard4-3; compromises systemic acquired resistance (SAR).
- G138 (= G143) mutation to D: In sard4-4; compromises systemic acquired resistance (SAR).
- S205 (≠ A209) mutation to N: In sard4-1; compromises systemic acquired resistance (SAR).
Query Sequence
>Ac3H11_4531 FitnessBrowser__acidovorax_3H11:Ac3H11_4531
MAAPQHFSTLYLSAPDVIALVQRKGIEPCLRGIADYIHADFLRWGAFDKSARVASHSRDG
VIELMPIADGETYAFKYVNGHPKNTRWGLPTVMAFGVLADVATGAPLLLSELTLTTALRT
AAMSAVAARALARPGSRTMALIGNGAQSEFQALAFHHLLGIDTLRLFDTDPAATAKLQAN
LKGTGPRTVACTSTAEAVRGADVVTTVTADKTNATILTPDMLAPGMHINAVGGDCPGKTE
LHADVLRQAQVFVEYAPQTRIEGDIQQLPADFAVTELWEVLAGQHGGRASDAAVTVFDSV
GFALEDFSALRFLRDAAAELGMGQPIELIPQLSDPKNLFGLLHTRSPLLRVVA
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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