SitesBLAST
Comparing GFF3435 FitnessBrowser__WCS417:GFF3435 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)
Q88H32 Ornithine cyclodeaminase; OCD; EC 4.3.1.12 from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
62% identity, 96% coverage: 1:335/348 of query aligns to 1:336/350 of Q88H32
- R45 (= R45) binding
- K69 (= K69) binding
- T84 (= T84) binding
- R112 (= R112) binding ; binding
- AQ 139:140 (≠ SQ 139:140) binding
- D161 (= D161) binding
- T202 (= T202) binding
- VGGD 225:228 (= VGGD 225:228) binding
- D228 (= D228) binding
- K232 (= K232) binding
- S293 (= S293) binding
- V294 (= V294) binding
- K331 (= K330) binding
1x7dA Crystal structure analysis of ornithine cyclodeaminase complexed with NAD and ornithine to 1.6 angstroms (see paper)
62% identity, 96% coverage: 2:335/348 of query aligns to 1:335/340 of 1x7dA
- active site: E55 (= E56), D227 (= D228)
- binding nicotinamide-adenine-dinucleotide: T83 (= T84), R111 (= R112), T112 (= T113), G137 (= G138), A138 (≠ S139), Q139 (= Q140), D160 (= D161), T161 (≠ I162), V200 (= V201), T201 (= T202), A202 (= A203), I209 (= I210), V224 (= V225), G225 (= G226), D227 (= D228), K231 (= K232), S292 (= S293), V293 (= V294), G294 (= G295)
- binding L-ornithine: R44 (= R45), V53 (= V54), E55 (= E56), M57 (= M58), K68 (= K69), V70 (= V71), N71 (= N72), G72 (= G73), R111 (= R112), D227 (= D228), V293 (= V294)
1u7hA Structure and a proposed mechanism for ornithine cyclodeaminase from pseudomonas putida (see paper)
62% identity, 96% coverage: 2:335/348 of query aligns to 1:335/341 of 1u7hA
- active site: E55 (= E56), D227 (= D228)
- binding nicotinamide-adenine-dinucleotide: T83 (= T84), R111 (= R112), T112 (= T113), G137 (= G138), A138 (≠ S139), Q139 (= Q140), D160 (= D161), T161 (≠ I162), V200 (= V201), T201 (= T202), A202 (= A203), I209 (= I210), V224 (= V225), G225 (= G226), D227 (= D228), K231 (= K232), S292 (= S293), V293 (= V294), G294 (= G295)
1omoA Alanine dehydrogenase dimer w/bound NAD (archaeal) (see paper)
34% identity, 78% coverage: 53:322/348 of query aligns to 49:319/320 of 1omoA
- active site: R52 (≠ E56), D219 (= D228)
- binding nicotinamide-adenine-dinucleotide: T109 (= T113), G134 (= G138), T135 (≠ S139), Q136 (= Q140), Y156 (≠ F160), D157 (= D161), V158 (≠ I162), R159 (≠ D163), T195 (= T202), P196 (≠ A203), G217 (= G226), D219 (= D228), K223 (= K232), S290 (= S293), T291 (≠ V294), G292 (= G295)
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)
34% identity, 78% coverage: 53:322/348 of query aligns to 49:319/322 of O28608
6t3eB Structure of thermococcus litoralis delta(1)-pyrroline-2-carboxylate reductase in complex with nadh and l-proline (see paper)
33% identity, 78% coverage: 52:322/348 of query aligns to 48:325/325 of 6t3eB
- binding 1,4-dihydronicotinamide adenine dinucleotide: S82 (≠ T84), T111 (= T113), G136 (= G138), V137 (≠ S139), Q138 (= Q140), D159 (= D161), I160 (= I162), A199 (= A203), T200 (≠ D204), T201 (≠ K205), A202 (= A206), V206 (≠ I210), V221 (= V225), G222 (= G226), W223 (≠ G227), S296 (= S293), V297 (= V294), G298 (= G295)
- binding proline: M54 (= M58), K67 (= K69), R110 (= R112)
Sites not aligning to the query:
5yu4A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
34% identity, 76% coverage: 53:317/348 of query aligns to 60:325/344 of 5yu4A
- binding 2,4-diaminobutyric acid: E63 (= E56), K77 (= K69), R121 (= R112), T302 (≠ V294), G303 (= G295)
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ G73), T93 (= T84), I94 (≠ V85), R121 (= R112), T122 (= T113), G147 (= G138), A148 (≠ S139), Q149 (= Q140), D170 (= D161), T171 (≠ I162), H175 (≠ T167), A208 (≠ V201), T209 (= T202), S210 (≠ A203), V211 (≠ D204), V218 (≠ I210), V233 (= V225), A235 (≠ G227), S301 (= S293), T302 (≠ V294), G303 (= G295)
5yu3A Structural basis for recognition of l-lysine, l-ornithine, and l-2,4- diamino butyric acid by lysine cyclodeaminase (see paper)
34% identity, 76% coverage: 53:317/348 of query aligns to 60:325/344 of 5yu3A
- binding nicotinamide-adenine-dinucleotide: Y81 (≠ G73), T93 (= T84), I94 (≠ V85), T122 (= T113), G147 (= G138), A148 (≠ S139), Q149 (= Q140), D170 (= D161), T171 (≠ I162), A208 (≠ V201), T209 (= T202), S210 (≠ A203), V211 (≠ D204), V233 (= V225), A235 (≠ G227), S301 (= S293), T302 (≠ V294), G303 (= G295)
- binding proline: M65 (= M58), K77 (= K69), R121 (= R112)
5gzlA Cyclodeaminase_pa
34% identity, 76% coverage: 53:317/348 of query aligns to 64:329/357 of 5gzlA
- binding lysine: I65 (≠ V54), E67 (= E56), D240 (= D228), R267 (≠ I255), E268 (= E256)
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ G73), T97 (= T84), I98 (≠ V85), T126 (= T113), G151 (= G138), A152 (≠ S139), Q153 (= Q140), D174 (= D161), T175 (≠ I162), H179 (≠ T167), A212 (≠ V201), T213 (= T202), S214 (≠ A203), V222 (≠ I210), V237 (= V225), G238 (= G226), A239 (≠ G227), D240 (= D228), K244 (= K232), S305 (= S293), T306 (≠ V294), G307 (= G295)
Sites not aligning to the query:
5gziA Cyclodeaminase_pa
34% identity, 76% coverage: 53:317/348 of query aligns to 64:329/354 of 5gziA
- binding nicotinamide-adenine-dinucleotide: Y85 (≠ G73), T97 (= T84), R125 (= R112), T126 (= T113), G151 (= G138), A152 (≠ S139), Q153 (= Q140), D174 (= D161), T175 (≠ I162), H179 (≠ T167), A212 (≠ V201), T213 (= T202), S214 (≠ A203), V215 (≠ D204), V237 (= V225), G238 (= G226), A239 (≠ G227), S305 (= S293), T306 (≠ V294), G307 (= G295)
- binding (2S)-piperidine-2-carboxylic acid: K81 (= K69), R125 (= R112), A239 (≠ G227), T306 (≠ V294), G307 (= G295)
Sites not aligning to the query:
6rqaB Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
31% identity, 73% coverage: 70:322/348 of query aligns to 74:322/322 of 6rqaB
- binding Tb-Xo4: N76 (= N72)
- binding nicotinamide-adenine-dinucleotide: T113 (= T113), G138 (= G138), Q140 (= Q140), P162 (≠ I162), H163 (≠ D163), I199 (≠ V201), T200 (= T202), S201 (≠ A203), S202 (≠ A206), M221 (≠ V225), G222 (= G226), D224 (= D228), K228 (= K232), G293 (≠ S293), T294 (≠ V294), G295 (= G295)
Sites not aligning to the query:
6rqaA Crystal structure of the iminosuccinate reductase of paracoccus denitrificans in complex with NAD+ (see paper)
31% identity, 73% coverage: 70:322/348 of query aligns to 74:322/322 of 6rqaA
- binding nicotinamide-adenine-dinucleotide: H85 (≠ G81), T113 (= T113), G138 (= G138), H139 (≠ S139), Q140 (= Q140), N161 (≠ D161), P162 (≠ I162), H163 (≠ D163), M166 (≠ A166), I199 (≠ V201), T200 (= T202), S201 (≠ A203), S202 (≠ A206), M221 (≠ V225), G222 (= G226), D224 (= D228), K228 (= K232), G293 (≠ S293)
A1B8Z0 Iminosuccinate reductase; EC 1.4.1.- from Paracoccus denitrificans (strain Pd 1222) (see paper)
31% identity, 73% coverage: 70:322/348 of query aligns to 72:320/320 of A1B8Z0
Q14894 Ketimine reductase mu-crystallin; NADP-regulated thyroid-hormone-binding protein; EC 1.5.1.25 from Homo sapiens (Human) (see paper)
32% identity, 60% coverage: 101:309/348 of query aligns to 106:308/314 of Q14894
2i99A Crystal structure of human mu_crystallin at 2.6 angstrom (see paper)
32% identity, 60% coverage: 101:309/348 of query aligns to 105:307/312 of 2i99A
- active site: S228 (≠ D228)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R118 (= R112), T119 (= T113), G142 (= G136), A143 (≠ N137), G144 (= G138), V145 (≠ S139), Q146 (= Q140), N167 (≠ D161), R168 (≠ I162), T169 (≠ D163), V203 (= V201), T204 (= T202), L205 (≠ A203), A206 (= A206), V225 (= V225), G226 (= G226), S291 (= S293), L292 (≠ V294), G293 (= G295)
Sites not aligning to the query:
4bv9A Crystal structure of the NADPH form of mouse mu-crystallin. (see paper)
32% identity, 60% coverage: 101:309/348 of query aligns to 97:299/303 of 4bv9A
- active site: S220 (≠ D228)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T111 (= T113), G134 (= G136), G136 (= G138), V137 (≠ S139), Q138 (= Q140), N159 (≠ D161), R160 (≠ I162), T161 (≠ D163), V195 (= V201), T196 (= T202), M197 (≠ K205), A198 (= A206), V217 (= V225), G218 (= G226), S283 (= S293), L284 (≠ V294), G285 (= G295)
- binding pyruvic acid: R110 (= R112)
Sites not aligning to the query:
4bvaA Crystal structure of the NADPH-t3 form of mouse mu-crystallin. (see paper)
32% identity, 60% coverage: 101:309/348 of query aligns to 96:298/303 of 4bvaA
- active site: S219 (≠ D228)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: T106 (= T109), R109 (= R112), T110 (= T113), G135 (= G138), V136 (≠ S139), Q137 (= Q140), N158 (≠ D161), R159 (≠ I162), T160 (≠ D163), N163 (≠ A166), V194 (= V201), T195 (= T202), M196 (≠ K205), A197 (= A206), V216 (= V225), S282 (= S293), L283 (≠ V294), G284 (= G295)
- binding 3,5,3'triiodothyronine: S219 (≠ D228), R220 (≠ C229), W223 (≠ K232), E247 (= E256)
Sites not aligning to the query:
4mpdA Staphyloferrin b precursor biosynthetic enzyme sbnb bound a- ketoglutarate and NAD+ (see paper)
24% identity, 67% coverage: 91:322/348 of query aligns to 87:317/318 of 4mpdA
Sites not aligning to the query:
4m54A The structure of the staphyloferrin b precursor biosynthetic enzyme sbnb bound to n-(1-amino-1-carboxyl-2-ethyl)-glutamic acid and nadh (see paper)
24% identity, 67% coverage: 91:322/348 of query aligns to 94:309/310 of 4m54A
Sites not aligning to the query:
4mp6A Staphyloferrin b precursor biosynthetic enzyme sbnb bound to citrate and NAD+ (see paper)
24% identity, 67% coverage: 91:322/348 of query aligns to 99:333/334 of 4mp6A
- active site: M236 (≠ T233)
- binding nicotinamide-adenine-dinucleotide: R120 (= R112), T121 (= T113), G146 (= G138), L147 (vs. gap), I148 (vs. gap), D170 (= D161), Q171 (≠ I162), C211 (≠ V201), T212 (= T202), V213 (vs. gap), I233 (≠ V225), G306 (= G295)
Sites not aligning to the query:
Query Sequence
>GFF3435 FitnessBrowser__WCS417:GFF3435
MTRYIDVNDLCYLVSQKGLQTCITEMAEYIRADYLRWQDFEKCARLANHSPDGVIELMPV
SDASLYAFKYVNGHPKNTLAGMLTVMAFGALGDVDTGLPVLLAEMTLTTAIRTAATSALV
ARYLARDNSRSMALIGNGSQSEFQALAFHAMLGITEIRLFDIDAKATAKLAANLKAFPAI
KVILAGSVAEAVKGADIVTTVTADKAYATILTDEMIEPGMHLNAVGGDCPGKTELDRRIV
ERARVIVEYEPQSRIEGEIQHMPEDSPVTELWQVINGQQPGRENARQVTLFDSVGFAIED
YSALRYVLDVAKALDVGSDLELVPDLADPKDLFARLAQQPRAQQKKRA
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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