SitesBLAST
Comparing WP_011970220.1 NCBI__GCF_000017145.1:WP_011970220.1 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)
5m4bA Alpha-amino epsilon-caprolactam racemase d210a mutant in complex with plp and geminal diamine intermediate
56% identity, 99% coverage: 4:437/437 of query aligns to 9:439/439 of 5m4bA
- active site: Q21 (≠ A16), Y140 (= Y136), E208 (= E204), D241 (= D237), K244 (= K240), K270 (= K266), T298 (= T294), E399 (= E395)
- binding [6-methyl-5-oxidanyl-4-[(~{E})-[(3~{R})-2-oxidanylideneazepan-3-yl]iminomethyl]pyridin-3-yl]methyl dihydrogen phosphate: W53 (= W48), S112 (= S108), G113 (= G109), S114 (= S110), Y140 (= Y136), H141 (= H137), E208 (= E204), D241 (= D237), V243 (= V239), K244 (= K240), K270 (= K266)
5m46A Alpha-amino epsilon-caprolactam racemase (aclr) from rhizobacterium freirei
56% identity, 99% coverage: 4:434/437 of query aligns to 9:429/429 of 5m46A
- active site: Q21 (≠ A16), Y141 (= Y136), E201 (= E204), D234 (= D237), K237 (= K240), K263 (= K266), T291 (= T294), E392 (= E395)
- binding pyridoxal-5'-phosphate: S113 (= S108), G114 (= G109), S115 (= S110), Y141 (= Y136), H142 (= H137), E201 (= E204), D234 (= D237), V236 (= V239), K237 (= K240), K263 (= K266)
5m49A Alpha-amino epsilon-caprolactam racemase in complex with plp and d/l alpha amino epsilon-caprolactam (internal aldimine)
56% identity, 99% coverage: 4:437/437 of query aligns to 3:423/423 of 5m49A
- active site: Q15 (≠ A16), Y134 (= Y136), E193 (= E204), D226 (= D237), K229 (= K240), K255 (= K266), T283 (= T294), E384 (= E395)
- binding (3~{R})-3-azanylazepan-2-one: W47 (= W48), Y134 (= Y136), D198 (= D209), K229 (= K240), K255 (= K266), W423 (= W437)
- binding (3~{S})-3-azanylazepan-2-one: L17 (= L18), W47 (= W48), Y134 (= Y136), D198 (= D209), K255 (= K266), W423 (= W437)
- binding pyridoxal-5'-phosphate: S106 (= S108), G107 (= G109), S108 (= S110), Y134 (= Y136), H135 (= H137), D226 (= D237), V228 (= V239), K229 (= K240), K255 (= K266)
Q7M181 2-aminohexano-6-lactam racemase; 2-amino-hexano-6-lactam racemase; Alpha-amino-epsilon-caprolactam racemase; EC 5.1.1.15 from Achromobacter obae (see paper)
54% identity, 99% coverage: 4:437/437 of query aligns to 5:436/436 of Q7M181
- T295 (= T294) binding pyridoxal 5'-phosphate
3dxvB The crystal structure of alpha-amino-epsilon-caprolactam racemase from achromobacter obae (see paper)
54% identity, 99% coverage: 4:437/437 of query aligns to 3:434/434 of 3dxvB
- active site: Q15 (≠ A16), Y135 (= Y136), E203 (= E204), D236 (= D237), K239 (= K240), K265 (= K266), T293 (= T294), E394 (= E395)
- binding pyridoxal-5'-phosphate: S107 (= S108), S109 (= S110), Y135 (= Y136), H136 (= H137), E203 (= E204), D236 (= D237), V238 (= V239), K265 (= K266), Q292 (= Q293), T293 (= T294)
6gioC Structure of amino acid amide racemase from ochrobactrum anthropi (see paper)
53% identity, 99% coverage: 4:434/437 of query aligns to 6:435/436 of 6gioC
- active site: G18 (≠ A16), Y138 (= Y136), D237 (= D237), K266 (= K266)
- binding pyridoxal-5'-phosphate: S110 (= S108), G111 (= G109), S112 (= S110), Y138 (= Y136), H139 (= H137), E204 (= E204), D237 (= D237), V239 (= V239), K240 (= K240), K266 (= K266), Q293 (= Q293), T294 (= T294)
2zukA The crystal structure of alpha-amino-epsilon-caprolactam racemase from achromobacter obae complexed with epsilon caprolactam (different binding mode) (see paper)
53% identity, 99% coverage: 4:437/437 of query aligns to 4:422/422 of 2zukA
- active site: Q16 (≠ A16), Y136 (= Y136), E191 (= E204), D224 (= D237), K227 (= K240), K253 (= K266), T281 (= T294), E382 (= E395)
- binding azepan-2-one: L18 (= L18), W48 (= W48), L77 (= L77), Y136 (= Y136), K227 (= K240), K253 (= K266), T281 (= T294), W422 (= W437)
- binding pyridoxal-5'-phosphate: G109 (= G109), S110 (= S110), Y136 (= Y136), H137 (= H137), D224 (= D237), V226 (= V239), K253 (= K266), Q280 (= Q293), T281 (= T294)
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
36% identity, 98% coverage: 4:431/437 of query aligns to 35:471/474 of O58478
- D251 (= D209) mutation to A: Loss of activity.
- K308 (= K266) mutation to A: Loss of activity.
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
35% identity, 97% coverage: 4:426/437 of query aligns to 8:437/439 of 5wyaA
- active site: A20 (= A16), Y140 (= Y136), E215 (= E204), D248 (= D237), N251 (≠ K240), K278 (= K266), T307 (= T294), R406 (≠ E395)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ W48), Y82 (vs. gap), S112 (= S108), G113 (= G109), S114 (= S110), Y140 (= Y136), H141 (= H137), E215 (= E204), D248 (= D237), V250 (= V239), N251 (≠ K240), K278 (= K266), F306 (≠ Q293), T307 (= T294), R406 (≠ E395)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
35% identity, 97% coverage: 4:426/437 of query aligns to 10:439/446 of 5wyfA
- active site: A22 (= A16), Y142 (= Y136), E217 (= E204), D250 (= D237), N253 (≠ K240), K280 (= K266), T309 (= T294), R408 (≠ E395)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ W48), Y84 (vs. gap), G115 (= G109), S116 (= S110), Y142 (= Y136), H143 (= H137), D222 (= D209), D250 (= D237), V252 (= V239), N253 (≠ K240), K280 (= K266), F308 (≠ Q293), T309 (= T294), R408 (≠ E395)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
35% identity, 97% coverage: 4:426/437 of query aligns to 17:446/448 of 4ysnC
- active site: A29 (= A16), Y149 (= Y136), E224 (= E204), D257 (= D237), N260 (≠ K240), K287 (= K266), T316 (= T294), R415 (≠ E395)
- binding pyridoxal-5'-phosphate: S121 (= S108), G122 (= G109), S123 (= S110), Y149 (= Y136), H150 (= H137), E224 (= E204), D257 (= D237), V259 (= V239), K287 (= K266), F315 (≠ Q293), T316 (= T294)
7vo1A Structure of aminotransferase-substrate complex (see paper)
36% identity, 90% coverage: 29:422/437 of query aligns to 42:444/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ W48), S121 (= S108), G122 (= G109), T123 (≠ S110), F149 (≠ Y136), H150 (= H137), R152 (≠ G139), E234 (≠ D209), D262 (= D237), V264 (= V239), Q265 (≠ K240), K291 (= K266), N318 (vs. gap), T319 (vs. gap), R417 (≠ E395)
7vntA Structure of aminotransferase-substrate complex (see paper)
36% identity, 90% coverage: 29:422/437 of query aligns to 42:444/452 of 7vntA
- binding L-ornithine: F149 (≠ Y136), R152 (≠ G139), E234 (≠ D209), K291 (= K266)
- binding pyridoxal-5'-phosphate: G122 (= G109), T123 (≠ S110), F149 (≠ Y136), H150 (= H137), E229 (= E204), D262 (= D237), V264 (= V239), Q265 (≠ K240), K291 (= K266)
7vnoA Structure of aminotransferase (see paper)
36% identity, 90% coverage: 29:422/437 of query aligns to 42:444/452 of 7vnoA
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
36% identity, 90% coverage: 29:422/437 of query aligns to 44:446/454 of O50131
- T92 (≠ L77) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ S78) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G109) binding pyridoxal 5'-phosphate
- T125 (≠ S110) binding pyridoxal 5'-phosphate
- Q267 (≠ K240) binding pyridoxal 5'-phosphate
- K293 (= K266) modified: N6-(pyridoxal phosphate)lysine
- T321 (vs. gap) binding pyridoxal 5'-phosphate
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
35% identity, 87% coverage: 37:418/437 of query aligns to 39:421/426 of P22256
- I50 (≠ W48) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (= GS 109:110) binding pyridoxal 5'-phosphate
- E211 (≠ D209) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V239) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (≠ K240) binding pyridoxal 5'-phosphate
- K268 (= K266) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T294) binding pyridoxal 5'-phosphate
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
35% identity, 87% coverage: 37:418/437 of query aligns to 38:420/425 of 1sffA
- active site: Y137 (= Y136), E205 (= E204), D238 (= D237), Q241 (≠ K240), K267 (= K266), T296 (= T294), R397 (≠ E395)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ L77), G110 (= G109), S111 (= S110), Y137 (= Y136), H138 (= H137), R140 (≠ G139), E205 (= E204), D238 (= D237), V240 (= V239), Q241 (≠ K240), K267 (= K266), T296 (= T294)
- binding sulfate ion: N152 (≠ G154), Y393 (≠ S391)
Sites not aligning to the query:
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
35% identity, 87% coverage: 37:418/437 of query aligns to 38:420/425 of 1sf2A
- active site: Y137 (= Y136), E205 (= E204), D238 (= D237), Q241 (≠ K240), K267 (= K266), T296 (= T294), R397 (≠ E395)
- binding pyridoxal-5'-phosphate: G110 (= G109), S111 (= S110), Y137 (= Y136), H138 (= H137), E205 (= E204), D238 (= D237), V240 (= V239), Q241 (≠ K240), K267 (= K266)
- binding sulfate ion: N152 (≠ G154), Y393 (≠ S391)
Sites not aligning to the query:
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
35% identity, 87% coverage: 37:418/437 of query aligns to 38:420/425 of 1szkA
- active site: Y137 (= Y136), E205 (= E204), D238 (= D237), Q241 (≠ K240), K267 (= K266), T296 (= T294), R397 (≠ E395)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G109), S111 (= S110), Y137 (= Y136), H138 (= H137), E205 (= E204), D238 (= D237), V240 (= V239), Q241 (≠ K240), K267 (= K266)
Sites not aligning to the query:
8ht4B Crystal structure of acetylornithine aminotransferase complex with plp from corynebacterium glutamicum (see paper)
36% identity, 91% coverage: 22:419/437 of query aligns to 18:390/390 of 8ht4B
Query Sequence
>WP_011970220.1 NCBI__GCF_000017145.1:WP_011970220.1
MPGLYARESRSISSMAHLRFFPQAVVGGSGAYLTADDGRRLLDFSASWGAASLGHSHPAI
REAVDRALSDQAGASYLSTANEPCVLLAEKLLSLVPERARGRIWFGHSGSDANETVARMV
VAATGRPRILAFEGAYHGGTVGSMGISGHPAQQGGRAEGLTLVPYPNSYAAGSPEAAKDA
ALARLQHLFATELPPGEVAAFFIEPIQSDGGMLLPPDGFFKAVEALCRKHGILIVSDEVK
VGLGRSGRFNAFEQSGIEPDIIVFGKGLGGGLPISAVVGPEAVMNHAVAFSLQTVHGNPI
CAAAALAVLQTIERNRLAENAERTGGVLRESLDRLAARHRLIGDVRGRGLALGVELVEDR
TSRKPASRQTALTVYRAFQLGLVLYYVGVRSNVLELTPPLTLTQAEAREGVAILDQALAD
VAAGRIDDAVLEDFAGW
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