SitesBLAST
Comparing WP_020175324.1 NCBI__GCF_000385335.1:WP_020175324.1 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)
A0R5R7 Putative aminotransferase MSMEG_6286/MSMEI_6121 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
55% identity, 92% coverage: 22:413/425 of query aligns to 21:415/428 of A0R5R7
- K339 (≠ G337) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3pplA Crystal structure of an aspartate transaminase (ncgl0237, cgl0240) from corynebacterium glutamicum atcc 13032 kitasato at 1.25 a resolution
52% identity, 95% coverage: 19:420/425 of query aligns to 20:421/424 of 3pplA
5hxxA Crystal structure of aspat from corynebacterium glutamicum
52% identity, 95% coverage: 19:420/425 of query aligns to 18:419/424 of 5hxxA
- binding 2-oxoglutaric acid: G37 (= G38), Y139 (= Y140), R141 (= R142), K256 (= K257)
- binding glutamic acid: Y70 (= Y71), I286 (= I287)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: S100 (= S101), S101 (= S102), L102 (= L103), Y139 (= Y140), V183 (= V184), D217 (= D218), A219 (= A220), Y220 (= Y221), S253 (= S254), S255 (= S256), K256 (= K257)
Q8NTR2 Aspartate aminotransferase; AspAT; EC 2.6.1.1 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
52% identity, 95% coverage: 19:420/425 of query aligns to 27:428/432 of Q8NTR2
- R45 (= R37) mutation to A: Loss of activity.
- RG 45:46 (= RG 37:38) binding substrate
- K47 (= K39) mutation to A: 40% decrease in activity.
- Y79 (= Y71) mutation to A: Loss of activity.
- S109 (= S101) mutation to A: 30% decrease in activity.
- SSL 109:111 (= SSL 101:103) binding pyridoxal 5'-phosphate
- S110 (= S102) mutation to A: 30% decrease in activity.
- Y148 (= Y140) mutation to A: Loss of activity.
- YDR 148:150 (= YDR 140:142) binding substrate
- R150 (= R142) mutation to A: 80% decrease in activity.
- N197 (= N189) binding pyridoxal 5'-phosphate; mutation to A: Loss of activity.
- D226 (= D218) mutation to A: Loss of activity.
- Y229 (= Y221) binding pyridoxal 5'-phosphate; mutation to A: Loss of activity.
- STSK 262:265 (= STSK 254:257) binding pyridoxal 5'-phosphate
- S264 (= S256) mutation to A: 30% decrease in activity.
- K265 (= K257) mutation to A: Loss of activity.
- R400 (= R392) binding substrate; mutation to A: Loss of activity.
5iwqB Crystal structure of aspartate aminotransferase (aspat) from corynebacterium glutamicum atcc 13032 (see paper)
52% identity, 95% coverage: 19:420/425 of query aligns to 18:419/424 of 5iwqB
- binding citrate anion: R36 (= R37), G37 (= G38), Y139 (= Y140), R141 (= R142), K256 (= K257)
- binding pyridoxal-5'-phosphate: S100 (= S101), S101 (= S102), L102 (= L103), Y139 (= Y140), D217 (= D218), A219 (= A220), Y220 (= Y221), S253 (= S254), S255 (= S256), K256 (= K257)
6u7aD Rv3722c in complex with kynurenine (see paper)
51% identity, 98% coverage: 3:420/425 of query aligns to 1:419/429 of 6u7aD
- binding 4-hydroxyquinoline-2-carboxylic acid: G36 (= G38), Y138 (= Y140), R140 (= R142), K256 (= K257), F348 (= F349)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: S98 (= S101), S99 (= S102), L100 (= L103), Y138 (= Y140), D217 (= D218), A219 (= A220), Y220 (= Y221), S253 (= S254), S255 (= S256), K256 (= K257)
6u7aA Rv3722c in complex with kynurenine (see paper)
51% identity, 98% coverage: 3:420/425 of query aligns to 1:419/423 of 6u7aA
- binding phosphate ion: R58 (≠ L61), D64 (= D67)
- binding (2S)-4-(2-aminophenyl)-2-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-oxobutanoic acid: R35 (= R37), G36 (= G38), K37 (= K39), S98 (= S101), S99 (= S102), L100 (= L103), Y138 (= Y140), R140 (= R142), N188 (= N189), D217 (= D218), A219 (= A220), Y220 (= Y221), S253 (= S254), S255 (= S256), K256 (= K257), F348 (= F349), R391 (= R392)
O69689 Aspartate aminotransferase; AspAT; EC 2.6.1.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
51% identity, 98% coverage: 3:420/425 of query aligns to 2:420/435 of O69689
- Y69 (= Y71) binding pyridoxal 5'-phosphate
- SL 100:101 (= SL 102:103) binding pyridoxal 5'-phosphate
- YDR 139:141 (= YDR 140:142) binding substrate
- N189 (= N189) binding pyridoxal 5'-phosphate
- Y221 (= Y221) binding pyridoxal 5'-phosphate
- STS 254:256 (= STS 254:256) binding pyridoxal 5'-phosphate
- R392 (= R392) binding substrate
6u78B Rv3722c in complex with glutamic acid (see paper)
51% identity, 98% coverage: 3:420/425 of query aligns to 1:419/421 of 6u78B
5c6uA Rv3722c aminotransferase from mycobacterium tuberculosis
51% identity, 97% coverage: 7:420/425 of query aligns to 5:419/427 of 5c6uA
2zyjA Crystal structure of lysn, alpha-aminoadipate aminotransferase (complexed with n-(5'-phosphopyridoxyl)-l-glutamate), from thermus thermophilus hb27 (see paper)
25% identity, 79% coverage: 61:394/425 of query aligns to 60:370/397 of 2zyjA
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: G99 (≠ N100), S100 (= S101), Q101 (≠ S102), Y125 (= Y140), N174 (= N189), D202 (= D218), Y205 (= Y221), S235 (= S254), S237 (= S256), K238 (= K257), R245 (≠ G264), R368 (= R392)
Sites not aligning to the query:
Q72LL6 2-aminoadipate transaminase; 2-aminoadipate aminotransferase; Alpha-aminoadipate aminotransferase; AAA-AT; AadAT; EC 2.6.1.39 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see 2 papers)
25% identity, 79% coverage: 61:394/425 of query aligns to 60:370/397 of Q72LL6
- Y70 (= Y71) binding pyridoxal 5'-phosphate
- N174 (= N189) binding pyridoxal 5'-phosphate; binding substrate
- R245 (≠ G264) binding pyridoxal 5'-phosphate
- R368 (= R392) binding substrate
Sites not aligning to the query:
- 20 S→E: Strongly decreases the affinity for AAA and Glu. A mild decrease of affinity is observed for 2-oxoglutarate. Increases the affinity for leucine and 2-oxoisocaproate.
- 23 R→A: Strongly decreases the affinity for AAA and Glu. A mild decrease of affinity is observed for 2-oxoglutarate which has the same chain length as Glu, but differs by the presence of a 2-oxo group which is not recognized by R-23. Increases the affinity for leucine and 2-oxoisocaproate due to the absence of gamma-carboxyl group.; R→Q: Strongly decreases the affinity for AAA and Glu. A mild decrease of affinity is observed for 2-oxoglutarate which has the same chain length as Glu, but differs by the presence of a 2-oxo group which is not recognized by R-23. Increases the affinity for leucine and 2-oxoisocaproate due to the absence of gamma-carboxyl group.
- 40 binding substrate
3cbfA Crystal structure of lysn, alpha-aminoadipate aminotransferase, from thermus thermophilus hb27 (see paper)
25% identity, 79% coverage: 61:394/425 of query aligns to 56:366/392 of 3cbfA
- binding (2S)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]hexanedioic acid: G95 (≠ N100), S96 (= S101), Q97 (≠ S102), Y121 (= Y140), N170 (= N189), D198 (= D218), Y201 (= Y221), S231 (= S254), S233 (= S256), K234 (= K257), R241 (≠ G264), R364 (= R392)
Sites not aligning to the query:
2egyA Crystal structure of lysn, alpha-aminoadipate aminotransferase (substrate free form), from thermus thermophilus hb27
25% identity, 79% coverage: 61:394/425 of query aligns to 56:366/392 of 2egyA
- binding pyridoxal-5'-phosphate: G95 (≠ N100), S96 (= S101), Q97 (≠ S102), Y121 (= Y140), N170 (= N189), D198 (= D218), A200 (= A220), Y201 (= Y221), S231 (= S254), S233 (= S256), K234 (= K257), R241 (≠ G264)
2z1yA Crystal structure of lysn, alpha-aminoadipate aminotransferase (complexed with n-(5'-phosphopyridoxyl)-l-leucine), from thermus thermophilus hb27
25% identity, 79% coverage: 61:394/425 of query aligns to 52:362/389 of 2z1yA
- binding leucine: Y117 (= Y140), R360 (= R392)
- binding pyridoxal-5'-phosphate: G91 (≠ N100), S92 (= S101), Q93 (≠ S102), Y117 (= Y140), N166 (= N189), D194 (= D218), Y197 (= Y221), S227 (= S254), S229 (= S256), K230 (= K257), R237 (≠ G264)
Sites not aligning to the query:
3wx9A Crystal structure of pyrococcus horikoshii kynurenine aminotransferase in complex with pmp, gla, 4ad, 2og, glu and kya
26% identity, 48% coverage: 178:380/425 of query aligns to 173:366/404 of 3wx9A
- binding 2-oxoglutaric acid: D213 (≠ N219), P214 (≠ A220), Y215 (= Y221), G216 (≠ A222), E217 (≠ L223), G241 (≠ A253), T242 (≠ S254), I246 (≠ M258)
- binding (2E)-pent-2-enedioic acid: N184 (= N189)
- binding glutamic acid: V360 (≠ T374), A364 (= A378)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: N184 (= N189), D212 (= D218), P214 (≠ A220), Y215 (= Y221), T242 (≠ S254), S244 (= S256), K245 (= K257), R252 (≠ G264)
Sites not aligning to the query:
- binding 4-(2-aminophenyl)-2,4-dioxobutanoic acid: 23, 40, 41
- binding (2E)-pent-2-enedioic acid: 40, 130, 376
- binding glutamic acid: 20, 22, 131, 369
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: 104, 105, 106, 130
3av7A Crystal structure of pyrococcus horikoshii kynurenine aminotransferase in complex with pmp, kyn as substrates and kya as products
26% identity, 48% coverage: 178:380/425 of query aligns to 173:366/404 of 3av7A
Sites not aligning to the query:
- binding 4-hydroxyquinoline-2-carboxylic acid: 20, 22, 23, 131, 135, 369
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: 23, 40, 130, 131, 132, 376
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: 104, 105, 106, 130
3aowC Crystal structure of pyrococcus horikoshii kynurenine aminotransferase in complex with akg
26% identity, 48% coverage: 178:380/425 of query aligns to 173:366/404 of 3aowC
Sites not aligning to the query:
3aovA Crystal structure of pyrococcus horikoshii kynurenine aminotransferase in complex with plp
26% identity, 48% coverage: 178:380/425 of query aligns to 173:366/404 of 3aovA
Sites not aligning to the query:
1vp4A Crystal structure of a putative aminotransferase (tm1131) from thermotoga maritima msb8 at 1.82 a resolution
23% identity, 66% coverage: 131:410/425 of query aligns to 136:403/420 of 1vp4A
Sites not aligning to the query:
Query Sequence
>WP_020175324.1 NCBI__GCF_000385335.1:WP_020175324.1
MTSIAELSSADHQALLTKVRGEYDAFRAAGHKLDMTRGKPSPEQLDLSNGMLALPGNGDY
LTEANEDARNYGGLQGIAEARALFAPVLGAPADRVIIGDNSSLAMMHDSIVWALLKGVPG
GTAPWSKESAPAFLCPVPGYDRHFAILEEYGIKMIPVRLTGQGPDMDEVERLVADPAVKG
MWCVPKYANPSGEIYSEETAKRLAAMKTGAPDFRIFWDNAYALHHLTATKHEVANILELC
EAAGNPDRAFVYASTSKMTLAGAGLAFFASSPTNVKWYLARAGKRTIGPDKLNQIRHVRF
LKNIDGLHQLMDGHRALIAPKFAAVEEALDRRLTGTGVARWTKPEGGYFVSVDMADGLAS
KVVSLAKDAGLALTPAGATWPLGQDPQDSNLRLAPTFPSLGDVKVAAEGIALCMLLAGLE
KRDAA
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