SitesBLAST
Comparing WP_078428542.1 NCBI__GCF_002019605.1:WP_078428542.1 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)
P97084 Threonine-phosphate decarboxylase; L-threonine-O-3-phosphate decarboxylase; EC 4.1.1.81 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
35% identity, 97% coverage: 5:353/360 of query aligns to 7:353/364 of P97084
- HG 8:9 (= HG 6:7) binding O-phospho-L-threonine
- N32 (= N31) binding O-phospho-L-threonine
- N157 (= N156) binding O-phospho-L-threonine
- K216 (= K215) modified: N6-(pyridoxal phosphate)lysine
- R323 (= R323) binding O-phospho-L-threonine
- R337 (= R337) binding O-phospho-L-threonine
1lc8A Crystal structure of l-threonine-o-3-phosphate decarboxylase from s. Enterica complexed with its reaction intermediate (see paper)
35% identity, 97% coverage: 5:353/360 of query aligns to 1:347/356 of 1lc8A
- binding {3-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-propyl}-phosphonic acid: H2 (= H6), G3 (= G7), G78 (= G83), E79 (≠ A84), T80 (≠ A85), F102 (= F107), N151 (= N156), D179 (= D184), A181 (= A186), S207 (= S212), T209 (= T214), K210 (= K215), R218 (= R223), R317 (= R323), R331 (= R337)
1lc7A Crystal structure of l-threonine-o-3-phosphate decarboxylase from s. Enterica complexed with a substrate (see paper)
35% identity, 97% coverage: 5:353/360 of query aligns to 4:350/358 of 1lc7A
- binding phosphate ion: G81 (= G83), E82 (≠ A84), T83 (≠ A85), S210 (= S212), T212 (= T214), R221 (= R223)
- binding phosphothreonine: H5 (= H6), G6 (= G7), A28 (≠ E30), N29 (= N31), F105 (= F107), N154 (= N156), K213 (= K215), R320 (= R323), R334 (= R337)
1lkcA Crystal structure of l-threonine-o-3-phosphate decarboxylase from salmonella enterica (see paper)
35% identity, 97% coverage: 6:353/360 of query aligns to 1:346/355 of 1lkcA
- binding pyridoxal-5'-phosphate: G77 (= G83), E78 (≠ A84), T79 (≠ A85), F101 (= F107), D178 (= D184), A180 (= A186), F181 (= F187), S206 (= S212), T208 (= T214), K209 (= K215), R217 (= R223)
- binding phosphate ion: H1 (= H6), G2 (= G7), N150 (= N156), R316 (= R323), R330 (= R337)
8bj3A Crystal structure of medicago truncatula histidinol-phosphate aminotransferase (hisn6) in complex with histidinol-phosphate (see paper)
29% identity, 93% coverage: 22:357/360 of query aligns to 31:360/360 of 8bj3A
- binding [(2~{S})-3-(1~{H}-imidazol-4-yl)-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]propyl] dihydrogen phosphate: Y63 (= Y55), G91 (= G83), A92 (= A84), D93 (≠ A85), F117 (= F107), M119 (≠ E109), N166 (= N156), D190 (= D184), A192 (= A186), Y193 (≠ F187), T217 (≠ S212), S219 (≠ T214), K220 (= K215), R228 (= R223), Y249 (≠ W244), R328 (= R323), R340 (= R337)
Sites not aligning to the query:
2f8jA Crystal structure of histidinol-phosphate aminotransferase (ec 2.6.1.9) (imidazole acetol-phosphate transferase) (tm1040) from thermotoga maritima at 2.40 a resolution
27% identity, 90% coverage: 31:354/360 of query aligns to 28:333/335 of 2f8jA
1uu0A Histidinol-phosphate aminotransferase (hisc) from thermotoga maritima (apo-form) (see paper)
27% identity, 90% coverage: 31:354/360 of query aligns to 21:326/328 of 1uu0A
1uu1A Complex of histidinol-phosphate aminotransferase (hisc) from thermotoga maritima (apo-form) (see paper)
27% identity, 90% coverage: 31:354/360 of query aligns to 22:327/329 of 1uu1A
- binding phosphoric acid mono-[2-amino-3-(3h-imidazol-4-yl)-propyl]ester: Y48 (= Y55), D81 (≠ A85), Y101 (≠ F107), S102 (= S108), N144 (= N156), F226 (≠ W244), R310 (= R337)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G79 (= G83), A80 (= A84), D81 (≠ A85), Y101 (≠ F107), N144 (= N156), D168 (= D184), A170 (= A186), Y171 (≠ F187), T194 (≠ S212), S196 (≠ T214), K197 (= K215), R205 (= R223)
1h1cA Histidinol-phosphate aminotransferase (hisc) from thermotoga maritima (see paper)
27% identity, 90% coverage: 31:354/360 of query aligns to 22:327/329 of 1h1cA
- binding pyridoxal-5'-phosphate: G79 (= G83), A80 (= A84), D81 (≠ A85), Y101 (≠ F107), D168 (= D184), A170 (= A186), Y171 (≠ F187), T194 (≠ S212), S196 (≠ T214), K197 (= K215), R205 (= R223)
Q9X0D0 Histidinol-phosphate aminotransferase; Imidazole acetol-phosphate transaminase; EC 2.6.1.9 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
27% identity, 90% coverage: 31:354/360 of query aligns to 27:332/335 of Q9X0D0
- K202 (= K215) modified: N6-(pyridoxal phosphate)lysine
P0DV65 L-serine phosphate decarboxylase; CobD homolog SMUL_1544; SmCobD; L-serine O-phosphate decarboxylase; L-Ser-P decarboxylase; Norcobamide biosynthesis protein SMUL_1544; Threonine phosphate decarboxylase-like enzyme; EC 4.1.1.- from Sulfurospirillum multivorans (strain DM 12446 / JCM 15788 / NBRC 109480) (see paper)
26% identity, 86% coverage: 46:354/360 of query aligns to 70:385/392 of P0DV65
- S242 (≠ T214) mutation to T: Increased enzyme activity with of L-threonine phosphate and a decreased activity with L-serine phosphate. Exhibits similar activity rates with both substrates.
Sites not aligning to the query:
- 2:6 mutation Missing: No effect on enzyme activity with L-serine phosphate or with L-threonine phosphate.
- 2:11 mutation Missing: Decreased enzyme activity by about 30% compared to wild-type with L-serine phosphate. No effect on enzyme activity with L-threonine phosphate.
- 2:16 mutation Missing: Decreased enzyme activity by about 30% compared to wild-type with L-serine phosphate. No effect on enzyme activity with L-threonine phosphate.
- 2:21 mutation Missing: Decreased enzyme activity by about 30% compared to wild-type with L-serine phosphate. No effect on enzyme activity with L-threonine phosphate.
- 2:29 mutation Missing: Loss of enzyme activity with L-serine phosphate and with L-threonine phosphate. No effect in pyridoxal phosphate (PLP)-binding.
- 22:29 Required for catalytic activity
- 26 H→A: Significantly decreased enzyme activity. No effect in pyridoxal phosphate (PLP)-binding.
7szpA Crystal structure of histidinol-phosphate aminotransferase from klebsiella pneumoniae subsp. Pneumoniae (strain hs11286)
26% identity, 84% coverage: 50:353/360 of query aligns to 48:349/353 of 7szpA
- binding pyridoxal-5'-phosphate: G81 (= G83), A82 (= A84), D83 (≠ A85), Y108 (≠ F107), D182 (= D184), A184 (= A186), Y185 (≠ F187), T209 (≠ S212), S211 (≠ T214), K212 (= K215), R220 (= R223)
1fg7A Crystal structure of l-histidinol phosphate aminotransferase with pyridoxal-5'-phosphate (see paper)
25% identity, 84% coverage: 50:353/360 of query aligns to 48:349/354 of 1fg7A
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G81 (= G83), A82 (= A84), D83 (≠ A85), Y108 (≠ F107), N155 (= N156), D182 (= D184), A184 (= A186), Y185 (≠ F187), T209 (≠ S212), S211 (≠ T214), K212 (= K215), R220 (= R223)
1fg3A Crystal structure of l-histidinol phosphate aminotransferase complexed with l-histidinol (see paper)
25% identity, 84% coverage: 50:353/360 of query aligns to 48:349/354 of 1fg3A