SitesBLAST
Comparing WP_177193515.1 NCBI__GCF_900114975.1:WP_177193515.1 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)
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, 96% coverage: 4:368/379 of query aligns to 5:364/364 of P97084
- HG 8:9 (= HG 7:8) binding O-phospho-L-threonine
- N32 (≠ S31) binding O-phospho-L-threonine
- N157 (≠ S158) binding O-phospho-L-threonine
- K216 (= K216) modified: N6-(pyridoxal phosphate)lysine
- R323 (= R327) binding O-phospho-L-threonine
- R337 (= R341) 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)
36% identity, 95% coverage: 6:366/379 of query aligns to 1:356/356 of 1lc8A
- binding {3-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-propyl}-phosphonic acid: H2 (= H7), G3 (= G8), G78 (= G83), E79 (≠ S84), T80 (= T85), F102 (= F107), N151 (≠ S158), D179 (= D186), A181 (≠ V188), S207 (= S213), T209 (= T215), K210 (= K216), R218 (= R224), R317 (= R327), R331 (= R341)
1lkcA Crystal structure of l-threonine-o-3-phosphate decarboxylase from salmonella enterica (see paper)
36% identity, 95% coverage: 7:366/379 of query aligns to 1:355/355 of 1lkcA
- binding pyridoxal-5'-phosphate: G77 (= G83), E78 (≠ S84), T79 (= T85), F101 (= F107), D178 (= D186), A180 (≠ V188), F181 (= F189), S206 (= S213), T208 (= T215), K209 (= K216), R217 (= R224)
- binding phosphate ion: H1 (= H7), G2 (= G8), N150 (≠ S158), R316 (= R327), R330 (= R341)
1lc7A Crystal structure of l-threonine-o-3-phosphate decarboxylase from s. Enterica complexed with a substrate (see paper)
36% identity, 94% coverage: 6:361/379 of query aligns to 4:354/358 of 1lc7A
- binding phosphate ion: G81 (= G83), E82 (≠ S84), T83 (= T85), S210 (= S213), T212 (= T215), R221 (= R224)
- binding phosphothreonine: H5 (= H7), G6 (= G8), A28 (= A30), N29 (≠ S31), F105 (= F107), N154 (≠ S158), K213 (= K216), R320 (= R327), R334 (= R341)
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)
27% identity, 82% coverage: 52:363/379 of query aligns to 76:390/392 of P0DV65
- S242 (≠ T215) 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.
8bj3A Crystal structure of medicago truncatula histidinol-phosphate aminotransferase (hisn6) in complex with histidinol-phosphate (see paper)
25% identity, 89% coverage: 19:357/379 of query aligns to 28:356/360 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 (≠ S84), D93 (≠ T85), F117 (= F107), M119 (≠ E109), N166 (≠ S158), D190 (= D186), A192 (≠ V188), Y193 (≠ F189), T217 (≠ S213), S219 (≠ T215), K220 (= K216), R228 (= R224), Y249 (≠ W245), R328 (= R327), R340 (= R341)
Sites not aligning to the query:
1fg7A Crystal structure of l-histidinol phosphate aminotransferase with pyridoxal-5'-phosphate (see paper)
26% identity, 80% coverage: 54:358/379 of query aligns to 52:350/354 of 1fg7A
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G81 (= G83), A82 (≠ S84), D83 (≠ T85), Y108 (≠ F107), N155 (≠ S158), D182 (= D186), A184 (≠ V188), Y185 (≠ F189), T209 (≠ S213), S211 (≠ T215), K212 (= K216), R220 (= R224)
1fg3A Crystal structure of l-histidinol phosphate aminotransferase complexed with l-histidinol (see paper)
26% identity, 80% coverage: 54:358/379 of query aligns to 52:350/354 of 1fg3A
- binding phosphoric acid mono-[2-amino-3-(3h-imidazol-4-yl)-propyl]ester: D83 (≠ T85), Y108 (≠ F107), N155 (≠ S158), K212 (= K216), R320 (= R327), R333 (= R341)
- binding pyridoxal-5'-phosphate: G81 (= G83), A82 (≠ S84), D83 (≠ T85), Y108 (≠ F107), N155 (≠ S158), D182 (= D186), A184 (≠ V188), Y185 (≠ F189), T209 (≠ S213), S211 (≠ T215), K212 (= K216), R220 (= R224)
Sites not aligning to the query:
1geyA Crystal structure of histidinol-phosphate aminotransferase complexed with n-(5'-phosphopyridoxyl)-l-glutamate (see paper)
26% identity, 80% coverage: 54:357/379 of query aligns to 38:335/335 of 1geyA
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: G67 (= G83), A68 (≠ S84), D69 (≠ T85), Y94 (≠ F107), N141 (≠ S158), D168 (= D186), A170 (≠ V188), Y171 (≠ F189), T195 (≠ S213), S197 (≠ T215), K198 (= K216), R206 (= R224), R319 (= R341)
Sites not aligning to the query:
3cq6A Histidinol-phosphate aminotransferase from corynebacterium glutamicum holo-form (plp covalently bound ) (see paper)
24% identity, 89% coverage: 26:361/379 of query aligns to 28:360/364 of 3cq6A
Sites not aligning to the query:
3cq5B Histidinol-phosphate aminotransferase from corynebacterium glutamicum in complex with pmp (see paper)
24% identity, 89% coverage: 26:361/379 of query aligns to 30:362/366 of 3cq5B
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G97 (= G83), S98 (= S84), N99 (≠ T85), Y123 (≠ F107), N172 (≠ S158), D197 (= D186), A199 (≠ V188), Y200 (≠ F189), T225 (≠ S213), S227 (≠ T215), K228 (= K216), R236 (= R224)
7szpA Crystal structure of histidinol-phosphate aminotransferase from klebsiella pneumoniae subsp. Pneumoniae (strain hs11286)
26% identity, 91% coverage: 12:357/379 of query aligns to 18:349/353 of 7szpA
- binding pyridoxal-5'-phosphate: G81 (= G83), A82 (≠ S84), D83 (≠ T85), Y108 (≠ F107), D182 (= D186), A184 (≠ V188), Y185 (≠ F189), T209 (≠ S213), S211 (≠ T215), K212 (= K216), R220 (= R224)
Q0ZQ41 CMP-5'-(3-aminopropyl)phosphonate synthase; EC 2.7.7.-; EC 4.1.1.- from Streptomyces rubellomurinus (strain ATCC 31215) (see paper)
29% identity, 81% coverage: 37:343/379 of query aligns to 291:593/628 of Q0ZQ41
- K466 (= K216) mutation to A: Lack of decarboxylase activity, produces only CMP-5'-2APn.
Sites not aligning to the query:
- 37 K→A: Strong decrease in nucleotide transferase activity.
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
26% identity, 87% coverage: 28:357/379 of query aligns to 25:332/335 of 2f8jA