SitesBLAST
Comparing WP_073952367.1 NCBI__GCF_001906585.1:WP_073952367.1 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
44% identity, 91% coverage: 44:505/508 of query aligns to 46:502/504 of 1eyyA
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
27% identity, 77% coverage: 7:397/508 of query aligns to 441:826/902 of P28037
- IPW 571:573 (≠ AAS 137:139) binding NADP(+)
- K-----PAQ 597:600 (≠ KAHPDHPA- 165:172) binding NADP(+)
- GSLVGQ 630:635 (≠ GFEAGI 200:205) binding NADP(+)
- GS 650:651 (= GS 220:221) binding NADP(+)
- E673 (= E244) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 244:245) binding NADP(+)
- C707 (= C281) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ F323) binding NADP(+)
- ESF 804:806 (≠ ECF 374:376) binding NADP(+)
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
27% identity, 77% coverage: 7:397/508 of query aligns to 37:422/498 of 4go2A
- active site: N170 (= N140), K193 (= K165), E269 (= E244), C303 (= C281), E400 (= E374)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ Y136), I167 (≠ A137), P168 (≠ A138), W169 (≠ S139), K193 (= K165), A195 (= A172), Q196 (vs. gap), S225 (≠ H199), G226 (= G200), G230 (= G204), Q231 (≠ I205), F244 (= F218), G246 (= G220), S247 (= S221), V250 (≠ G224), I254 (≠ L228), E269 (= E244), G271 (= G246), C303 (= C281), E400 (= E374), F402 (= F376)
Sites not aligning to the query:
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
27% identity, 77% coverage: 7:397/508 of query aligns to 37:422/498 of 2o2rA
- active site: N170 (= N140), K193 (= K165), E269 (= E244), C303 (= C281), E400 (= E374)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ Y136), I167 (≠ A137), W169 (≠ S139), K193 (= K165), A195 (= A172), Q196 (vs. gap), S225 (≠ H199), G226 (= G200), G230 (= G204), Q231 (≠ I205), F244 (= F218), S247 (= S221), V250 (≠ G224), I254 (≠ L228)
Sites not aligning to the query:
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
27% identity, 77% coverage: 7:397/508 of query aligns to 122:507/583 of 7rluA
Sites not aligning to the query:
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
28% identity, 67% coverage: 48:386/508 of query aligns to 120:450/535 of P51649
- G176 (≠ L105) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ T117) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P119) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ A148) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C160) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KAHP 165:168) binding NAD(+)
- T233 (≠ H170) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (vs. gap) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ G196) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G204) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVRGG 220:225) binding NAD(+)
- R334 (≠ M275) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ G276) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C281) modified: Disulfide link with 342, In inhibited form
- C342 (≠ K283) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (vs. gap) natural variant: N -> S
- P382 (≠ V313) to L: in SSADHD; 2% of activity
- V406 (vs. gap) to I: in dbSNP:rs143741652
- G409 (vs. gap) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 93 C → F: in SSADHD; 3% of activity; dbSNP:rs765561257
- 498 binding substrate; S→A: Reduces catalytic activity to less than 15% of wild-type.
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
O75891 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; EC 1.5.1.6 from Homo sapiens (Human) (see 2 papers)
27% identity, 69% coverage: 48:397/508 of query aligns to 485:826/902 of O75891
- A511 (= A72) to V: in a colorectal cancer sample; somatic mutation; dbSNP:rs768309358
Sites not aligning to the query:
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation by AASDHPPT. Loss of formyltetrahydrofolate dehydrogenase activity.
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex (see paper)
27% identity, 69% coverage: 48:397/508 of query aligns to 81:422/498 of 7yjjC
Sites not aligning to the query:
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
28% identity, 67% coverage: 48:386/508 of query aligns to 70:400/485 of 2w8rA
Sites not aligning to the query:
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
28% identity, 67% coverage: 48:386/508 of query aligns to 70:400/485 of 2w8qA
Sites not aligning to the query:
4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 62% coverage: 127:441/508 of query aligns to 134:438/476 of 4yweA
Sites not aligning to the query:
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
32% identity, 54% coverage: 127:402/508 of query aligns to 138:408/476 of 5x5uA
- active site: N151 (= N140), K174 (= K165), E249 (= E244), C283 (= C281), E380 (= E374)
- binding nicotinamide-adenine-dinucleotide: P149 (≠ A138), P207 (≠ E202), A208 (= A203), S211 (≠ E206), G227 (= G220), S228 (= S221), V231 (≠ G224), R329 (≠ A328), R330 (≠ E329), E380 (= E374), F382 (= F376)
Sites not aligning to the query:
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
32% identity, 54% coverage: 127:402/508 of query aligns to 138:408/476 of 5x5tA