SitesBLAST
Comparing H281DRAFT_03540 FitnessBrowser__Burk376:H281DRAFT_03540 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)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
62% identity, 99% coverage: 2:475/479 of query aligns to 6:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
62% identity, 99% coverage: 2:475/479 of query aligns to 5:480/481 of 3jz4A
- active site: N156 (= N151), K179 (= K174), E254 (= E249), C288 (= C283), E385 (= E380), E462 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P149), W155 (= W150), K179 (= K174), A181 (≠ S176), S182 (≠ E177), A212 (= A207), G216 (= G211), G232 (= G227), S233 (= S228), I236 (≠ V231), C288 (= C283), K338 (= K333), E385 (= E380), F387 (= F382)
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)
56% identity, 99% coverage: 4:477/479 of query aligns to 58:535/535 of P51649
- C93 (≠ G39) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G122) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P126) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P128) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R159) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C169) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPSE 174:177) binding
- T233 (= T179) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A183) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N201) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G211) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTRVG 227:232) binding
- R334 (= R277) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N278) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C283) modified: Disulfide link with 342, In inhibited form
- C342 (= C285) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N314) natural variant: N -> S
- P382 (= P324) to L: in SSADHD; 2% of activity
- V406 (= V348) to I: in dbSNP:rs143741652
- G409 (= G351) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S440) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G475) to R: in SSADHD; <1% of activity; dbSNP:rs72552284
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
56% identity, 99% coverage: 4:477/479 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 99% coverage: 4:477/479 of query aligns to 8:485/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
56% identity, 99% coverage: 4:477/479 of query aligns to 7:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I147), T153 (= T148), P154 (= P149), K179 (= K174), A212 (= A207), K213 (≠ V208), F230 (= F225), T231 (= T226), G232 (= G227), S233 (= S228), V236 (= V231), W239 (≠ L234), G256 (= G251)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 98% coverage: 4:474/479 of query aligns to 2:474/476 of 5x5uA
- active site: N151 (= N151), K174 (= K174), E249 (= E249), C283 (= C283), E380 (= E380), E457 (= E457)
- binding glycerol: D15 (≠ E17), A16 (≠ G18), A17 (= A19), G19 (vs. gap)
- binding nicotinamide-adenine-dinucleotide: P149 (= P149), P207 (≠ A207), A208 (≠ V208), S211 (≠ G211), G227 (= G227), S228 (= S228), V231 (= V231), R329 (≠ A329), R330 (≠ A330), E380 (= E380), F382 (= F382)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 98% coverage: 4:474/479 of query aligns to 2:474/476 of 5x5tA
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
39% identity, 98% coverage: 3:473/479 of query aligns to 14:492/505 of 4neaA
- active site: N166 (= N151), K189 (= K174), E264 (= E249), C298 (= C283), E399 (= E380), E476 (= E457)
- binding nicotinamide-adenine-dinucleotide: P164 (= P149), K189 (= K174), E192 (= E177), G222 (≠ A207), G226 (= G211), G242 (= G227), G243 (≠ S228), T246 (≠ V231), H249 (≠ L234), I250 (≠ L235), C298 (= C283), E399 (= E380), F401 (= F382)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 96% coverage: 10:470/479 of query aligns to 5:471/477 of 6j76A
- active site: N148 (= N151), E246 (= E249), C280 (= C283), E458 (= E457)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I147), T145 (= T148), A146 (≠ P149), W147 (= W150), N148 (= N151), K171 (= K174), T173 (≠ S176), S174 (≠ E177), G204 (≠ A207), G208 (= G211), T223 (= T226), G224 (= G227), S225 (= S228), A228 (≠ V231), S231 (≠ L234), I232 (≠ L235), E246 (= E249), L247 (= L250), C280 (= C283), E381 (= E380), F383 (= F382), H447 (≠ F446)
7radA Crystal structure analysis of aldh1b1
40% identity, 97% coverage: 10:474/479 of query aligns to 16:486/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ T148), P160 (= P149), W161 (= W150), N162 (= N151), M167 (= M156), K185 (= K174), E188 (= E177), G218 (≠ A207), G222 (= G211), A223 (≠ G212), T237 (= T226), G238 (= G227), S239 (= S228), V242 (= V231), E261 (= E249), L262 (= L250), C295 (= C283), E392 (= E380), F394 (= F382)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ Y105), F163 (= F152), E285 (≠ A273), F289 (≠ R277), N450 (≠ I438), V452 (≠ S440)
7mjdA Crystal structure analysis of aldh1b1
40% identity, 97% coverage: 10:474/479 of query aligns to 16:486/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ T148), P160 (= P149), W161 (= W150), N162 (= N151), M167 (= M156), K185 (= K174), E188 (= E177), G218 (≠ A207), G222 (= G211), F236 (= F225), T237 (= T226), G238 (= G227), S239 (= S228), V242 (= V231), E261 (= E249), L262 (= L250), C295 (= C283), E392 (= E380), F394 (= F382)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ Y105), E285 (≠ A273), F289 (≠ R277), N450 (≠ I438), V452 (≠ S440)
7mjcA Crystal structure analysis of aldh1b1
40% identity, 97% coverage: 10:474/479 of query aligns to 16:486/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I147), I159 (≠ T148), P160 (= P149), W161 (= W150), N162 (= N151), K185 (= K174), E188 (= E177), G218 (≠ A207), G222 (= G211), T237 (= T226), G238 (= G227), S239 (= S228), V242 (= V231), E261 (= E249), L262 (= L250), C295 (= C283), E392 (= E380), F394 (= F382)
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
39% identity, 96% coverage: 10:470/479 of query aligns to 106:577/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K174), S310 (≠ D206), G311 (≠ A207), G315 (= G211), G331 (= G227), S332 (= S228), V335 (= V231)
- binding 4'-phosphopantetheine: K201 (≠ R100), F382 (≠ R277), N387 (≠ T282), C388 (= C283), N545 (≠ I438)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
39% identity, 96% coverage: 10:470/479 of query aligns to 21:492/498 of 4go2A
- active site: N170 (= N151), K193 (= K174), E269 (= E249), C303 (= C283), E400 (= E380), D479 (≠ E457)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I147), I167 (≠ T148), P168 (= P149), W169 (= W150), K193 (= K174), A195 (≠ S176), Q196 (≠ E177), S225 (≠ D206), G226 (≠ A207), G230 (= G211), Q231 (≠ G212), F244 (= F225), G246 (= G227), S247 (= S228), V250 (= V231), I254 (≠ L235), E269 (= E249), G271 (= G251), C303 (= C283), E400 (= E380), F402 (= F382)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
39% identity, 96% coverage: 10:470/479 of query aligns to 21:492/498 of 2o2rA
- active site: N170 (= N151), K193 (= K174), E269 (= E249), C303 (= C283), E400 (= E380), D479 (≠ E457)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I147), I167 (≠ T148), W169 (= W150), K193 (= K174), A195 (≠ S176), Q196 (≠ E177), S225 (≠ D206), G226 (≠ A207), G230 (= G211), Q231 (≠ G212), F244 (= F225), S247 (= S228), V250 (= V231), I254 (≠ L235)
7yjjC Human cytosolic 10-formyltetrahydrofolate dehydrogenase and gossypol complex
40% identity, 96% coverage: 10:470/479 of query aligns to 21:492/498 of 7yjjC
P15437 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Equus caballus (Horse) (see paper)
40% identity, 98% coverage: 3:470/479 of query aligns to 17:490/501 of P15437
Sites not aligning to the query:
- 2 modified: N-acetylserine
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)
39% identity, 96% coverage: 10:470/479 of query aligns to 425:896/902 of P28037
- IPW 571:573 (≠ TPW 148:150) binding
- KPAQ 597:600 (≠ KPSE 174:177) binding
- GSLVGQ 630:635 (≠ AVAIGG 207:212) binding
- GS 650:651 (= GS 227:228) binding
- E673 (= E249) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (= EL 249:250) binding
- C707 (= C283) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (= K333) binding
- ESF 804:806 (≠ ETF 380:382) binding
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.
7qk9A Crystal structure of the aldh1a3-atp complex (see paper)
40% identity, 98% coverage: 7:474/479 of query aligns to 13:486/489 of 7qk9A
- binding adenosine-5'-triphosphate: I158 (= I147), T159 (= T148), P160 (= P149), W161 (= W150), K185 (= K174), E188 (= E177), G218 (≠ A207), G222 (= G211), F236 (= F225), S239 (= S228), V242 (= V231)
Query Sequence
>H281DRAFT_03540 FitnessBrowser__Burk376:H281DRAFT_03540
MNEFLRTGHYIGGEWYEGASTYPVLNPATGEVIAQVAKGGAVEATQAIAAAERAFPAWRS
LTAKERSARVKRWGELMLEHRDALAALLTREQGKPLAEARGEVGYAASFFEWFAEEAKRA
YGDVIPSPNPNAKIIVTREPVGVVAAITPWNFPLAMITRKAGPALAAGCTMVLKPSEETP
LSALALAVLAEKAGIPPGVFNVVSGDAVAIGGALTESDVVRKLSFTGSTRVGKLLAKQSA
DTLKKLSLELGGNAPFIVFDDADLDAAVQGAMASKFRNTGQTCVCVNRFYVQDGIYDAFT
LALAQAARKMRVGNALQGDVEQGPLINQAALTKVEAHVADALQKGAKVLTGAKPHALGGT
FYEPTVLVDASSSMLIAQEETFGPVAACFRFKTEDEAVAAANATPFGLSAYFYTRDLARA
WRVGEALESGMVGINEGILSTEVAPFGGVKQSGLGREGSKYGLDEYTELKYMMMGGLGR
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