SitesBLAST
Comparing GFF863 FitnessBrowser__Phaeo:GFF863 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)
2gagA Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
37% identity, 99% coverage: 15:973/973 of query aligns to 23:965/965 of 2gagA
- active site: L350 (≠ S376), L375 (= L393), D677 (= D688)
- binding flavin mononucleotide: K510 (= K521), R511 (= R522), T517 (≠ M528), Q521 (= Q532), T549 (= T559), R551 (= R561)
- binding 2-furoic acid: N647 (≠ D658), G653 (= G664), T655 (≠ A666), K851 (= K859)
- binding nicotinamide-adenine-dinucleotide: V134 (≠ I171), G135 (= G172), G137 (= G174), P138 (= P175), A139 (= A176), D158 (= D195), E159 (= E196), R160 (≠ D197), G165 (= G202), T166 (≠ R203), T204 (≠ S240), V205 (= V241), T249 (≠ A280), G250 (= G281), S295 (≠ D326), F381 (≠ W399), G417 (= G436), A418 (= A437), L423 (≠ F442), D424 (≠ T443), T425 (= T444), Y554 (= Y564)
Q46337 Sarcosine oxidase subunit alpha; Sarcosine oxidase subunit A; Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit alpha; Tetrameric sarcosine oxidase subunit alpha; TSOX subunit alpha; EC 1.5.3.24 from Corynebacterium sp. (strain P-1) (see 2 papers)
37% identity, 98% coverage: 17:973/973 of query aligns to 27:967/967 of Q46337
- G139 (= G174) mutation to A: Does not affect activity and binding of NAD(+).
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q50LF0 Sarcosine oxidase subunit alpha; Sarcosine oxidase subunit A; Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit alpha; Tetrameric sarcosine oxidase subunit alpha; TSOX subunit alpha; EC 1.5.3.24 from Corynebacterium sp. (strain U-96) (see 2 papers)
37% identity, 98% coverage: 17:973/973 of query aligns to 25:965/965 of Q50LF0
- A139 (= A176) binding
- D158 (= D195) binding
- E159 (= E196) binding
- R160 (≠ D197) binding
- T166 (≠ R203) binding
- V205 (= V241) binding
- A418 (= A437) binding
- L423 (≠ F442) binding
- T425 (= T444) binding
3ad7A Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with methylthio acetate (see paper)
37% identity, 98% coverage: 17:970/973 of query aligns to 24:961/963 of 3ad7A
- active site: L349 (= L374), L374 (= L393), D676 (= D688)
- binding flavin mononucleotide: K509 (= K521), R510 (= R522), T516 (≠ M528), Q520 (= Q532), T548 (= T559), R550 (= R561)
- binding nicotinamide-adenine-dinucleotide: G134 (= G172), G136 (= G174), P137 (= P175), A138 (= A176), D157 (= D195), E158 (= E196), R159 (≠ D197), T165 (≠ R203), V204 (= V241), T248 (≠ A280), A249 (≠ G281), S294 (≠ D326), F380 (≠ W399), G416 (= G436), L422 (≠ F442), D423 (≠ T443), T424 (= T444)
1vrqA Crystal structure of heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with folinic acid (see paper)
37% identity, 98% coverage: 17:970/973 of query aligns to 24:961/963 of 1vrqA
- active site: L349 (= L374), L374 (= L393), D676 (= D688)
- binding flavin mononucleotide: K509 (= K521), R510 (= R522), T516 (≠ M528), Q520 (= Q532), T548 (= T559), R550 (= R561)
- binding N-{[4-({[(6R)-2-amino-5-formyl-4-oxo-1,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)phenyl]carbonyl}-L-glutamic acid: L631 (= L643), Y663 (= Y675), G677 (= G689), H690 (≠ T702), I774 (= I784), F776 (= F786), E783 (= E793), K822 (= K832), F824 (= F834)
- binding nicotinamide-adenine-dinucleotide: G134 (= G172), G136 (= G174), P137 (= P175), A138 (= A176), D157 (= D195), E158 (= E196), R159 (≠ D197), T165 (≠ R203), V204 (= V241), T248 (≠ A280), A249 (≠ G281), S294 (≠ D326), F380 (≠ W399), G416 (= G436), L422 (≠ F442), D423 (≠ T443), T424 (= T444)
1worA Crystal structure of t-protein of the glycine cleavage system (see paper)
26% identity, 36% coverage: 595:946/973 of query aligns to 12:339/362 of 1worA
1wopA Crystal structure of t-protein of the glycine cleavage system (see paper)
26% identity, 36% coverage: 595:946/973 of query aligns to 12:339/362 of 1wopA
- active site: D96 (= D688)
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: M51 (≠ L643), L55 (≠ D647), Y83 (= Y675), D96 (= D688), V98 (≠ T690), E106 (≠ H698), L108 (≠ V700), V110 (≠ T702), N112 (≠ T704), I137 (≠ V733), E160 (≠ G756), Y168 (≠ F766), Y169 (≠ M767), K173 (≠ E771), S174 (≠ I772), I175 (≠ A773), E180 (≠ P778), T181 (≠ A779), Y188 (≠ F786), E195 (= E793), M197 (≠ A795), R227 (≠ L825), Y236 (≠ F834)
Sites not aligning to the query:
1wooA Crystal structure of t-protein of the glycine cleavage system (see paper)
26% identity, 36% coverage: 595:946/973 of query aligns to 12:339/362 of 1wooA
- active site: D96 (= D688)
- binding (6s)-5,6,7,8-tetrahydrofolate: M51 (≠ L643), Y83 (= Y675), D96 (= D688), V98 (≠ T690), V110 (≠ T702), N112 (≠ T704), Y168 (≠ F766), Y169 (≠ M767), Y188 (≠ F786), E195 (= E793), Y236 (≠ F834)
Sites not aligning to the query:
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
29% identity, 24% coverage: 606:834/973 of query aligns to 490:724/866 of Q9UI17
- A530 (≠ G636) to G: in dbSNP:rs1805073
- S646 (≠ G756) to P: in dbSNP:rs1805074
Sites not aligning to the query:
- 59:60 binding
- 80:81 binding
- 87:95 binding
- 91 modified: Tele-8alpha-FAD histidine
- 109 H → R: in DMGDHD; shows 10 fold lower catalytic efficiency due to lower cofactor saturation and reduced thermal stability; dbSNP:rs121908331
- 219 binding
- 279 S → P: in dbSNP:rs532964
- 397:402 binding
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
26% identity, 35% coverage: 606:945/973 of query aligns to 446:787/824 of 4pabB
- active site: E536 (≠ D688)
- binding (6s)-5,6,7,8-tetrahydrofolate: I523 (≠ Y675), E536 (≠ D688), T538 (= T690), I550 (≠ T702), F612 (= F766), L613 (≠ M767), Y632 (≠ F786), E639 (= E793), F680 (= F834), Y700 (≠ G853)
Sites not aligning to the query:
- active site: 53, 102, 226, 255
- binding flavin-adenine dinucleotide: 11, 12, 14, 15, 16, 35, 36, 37, 43, 44, 45, 47, 48, 49, 50, 51, 175, 204, 205, 207, 226, 228, 326, 328, 353, 355, 356, 357, 358
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
26% identity, 35% coverage: 606:945/973 of query aligns to 483:824/857 of Q63342
Sites not aligning to the query:
- 52:53 binding
- 73:74 binding
- 80:88 binding
- 84 modified: Tele-8alpha-FAD histidine
- 212 binding
- 244 binding
- 390:395 binding
1pj6A Crystal structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folic acid (see paper)
26% identity, 40% coverage: 581:973/973 of query aligns to 423:828/828 of 1pj6A
Sites not aligning to the query:
- active site: 223, 257
- binding flavin-adenine dinucleotide: 9, 11, 12, 13, 33, 34, 42, 43, 44, 46, 48, 50, 172, 201, 202, 204, 223, 257, 331, 332, 358, 359, 360, 361
Q9AGP8 Dimethylglycine oxidase; DMGO; EC 1.5.3.10 from Arthrobacter globiformis (see 2 papers)
26% identity, 40% coverage: 581:973/973 of query aligns to 425:830/830 of Q9AGP8
- Y539 (= Y675) binding
- D552 (= D688) Important for catalytic activity; mutation to A: No effect on the activity.; mutation to N: Reduces activity 3-fold.
Sites not aligning to the query:
- 14:15 binding
- 35:36 binding
- 45:48 binding
- 52 binding
- 174 binding
- 225 Important for catalytic activity; H→Q: Reduces catalytic efficiency 3-fold and substrate affinity 30-fold.
- 259 Important for catalytic activity; binding ; Y→F: Reduces catalytic efficiency 225-fold and substrate affinity 25-fold.
- 360:363 binding
1pj7A Structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folinic acid (see paper)
26% identity, 40% coverage: 581:973/973 of query aligns to 422:827/827 of 1pj7A
- active site: D549 (= D688)
- binding N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid: L505 (= L643), Y536 (= Y675), D549 (= D688), T551 (= T690), G563 (≠ A706), F629 (≠ M767), Y648 (≠ F786), E655 (= E793), Y696 (≠ F834)
Sites not aligning to the query:
- active site: 222, 256
- binding flavin-adenine dinucleotide: 8, 10, 11, 12, 32, 33, 41, 42, 43, 45, 47, 49, 170, 171, 200, 201, 203, 222, 256, 331, 357, 358, 359, 360
Q8GAI3 4-methylaminobutanoate oxidase (formaldehyde-forming); MABO; Demethylating gamma-N-methylaminobutyrate oxidase; Gamma-N-methylaminobutyrate oxidase 1; EC 1.5.3.19 from Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans) (see paper)
27% identity, 40% coverage: 584:973/973 of query aligns to 438:824/824 of Q8GAI3
Sites not aligning to the query:
- 66 mutation W->F,S: Contains a non-covalently bound FAD. Loss of enzyme activity.
- 67 H→A: Contains a non-covalently bound FAD. Exhibits about 10% of the wild-type enzyme activity.
3gsiA Crystal structure of d552a dimethylglycine oxidase mutant of arthrobacter globiformis in complex with tetrahydrofolate (see paper)
26% identity, 40% coverage: 581:973/973 of query aligns to 422:827/827 of 3gsiA
- active site: A549 (≠ D688)
- binding (6s)-5,6,7,8-tetrahydrofolate: L505 (= L643), Y536 (= Y675), T551 (= T690), G563 (≠ A706), F629 (≠ M767), Y648 (≠ F786), E655 (= E793), Y696 (≠ F834)
Sites not aligning to the query:
- active site: 222, 256
- binding flavin-adenine dinucleotide: 10, 11, 12, 32, 33, 41, 42, 43, 45, 47, 49, 170, 171, 200, 201, 203, 222, 256, 330, 331, 332, 357, 358, 359, 360
- binding magnesium ion: 254, 409
1y56A Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
24% identity, 38% coverage: 207:572/973 of query aligns to 144:482/484 of 1y56A
- binding adenosine-5'-triphosphate: A175 (≠ V241), T207 (≠ A280), G208 (= G281), R303 (≠ W399), G342 (= G436), S343 (≠ A437), H350 (≠ T444), N353 (≠ V447)
- binding fe (iii) ion: G439 (≠ A529), C441 (≠ D531)
- binding flavin mononucleotide: R432 (= R522), M438 (= M528), R471 (= R561)
Sites not aligning to the query:
3a8iA Crystal structure of et-ehred-5-ch3-thf complex (see paper)
26% identity, 35% coverage: 619:963/973 of query aligns to 28:355/363 of 3a8iA
- active site: D97 (= D688)
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M51 (≠ L643), Y84 (= Y675), D97 (= D688), I99 (≠ T690), V111 (≠ T702), N113 (≠ T704), F173 (≠ C769), Y188 (≠ F786), E195 (= E793), R223 (≠ L825), M232 (≠ F834), W252 (≠ G853)
3tfjA Dmsp-dependent demethylase from p. Ubique - with cofactor thf (see paper)
22% identity, 32% coverage: 623:933/973 of query aligns to 43:340/369 of 3tfjA
- active site: D108 (= D688)
- binding (6s)-5,6,7,8-tetrahydrofolate: E63 (≠ L643), Y95 (= Y675), D108 (= D688), V110 (≠ T690), S122 (≠ T702), I123 (≠ T703), A124 (≠ T704), F178 (≠ M767), W197 (≠ F786), E204 (= E793), Y265 (≠ M854)
Sites not aligning to the query:
3tfiA Dmsp-dependent demethylase from p. Ubique - with substrate dmsp (see paper)
22% identity, 32% coverage: 623:933/973 of query aligns to 43:340/369 of 3tfiA
Sites not aligning to the query:
Query Sequence
>GFF863 FitnessBrowser__Phaeo:GFF863
MRIAGWAGRSDTREVGFSFNGRALTGREGEPLAAALLANNIHLVGRSFKYHRPRGILTAG
SEEPNALVTVGEGAAQEPNLRATTLPLYEGLAARSQNCWPSVGFDVMAVNDLAAPFLGAG
FYYKTFMWPAAFWEKIYEPVIRRAAGLGALSGAPDDGIYEKAYGFCDLLVIGAGPAGLMA
ALTAARGGADVILCDEDSQPGGRLLSEQETINGNPAQQWVAATLAELDSLNNVRRMARTS
VTGVYDQGTYGALETVPAGGGKPARACFWRLVAKRAILAAGALERPVAFANNDRPGIMLA
GAVRSYLNRWGVAPGERVTVFANNDDAHRTARDLLAAGVHVAAVIDSRHDAPQSDAFRVI
RGAQVCNASGRQRLESLTLRSVSGEEKLQTDCLAMSGGWNPTLHLTCHLNGRPRWRRDLA
CFVPQDGAVPGLEAVGACRGRFTTMAVLQDGAEAGARALEALGKRAVAAELPEAEQAEYR
ISPLWSVPGRGRAWVDFQNDVTVKDICQAGRENFRSAEHMKRYTTQGMATDQGKSSNVVA
LAVLAEATGRSIPETGTTTFRPPYVPVPIGVMGAGAEDQGFAPRRLLTSHRLAEDMGAHM
MEVGLWYRASYFPKPGETHWRQSCDREVGYVRNAVGVADVSTLGKIDIQGPDAARLLDFV
YANGFAKLKPGRVRYGLMLREDGFVMDDGTTACLAPNHYVMTTTTAAAGQVMAHLEFVTQ
ALHPDWDVRINSVTEQWAQFSVAGPKARALLQGLLGVAFEPADWPFMACGEIALGEIPAR
LFRISFSGEEAYELAVPARYGDSLFDELLRRAEGLGGGAYGLEALNVLRIEKGFLTHAEI
NGTATLHDLGFGGMLASGKPCVGRELAQREGLTAKDRMRLVGIKPIGAVQQLTAGAHLFD
PQDPVERVHDQGYVTSVGYSPTLGHMIGLALIKAGPDRIGDPIRMVDHTAGLDTLCEIVE
PVFFDPEGERARG
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