SitesBLAST
Comparing WP_084191695.1 NCBI__GCF_000733765.1:WP_084191695.1 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)
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)
32% identity, 99% coverage: 1:940/947 of query aligns to 25:965/967 of Q46337
- G139 (= G155) mutation to A: Does not affect activity and binding of NAD(+).
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2gagA Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
32% identity, 99% coverage: 1:940/947 of query aligns to 23:963/965 of 2gagA
- active site: L350 (vs. gap), L375 (≠ V378), D677 (= D666)
- binding flavin mononucleotide: K510 (= K505), R511 (= R506), T517 (≠ M512), Q521 (= Q516), T549 (= T543), R551 (= R545)
- binding 2-furoic acid: N647 (≠ E636), G653 (≠ R642), T655 (= T644), K851 (= K835)
- binding nicotinamide-adenine-dinucleotide: V134 (= V152), G135 (= G153), G137 (= G155), P138 (= P156), A139 (= A157), D158 (= D176), E159 (≠ D177), R160 (≠ N178), G165 (= G183), T166 (≠ S184), T204 (≠ V219), V205 (≠ A220), T249 (= T249), G250 (= G250), S295 (≠ E295), F381 (≠ W384), G417 (= G420), A418 (≠ R421), L423 (≠ F426), D424 (≠ T427), T425 (≠ L428), Y554 (≠ V548)
3ad7A Heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with methylthio acetate (see paper)
33% identity, 86% coverage: 126:940/947 of query aligns to 107:962/963 of 3ad7A
- active site: L349 (≠ V351), L374 (≠ V378), D676 (= D666)
- binding flavin mononucleotide: K509 (= K505), R510 (= R506), T516 (≠ M512), Q520 (= Q516), T548 (= T543), R550 (= R545)
- binding nicotinamide-adenine-dinucleotide: G134 (= G153), G136 (= G155), P137 (= P156), A138 (= A157), D157 (= D176), E158 (≠ D177), R159 (≠ N178), T165 (≠ S184), V204 (≠ A220), T248 (= T249), A249 (≠ G250), S294 (≠ E295), F380 (≠ W384), G416 (= G420), L422 (≠ F426), D423 (≠ T427), T424 (≠ L428)
1vrqA Crystal structure of heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with folinic acid (see paper)
33% identity, 86% coverage: 126:940/947 of query aligns to 107:962/963 of 1vrqA
- active site: L349 (≠ V351), L374 (≠ V378), D676 (= D666)
- binding flavin mononucleotide: K509 (= K505), R510 (= R506), T516 (≠ M512), Q520 (= Q516), T548 (= T543), R550 (= R545)
- 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 (= L621), Y663 (= Y653), G677 (= G667), H690 (≠ T680), I774 (≠ V761), F776 (= F763), E783 (= E770), K822 (= K807), F824 (≠ H809)
- binding nicotinamide-adenine-dinucleotide: G134 (= G153), G136 (= G155), P137 (= P156), A138 (= A157), D157 (= D176), E158 (≠ D177), R159 (≠ N178), T165 (≠ S184), V204 (≠ A220), T248 (= T249), A249 (≠ G250), S294 (≠ E295), F380 (≠ W384), G416 (= G420), L422 (≠ F426), D423 (≠ T427), T424 (≠ L428)
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)
33% identity, 86% coverage: 126:940/947 of query aligns to 108:963/965 of Q50LF0
- A139 (= A157) binding NAD(+)
- D158 (= D176) binding NAD(+)
- E159 (≠ D177) binding NAD(+)
- R160 (≠ N178) binding NAD(+)
- T166 (≠ S184) binding NAD(+)
- V205 (≠ A220) binding NAD(+)
- A418 (≠ R421) binding NAD(+)
- L423 (≠ F426) binding NAD(+)
- T425 (≠ L428) binding NAD(+)
1worA Crystal structure of t-protein of the glycine cleavage system (see paper)
32% identity, 39% coverage: 567:933/947 of query aligns to 4:356/362 of 1worA
1wopA Crystal structure of t-protein of the glycine cleavage system (see paper)
32% identity, 39% coverage: 567:933/947 of query aligns to 4:356/362 of 1wopA
- active site: D96 (= D666)
- 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 (≠ L621), L55 (≠ E625), Y83 (= Y653), D96 (= D666), V98 (≠ I668), E106 (≠ R676), L108 (≠ Y678), V110 (≠ T680), N112 (≠ T682), I137 (≠ L707), E160 (≠ S732), Y168 (= Y743), Y169 (≠ L744), K173 (≠ E748), S174 (≠ G749), I175 (≠ R750), E180 (≠ P755), T181 (≠ A756), Y188 (≠ F763), E195 (= E770), M197 (≠ H772), R227 (≠ Q800), Y236 (≠ H809)
Sites not aligning to the query:
1wooA Crystal structure of t-protein of the glycine cleavage system (see paper)
32% identity, 39% coverage: 567:933/947 of query aligns to 4:356/362 of 1wooA
- active site: D96 (= D666)
- binding (6s)-5,6,7,8-tetrahydrofolate: M51 (≠ L621), Y83 (= Y653), D96 (= D666), V98 (≠ I668), V110 (≠ T680), N112 (≠ T682), Y168 (= Y743), Y169 (≠ L744), Y188 (≠ F763), E195 (= E770), Y236 (≠ H809)
Sites not aligning to the query:
1pj6A Crystal structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folic acid (see paper)
31% identity, 40% coverage: 560:939/947 of query aligns to 422:825/828 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
1pj7A Structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folinic acid (see paper)
31% identity, 40% coverage: 560:939/947 of query aligns to 421:824/827 of 1pj7A
- active site: D549 (= D666)
- 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 (= L621), Y536 (= Y653), D549 (= D666), T551 (≠ I668), G563 (vs. gap), F629 (≠ L744), Y648 (≠ F763), E655 (= E770), Y696 (≠ H809)
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
Q9AGP8 Dimethylglycine oxidase; DMGO; EC 1.5.3.10 from Arthrobacter globiformis (see 2 papers)
31% identity, 40% coverage: 560:939/947 of query aligns to 424:827/830 of Q9AGP8
- Y539 (= Y653) binding (6S)-5,6,7,8-tetrahydrofolate
- D552 (= D666) 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 FAD
- 35:36 binding FAD
- 45:48 binding FAD
- 52 binding FAD
- 174 binding FAD
- 225 Important for catalytic activity; H→Q: Reduces catalytic efficiency 3-fold and substrate affinity 30-fold.
- 259 Important for catalytic activity; binding FAD; Y→F: Reduces catalytic efficiency 225-fold and substrate affinity 25-fold.
- 360:363 binding FAD
3gsiA Crystal structure of d552a dimethylglycine oxidase mutant of arthrobacter globiformis in complex with tetrahydrofolate (see paper)
30% identity, 40% coverage: 560:939/947 of query aligns to 421:824/827 of 3gsiA
- active site: A549 (≠ D666)
- binding (6s)-5,6,7,8-tetrahydrofolate: L505 (= L621), Y536 (= Y653), T551 (≠ I668), G563 (vs. gap), F629 (≠ L744), Y648 (≠ F763), E655 (= E770), Y696 (≠ H809)
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
4pabB Crystal structure of the precursor form of rat dmgdh complexed with tetrahydrofolate (see paper)
29% identity, 35% coverage: 586:915/947 of query aligns to 470:787/824 of 4pabB
- active site: E536 (≠ D666)
- binding (6s)-5,6,7,8-tetrahydrofolate: I523 (≠ Y653), E536 (≠ D666), T538 (≠ I668), I550 (≠ T680), F612 (≠ Y743), L613 (= L744), Y632 (≠ F763), E639 (= E770), F680 (≠ H809), Y700 (≠ W829)
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
Q9UI17 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Homo sapiens (Human) (see 4 papers)
28% identity, 38% coverage: 554:916/947 of query aligns to 461:832/866 of Q9UI17
- A530 (≠ G614) to G: in dbSNP:rs1805073
- S646 (= S732) to P: in dbSNP:rs1805074
Sites not aligning to the query:
- 59:60 binding FAD
- 80:81 binding FAD
- 87:95 binding FAD
- 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 FAD
- 279 S → P: in dbSNP:rs532964
- 397:402 binding FAD
Q63342 Dimethylglycine dehydrogenase, mitochondrial; ME2GLYDH; EC 1.5.8.4 from Rattus norvegicus (Rat) (see 2 papers)
29% identity, 35% coverage: 586:915/947 of query aligns to 507:824/857 of Q63342
- ELT 573:575 (≠ DGI 666:668) binding (6S)-5,6,7,8-tetrahydrofolate
- Y669 (≠ F763) binding (6S)-5,6,7,8-tetrahydrofolate
- ELY 676:678 (≠ ELH 770:772) binding (6S)-5,6,7,8-tetrahydrofolate
- Y737 (≠ W829) binding (6S)-5,6,7,8-tetrahydrofolate
Sites not aligning to the query:
- 52:53 binding FAD
- 73:74 binding FAD
- 80:88 binding FAD
- 84 modified: Tele-8alpha-FAD histidine
- 212 binding FAD
- 244 binding FAD
- 390:395 binding FAD
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)
31% identity, 40% coverage: 562:941/947 of query aligns to 435:823/824 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.
3a8iA Crystal structure of et-ehred-5-ch3-thf complex (see paper)
29% identity, 37% coverage: 567:916/947 of query aligns to 4:342/363 of 3a8iA
- active site: D97 (= D666)
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M51 (≠ L621), Y84 (= Y653), D97 (= D666), I99 (= I668), V111 (≠ T680), N113 (≠ T682), F173 (≠ Y743), Y188 (≠ F763), E195 (= E770), R223 (≠ Q800), M232 (≠ H809), W252 (= W829)
P48728 Aminomethyltransferase, mitochondrial; Glycine cleavage system T protein; GCVT; EC 2.1.2.10 from Homo sapiens (Human) (see 4 papers)
27% identity, 37% coverage: 565:915/947 of query aligns to 34:378/403 of P48728
- D129 (= D666) mutation D->A,N: Loss of aminomethyltransferase activity.
- N145 (≠ T682) to I: in GCE2; loss of aminomethyltransferase activity; dbSNP:rs386833682
- E232 (= E770) binding substrate
- R261 (≠ Q800) binding substrate
- G269 (= G808) to D: in GCE2; decreased aminomethyltransferase activity; dbSNP:rs121964981
- R320 (≠ L855) to H: in GCE2; loss of aminomethyltransferase activity; dbSNP:rs121964985
Sites not aligning to the query:
1wsvA Crystal structure of human t-protein of glycine cleavage system (see paper)
27% identity, 37% coverage: 565:915/947 of query aligns to 3:347/371 of 1wsvA
- active site: D98 (= D666)
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: M53 (≠ L621), L85 (≠ Y653), D98 (= D666), L99 (≠ G667), I100 (= I668), V112 (≠ T680), N114 (≠ T682), F173 (≠ Y743), G193 (= G762), Y194 (≠ F763), E201 (= E770), R230 (≠ Q800), L239 (≠ H809)
Sites not aligning to the query:
1y56A Crystal structure of l-proline dehydrogenase from p.Horikoshii (see paper)
20% identity, 39% coverage: 192:557/947 of query aligns to 149:483/484 of 1y56A
- binding adenosine-5'-triphosphate: A175 (= A218), T207 (= T249), G208 (= G250), R303 (≠ W384), G342 (vs. gap), S343 (vs. gap), H350 (vs. gap), N353 (vs. gap)
- binding fe (iii) ion: G439 (= G513), C441 (≠ S515)
- binding flavin mononucleotide: R432 (= R506), M438 (= M512), R471 (= R545)
Sites not aligning to the query:
Query Sequence
>WP_084191695.1 NCBI__GCF_000733765.1:WP_084191695.1
MAFHFEGQEYSAHPGDTLSSALLANGVTLLGRSFKYHRPRGAFSLADHDVNALFCTKQDT
HLRGDVTTLRDGRDLYPVNVRGTLANDADRYLDRLARFLPVGFYYKAFYRPRALFPKWER
AIRKRAGLGSVDRSWKAQRRPKRNEHCDVLVVGAGPAGLSAALAAAEAGFSVVIADDNAH
PGGSFDYQWLHDEAAQRTRDALIAAVTAHPDIRLLCPAVALGHYADHLVPLSTPAGIVKM
RARGVIVATGLIEQPAVFRNNDRPGVMLASGAQRLLHRFGVAPCRRAVVLTANSEGYAVA
LDMHRAGVEVAAVLDMREGEEASPAAATLAQAGVPLLYGHAIYEAHGAEAVEAVTAAPLG
SPGRCNTVGAQRIACDGVLLSTGWAPAGALLYQAGGSFRYDAHLAMPVPERWPETVVPAG
RLNGAFTLAQQQADARDAAQRLVAALRGDRVPASADHRDDQAHGSEWPVIRHPEGRNFVD
LDEDLQLKDLEQAAREGFDNIELLKRYSTVGMGPSQGKHSNLNAIRILADHLGQGIDETG
STTARPMVRPVRLEDLAGRRLRPQRLTPLHEAHQALGAHFMEAGEWLRPAFYGDAAEADS
AIAAEVAAVRSRAGLIDVSTLGKIEVLGADAGRLLEAAYTMRMTNIAVGRTRYALMVDSS
GVIVDDGIVGRLAEDRYYVTTTSGHAAATFRTLSRCALEWGLDVHLLNRTGQLGALNLAG
PEARRLLAPLVSDVGLDEDAFPYLGIREGRVCGHPARLARVGFVGELGYELHLDARATAE
VWQALMRDADAPRPFGVEAQRLLRLEKGHIIVGQDTDGLSDPFEAGMGWAVHFKKPFFNG
RAALQQLKPRMRRRLVGFALPAGVETLPRECHLVIRDGVIAGRVTSIAHSPTLRHPVGLA
MVDAALADSGEALQIRGDDGRMHRAEQRATPFYDPEGLRQKAGEATA
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