SitesBLAST

Q50LF2 Sarcosine oxidase subunit beta; Sarcosine oxidase subunit B; Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit beta; Tetrameric sarcosine oxidase subunit beta; TSOX subunit beta; EC 1.5.3.24 from Corynebacterium sp. (strain U-96) (see 4 papers)
27% identity, 48% coverage: 208:405/410 of query aligns to 180:372/405 of Q50LF2

query
sites
Q50LF2

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V197 (= V225) binding
H270 (≠ R304) mutation to A: 10-fold decrease in catalytic efficiency.
Y272 (≠ T306) mutation to A: 13000-fold decrease in catalytic efficiency.; mutation to F: 130-fold decrease in catalytic efficiency.
G354 (= G387) binding
G357 (= G390) binding
K359 (≠ T392) binding ; mutation K->A,D: Loss of activity.; mutation to R: Retains 0.07% of wild-type activity. Shows higher apparent KM for sarcosine.

Sites not aligning to the query:

31 binding
32 binding
53 binding
61 binding
62 binding
66 binding
68 binding
172 K→A: Retains 39% of wild-type activity.; K→D: Retains 32% of wild-type activity.; K→R: Retains 58% of wild-type activity.
173 modified: Tele-8alpha-FMN histidine

1vrqB Crystal structure of heterotetrameric sarcosine oxidase from corynebacterium sp. U-96 in complex with folinic acid (see paper)
27% identity, 48% coverage: 208:405/410 of query aligns to 179:371/402 of 1vrqB

query
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1vrqB

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active site: G326 (= G360), K358 (≠ T392)
binding n,n-dimethylglycine: K358 (≠ T392)
binding flavin-adenine dinucleotide: V196 (= V225), A224 (= A258), G225 (≠ A259), H228 (≠ Y262), L247 (= L279), G353 (= G387), T354 (≠ A388), G355 (≠ L389), G356 (= G390), F357 (≠ M391), K358 (≠ T392)
binding flavin mononucleotide: V251 (≠ S283), E279 (≠ D313), R322 (≠ Q356), W324 (= W358)

Sites not aligning to the query:

active site: 62, 65, 66
binding n,n-dimethylglycine: 65, 67, 69, 401
binding flavin-adenine dinucleotide: 26, 27, 29, 30, 31, 51, 52, 53, 59, 60, 61, 63, 64, 65, 67
binding flavin mononucleotide: 62, 63, 172

P40875 Sarcosine oxidase subunit beta; Sarcosine oxidase subunit B; Sarcosine oxidase (5,10-methylenetetrahydrofolate-forming) subunit beta; Tetrameric sarcosine oxidase subunit beta; TSOX subunit beta; EC 1.5.3.24 from Corynebacterium sp. (strain P-1) (see 3 papers)
26% identity, 48% coverage: 208:405/410 of query aligns to 180:372/405 of P40875

query
sites
P40875

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C195 (≠ S223) mutation to S: No change in activity.
C351 (= C384) mutation to A: No change in activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
30 G→A: Prevents covalent attachment of FMN. Blocks subunit assembly.
146 C→S: No change in activity.
173 modified: Tele-8alpha-FMN histidine; H→N: Prevents covalent attachment of FMN. Loss of activity. The mutant is considerably less stable than wild-type enzyme, the beta and delta subunits are lost during purification, which yields a stable alpha-gamma complex.
175 H→A: No effect on FMN binding and activity.

2gagB Heteroteterameric sarcosine: structure of a diflavin metaloenzyme at 1.85 a resolution (see paper)
25% identity, 48% coverage: 208:405/410 of query aligns to 178:370/403 of 2gagB

query
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2gagB

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binding flavin-adenine dinucleotide: V195 (= V225), G224 (≠ A259), A225 (≠ G260), H227 (≠ Y262), L231 (= L266), L246 (= L279), G352 (= G387), T353 (≠ A388), G354 (≠ L389), G355 (= G390), F356 (≠ M391), K357 (≠ T392)
binding flavin mononucleotide: V250 (≠ S283), E278 (≠ D313), R321 (≠ Q356), W323 (= W358)
binding 2-furoic acid: M263 (≠ V299), Y270 (≠ T306), K357 (≠ T392)
binding sulfite ion: K276 (≠ I311)

Sites not aligning to the query:

active site: 61, 64, 65
binding flavin-adenine dinucleotide: 26, 28, 29, 30, 51, 52, 58, 59, 60, 62, 63, 64, 66
binding flavin mononucleotide: 61, 62, 171
binding 2-furoic acid: 64, 66, 68, 401
binding sulfite ion: 170

1pj6A Crystal structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folic acid (see paper)
23% identity, 48% coverage: 123:317/410 of query aligns to 74:267/828 of 1pj6A

query
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1pj6A

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active site: H223 (≠ K280), Y257 (≠ F308)
binding flavin-adenine dinucleotide: V172 (= V225), A201 (= A259), G202 (= G260), W204 (≠ Y262), H223 (≠ K280), Y257 (≠ F308)

Sites not aligning to the query:

active site: 550
binding flavin-adenine dinucleotide: 9, 11, 12, 13, 33, 34, 42, 43, 44, 46, 48, 50, 331, 332, 358, 359, 360, 361

1pj7A Structure of dimethylglycine oxidase of arthrobacter globiformis in complex with folinic acid (see paper)
23% identity, 48% coverage: 123:317/410 of query aligns to 73:266/827 of 1pj7A

query
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1pj7A

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G

Y

-

K

-

K

E

A

N

F

I

H

L

G

G

A

G

I

L

H

H

T

V

D

P

S

S

E

D

C

G

A

L

V

A

D

S

G

A

R

A

K

R

L

A

C

V

Q

Q

E

L

L

L

A

I

R

K

L

R

L

T

S

E

T

S

Q

A

G

G

V

V

R

T

F

Y

L

R

F

G

D

S

S

T

E
x
T

V
|
V

A

T

A

G

F

I

R

E

R

Q

E

S

R

G

G

G

R

R

I

V

T

T

A

G

L

V

E

Q

I

T

H

-

A

-

I

-

E

-

G

A

P

D

G

G

L

V

L

I

G

P

T

A

Q

D

A

I

V

V

L

S

A

C

A
|
A

G
|
G

A

F

Y
x
W

S

G

A

A

G

K

L

I

L

G

S

A

A

M

F

I

G

G

V

M

R

A

M

V

P

P

V

L

Y

L

P

P

L

L

-

A

K
x
H

G

Q

Y

Y

S

V

I

K

T

T

L

T

P

P

I

V

-

P

-

A

-

Q

-

G

-

R

T

N

D

D

S

Q

M

P

N

N

A

G

P

A

T

R

V

L

S

P

V

I

T

L

D

R

M

H

R

Q

R

D

K

Q

T

D

V

L

F
x
Y

A

Y

R

R

-

E

I

H

G

G

D

D

R

R

L

Y

R

G

V

I

active site: H222 (≠ K280), Y256 (≠ F308)
binding flavin-adenine dinucleotide: T170 (≠ E224), V171 (= V225), A200 (= A259), G201 (= G260), W203 (≠ Y262), H222 (≠ K280), Y256 (≠ F308)

Sites not aligning to the query:

active site: 549
binding flavin-adenine dinucleotide: 8, 10, 11, 12, 32, 33, 41, 42, 43, 45, 47, 49, 331, 357, 358, 359, 360
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: 505, 536, 549, 551, 563, 629, 648, 655, 696

3gsiA Crystal structure of d552a dimethylglycine oxidase mutant of arthrobacter globiformis in complex with tetrahydrofolate (see paper)
23% identity, 48% coverage: 123:317/410 of query aligns to 73:266/827 of 3gsiA

query
sites
3gsiA

I

L

S

T

Q

E

E

D

K

G

V

V

Q

S

C

C

D

-

F

F

A

N

R

Q

T

V

G

G

K

G

L

L

V

E

L

V

Y

A

P

T

D

T

A

E

E

T

S

R

L

L

R

A

K

D

A

L

G

K

D

R

Q

K

V

L

K

G

F

Y

Q

A

A

A

Q

W

G

G

A

I

R

-

Q

E

Q

G

K

R

I

L

V

L

S

S

P

P

A

A

E

E

A

C

L

Q

S

E

I

L

E

Y

P

P

A

L

L

L

E

D

G

G

Y

-

K

-

K

E

A

N

F

I

H

L

G

G

A

G

I

L

H

H

T

V

D

P

S

S

E

D

C

G

A

L

V

A

D

S

G

A

R

A

K

R

L

A

C

V

Q

Q

E

L

L

L

A

I

R

K

L

R

L

T

S

E

T

S

Q

A

G

G

V

V

R

T

F

Y

L

R

F

G

D

S

S

T

E
x
T

V
|
V

A

T

A

G

F

I

R

E

R

Q

E

S

R

G

G

G

R

R

I

V

T

T

A

G

L

V

E

Q

I

T

H

-

A

-

I

-

E

-

G

A

P

D

G

G

L

V

L

I

G

P

T

A

Q

D

A

I

V

V

L

S

A

C

A
|
A

G
|
G

A

F

Y
x
W

S

G

A

A

G

K

L

I

L

G

S

A

A

M

F

I

G

G

V

M

R

A

M

V

P

P

V

L

Y

L

P

P

L

L

-

A

K
x
H

G

Q

Y

Y

S

V

I

K

T

T

L

T

P

P

I

V

-

P

-

A

-

Q

-

G

-

R

T

N

D

D

S

Q

M

P

N

N

A

G

P

A

T

R

V

L

S

P

V

I

T

L

D

R

M

H

R

Q

R

D

K

Q

T
x
D

V

L

F
x
Y

A

Y

R

R

-

E

I

H

G

G

D

D

R

R

L

Y

R

G

V

I

active site: H222 (≠ K280), Y256 (≠ F308)
binding flavin-adenine dinucleotide: T170 (≠ E224), V171 (= V225), A200 (= A259), G201 (= G260), W203 (≠ Y262), H222 (≠ K280), Y256 (≠ F308)
binding magnesium ion: D254 (≠ T306)

Sites not aligning to the query:

active site: 549
binding flavin-adenine dinucleotide: 10, 11, 12, 32, 33, 41, 42, 43, 45, 47, 49, 330, 331, 332, 357, 358, 359, 360
binding magnesium ion: 409
binding (6s)-5,6,7,8-tetrahydrofolate: 505, 536, 551, 563, 629, 648, 655, 696

Q9AGP8 Dimethylglycine oxidase; DMGO; EC 1.5.3.10 from Arthrobacter globiformis (see 2 papers)
23% identity, 48% coverage: 123:317/410 of query aligns to 76:269/830 of Q9AGP8

query
sites
Q9AGP8

I

L

S

T

Q

E

E

D

K

G

V

V

Q

S

C

C

D

-

F

F

A

N

R

Q

T

V

G

G

K

G

L

L

V

E

L

V

Y

A

P

T

D

T

A

E

E

T

S

R

L

L

R

A

K

D

A

L

G

K

D

R

Q

K

V

L

K

G

F

Y

Q

A

A

A

Q

W

G

G

A

I

R

-

Q

E

Q

G

K

R

I

L

V

L

S

S

P

P

A

A

E

E

A

C

L

Q

S

E

I

L

E

Y

P

P

A

L

L

L

E

D

G

G

Y

-

K

-

K

E

A

N

F

I

H

L

G

G

A

G

I

L

H

H

T

V

D

P

S

S

E

D

C

G

A

L

V

A

D

S

G

A

R

A

K

R

L

A

C

V

Q

Q

E

L

L

L

A

I

R

K

L

R

L

T

S

E

T

S

Q

A

G

G

V

V

R

T

F

Y

L

R

F

G

D

S

S

T

E

T

V
|
V

A

T

A

G

F

I

R

E

R

Q

E

S

R

G

G

G

R

R

I

V

T

T

A

G

L

V

E

Q

I

T

H

-

A

-

I

-

E

-

G

A

P

D

G

G

L

V

L

I

G

P

T

A

Q

D

A

I

V

V

L

S

A

C

A

A

G

G

A

F

Y

W

S

G

A

A

G

K

L

I

L

G

S

A

A

M

F

I

G

G

V

M

R

A

M

V

P

P

V

L

Y

L

P

P

L

L

-

A

K
x
H

G

Q

Y

Y

S

V

I

K

T

T

L

T

P

P

I

V

-

P

-

A

-

Q

-

G

-

R

T

N

D

D

S

Q

M

P

N

N

A

G

P

A

T

R

V

L

S

P

V

I

T

L

D

R

M

H

R

Q

R

D

K

Q

T

D

V

L

F
x
Y

A

Y

R

R

-

E

I

H

G

G

D

D

R

R

L

Y

R

G

V

I

V174 (= V225) binding
H225 (≠ K280) Important for catalytic activity; mutation to Q: Reduces catalytic efficiency 3-fold and substrate affinity 30-fold.
Y259 (≠ F308) Important for catalytic activity; binding ; mutation to F: Reduces catalytic efficiency 225-fold and substrate affinity 25-fold.

Sites not aligning to the query:

14:15 binding
35:36 binding
45:48 binding
52 binding
360:363 binding
539 binding
552 Important for catalytic activity; D→A: No effect on the activity.; D→N: Reduces activity 3-fold.

Query Sequence

>Pf6N2E2_3402 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_3402
MEICVVGAGIVGLSSAWFLHKAGHTVTVIDRAGEAGMGASAANGAQLSYSYVQPLADPSL
LPGIPKMLLERNGPLKFSPQWSLEQWRWCVEFLAACRTSVSRQTTVELLELAHESRLALD
AFISQEKVQCDFARTGKLVLYPDAESLRKAGDQVKFQAAQGARQQKIVSPAEALSIEPAL
EGYKKAFHGAIHTDSECAVDGRKLCQELARLLSTQGVRFLFDSEVAAFRRERGRITALEI
HHAIEGPGLLGTQAVVLAAGAYSAGLLSAFGVRMPVYPLKGYSITLPITDSMNAPTVSVT
DMRRKTVFARIGDRLRVAGMVELCGLDASIPVKRIEQLKASTQALFGLEWNADDCQPWTG
WRPATPTGRPILAVSGCDNLYVNCGQGALGMTLAFGSAQRLVRLIGGTAL

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