SitesBLAST

V35 (≠ I33) mutation to A: Significantly reduces raffinose transport, enhances maltose transport.
S138 (≠ Q135) mutation to D: Significantly reduces raffinose transport, enhances maltose transport; when associated with L-139 and A-389.
S139 (= S136) mutation to L: Significantly reduces raffinose transport, enhances maltose transport; when associated with D-138 and A-389.
G389 (= G382) mutation to A: Significantly reduces raffinose transport, enhances maltose transport; when associated with D-138 and L-139.
I391 (≠ L384) mutation to S: Significantly reduces raffinose transport, enhances maltose transport.

P02920 Lactose permease; Lactose-proton symport from Escherichia coli (strain K12) (see 3 papers)
42% identity, 88% coverage: 33:396/413 of query aligns to 32:400/417 of P02920

query
sites
P02920

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L65 (≠ F66) mutation to V: No change in transport activity.
G96 (= G96) mutation to A: No change in transport activity.
A122 (≠ I122) mutation to S: No change in transport activity.
D237 (≠ G233) mutation D->N,G: Loss of activity.
V264 (≠ L260) mutation to A: No change in transport activity.
A279 (= A275) mutation to S: No change in transport activity.
C355 (≠ A351) mutation to Q: No change in transport activity.
K358 (≠ S354) mutation to T: Loss of activity.
V367 (≠ P363) mutation to A: Increases transport of melibiose and impairs transport of TMG.

Sites not aligning to the query:

1 modified: N-formylmethionine; partial

1pv7A Crystal structure of lactose permease with tdg (see paper)
42% identity, 88% coverage: 33:396/413 of query aligns to 32:400/417 of 1pv7A

query
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1pv7A

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binding beta-D-galactopyranose: D237 (≠ G233), K358 (≠ S354)
binding 1-thio-beta-D-galactopyranose: R144 (= R144), E269 (≠ V265)

Sites not aligning to the query:

binding 1-thio-beta-D-galactopyranose: 23

2y5yA Crystal structure of lacy in complex with an affinity inactivator (see paper)
42% identity, 88% coverage: 33:396/413 of query aligns to 29:383/386 of 2y5yA

query
sites
2y5yA

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binding 2-sulfanylethyl beta-D-galactopyranoside: C119 (≠ I122), E123 (= E126), A145 (≠ S148), W148 (= W151), E252 (≠ V265)

Sites not aligning to the query:

binding 2-sulfanylethyl beta-D-galactopyranoside: 17

4zyrA Crystal structure of e. Coli lactose permease g46w/g262w bound to p- nitrophenyl alpha-d-galactopyranoside (alpha-npg) (see paper)
41% identity, 88% coverage: 33:396/413 of query aligns to 27:379/387 of 4zyrA

query
sites
4zyrA

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F

N

V

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A

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x
E

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P

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x
V

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L

binding 4-nitrophenyl alpha-D-galactopyranoside: N114 (= N119), R139 (= R144), G142 (= G147), C143 (≠ S148), W146 (= W151), E248 (≠ V265), H301 (= H318), V305 (≠ L322)

Sites not aligning to the query:

binding 4-nitrophenyl alpha-D-galactopyranoside: 18, 22

P96517 Melibiose permease; Melibiose transporter MelY from Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56) (see 2 papers)
42% identity, 90% coverage: 31:401/413 of query aligns to 35:410/425 of P96517

query
sites
P96517

L

L

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P

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I

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Y

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P

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E

L88 (= L84) mutation to P: Does not affect melibiose transport. Increases affinity for maltose and maltose transport.
L91 (= L87) mutation to P: Does not affect melibiose transport. Increases affinity for maltose and maltose transport.
A182 (≠ G177) mutation to P: Does not affect melibiose transport. Increases affinity for maltose and maltose transport.
A367 (= A358) mutation to V: No change in transport activity.

Query Sequence

>BWI76_RS23415 FitnessBrowser__Koxy:BWI76_RS23415
MMKAHPSQSYPLLSALLFFFFVTWSSSGSLLSIWLHQEVGLKPGDTGIIFSVLSVSALFA
QVCYGFIQDKLGLRKNLLWYITVLLILSGPAYMLFGYLLKINVLLGSIFGGIYIGLTFNG
GIGVLESYTERVARQSQFEFGKARMWGSLGWAVATFFAGLLFNINPHLNFAVASCSGLVF
FILLARLRVSSAPHAMQEAVSGGKVTLEDALRLLTLPRFWALVFFVIGTCIYGVYDQQFP
VYFSSQFPTLQEGNEMYGYLNSFQVFLEAAGMFCAPWLVNRIGAKNGLIFAGMVMAMRMV
ASGLVEGPLLISITKLLHAVELPVLLVSIFKYNSLNFDKRLSSTLYLVGFACTSSVIATV
LSPLAGYSYEKYGFAQSYLIMGLLVFCTTFISIFLLRSSKSSSDPLMPQTSAI

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