SitesBLAST

Q99707 Methionine synthase; MS; 5-methyltetrahydrofolate--homocysteine methyltransferase; Cobalamin-dependent methionine synthase; Vitamin-B12 dependent methionine synthase; EC 2.1.1.13 from Homo sapiens (Human) (see 6 papers)
27% identity, 71% coverage: 3:108/149 of query aligns to 772:876/1265 of Q99707

query
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Q99707

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Sites not aligning to the query:

61 natural variant: R -> K
255 C → Y: in dbSNP:rs1140598
382:384 binding
449 binding
470 binding
537 binding
579 binding
585 binding
591 binding
919 D → G: in dbSNP:rs1805087
963 D→E: Decreases binding to MTRR; when associated with N-1071.
1071 K→N: Decreases binding to MTRR; when associated with E-963.

3koyA Crystal structure of ornithine 4,5 aminomutase in complex with ornithine (aerobic) (see paper)
36% identity, 60% coverage: 6:95/149 of query aligns to 596:693/728 of 3koyA

query
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3koyA

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active site: K617 (≠ V26)
binding cobalamin: E605 (≠ C15), H606 (= H16), S607 (≠ A17), V608 (= V18), V613 (= V22), S655 (= S61), I658 (≠ Y64), S659 (≠ G65), G689 (= G91), G690 (= G92), T691 (≠ N93)

Sites not aligning to the query:

active site: 183, 218, 290
binding cobalamin: 112, 483, 707, 710, 711
binding (E)-N~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-ornithine: 77, 105, 109, 110, 156, 158, 178, 183, 188, 218, 219, 290, 292

3koxA Crystal structure of ornithine 4,5 aminomutase in complex with 2,4- diaminobutyrate (anaerobic) (see paper)
36% identity, 60% coverage: 6:95/149 of query aligns to 596:693/728 of 3koxA

query
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active site: K617 (≠ V26)
binding cobalamin: E605 (≠ C15), H606 (= H16), S607 (≠ A17), V608 (= V18), G609 (= G19), A654 (≠ V60), S655 (= S61), I657 (= I63), S659 (≠ G65), G689 (= G91), G690 (= G92), T691 (≠ N93)

Sites not aligning to the query:

active site: 183, 218, 290
binding cobalamin: 112, 483, 707, 708, 710, 711
binding (2S)-2-amino-4-{[(1Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}butanoic acid: 77, 105, 108, 110, 156, 158, 183, 188, 218, 219, 290

3kowB Crystal structure of ornithine 4,5 aminomutase backsoaked complex (see paper)
36% identity, 60% coverage: 6:95/149 of query aligns to 596:693/728 of 3kowB

query
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active site: K617 (≠ V26)
binding cobalamin: E605 (≠ C15), H606 (= H16), S607 (≠ A17), V608 (= V18), G609 (= G19), L610 (vs. gap), I657 (= I63), G689 (= G91), G690 (= G92), T691 (≠ N93)

Sites not aligning to the query:

active site: 183, 218, 290
binding cobalamin: 707, 711
binding pyridoxal-5'-phosphate: 105, 110, 156, 158, 178, 183, 188, 218, 219

E3PY95 D-ornithine 4,5-aminomutase subunit beta; D-ornithine aminomutase E component; OAM-E; EC 5.4.3.5 from Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) (see 2 papers)
36% identity, 60% coverage: 6:95/149 of query aligns to 605:702/740 of E3PY95

query
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E3PY95

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EHS 614:616 (≠ CHA 15:17) binding
H615 (= H16) binding axial binding residue; mutation to G: Loss of corrinoid-binding ability.
K626 (≠ V26) modified: N6-(pyridoxal phosphate)lysine
STIISH 664:669 (≠ SSIYGH 61:66) binding

Sites not aligning to the query:

81 binding
182 binding

3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
25% identity, 69% coverage: 6:108/149 of query aligns to 99:200/576 of 3ivaA

query
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3ivaA

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active site: D107 (= D14), H109 (= H16), S160 (≠ D68)
binding cobalamin: H109 (= H16), G112 (= G19), V116 (≠ L23), G152 (≠ V59), L153 (≠ V60), S154 (= S61), L156 (≠ I63), I157 (≠ Y64), T158 (≠ G65), G183 (= G91), G184 (= G92)

Sites not aligning to the query:

binding cobalamin: 208, 209, 303, 443, 486, 488, 489, 495, 520, 521, 524, 527, 528
binding s-adenosyl-l-homocysteine: 447, 484, 485, 489, 491, 539

3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
25% identity, 69% coverage: 6:108/149 of query aligns to 99:200/577 of 3bulA

query
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3bulA

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active site: D107 (= D14), H109 (= H16), S160 (≠ D68)
binding cobalamin: H109 (= H16), V116 (≠ L23), G152 (≠ V59), L153 (≠ V60), S154 (= S61), L156 (≠ I63), I157 (≠ Y64), T158 (≠ G65), G183 (= G91), G184 (= G92)

Sites not aligning to the query:

binding cobalamin: 208, 209, 210, 213, 302, 443, 486, 487, 488, 489, 495, 498, 521, 524, 527, 528

P13009 Methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS; EC 2.1.1.13 from Escherichia coli (strain K12) (see 5 papers)
25% identity, 69% coverage: 6:108/149 of query aligns to 749:850/1227 of P13009

query
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P13009

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GDVHD 756:760 (≠ ADCHA 13:17) binding
D757 (= D14) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
H759 (= H16) binding axial binding residue; mutation to G: Loss of catalytic activity.
S804 (= S61) binding
T808 (≠ G65) binding
S810 (≠ D68) mutation to A: Decreases activity by about 40%.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
247 binding
310 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
311 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
694 binding
860 binding
946 binding
1134 binding
1189:1190 binding

1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
25% identity, 69% coverage: 6:108/149 of query aligns to 99:200/246 of 1bmtA

query
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active site: D107 (= D14), H109 (= H16), S160 (≠ D68)
binding co-methylcobalamin: D107 (= D14), V108 (≠ C15), H109 (= H16), D110 (≠ A17), I111 (≠ V18), I115 (≠ V22), G152 (≠ V59), L153 (≠ V60), S154 (= S61), L156 (≠ I63), I157 (≠ Y64), T158 (≠ G65), G183 (= G91), G184 (= G92), A185 (≠ N93)

Sites not aligning to the query:

binding co-methylcobalamin: 44, 48, 51, 55, 65, 68, 207, 209, 210

Query Sequence

>BWI76_RS08490 FitnessBrowser__Koxy:BWI76_RS08490
MKKSTLVIGVIGADCHAVGNKVLDRVFTAHDFRVINLGVMVSQDEYIDAAIETGADAIVV
SSIYGHGDIDCLGLRERCIERGIGDILLYVGGNLVVGKHDFADVEAKFKEMGFNRVFAPS
HDLEDVCQLMANDINQRHGVEQQCLEEAI

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