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Searching for up to 100 curated homologs for WP_011337253.1 NCBI__GCF_000015985.1:WP_011337253.1 (335 a.a.)

Found high-coverage hits (≥70%) to 27 curated proteins.

You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.

Hits with ≥ 30% identity

PGA1_c13370 Methionine synthase component, methyltransferase domain (EC:2.1.1.13) from Phaeobacter inhibens BS107
    69% identity, 97% coverage of query (465 bits)

DVU1585 Methionine synthase (cobalamin-dependent) (EC 2.1.1.13) from Desulfovibrio vulgaris Hildenborough JW710
    38% identity, 86% coverage of query (146 bits)

3bofA / Q9WYA5 Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
    33% identity, 87% coverage of query (141 bits)

Q9WYA5 methionine synthase (EC 2.1.1.13) from Thermotoga maritima (see paper)
    32% identity, 94% coverage of query (141 bits)

1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex)
    33% identity, 87% coverage of query (141 bits)

DvMF_0476 vitamin B12-dependent methionine synthase without a reactivation domain (EC 2.1.1.13) from Desulfovibrio vulgaris Miyazaki F
    33% identity, 85% coverage of query (133 bits)

8g3hA / A0A0A2XCD7 Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
    31% identity, 84% coverage of query (114 bits)

Build an alignment

Build an alignment for WP_011337253.1 and 7 homologs with ≥ 30% identity

Select sequences

Add sequences from UniProt, PDB, RefSeq, or MicrobesOnline (separate identifiers with commas or spaces):

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Change minimum %identity:

Additional hits (identity < 30%)

METH_RAT / Q9Z2Q4 Methionine synthase; MS; 5-methyltetrahydrofolate--homocysteine methyltransferase; Cobalamin-dependent methionine synthase; Vitamin-B12 dependent methionine synthase; EC 2.1.1.13 from Rattus norvegicus (Rat) (see 2 papers)
Q9Z2Q4 methionine synthase (EC 2.1.1.13) from Rattus norvegicus (see paper)
    28% identity, 91% coverage of query (108 bits)

metH / Q8NQD1 cobalamin-dependent methionine synthase (EC 2.1.1.13) from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
    30% identity, 87% coverage of query (105 bits)

MTR / Q99707 cobalamin-dependent methionine synthase (EC 2.1.1.13) from Homo sapiens (see 5 papers)
METH_HUMAN / 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 7 papers)
Q99707 methionine synthase (EC 2.1.1.13) from Homo sapiens (see paper)
    29% identity, 79% coverage of query (105 bits)

YITJ_BACSU / O06745 Bifunctional homocysteine S-methyltransferase/5,10-methylenetetrahydrofolate reductase; EC 2.1.1.10; EC 1.5.1.20 from Bacillus subtilis (strain 168) (see paper)
    28% identity, 85% coverage of query (96.7 bits)

MetH / b4019 cobalamin-dependent methionine synthase (EC 2.1.1.13) from Escherichia coli K-12 substr. MG1655 (see 60 papers)
metH / P13009 cobalamin-dependent methionine synthase (EC 2.1.1.13) from Escherichia coli (strain K12) (see 58 papers)
METH_ECOLI / P13009 Methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS; EC 2.1.1.13 from Escherichia coli (strain K12) (see 4 papers)
metH methionine synthase; EC 2.1.1.13 from Escherichia coli K12 (see 15 papers)
    31% identity, 77% coverage of query (96.7 bits)

4cczA / Q99707 Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
    27% identity, 79% coverage of query (80.9 bits)

1umyD / O09171 Bhmt from rat liver (see paper)
    27% identity, 76% coverage of query (73.9 bits)

Bhmt / O09171 betaine-homocysteine S-methyltransferase subunit (EC 2.1.1.5) from Rattus norvegicus (see paper)
BHMT1_RAT / O09171 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Rattus norvegicus (Rat) (see 3 papers)
O09171 homocysteine S-methyltransferase (EC 2.1.1.10); betaine-homocysteine S-methyltransferase (EC 2.1.1.5) from Rattus norvegicus (see 5 papers)
    27% identity, 76% coverage of query (73.2 bits)

YagD / b0261 CP4-6 prophage; homocysteine S-methyltransferase (EC 2.1.1.10) from Escherichia coli K-12 substr. MG1655 (see 8 papers)
mmuM / Q47690 CP4-6 prophage; homocysteine S-methyltransferase (EC 2.1.1.10) from Escherichia coli (strain K12) (see 5 papers)
MMUM_ECOLI / Q47690 Homocysteine S-methyltransferase; S-methylmethionine:homocysteine methyltransferase; EC 2.1.1.10 from Escherichia coli (strain K12) (see 2 papers)
Q47690 homocysteine S-methyltransferase (EC 2.1.1.10); selenocysteine Se-methyltransferase (EC 2.1.1.280) from Escherichia coli (see 3 papers)
    31% identity, 87% coverage of query (72.4 bits)

O35490 betaine-homocysteine S-methyltransferase (EC 2.1.1.5) from Mus musculus (see paper)
    27% identity, 76% coverage of query (68.6 bits)

5dmmA / Q47690 Crystal structure of the homocysteine methyltransferase mmum from escherichia coli, metallated form (see paper)
    31% identity, 86% coverage of query (68.2 bits)

1lt8A Reduced homo sapiens betaine-homocysteine s-methyltransferase in complex with s-(delta-carboxybutyl)-l-homocysteine
    26% identity, 76% coverage of query (68.2 bits)

BHMT / Q93088 betaine--homocysteine S-methyltransferase 1 (EC 2.1.1.5) from Homo sapiens (see 7 papers)
BHMT1_HUMAN / Q93088 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Homo sapiens (Human) (see 5 papers)
Q93088 betaine-homocysteine S-methyltransferase (EC 2.1.1.5) from Homo sapiens (see 8 papers)
    26% identity, 76% coverage of query (67.4 bits)

BHMT2 / Q9H2M3 S-methylmethionine--homocysteine S-methyltransferase (EC 2.1.1.10) from Homo sapiens (see 4 papers)
BHMT2_HUMAN / Q9H2M3 S-methylmethionine--homocysteine S-methyltransferase BHMT2; SMM-hcy methyltransferase; Betaine--homocysteine S-methyltransferase 2; EC 2.1.1.10 from Homo sapiens (Human) (see 2 papers)
    26% identity, 84% coverage of query (65.5 bits)

4m3pA Betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine
    25% identity, 76% coverage of query (62.0 bits)

HMT3 / Q8LAX0 homocysteine S-methyltransferase 3 (EC 2.1.1.10) from Arabidopsis thaliana (see 2 papers)
HMT3_ARATH / Q8LAX0 Homocysteine S-methyltransferase 3; S-methylmethionine:homocysteine methyltransferase 3; AtHMT-3; SMM:Hcy S-methyltransferase 3; EC 2.1.1.10 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
Q8LAX0 homocysteine S-methyltransferase (EC 2.1.1.10) from Arabidopsis thaliana (see paper)
    25% identity, 89% coverage of query (58.9 bits)

HMT_BACSU / O31463 Homocysteine S-methyltransferase YbgG; S-methylmethionine:homocysteine methyltransferase; EC 2.1.1.10 from Bacillus subtilis (strain 168) (see paper)
    28% identity, 86% coverage of query (56.6 bits)

SAM4_YEAST / Q08985 Homocysteine S-methyltransferase 2; S-adenosylmethionine metabolism protein 4; S-methylmethionine:homocysteine methyltransferase 2; SMM:Hcy S-methyltransferase 2; EC 2.1.1.10 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
    23% identity, 84% coverage of query (54.3 bits)

BHMT2_MOUSE / Q91WS4 S-methylmethionine--homocysteine S-methyltransferase BHMT2; SMM-hcy methyltransferase; Betaine--homocysteine S-methyltransferase 2; EC 2.1.1.10 from Mus musculus (Mouse) (see 2 papers)
    25% identity, 76% coverage of query (51.2 bits)

HMT1 / Q9SDL7 homocysteine S-methyltransferase 1 (EC 2.1.1.10) from Arabidopsis thaliana (see 2 papers)
HMT1_ARATH / Q9SDL7 Homocysteine S-methyltransferase 1; S-methylmethionine:homocysteine methyltransferase 1; AtHMT-1; SMM:Hcy S-methyltransferase 1; EC 2.1.1.10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
Q9SDL7 homocysteine S-methyltransferase (EC 2.1.1.10) from Arabidopsis thaliana (see paper)
    24% identity, 84% coverage of query (50.8 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory