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Searching for up to 100 curated homologs for 8499412 FitnessBrowser__Miya:8499412 (283 a.a.)

Found high-coverage hits (≥70%) to 23 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

Q4J6I8 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) from Sulfolobus acidocaldarius (see paper)
    42% identity, 93% coverage of query (223 bits)

OFOB_SACSO / A0A0E3KBH3 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11 from Saccharolobus solfataricus (Sulfolobus solfataricus) (see paper)
    45% identity, 83% coverage of query (217 bits)

Q8RJQ9 2-oxoglutarate synthase (subunit 1/2) (EC 1.2.7.3) from Thauera aromatica (see paper)
    46% identity, 89% coverage of query (213 bits)

OFOB2_SULTO / Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see paper)
Q96XT4 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) from Sulfurisphaera tokodaii (see paper)
    40% identity, 93% coverage of query (206 bits)

5b46B / Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2 from sulfolobus tokodai - ligand free form (see paper)
    40% identity, 93% coverage of query (206 bits)

korB / Q9AJL9 2-oxoglutarate ferredoxin oxidoreductase β subunit (EC 1.2.7.3) from Hydrogenobacter thermophilus (see paper)
Q9AJL9 2-oxoglutarate synthase (subunit 1/2) (EC 1.2.7.3) from Hydrogenobacter thermophilus (see 3 papers)
    39% identity, 88% coverage of query (206 bits)

P72579 2-oxoacid:ferredoxin oxidoreductase β subunit (EC 1.2.7.11; EC 1.2.7.1; EC 1.2.7.3; EC 1.2.7.7) from Sulfolobus sp. (see 2 papers)
OFOB_SULSP / P72579 2-oxoacid:ferredoxin oxidoreductase subunit beta; OFOR; EC 1.2.7.11 from Sulfolobus sp. (see 3 papers)
P72579 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) from Sulfolobus sp. (see 2 papers)
    44% identity, 83% coverage of query (202 bits)

OFOB1_SULTO / Q96Y68 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11 from Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii) (see 2 papers)
Q96Y68 2-oxoacid oxidoreductase (ferredoxin) (subunit 1/2) (EC 1.2.7.11) from Sulfurisphaera tokodaii (see paper)
    44% identity, 83% coverage of query (202 bits)

A0L8G5 2-oxoglutarate synthase (subunit 1/2) (EC 1.2.7.3) from Magnetococcus marinus (see paper)
    35% identity, 95% coverage of query (200 bits)

6n2nB / A0L8G5 Crystal structure of 2-oxoglutarate:ferredoxin oxidoreductase from magnetococcus marinus (see paper)
    35% identity, 95% coverage of query (200 bits)

6n2oD 2-oxoglutarate:ferredoxin oxidoreductase from magnetococcus marinus with 2-oxoglutarate, coenzyme a and succinyl-coa bound
    35% identity, 95% coverage of query (200 bits)

6n2oB 2-oxoglutarate:ferredoxin oxidoreductase from magnetococcus marinus with 2-oxoglutarate, coenzyme a and succinyl-coa bound
    35% identity, 95% coverage of query (200 bits)

korB / B0R3F9 2-oxoglutarate--ferredoxin oxidoreductase β subunit (EC 1.2.7.3) from Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) (see 2 papers)
    45% identity, 74% coverage of query (199 bits)

OFOB1_AERPE / Q9YA11 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta; OFOR1; EC 1.2.7.11 from Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) (see paper)
    46% identity, 83% coverage of query (198 bits)

OFOB2_AERPE / Q9YBX8 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta; OFOR2; EC 1.2.7.11 from Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) (see paper)
    39% identity, 94% coverage of query (197 bits)

5b48B / Q96Y68 2-oxoacid:ferredoxin oxidoreductase 1 from sulfolobus tokodai (see paper)
    40% identity, 92% coverage of query (189 bits)

5b47B / Q96XT4 2-oxoacid:ferredoxin oxidoreductase 2 from sulfolobus tokodai - pyruvate complex (see paper)
    37% identity, 93% coverage of query (169 bits)

korB / O53181 2-oxoglutarate:ferredoxin oxidoreductase β subunit (EC 1.2.7.3) from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
KORB_MYCTU / O53181 2-oxoglutarate oxidoreductase subunit KorB; Alpha-ketoglutarate oxidoreductase subunit beta; KG oxidoreductase subunit beta; KGO subunit beta; KOR subunit beta; EC 1.2.7.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
    37% identity, 73% coverage of query (168 bits)

porB / B0R4X5 pyruvate—ferredoxin oxidoreductase β subunit (EC 1.2.7.1) from Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1) (see 10 papers)
    38% identity, 91% coverage of query (167 bits)

oorB / O25312 2-oxoglutarate-acceptor oxidoreductase subunit OorB (EC 1.2.7.3) from Helicobacter pylori (strain ATCC 700392 / 26695) (see 2 papers)
    33% identity, 93% coverage of query (144 bits)

Build an alignment

Build an alignment for 8499412 and 20 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%)

korB / Q6LXN3 2-oxoglutarate ferredoxin oxidoreductase β subunit (EC 1.2.7.3) from Methanococcus maripaludis (strain S2 / LL) (see 2 papers)
    29% identity, 88% coverage of query (119 bits)

VORA_METTM / P80907 Ketoisovalerate oxidoreductase subunit VorA; VOR; 2-oxoisovalerate oxidoreductase alpha chain; 2-oxoisovalerate-ferredoxin oxidoreductase subunit alpha; EC 1.-.-.- from Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) (see paper)
    24% identity, 74% coverage of query (70.1 bits)

Q93RA2 2-oxoglutarate synthase (subunit 1/2) (EC 1.2.7.3) from Hydrogenobacter thermophilus (see paper)
D3DIA2 2-oxoglutarate synthase (subunit 4/5) (EC 1.2.7.3) from Hydrogenobacter thermophilus (see 2 papers)
    24% identity, 80% coverage of query (57.0 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory