Searching for up to 100 curated homologs for AO356_28780 FitnessBrowser__pseudo5_N2C3_1:AO356_28780 (296 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.
Q9I562 (S)-citramalyl-CoA lyase (EC 4.1.3.25) from Pseudomonas aeruginosa (see paper)
39% identity, 92% coverage of query (140 bits)
A0A172MLA1 (S)-citramalyl-CoA lyase (EC 4.1.3.25); (R)-citramalyl-CoA lyase (EC 4.1.3.46) from Aspergillus terreus (see paper)
33% identity, 97% coverage of query (127 bits)
CITEL_DEIRA / Q9RUZ0 Citrate lyase subunit beta-like protein; EC 4.1.-.- from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
34% identity, 90% coverage of query (122 bits)
1sgjA / Q9RUZ0 Crystal structure of citrate lyase beta subunit
34% identity, 76% coverage of query (113 bits)
1sgjB Crystal structure of citrate lyase beta subunit
34% identity, 76% coverage of query (113 bits)
Build an alignment for AO356_28780 and 5 homologs with ≥ 30% identity
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mclA / P71503 malyl coenzyme A lyase subunit (EC 4.1.3.24) from Methylorubrum extorquens (see paper)
C5B113 malyl-CoA lyase (EC 4.1.3.24) from Methylorubrum extorquens (see paper)
29% identity, 91% coverage of query (105 bits)
5ugrA / C5B113 Malyl-coa lyase from methylobacterium extorquens (see paper)
29% identity, 91% coverage of query (105 bits)
CLYBL / Q8N0X4 malate/β-methylmalate synthase (EC 2.3.3.9) from Homo sapiens (see 3 papers)
CLYBL_HUMAN / Q8N0X4 Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9 from Homo sapiens (Human) (see 3 papers)
Q8N0X4 citrate (pro-3S)-lyase (EC 4.1.3.6) from Homo sapiens (see paper)
28% identity, 91% coverage of query (104 bits)
5vxcA / Q8N0X4 Crystal structure analysis of human clybl in complex with free coash (see paper)
28% identity, 91% coverage of query (104 bits)
5vxoA Crystal structure analysis of human clybl in complex with propionyl- coa
28% identity, 91% coverage of query (104 bits)
6aq4C Crystal structure of protein cite from mycobacterium tuberculosis in complex with magnesium, pyruvate and citramalyl-coa
34% identity, 90% coverage of query (104 bits)
6as5A Crystal structure of protein cite from mycobacterium tuberculosis in complex with magnesium, acetoacetate and coenzyme a
34% identity, 90% coverage of query (104 bits)
6aq4B / P9WPE1 Crystal structure of protein cite from mycobacterium tuberculosis in complex with magnesium, pyruvate and citramalyl-coa (see paper)
34% identity, 90% coverage of query (103 bits)
CITEL_MYCTU / P9WPE1 Citrate lyase subunit beta-like protein; EC 4.1.-.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 90% coverage of query (103 bits)
6arbA Crystal structure of protein cite from mycobacterium tuberculosis in complex with magnesium, pyruvate and coenzyme a
34% identity, 90% coverage of query (103 bits)
MCTE_CERS4 / D3JV05 (3S)-malyl-CoA thioesterase; (3S)-malyl-CoA thiolesterase; EC 3.1.2.30 from Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides) (see paper)
D3JV05 (3S)-malyl-CoA thioesterase (EC 3.1.2.30) from Cereibacter sphaeroides (see paper)
30% identity, 86% coverage of query (100 bits)
CLYBL_MOUSE / Q8R4N0 Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein, mitochondrial; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9 from Mus musculus (Mouse) (see 4 papers)
Q8R4N0 citrate (pro-3S)-lyase (EC 4.1.3.6) from Mus musculus (see paper)
28% identity, 91% coverage of query (100 bits)
Q037K5 citrate (pro-3S)-lyase (EC 4.1.3.6) from Lacticaseibacillus casei (see paper)
29% identity, 92% coverage of query (93.2 bits)
mcl1 / B6E2X2 malyl-CoA lyase subunit (EC 4.1.3.24) from Rhodobacter capsulatus (see 2 papers)
MCAL_RHOCA / B6E2X2 L-malyl-CoA/beta-methylmalyl-CoA lyase; (3S)-malyl-CoA/beta-methylmalyl-CoA lyase; EC 4.1.3.24 from Rhodobacter capsulatus (Rhodopseudomonas capsulata) (see paper)
28% identity, 96% coverage of query (92.8 bits)
MCAL_CERS4 / Q3J5L6 L-malyl-CoA/beta-methylmalyl-CoA lyase; (3S)-malyl-CoA/beta-methylmalyl-CoA lyase; (S)-citramalyl-CoA lyase; EC 4.1.3.24; EC 4.1.3.25 from Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides) (see 2 papers)
Q3J5L6 malyl-CoA lyase (EC 4.1.3.24) from Cereibacter sphaeroides (see 2 papers)
29% identity, 91% coverage of query (90.9 bits)
4l9yC / Q3J5L6 Crystal structure of rhodobacter sphaeroides malyl-coa lyase in complex with magnesium, glyoxylate, and propionyl-coa (see paper)
29% identity, 91% coverage of query (90.9 bits)
4l9zA Crystal structure of rhodobacter sphaeroides malyl-coa lyase in complex with magnesium, oxalate, and coa
29% identity, 91% coverage of query (90.9 bits)
4l9yA Crystal structure of rhodobacter sphaeroides malyl-coa lyase in complex with magnesium, glyoxylate, and propionyl-coa
29% identity, 91% coverage of query (90.9 bits)
PGA1_c03680 (3S)-malyl-CoA thioesterase [EC:3.1.2.30] from Phaeobacter inhibens BS107
28% identity, 95% coverage of query (84.7 bits)
PGA1_c30490 Malyl-CoA lyase (EC 4.1.3.24) from Phaeobacter inhibens BS107
27% identity, 92% coverage of query (80.9 bits)
citE / P17725 citrate lyase β subunit (EC 4.1.3.34) from Klebsiella pneumoniae (see 2 papers)
citE / CAA56216.1 citrate lyase beta-subunit from Klebsiella pneumoniae (see paper)
26% identity, 90% coverage of query (77.0 bits)
YbdW / b0616 citrate lyase β subunit from Escherichia coli K-12 substr. MG1655 (see 2 papers)
CITE_ECOLI / P0A9I1 Citrate lyase subunit beta; Citrase beta chain; Citrate (pro-3S)-lyase subunit beta; Citryl-CoA lyase subunit; EC 4.1.3.6; EC 4.1.3.34 from Escherichia coli (strain K12) (see paper)
25% identity, 93% coverage of query (75.5 bits)
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Lawrence Berkeley National Laboratory