Family Search for PF05853 (BKACE)

PF05853 hits 45 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

PS417_07250 2-deoxy-3-keto-D-ribonoate cleavage enzyme from Pseudomonas simiae WCS417
Aligns to 6:302 / 310 (95.8%), covers 100.0% of PF05853, 372.7 bits

• mutant phenotype: # Specifically important in carbon source 2-Deoxy-D-Ribose; carbon source 2-Deoxy-D-ribonic acid lithium salt; this is a beta keto acid cleavage enzyme, see PMID:24240508

kce / Q8RHX2 3-keto,5-aminohexanoate cleavage enzyme subunit (EC 2.3.1.247) from Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) (see 2 papers)
KCE_FUSNN / Q8RHX2 3-keto-5-aminohexanoate cleavage enzyme; EC 2.3.1.247 from Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) (see 2 papers)
Q8RHX2 3-keto-5-aminohexanoate cleavage enzyme (EC 2.3.1.247) from Fusobacterium nucleatum subsp. nucleatum (see 2 papers)
Aligns to 4:270 / 272 (98.2%), covers 100.0% of PF05853, 369.6 bits

• function: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety. It can also use beta-alanyl-CoA as substrate.
  catalytic activity: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = (3S)-3- aminobutanoyl-CoA + acetoacetate (RHEA:31555)
  cofactor: Zn(2+)
  subunit: Homotetramer.

H281DRAFT_00641 2-deoxy-3-keto-D-ribonate cleavage enzyme from Paraburkholderia bryophila 376MFSha3.1
Aligns to 7:304 / 312 (95.5%), covers 100.0% of PF05853, 361.1 bits

• mutant phenotype: Important for utilization of deoxyribose and deoxyribonate. This is expected to be the next step after the oxidation of deoxyribonate. It would release glyceryl-CoA and acetoacetate.

DOHCE_PARG4 / B1G5Y9 3,5-dioxohexanoate:acetyl-CoA acetone transferase; 3,5-dioxohexanoate cleavage enzyme; BKACE_274; EC 2.3.1.319 from Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M) (see paper)
Aligns to 6:302 / 310 (95.8%), covers 100.0% of PF05853, 360.3 bits

• function: Catalyzes the condensation of 3,5-dioxohexanoate and acetyl- CoA, forming acetoacetate and acetoacetyl-CoA (PubMed:24240508). May be involved in fatty acid biosynthesis rescue via triacetic acid lactone (PubMed:24240508).
  catalytic activity: 3,5-dioxohexanoate + acetyl-CoA = acetoacetyl-CoA + acetoacetate (RHEA:79655)
  cofactor: Zn(2+)

KCE_CLOAI / B0VHH0 3-keto-5-aminohexanoate cleavage enzyme; EC 2.3.1.247 from Cloacimonas acidaminovorans (strain Evry) (see paper)
B0VHH0 3-keto-5-aminohexanoate cleavage enzyme (EC 2.3.1.247) from Candidatus Cloacimonas acidaminovorans (see paper)
Aligns to 3:274 / 276 (98.6%), covers 100.0% of PF05853, 349.7 bits

• function: Involved in the anaerobic fermentation of lysine. Catalyzes the reversible reaction between 3-keto-5-aminohexanoate (KAH) and acetyl-CoA to form 3-aminobutyryl-CoA and acetoacetate. The reaction involves the deprotonation of KAH, the nucleophilic addition onto acetyl-CoA and the intramolecular transfer of the CoA moiety.
  catalytic activity: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = (3S)-3- aminobutanoyl-CoA + acetoacetate (RHEA:31555)
  cofactor: Zn(2+)
  subunit: Homotetramer.

DHCCE_RHIME / Q92NF6 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase; 3-dehydrocarnitine cleavage enzyme; EC 2.3.1.317 from Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) (see paper)
Aligns to 8:297 / 300 (96.7%), covers 99.6% of PF05853, 331.8 bits

• function: Catalyzes the condensation of dehydrocarnitine and acetyl- CoA, forming acetoacetate and betainyl-CoA (N,N,N-trimethylglycyl-CoA) (PubMed:30670548). Is involved in a L-carnitine degradation pathway that allows R.meliloti to grow on L-carnitine as the sole source of carbon and nitrogen (PubMed:30670548).
  catalytic activity: 3-dehydrocarnitine + acetyl-CoA = N,N,N-trimethylglycyl-CoA + acetoacetate (RHEA:47044)
  cofactor: Zn(2+)
  subunit: Homotetramer.
  disruption phenotype: Disruption of the gene in strain Rm2011 abolishes growth on gamma-butyrobetaine (GBB).

Pf6N2E2_4692 dehydrocarnitine cleavage enzyme (EC 2.3.1.-) from Pseudomonas fluorescens FW300-N2E2
Aligns to 4:291 / 295 (97.6%), covers 99.6% of PF05853, 330.1 bits

• mutant phenotype: Specifically important for: Carnitine Hydrochloride. Similar to CdhC = PA5387

cdhC / Q9HTH7 3-dehydrocarnitine cleavage enzyme from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
DHCCE_PSEAE / Q9HTH7 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase; 3-dehydrocarnitine cleavage enzyme; EC 2.3.1.317 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
Aligns to 4:291 / 294 (98.0%), covers 99.6% of PF05853, 327.8 bits

• function: Catalyzes the condensation of dehydrocarnitine and acetyl- CoA, forming acetoacetate and betainyl-CoA (N,N,N-trimethylglycyl-CoA) (PubMed:24240508). Is involved in a L-carnitine degradation pathway that allows P.aeruginosa to grow on L-carnitine as the sole source of carbon and nitrogen (PubMed:19406895).
  catalytic activity: 3-dehydrocarnitine + acetyl-CoA = N,N,N-trimethylglycyl-CoA + acetoacetate (RHEA:47044)
  cofactor: Zn(2+)
  disruption phenotype: Cells are incapable of growth on carnitine.

3OXCE_CUPNH / Q0KAA1 3-oxoadipate:acetyl-CoA acetyltransferase; 3-oxoadipate cleavage enzyme; BKACE_378; EC 2.3.1.318 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see paper)
Aligns to 4:273 / 284 (95.1%), covers 100.0% of PF05853, 315.1 bits

• function: Catalyzes the condensation of 3-oxoadipate (beta-ketoadipate) and acetyl-CoA, forming acetoacetate and succinyl-CoA (PubMed:24240508). Is likely involved is the degradation of 3- oxoadipate through an alternative pathway, within catechol degradation (PubMed:24240508).
  catalytic activity: 3-oxoadipate + acetyl-CoA = acetoacetate + succinyl-CoA (RHEA:79651)
  cofactor: Zn(2+)

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