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Conserved domains on  [gi|1967468217|ref|NP_001378930|]
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kynurenine formamidase isoform 5 [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11429202)

alpha/beta hydrolase catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
77-151 1.39e-15

Acetyl esterase/lipase [Lipid transport and metabolism];


:

Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 71.06  E-value: 1.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1967468217  77 DIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQ-GVAVVIVAYGIAPKGTLDHMVDQVTRSVAFVQKR 151
Cdd:COG0657     2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARaGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
77-151 1.39e-15

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 71.06  E-value: 1.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1967468217  77 DIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQ-GVAVVIVAYGIAPKGTLDHMVDQVTRSVAFVQKR 151
Cdd:COG0657     2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARaGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 77-126 3.58e-04

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 39.47  E-value: 3.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1967468217  77 DIYFPDESSEALPFFLFFHGGYWQSGSK----DESAFMVHPLTAQGVAVVIVAY 126
Cdd:pfam20434   2 DIYLPKNAKGPYPVVIWIHGGGWNSGDKeadmGFMTNTVKALLKAGYAVASINY 55
 
Name Accession Description Interval E-value
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
77-151 1.39e-15

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 71.06  E-value: 1.39e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1967468217  77 DIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQ-GVAVVIVAYGIAPKGTLDHMVDQVTRSVAFVQKR 151
Cdd:COG0657     2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARaGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRAN 77
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 77-126 3.58e-04

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 39.47  E-value: 3.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1967468217  77 DIYFPDESSEALPFFLFFHGGYWQSGSK----DESAFMVHPLTAQGVAVVIVAY 126
Cdd:pfam20434   2 DIYLPKNAKGPYPVVIWIHGGGWNSGDKeadmGFMTNTVKALLKAGYAVASINY 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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