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Conserved domains on  [gi|514061882|ref|WP_016528193|]
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serine dehydratase beta chain [Glaesserella parasuis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SDH_alpha super family cl27283
Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
 2-45 1.34e-20

Serine dehydratase alpha chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.


The actual alignment was detected with superfamily member TIGR00720:

Pssm-ID: 452735 [Multi-domain]  Cd Length: 450  Bit Score: 81.62  E-value: 1.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 514061882    2 ISVFDMFKVGIGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:TIGR00720   1 ISVFDLFKIGIGPSSSHTVGPMRAAKQFADDLRDKGLLEQTTRV 44
 
Name Accession Description Interval E-value
sda_mono TIGR00720
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called ...
 2-45 1.34e-20

L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273233 [Multi-domain]  Cd Length: 450  Bit Score: 81.62  E-value: 1.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 514061882    2 ISVFDMFKVGIGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:TIGR00720   1 ISVFDLFKIGIGPSSSHTVGPMRAAKQFADDLRDKGLLEQTTRV 44
PRK15040 PRK15040
L-serine ammonia-lyase;
1-45 4.53e-17

L-serine ammonia-lyase;


Pssm-ID: 185000 [Multi-domain]  Cd Length: 454  Bit Score: 72.00  E-value: 4.53e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 514061882   1 MISVFDMFKVGIGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:PRK15040   1 MISAFDIFKIGIGPSSSHTVGPMNAGKSFIDRLESSGLLTATSHI 45
SDH_beta pfam03315
Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
 12-45 4.69e-14

Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.


Pssm-ID: 427239 [Multi-domain]  Cd Length: 146  Bit Score: 60.88  E-value: 4.69e-14
                          10        20        30
                  ....*....|....*....|....*....|....
gi 514061882   12 IGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:pfam03315   1 IGPSSSHTVGPMRAAARFLDELREKGLLDRVARV 34
 
Name Accession Description Interval E-value
sda_mono TIGR00720
L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called ...
 2-45 1.34e-20

L-serine dehydratase, iron-sulfur-dependent, single chain form; This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273233 [Multi-domain]  Cd Length: 450  Bit Score: 81.62  E-value: 1.34e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 514061882    2 ISVFDMFKVGIGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:TIGR00720   1 ISVFDLFKIGIGPSSSHTVGPMRAAKQFADDLRDKGLLEQTTRV 44
PRK15040 PRK15040
L-serine ammonia-lyase;
1-45 4.53e-17

L-serine ammonia-lyase;


Pssm-ID: 185000 [Multi-domain]  Cd Length: 454  Bit Score: 72.00  E-value: 4.53e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 514061882   1 MISVFDMFKVGIGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:PRK15040   1 MISAFDIFKIGIGPSSSHTVGPMNAGKSFIDRLESSGLLTATSHI 45
PRK15023 PRK15023
L-serine deaminase; Provisional
 1-35 5.13e-15

L-serine deaminase; Provisional


Pssm-ID: 184984 [Multi-domain]  Cd Length: 454  Bit Score: 65.86  E-value: 5.13e-15
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 514061882   1 MISVFDMFKVGIGPSSSYTVGPMKAGKEFIDHLID 35
Cdd:PRK15023   1 MISLFDMFKVGIGPSSSHTVGPMKAGKQFVDDLVE 35
SDH_beta pfam03315
Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer ...
 12-45 4.69e-14

Serine dehydratase beta chain; L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyzes the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway.


Pssm-ID: 427239 [Multi-domain]  Cd Length: 146  Bit Score: 60.88  E-value: 4.69e-14
                          10        20        30
                  ....*....|....*....|....*....|....
gi 514061882   12 IGPSSSYTVGPMKAGKEFIDHLIDCKKLAETDRL 45
Cdd:pfam03315   1 IGPSSSHTVGPMRAAARFLDELREKGLLDRVARV 34
 
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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