NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1754852476|gb|KAB0541839|]
View 

class II poly(R)-hydroxyalkanoic acid synthase, partial [Pseudomonas palleroniana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PhaC_N super family cl37752
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ...
 1-137 8.88e-76

Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain.


The actual alignment was detected with superfamily member pfam07167:

Pssm-ID: 462110 [Multi-domain]  Cd Length: 173  Bit Score: 223.29  E-value: 8.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754852476   1 WIDES-TMSQDDRARAHFAFALLNDAVSPSNTLL-NPLAVKELFNSGGTSLVRGLSHLVDDLLHNDG--LPRQVTPHAFE 76
Cdd:pfam07167  33 WVDEVeGLDPKTRARAEFFTRQLIDALAPSNFLAtNPEALKETFESGGESLVRGLENLLEDLERGGGdlKISQTDESAFE 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1754852476  77 VGKTLATTPGAVVFRNELLELIQYRSMSEKQYAKPLLIVPPQINKFYIFDLSPSNSFVQYA 137
Cdd:pfam07167 113 VGKNLATTPGKVVFRNELMELIQYKPTTEKVHKRPLLIVPPWINKFYILDLSPQNSLVRWA 173
 
Name Accession Description Interval E-value
PhaC_N pfam07167
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ...
 1-137 8.88e-76

Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain.


Pssm-ID: 462110 [Multi-domain]  Cd Length: 173  Bit Score: 223.29  E-value: 8.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754852476   1 WIDES-TMSQDDRARAHFAFALLNDAVSPSNTLL-NPLAVKELFNSGGTSLVRGLSHLVDDLLHNDG--LPRQVTPHAFE 76
Cdd:pfam07167  33 WVDEVeGLDPKTRARAEFFTRQLIDALAPSNFLAtNPEALKETFESGGESLVRGLENLLEDLERGGGdlKISQTDESAFE 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1754852476  77 VGKTLATTPGAVVFRNELLELIQYRSMSEKQYAKPLLIVPPQINKFYIFDLSPSNSFVQYA 137
Cdd:pfam07167 113 VGKNLATTPGKVVFRNELMELIQYKPTTEKVHKRPLLIVPPWINKFYILDLSPQNSLVRWA 173
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
1-153 3.93e-64

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 204.80  E-value: 3.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754852476   1 WIDESTMSQDDRARAHFAFALLNDAVSPSNTLL-NPLAVKELFNSGGTSLVRGLSHLVDDLLHndGLPRQVTPHAFEVGK 79
Cdd:COG3243    96 VADVEGLDPKTRRRVRFYTRQILDAMSPSNFLAtNPEALKETLETGGESLVRGLENLLEDLER--GAISQTDESAFEVGE 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1754852476  80 TLATTPGAVVFRNELLELIQYRSMSEKQYAKPLLIVPPQINKFYIFDLSPSNSFVQYALKNGLQVFILSRRNPD 153
Cdd:COG3243   174 NVATTPGKVVYRNDLMELIQYAPTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWGNPD 247
PRK07239 PRK07239
bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated
 45-105 3.88e-03

bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated


Pssm-ID: 235981 [Multi-domain]  Cd Length: 381  Bit Score: 36.50  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1754852476  45 GGTSLVRGLSHLVDdllhndGLPRQVTPHAFEVGKTLATTPGAVVFRNELLELIQYRSMSE 105
Cdd:PRK07239  288 GHVLEIRGHAVVVD------GEVKPLSPAPMALLRALAARPGRVVSREDLLAALPGGGTDE 342
 
Name Accession Description Interval E-value
PhaC_N pfam07167
Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal ...
 1-137 8.88e-76

Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; This family represents the N-terminal region of the bacterial poly-beta-hydroxybutyrate polymerase (PhaC). Polyhydroxyalkanoic acids (PHAs) are carbon and energy reserve polymers produced in some bacteria when carbon sources are plentiful and another nutrient, such as nitrogen, phosphate, oxygen, or sulfur, becomes limiting. PHAs composed of monomeric units ranging from 3 to 14 carbons exist in nature. When the carbon source is exhausted, PHA is utilized by the bacterium. PhaC links D-(-)-3-hydroxybutyrl-CoA to an existing PHA molecule by the formation of an ester bond. This family appears to be a partial segment of an alpha/beta hydrolase domain.


Pssm-ID: 462110 [Multi-domain]  Cd Length: 173  Bit Score: 223.29  E-value: 8.88e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754852476   1 WIDES-TMSQDDRARAHFAFALLNDAVSPSNTLL-NPLAVKELFNSGGTSLVRGLSHLVDDLLHNDG--LPRQVTPHAFE 76
Cdd:pfam07167  33 WVDEVeGLDPKTRARAEFFTRQLIDALAPSNFLAtNPEALKETFESGGESLVRGLENLLEDLERGGGdlKISQTDESAFE 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1754852476  77 VGKTLATTPGAVVFRNELLELIQYRSMSEKQYAKPLLIVPPQINKFYIFDLSPSNSFVQYA 137
Cdd:pfam07167 113 VGKNLATTPGKVVFRNELMELIQYKPTTEKVHKRPLLIVPPWINKFYILDLSPQNSLVRWA 173
PhaC COG3243
Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];
1-153 3.93e-64

Poly-beta-hydroxybutyrate synthase [Lipid transport and metabolism];


Pssm-ID: 442475 [Multi-domain]  Cd Length: 545  Bit Score: 204.80  E-value: 3.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754852476   1 WIDESTMSQDDRARAHFAFALLNDAVSPSNTLL-NPLAVKELFNSGGTSLVRGLSHLVDDLLHndGLPRQVTPHAFEVGK 79
Cdd:COG3243    96 VADVEGLDPKTRRRVRFYTRQILDAMSPSNFLAtNPEALKETLETGGESLVRGLENLLEDLER--GAISQTDESAFEVGE 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1754852476  80 TLATTPGAVVFRNELLELIQYRSMSEKQYAKPLLIVPPQINKFYIFDLSPSNSFVQYALKNGLQVFILSRRNPD 153
Cdd:COG3243   174 NVATTPGKVVYRNDLMELIQYAPTTEKVHKTPLLIVPPWINKYYILDLQPGNSLVRYLVDQGFTVFLISWGNPD 247
PRK07239 PRK07239
bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated
 45-105 3.88e-03

bifunctional uroporphyrinogen-III synthetase/response regulator domain protein; Validated


Pssm-ID: 235981 [Multi-domain]  Cd Length: 381  Bit Score: 36.50  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1754852476  45 GGTSLVRGLSHLVDdllhndGLPRQVTPHAFEVGKTLATTPGAVVFRNELLELIQYRSMSE 105
Cdd:PRK07239  288 GHVLEIRGHAVVVD------GEVKPLSPAPMALLRALAARPGRVVSREDLLAALPGGGTDE 342
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH