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Conserved domains on  [gi|90111355|ref|NP_416429|]
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D-cysteine desulfhydrase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

D-cysteine desulfhydrase family protein( domain architecture ID 10012093)

D-cysteine desulfhydrase family protein such as D-cysteine desulfhydrase, which catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives.

EC:  4.4.1.-
Gene Ontology:  GO:0030170|GO:0016846

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-328 0e+00

D-cysteine desulfhydrase; Validated


:

Pssm-ID: 179673  Cd Length: 331  Bit Score: 571.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    4 HNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   84 TAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  164 LGALGYVESALEIAQQC-EGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKEL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  243 ELT---ASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 90111355  320 ALFAYHPHV 328
Cdd:PRK03910 321 ALFAYADAF 329
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-328 0e+00

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 571.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    4 HNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   84 TAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  164 LGALGYVESALEIAQQC-EGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKEL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  243 ELT---ASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 90111355  320 ALFAYHPHV 328
Cdd:PRK03910 321 ALFAYADAF 329
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 12-328 0e+00

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 555.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    12 LEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    92 GLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQ--IEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAEtrIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   170 VESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASAE 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111355   250 ILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEgPILFIHTGGAPALFAYHPHV 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 1.14e-158

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 445.71  E-value: 1.14e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  19 TPLEYLPRFSDYLG--REIFIKRDDVTPM-AMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHC 95
Cdd:cd06449   1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSGlAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  96 VALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDAL--TDPNAQLEELATRVEAQGFRPYVIPVGGS-NALGALGYVES 172
Cdd:cd06449  81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 173 ALEIAQQCEGA-VNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQA-IAKELELTASAEI 250
Cdd:cd06449 161 VLEIAQQEEELgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAkLAEEGLEVKEEDV 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111355 251 LLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGG 317
Cdd:cd06449 241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 8-326 2.74e-154

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];


Pssm-ID: 442005 [Multi-domain]  Cd Length: 317  Bit Score: 434.99  E-value: 2.74e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   8 RFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAV 87
Cdd:COG2515   1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  88 AAKLGLHCVALLENPigttaENYLTNGNRLLLDLFNTQIEMCDALT--DPNAQLEELATRVEAQGFRPYVIPVGGSNALG 165
Cdd:COG2515  81 AAKLGLKCVLVLRGE-----EPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 166 ALGYVESALEIAQQC-EGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELEL 244
Cdd:COG2515 156 ALGYVEAAAELAAQLaELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 245 TASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAY 324
Cdd:COG2515 236 VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315


                ..
gi 90111355 325 HP 326
Cdd:COG2515 316 AE 317
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 4.35e-56

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 184.05  E-value: 4.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    12 LEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMamGGNKLRKLEFLAADALRE-GADTLITAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    91 LGLHCVALLenPIGTTAENyltngnRLLLDLFNTQIEMCDALTDpnaQLEELATRVEAQGFRPYVIPVGGsNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVV--PEDAPPGK------LLLMRALGAEVVLVGGDYD---EAVAAARELAAEGPGAYYINQYD-NPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   171 ESALEIAQQCEGAVNIssVVVASGSAGTHAGLAVGLEHLMPESELIGV------TVSRSVADQLPKVVNLQQAIAKELEL 244
Cdd:pfam00291 145 TIGLEILEQLGGDPDA--VVVPVGGGGLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111355   245 TASAEILLW---DDYFAPGYGVPNDEGMEAVKLLARLEGILLDPvYTGKAMAGLiDGISQKRFKDEGPILFIHTG 316
Cdd:pfam00291 223 GDEPGALALdllDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-328 0e+00

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 571.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    4 HNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   84 TAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  164 LGALGYVESALEIAQQC-EGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKEL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  243 ELT---ASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 90111355  320 ALFAYHPHV 328
Cdd:PRK03910 321 ALFAYADAF 329
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 12-328 0e+00

pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents a family of pyridoxal phosphate-dependent enzymes closely related to (and often designated as putative examples of) 1-aminocyclopropane-1-carboxylate deaminase. It appears that members of this family include both D-cysteine desulfhydrase (EC 4.4.1.15) and 1-aminocyclopropane-1-carboxylate deaminase (EC 3.5.99.7).


Pssm-ID: 273533 [Multi-domain]  Cd Length: 318  Bit Score: 555.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    12 LEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    92 GLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQ--IEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAEtrIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   170 VESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASAE 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111355   250 ILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEgPILFIHTGGAPALFAYHPHV 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 1.14e-158

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 445.71  E-value: 1.14e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  19 TPLEYLPRFSDYLG--REIFIKRDDVTPM-AMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHC 95
Cdd:cd06449   1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSGlAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  96 VALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDAL--TDPNAQLEELATRVEAQGFRPYVIPVGGS-NALGALGYVES 172
Cdd:cd06449  81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 173 ALEIAQQCEGA-VNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQA-IAKELELTASAEI 250
Cdd:cd06449 161 VLEIAQQEEELgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAkLAEEGLEVKEEDV 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111355 251 LLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGG 317
Cdd:cd06449 241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 8-326 2.74e-154

1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family [Amino acid transport and metabolism];


Pssm-ID: 442005 [Multi-domain]  Cd Length: 317  Bit Score: 434.99  E-value: 2.74e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   8 RFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAV 87
Cdd:COG2515   1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  88 AAKLGLHCVALLENPigttaENYLTNGNRLLLDLFNTQIEMCDALT--DPNAQLEELATRVEAQGFRPYVIPVGGSNALG 165
Cdd:COG2515  81 AAKLGLKCVLVLRGE-----EPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 166 ALGYVESALEIAQQC-EGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELEL 244
Cdd:COG2515 156 ALGYVEAAAELAAQLaELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 245 TASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAY 324
Cdd:COG2515 236 VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315


                ..
gi 90111355 325 HP 326
Cdd:COG2515 316 AE 317
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 5-324 7.84e-85

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 259.19  E-value: 7.84e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    5 NLTRFPRLEFIGAPTPLEYLPRFSDYLGR--EIFIKRDDVTP-MAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHV 81
Cdd:PRK12390   2 NLQKFPRYPLTFGPTPIHPLKRLSAHLGGkvELYAKREDCNSgLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   82 RQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQ--LEELATRVEAQGFRPYVIPVG 159
Cdd:PRK12390  82 RQVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVPDGFDIGIRksWEDALEDVRAAGGKPYAIPAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  160 GS-NALGALGYVESALEIAQQ-CEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQA 237
Cdd:PRK12390 162 ASdHPLGGLGFVGFAEEVRAQeAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRIARN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  238 IAKELEL---TASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIH 314
Cdd:PRK12390 242 TAELVELgrdITEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAH 321

                        330
                 ....*....|
gi 90111355  315 TGGAPALFAY 324
Cdd:PRK12390 322 LGGVPALNAY 331
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 6-324 2.32e-75

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 234.78  E-value: 2.32e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    6 LTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTA 85
Cdd:PRK14045   9 LSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   86 AVAAKLGLHCVALLEnpigttAENYLtNGNRLLLDLFNTQIEMCDAltDPNAQL----EELATRVEAQGFRPYVIPVGGS 161
Cdd:PRK14045  89 LAAKKLGLDAVLVLR------GKEEL-KGNYLLDKIMGIETRVYEA--KDSFELmkyaEEVAEELKGEGRKPYIIPPGGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  162 NALGALGYVESALEIAQQCEG-AVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAK 240
Cdd:PRK14045 160 SPVGTLGYVRAVGEIATQVKKlGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  241 ELELTASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEgpILFIHTGGAPA 320
Cdd:PRK14045 240 LLGVKVKVQEPELYDYSFGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGELGEK--ILFIHTGGISG 317


                 ....
gi 90111355  321 LFAY 324
Cdd:PRK14045 318 TFHY 321
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 4.35e-56

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 184.05  E-value: 4.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    12 LEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMamGGNKLRKLEFLAADALRE-GADTLITAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    91 LGLHCVALLenPIGTTAENyltngnRLLLDLFNTQIEMCDALTDpnaQLEELATRVEAQGFRPYVIPVGGsNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVV--PEDAPPGK------LLLMRALGAEVVLVGGDYD---EAVAAARELAAEGPGAYYINQYD-NPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   171 ESALEIAQQCEGAVNIssVVVASGSAGTHAGLAVGLEHLMPESELIGV------TVSRSVADQLPKVVNLQQAIAKELEL 244
Cdd:pfam00291 145 TIGLEILEQLGGDPDA--VVVPVGGGGLIAGIARGLKELGPDVRVIGVepegapALARSLAAGRPVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111355   245 TASAEILLW---DDYFAPGYGVPNDEGMEAVKLLARLEGILLDPvYTGKAMAGLiDGISQKRFKDEGPILFIHTG 316
Cdd:pfam00291 223 GDEPGALALdllDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 19-317 8.23e-36

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 129.56  E-value: 8.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  19 TPLEYLPRFSDYLGREIFIKRDDVTPMamGGNKLRKLEFLAADALREG---ADTLITAGAiqSNHVRQTAAVAAKLGLHC 95
Cdd:cd00640   1 TPLVRLKRLSKLGGANIYLKLEFLNPT--GSFKDRGALNLILLAEEEGklpKGVIIESTG--GNTGIALAAAAARLGLKC 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  96 VALLenPIGTTAENyltngnRLLLDLFNTQIEMCDALTDpNAQleELATRVEAQGFRPYVIPvGGSNALGALGYVESALE 175
Cdd:cd00640  77 TIVM--PEGASPEK------VAQMRALGAEVVLVPGDFD-DAI--ALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGLE 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 176 IAQQCEGAvNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTvsrsvadqlPKVVNlqqaiakeleltasaeillwdd 255
Cdd:cd00640 145 ILEQLGGQ-KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVE---------PEVVT---------------------- 192

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111355 256 yfapgygVPNDEGMEAVKLLARLEGILLDPVyTGKAMAGLIDGIsqKRFKDEGPILFIHTGG 317
Cdd:cd00640 193 -------VSDEEALEAIRLLAREEGILVEPS-SAAALAAALKLA--KKLGKGKTVVVILTGG 244
PRK12483 PRK12483
threonine dehydratase; Reviewed
 19-239 2.32e-08

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 55.19  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   19 TPLEYLPRFSDYLGREIFIKRDDVTPMAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGLH 94
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVF--SFKIRgaynKMARLPAEQLARG---VITASA--GNHAQGVALAAARLGVK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   95 CVALLenPIGT---TAENYLTNGNRLLLdlfntqieMCDALTDPNAQLEELAtrvEAQGFrPYVIPVGGSNALGALGYVe 171
Cdd:PRK12483 111 AVIVM--PRTTpqlKVDGVRAHGGEVVL--------HGESFPDALAHALKLA---EEEGL-TFVPPFDDPDVIAGQGTV- 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111355  172 sALEIAQQCEGAvnISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVAdqlpkvvnLQQAIA 239
Cdd:PRK12483 176 -AMEILRQHPGP--LDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNC--------LQAALA 232
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 19-316 2.71e-08

Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 54.82  E-value: 2.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  19 TPLEYLPRFSDYLGREIFIKRDDVTP--------MAMGGNKlrkleflaadALREGADTLITA--GaiqsNHVRQTAAVA 88
Cdd:COG0498  67 TPLVKAPRLADELGKNLYVKEEGHNPtgsfkdraMQVAVSL----------ALERGAKTIVCAssG----NGSAALAAYA 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  89 AKLGLHCVALLenPIGTTAEnyltnGNR---LLLDLFNTQIE--------MCDALtdpnAQLEELAT-------RVEAQ- 149
Cdd:COG0498 133 ARAGIEVFVFV--PEGKVSP-----GQLaqmLTYGAHVIAVDgnfddaqrLVKEL----AADEGLYAvnsinpaRLEGQk 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 150 --GF----------RPYVIPVG-GSNALGALgyvesaleIAQQCEGAVNISS------VVVASGSAGTHAGLAVGLEHLM 210
Cdd:COG0498 202 tyAFeiaeqlgrvpDWVVVPTGnGGNILAGY--------KAFKELKELGLIDrlprliAVQATGCNPILTAFETGRDEYE 273

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 211 PESEligVTVSRSVADQLPkvVNLQQAIAkelELTASAEIllwddyfapGYGVPNDEGMEAVKLLARLEGILLDPvYTGK 290
Cdd:COG0498 274 PERP---ETIAPSMDIGNP--SNGERALF---ALRESGGT---------AVAVSDEEILEAIRLLARREGIFVEP-ATAV 335

                       330       340
                ....*....|....*....|....*.
gi 90111355 291 AMAGLIDGISQKRFKDEGPILFIHTG 316
Cdd:COG0498 336 AVAGLRKLREEGEIDPDEPVVVLSTG 361
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 19-283 7.59e-07

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 49.82  E-value: 7.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  19 TPLEYLPRFSDYLGREIFIKRDDVTPmaMGGNKLRKLEFLAADALREGA----DTLI--TAG----AIqsnhvrqtAAVA 88
Cdd:cd01561   3 TPLVRLNRLSPGTGAEIYAKLEFFNP--GGSVKDRIALYMIEDAEKRGLlkpgTTIIepTSGntgiGL--------AMVA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  89 AKLGLHCVALLenPIGTTAEnyltngNRLLLDLFNTQIEMCDA--LTDPNAQLeELATRVEAQGFRpYVIPVGGSNALGA 166
Cdd:cd01561  73 AAKGYRFIIVM--PETMSEE------KRKLLRALGAEVILTPEaeADGMKGAI-AKARELAAETPN-AFWLNQFENPANP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 167 LGYVES-ALEIAQQCEGAVNIssVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVadqlpkVVNLQQAIAKELE-- 243
Cdd:cd01561 143 EAHYETtAPEIWEQLDGKVDA--FVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSV------LFSGGPPGPHKIEgi 214

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 90111355 244 ----LTASAEILLWDDyfapGYGVPNDEGMEAVKLLARLEGILL 283
Cdd:cd01561 215 gagfIPENLDRSLIDE----VVRVSDEEAFAMARRLAREEGLLV 254
PLN02550 PLN02550
threonine dehydratase
 19-218 9.82e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 50.30  E-value: 9.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   19 TPLEYLPRFSDYLGREIFIKRDDVTPMAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGlh 94
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVF--SFKLRgaynMMAKLPKEQLDKG---VICSSA--GNHAQGVALSAQRLG-- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   95 CVALLENPIgTTAENYLTNGNRllldLFNTQIEMCDALTDPNAQLEElatRVEAQGfRPYVIPVGGSNALGALGYVesAL 174
Cdd:PLN02550 181 CDAVIAMPV-TTPEIKWQSVER----LGATVVLVGDSYDEAQAYAKQ---RALEEG-RTFIPPFDHPDVIAGQGTV--GM 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 90111355  175 EIAQQCEGAVNisSVVVASGSAGTHAGLAVGLEHLMPESELIGV 218
Cdd:PLN02550 250 EIVRQHQGPLH--AIFVPVGGGGLIAGIAAYVKRVRPEVKIIGV 291
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
19-218 2.07e-06

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 48.98  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   19 TPLEYLPRFSDYLGREIFIKRDDVTPMAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGlh 94
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVF--SFKLRgaynKMAQLTEEQLARG---VITASA--GNHAQGVALSAARLG-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   95 CVALLENPIgTTAE-----------NYLTNGnrllldlfntqiemcDALTDPNAQLEELAtrvEAQGF-------RPYVI 156
Cdd:PRK09224  92 IKAVIVMPV-TTPDikvdavrafggEVVLHG---------------DSFDEAYAHAIELA---EEEGLtfihpfdDPDVI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111355  157 PVGGSnalgalgyveSALEIAQQCEGAvnISSVVVASGSAGTHAGLAVGLEHLMPESELIGV 218
Cdd:PRK09224 153 AGQGT----------IAMEILQQHPHP--LDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGV 202
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 13-96 4.94e-06

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 47.53  E-value: 4.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  13 EFIGAPTPLEYLPRFSDYLGR-EIFIKRDDVTPmaMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVRQTAAVAAK 90
Cdd:cd06446  29 DYVGRPTPLYRAKRLSEYLGGaKIYLKREDLNH--TGAHKINNALGQALLAKRMGKKRVIAeTGAGQ--HGVATATACAL 104


                ....*.
gi 90111355  91 LGLHCV 96
Cdd:cd06446 105 FGLECE 110
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 6-95 7.40e-06

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 47.50  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355    6 LTRFPRL--EFIGAPTPLEYLPRFSDYLGREIFIKRDDVTpmAMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVR 82
Cdd:PRK13803 257 QKTFKRLlqNYAGRPTPLTEAKRLSDIYGARIYLKREDLN--HTGSHKINNALGQALLAKRMGKTRIIAeTGAGQ--HGV 332

                         90
                 ....*....|...
gi 90111355   83 QTAAVAAKLGLHC 95
Cdd:PRK13803 333 ATATACALFGLKC 345
PRK06815 PRK06815
threonine/serine dehydratase;
17-218 8.62e-06

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 46.61  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   17 APTPLEYLPRFSDYLGREIFIKRDDVTPMamGGNKLRKleflAADALRegadtlitagaIQSNHVRQTAAVAAKLGLH-- 94
Cdd:PRK06815  19 RVTPLEHSPLLSQHTGCEVYLKCEHLQHT--GSFKFRG----ASNKLR-----------LLNEAQRQQGVITASSGNHgq 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   95 CVALLENPIGTTAENYLT-NGNRLLLDL---FNTQIEMCDalTDP-NAQLEelATRVEAQGFRPYVIPVGGSNALGALGY 169
Cdd:PRK06815  82 GVALAAKLAGIPVTVYAPeQASAIKLDAiraLGAEVRLYG--GDAlNAELA--ARRAAEQQGKVYISPYNDPQVIAGQGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 90111355  170 VesALEIAQQcegAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGV 218
Cdd:PRK06815 158 I--GMELVEQ---QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGC 201
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 19-310 9.82e-05

Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.


Pssm-ID: 107206 [Multi-domain]  Cd Length: 324  Bit Score: 43.35  E-value: 9.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  19 TPLEYLPRFSDYLG-REIFIKRDDVTPMamGGNKLRKLEFLAADALREGADTLITAGAiqSNHVRQTAAVAAKLGLHCVA 97
Cdd:cd01563  23 TPLVRAPRLGERLGgKNLYVKDEGLNPT--GSFKDRGMTVAVSKAKELGVKAVACAST--GNTSASLAAYAARAGIKCVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355  98 LLenPIGTTAENY---LTNGNRLLldlfntQIE--MCDALTdpnaqleelATRVEAQGFRPYVIPVggSNALGALGYVES 172
Cdd:cd01563  99 FL--PAGKALGKLaqaLAYGATVL------AVEgnFDDALR---------LVRELAEENWIYLSNS--LNPYRLEGQKTI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 173 ALEIAQQCEGAVNiSSVVVASGSAGTHAGLAVGLEHLMpESELIgvtvsrsvaDQLPKVVNLQQAIAKELeltASAEILL 252
Cdd:cd01563 160 AFEIAEQLGWEVP-DYVVVPVGNGGNITAIWKGFKELK-ELGLI---------DRLPRMVGVQAEGAAPI---VRAFKEG 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355 253 WDDY--------FAPGYGVPN-----------------------DEGMEAVKLLARLEGILLDPVyTGKAMAGLidgisq 301
Cdd:cd01563 226 KDDIepvenpetIATAIRIGNpasgpkalravresggtavavsdEEILEAQKLLARTEGIFVEPA-SAASLAGL------ 298


                ....*....
gi 90111355 302 KRFKDEGPI 310
Cdd:cd01563 299 KKLREEGII 307
PRK13802 PRK13802
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
 13-95 9.41e-04

bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 184335 [Multi-domain]  Cd Length: 695  Bit Score: 40.78  E-value: 9.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   13 EFIGAPTPLEYLPRFSDYLGRE------IFIKRDDVTpmAMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVRQTA 85
Cdd:PRK13802 321 RYVGRPSPLTEAPRFAERVKEKtgldarVFLKREDLN--HTGAHKINNALGQALLVKRMGKTRVIAeTGAGQ--HGVATA 396

                         90
                 ....*....|
gi 90111355   86 AVAAKLGLHC 95
Cdd:PRK13802 397 TVCAMLGLKC 406
PLN02618 PLN02618
tryptophan synthase, beta chain
 13-96 1.59e-03

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 40.12  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111355   13 EFIGAPTPLEYLPRFSDYLGR------EIFIKRDDVTpmAMGGNKLRKLEFLAADALREGADTLITA-GAIQsnHVRQTA 85
Cdd:PLN02618  61 DYVGRETPLYFAERLTEHYKRadgegpEIYLKREDLN--HTGAHKINNAVAQALLAKRLGKKRIIAEtGAGQ--HGVATA 136

                         90
                 ....*....|.
gi 90111355   86 AVAAKLGLHCV 96
Cdd:PLN02618 137 TVCARFGLECI 147
 
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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