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Conserved domains on  [gi|515713023|ref|WP_017145623|]
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MULTISPECIES: D-cysteine desulfhydrase [Klebsiella]

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

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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: 559.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   4 QNLTLFPRLELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  84 TAAVAAKLGLHCVALLENPMGTRAENYLTNGNRLLLDLFNTQVEMCDALTDPDAQLEELATRIEAQGYRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 164 LGALGYVESALEIAQQC-EGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 243 ELE---AKAGIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 515713023 320 ALFAYHPHI 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: 559.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   4 QNLTLFPRLELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  84 TAAVAAKLGLHCVALLENPMGTRAENYLTNGNRLLLDLFNTQVEMCDALTDPDAQLEELATRIEAQGYRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 164 LGALGYVESALEIAQQC-EGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 243 ELE---AKAGIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 515713023 320 ALFAYHPHI 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: 522.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   12 LELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   92 GLHCVALLENPMGTRAENYLTNGNRLLLDLFNTQ--VEMCDALTDPDAQLEELATRIEAQGYRPYVIPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAEtrIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  170 VESALEIAQQCEGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSLELEAKAG 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713023  250 IQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEgPILFVHTGGAPALFAYHPHI 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 9-326 5.03e-153

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: 431.53  E-value: 5.03e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   9 FPRLELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVA 88
Cdd:COG2515    2 FPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  89 AKLGLHCVALLENPmgtraENYLTNGNRLLLDLFNTQVEMCDALT--DPDAQLEELATRIEAQGYRPYVIPVGGSNALGA 166
Cdd:COG2515   82 AKLGLKCVLVLRGE-----EPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 167 LGYVESALEIAQQC-EGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSLELE 245
Cdd:COG2515  157 LGYVEAAAELAAQLaELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGLV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 246 AKAGIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGGAPALFAYH 325
Cdd:COG2515  237 SRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGYA 316


                 .
gi 515713023 326 P 326
Cdd:COG2515  317 E 317
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 3.05e-148

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: 419.13  E-value: 3.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLG--REIFIKRDDVTP-LAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHC 95
Cdd:cd06449    1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  96 VALLENPMGTRAENYLTNGNRLLLDLFNTQVEMCDAL--TDPDAQLEELATRIEAQGYRPYVIPVGGS-NALGALGYVES 172
Cdd:cd06449   81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 173 ALEIAQQCEGA-VELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSLELEAKAG-I 250
Cdd:cd06449  161 VLEIAQQEEELgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEEdV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713023 251 QLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGG 317
Cdd:cd06449  241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 5.65e-55

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: 180.97  E-value: 5.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   12 LELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLamGGNKLRKLEFLAADALRE-GADTLITAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   91 LGLHCVALLENPMgtraenylTNGNRLLLDLFNTQVEMCDALTDpdaQLEELATRIEAQGYRPYVIPvGGSNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVVPEDA--------PPGKLLLMRALGAEVVLVGGDYD---EAVAAARELAAEGPGAYYIN-QYDNPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  171 ESALEIAQQCEGAVElsSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVA----------DQLPKVAALQQAVAN 240
Cdd:pfam00291 145 TIGLEILEQLGGDPD--AVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPAlarslaagrpVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713023  241 SLELEAKAgIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPvYTGKAMAGLiDGISQKRFKDEGPILFVHTG 316
Cdd:pfam00291 223 GDEPGALA-LDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-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: 559.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   4 QNLTLFPRLELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  84 TAAVAAKLGLHCVALLENPMGTRAENYLTNGNRLLLDLFNTQVEMCDALTDPDAQLEELATRIEAQGYRPYVIPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 164 LGALGYVESALEIAQQC-EGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 243 ELE---AKAGIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*....
gi 515713023 320 ALFAYHPHI 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: 522.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   12 LELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   92 GLHCVALLENPMGTRAENYLTNGNRLLLDLFNTQ--VEMCDALTDPDAQLEELATRIEAQGYRPYVIPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAEtrIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  170 VESALEIAQQCEGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSLELEAKAG 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515713023  250 IQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEgPILFVHTGGAPALFAYHPHI 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 9-326 5.03e-153

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: 431.53  E-value: 5.03e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   9 FPRLELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVA 88
Cdd:COG2515    2 FPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  89 AKLGLHCVALLENPmgtraENYLTNGNRLLLDLFNTQVEMCDALT--DPDAQLEELATRIEAQGYRPYVIPVGGSNALGA 166
Cdd:COG2515   82 AKLGLKCVLVLRGE-----EPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLGA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 167 LGYVESALEIAQQC-EGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSLELE 245
Cdd:COG2515  157 LGYVEAAAELAAQLaELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGLV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 246 AKAGIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGGAPALFAYH 325
Cdd:COG2515  237 SRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGYA 316


                 .
gi 515713023 326 P 326
Cdd:COG2515  317 E 317
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 3.05e-148

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: 419.13  E-value: 3.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLG--REIFIKRDDVTP-LAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHC 95
Cdd:cd06449    1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  96 VALLENPMGTRAENYLTNGNRLLLDLFNTQVEMCDAL--TDPDAQLEELATRIEAQGYRPYVIPVGGS-NALGALGYVES 172
Cdd:cd06449   81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 173 ALEIAQQCEGA-VELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVANSLELEAKAG-I 250
Cdd:cd06449  161 VLEIAQQEEELgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEEdV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515713023 251 QLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVHTGG 317
Cdd:cd06449  241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 5-324 2.15e-82

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 253.03  E-value: 2.15e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   5 NLTLFPRLELIGAPTPLEYLPRLSDYLGR--EIFIKRDDVTP-LAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHV 81
Cdd:PRK12390   2 NLQKFPRYPLTFGPTPIHPLKRLSAHLGGkvELYAKREDCNSgLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  82 RQTAAVAAKLGLHCVALLENPMGTRAENYLTNGNRLLLDLFNTQVEMCDALTDPDAQ--LEELATRIEAQGYRPYVIPVG 159
Cdd:PRK12390  82 RQVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVPDGFDIGIRksWEDALEDVRAAGGKPYAIPAG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 160 GS-NALGALGYVESALEIAQQ-CEGAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQA 237
Cdd:PRK12390 162 ASdHPLGGLGFVGFAEEVRAQeAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRIARN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 238 VANSLELE---AKAGIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFVH 314
Cdd:PRK12390 242 TAELVELGrdiTEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAH 321

                        330
                 ....*....|
gi 515713023 315 TGGAPALFAY 324
Cdd:PRK12390 322 LGGVPALNAY 331
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 6-324 2.04e-73

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 229.78  E-value: 2.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   6 LTLFPRLELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTA 85
Cdd:PRK14045   9 LSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  86 AVAAKLGLHCVALLenpmgtRAENYLtNGNRLLLDLFNTQVEMCDAltDPDAQL----EELATRIEAQGYRPYVIPVGGS 161
Cdd:PRK14045  89 LAAKKLGLDAVLVL------RGKEEL-KGNYLLDKIMGIETRVYEA--KDSFELmkyaEEVAEELKGEGRKPYIIPPGGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 162 NALGALGYVESALEIAQQCEG-AVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVADQLPKVAALQQAVAN 240
Cdd:PRK14045 160 SPVGTLGYVRAVGEIATQVKKlGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 241 SLELEAKAG-IQLWDDYFAPgYGIPNDEGMAAVKLLAQLEGILLDPVYTGKAMAGLIDGISQKRFKDEgpILFVHTGGAP 319
Cdd:PRK14045 240 LLGVKVKVQePELYDYSFGE-YGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMDLAKKGELGEK--ILFIHTGGIS 316


                 ....*
gi 515713023 320 ALFAY 324
Cdd:PRK14045 317 GTFHY 321
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 5.65e-55

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: 180.97  E-value: 5.65e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   12 LELIGAPTPLEYLPRLSDYLGREIFIKRDDVTPLamGGNKLRKLEFLAADALRE-GADTLITAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023   91 LGLHCVALLENPMgtraenylTNGNRLLLDLFNTQVEMCDALTDpdaQLEELATRIEAQGYRPYVIPvGGSNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVVPEDA--------PPGKLLLMRALGAEVVLVGGDYD---EAVAAARELAAEGPGAYYIN-QYDNPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  171 ESALEIAQQCEGAVElsSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTVSRKVA----------DQLPKVAALQQAVAN 240
Cdd:pfam00291 145 TIGLEILEQLGGDPD--AVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPAlarslaagrpVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515713023  241 SLELEAKAgIQLWDDYFAPGYGIPNDEGMAAVKLLAQLEGILLDPvYTGKAMAGLiDGISQKRFKDEGPILFVHTG 316
Cdd:pfam00291 223 GDEPGALA-LDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 19-317 4.71e-37

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: 133.02  E-value: 4.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLGREIFIKRDDVTPlaMGGNKLRKLEFLAADALREG---ADTLITAGAiqSNHVRQTAAVAAKLGLHC 95
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNP--TGSFKDRGALNLILLAEEEGklpKGVIIESTG--GNTGIALAAAAARLGLKC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  96 VALLenPMGTRAENyltngnRLLLDLFNTQVEMCDALTDpDAQleELATRIEAQGYRPYVIPvGGSNALGALGYVESALE 175
Cdd:cd00640   77 TIVM--PEGASPEK------VAQMRALGAEVVLVPGDFD-DAI--ALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGLE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 176 IAQQCEGAvELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVTvsrkvadqlPKVAAlqqavansleleakagiqlwdd 255
Cdd:cd00640  145 ILEQLGGQ-KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVE---------PEVVT---------------------- 192

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515713023 256 yfapgygIPNDEGMAAVKLLAQLEGILLDPVyTGKAMAGLIDGIsqKRFKDEGPILFVHTGG 317
Cdd:cd00640  193 -------VSDEEALEAIRLLAREEGILVEPS-SAAALAAALKLA--KKLGKGKTVVVILTGG 244
PRK06815 PRK06815
threonine/serine dehydratase;
18-218 4.67e-09

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 56.62  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  18 PTPLEYLPRLSDYLGREIFIKRDDVTPlaMGGNKLRKleflAADALRegadtlitagaIQSNHVRQTAAVAAKLGLH--C 95
Cdd:PRK06815  20 VTPLEHSPLLSQHTGCEVYLKCEHLQH--TGSFKFRG----ASNKLR-----------LLNEAQRQQGVITASSGNHgqG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  96 VALLENPMGTRAENYLT-NGNRLLLDL---FNTQVEMCDAltdpDAQLEELATRIEA--QGyRPYVIPVGGSNALGALGY 169
Cdd:PRK06815  83 VALAAKLAGIPVTVYAPeQASAIKLDAiraLGAEVRLYGG----DALNAELAARRAAeqQG-KVYISPYNDPQVIAGQGT 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515713023 170 VesALEIAQQcegAVELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGV 218
Cdd:PRK06815 158 I--GMELVEQ---QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGC 201
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 19-316 6.05e-09

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: 56.75  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLGREIFIKRDDVTP--------LAMGGNKlrkleflaadALREGADTLITA--GaiqsNHVRQTAAVA 88
Cdd:COG0498   67 TPLVKAPRLADELGKNLYVKEEGHNPtgsfkdraMQVAVSL----------ALERGAKTIVCAssG----NGSAALAAYA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  89 AKLGLHCVALLenPmgtraENYLTNGNRLLLDLFNTQVEMCDALTDpDAQ--LEELATRIEaqgyrpyVIPVGGSNALGA 166
Cdd:COG0498  133 ARAGIEVFVFV--P-----EGKVSPGQLAQMLTYGAHVIAVDGNFD-DAQrlVKELAADEG-------LYAVNSINPARL 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 167 LGYVESALEIAQQCEGAVElsSVVVASGSAGTHAGLAVGLEQLMpnveLIGVTvsrkvaDQLPKVAALQQAVANSLELEA 246
Cdd:COG0498  198 EGQKTYAFEIAEQLGRVPD--WVVVPTGNGGNILAGYKAFKELK----ELGLI------DRLPRLIAVQATGCNPILTAF 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 247 KAGiqlWDDY-------FAPGYGIPN-----------------------DEGMAAVKLLAQLEGILLDPvYTGKAMAGLI 296
Cdd:COG0498  266 ETG---RDEYeperpetIAPSMDIGNpsngeralfalresggtavavsdEEILEAIRLLARREGIFVEP-ATAVAVAGLR 341

                        330       340
                 ....*....|....*....|
gi 515713023 297 DGISQKRFKDEGPILFVHTG 316
Cdd:COG0498  342 KLREEGEIDPDEPVVVLSTG 361
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 19-283 3.46e-08

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: 54.06  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLGREIFIKRDDVTPlaMGGNKLRKLEFLAADALREGA----DTLI--TAG----AIqsnhvrqtAAVA 88
Cdd:cd01561    3 TPLVRLNRLSPGTGAEIYAKLEFFNP--GGSVKDRIALYMIEDAEKRGLlkpgTTIIepTSGntgiGL--------AMVA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  89 AKLGLHCVALLENPMgtraenylTNGNRLLLDLFNTQVEMCDAltDPDAQLE---ELATRIEAQGYRpYVIPVGGSNALG 165
Cdd:cd01561   73 AAKGYRFIIVMPETM--------SEEKRKLLRALGAEVILTPE--AEADGMKgaiAKARELAAETPN-AFWLNQFENPAN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 166 ALGYVES-ALEIAQQCEGAVelSSVVVASGSAGTHAGLAVGLEQLMPNVELIGV-TVSRKVADQLPKVAALQQAVansle 243
Cdd:cd01561  142 PEAHYETtAPEIWEQLDGKV--DAFVAGVGTGGTITGVARYLKEKNPNVRIVGVdPVGSVLFSGGPPGPHKIEGI----- 214

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 515713023 244 leakaGIQLWDDYFAPG-----YGIPNDEGMAAVKLLAQLEGILL 283
Cdd:cd01561  215 -----GAGFIPENLDRSlidevVRVSDEEAFAMARRLAREEGLLV 254
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
19-218 4.05e-08

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 54.37  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLGREIFIKRDDVTPLAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGlh 94
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVF--SFKLRgaynKMAQLTEEQLARG---VITASA--GNHAQGVALSAARLG-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  95 CVALLENPMGT--------RAenyltngnrllldlFNTQVEMC-DALTDPDAQLEELAtriEAQGY-------RPYVIPV 158
Cdd:PRK09224  92 IKAVIVMPVTTpdikvdavRA--------------FGGEVVLHgDSFDEAYAHAIELA---EEEGLtfihpfdDPDVIAG 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 159 GGSnalgalgyveSALEIAQQCEGAVElsSVVVASGSAGTHAGLAVGLEQLMPNVELIGV 218
Cdd:PRK09224 155 QGT----------IAMEILQQHPHPLD--AVFVPVGGGGLIAGVAAYIKQLRPEIKVIGV 202
PRK12483 PRK12483
threonine dehydratase; Reviewed
 19-239 5.29e-08

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 54.03  E-value: 5.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLGREIFIKRDDVTPLAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGLH 94
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVF--SFKIRgaynKMARLPAEQLARG---VITASA--GNHAQGVALAAARLGVK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  95 CVALLenPMGT---RAENYLTNGNRLLLdlfntqveMCDALTDPDAQLEELAtriEAQGyRPYVIPVGGSNALGALGYVe 171
Cdd:PRK12483 111 AVIVM--PRTTpqlKVDGVRAHGGEVVL--------HGESFPDALAHALKLA---EEEG-LTFVPPFDDPDVIAGQGTV- 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515713023 172 sALEIAQQCEGAveLSSVVVASGSAGTHAGLAVGLEQLMPNVELIGVtvsrkvadQLPKVAALQQAVA 239
Cdd:PRK12483 176 -AMEILRQHPGP--LDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGV--------EPDDSNCLQAALA 232
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 19-310 1.05e-07

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: 52.60  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLG-REIFIKRDDVTPlaMGGNKLRKLEFLAADALREGADTLITAGAiqSNHVRQTAAVAAKLGLHCVA 97
Cdd:cd01563   23 TPLVRAPRLGERLGgKNLYVKDEGLNP--TGSFKDRGMTVAVSKAKELGVKAVACAST--GNTSASLAAYAARAGIKCVV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  98 LLenPMGTRAENY---LTNGNRLLldlfntQVEmcdalTDPDAQLEelATRIEAQGYRPYVIPVggSNALGALGYVESAL 174
Cdd:cd01563   99 FL--PAGKALGKLaqaLAYGATVL------AVE-----GNFDDALR--LVRELAEENWIYLSNS--LNPYRLEGQKTIAF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 175 EIAQQCEGAVElSSVVVASGSAGTHAGLAVGLEQLmpnvELIGVTvsrkvaDQLPKVAALQQAVANSLeleAKAGIQLWD 254
Cdd:cd01563  162 EIAEQLGWEVP-DYVVVPVGNGGNITAIWKGFKEL----KELGLI------DRLPRMVGVQAEGAAPI---VRAFKEGKD 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 255 DY--------FAPGYGIPN-----------------------DEGMAAVKLLAQLEGILLDPVyTGKAMAGLidgisqKR 303
Cdd:cd01563  228 DIepvenpetIATAIRIGNpasgpkalravresggtavavsdEEILEAQKLLARTEGIFVEPA-SAASLAGL------KK 300


                 ....*..
gi 515713023 304 FKDEGPI 310
Cdd:cd01563  301 LREEGII 307
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 18-218 1.42e-07

Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 52.10  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  18 PTPLEYLPRLSDYLGREIFIKRDDVTPlaMGGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGL 93
Cdd:cd01562   17 RTPLLTSPTLSELLGAEVYLKCENLQK--TGSFKIRgaynKLLSLSEEERAKG---VVAASA--GNHAQGVAYAAKLLGI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  94 HCVALLenPMGT------RAENYltngnrllldlfNTQVEMCDALTDpDAqlEELATRIEAQ-GYR-------PYVIpvg 159
Cdd:cd01562   90 PATIVM--PETApaakvdATRAY------------GAEVVLYGEDFD-EA--EAKARELAEEeGLTfihpfddPDVI--- 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515713023 160 gsnaLGAlGYVesALEIAQQCEgavELSSVVVASGSAGTHAGLAVGLEQLMPNVELIGV 218
Cdd:cd01562  150 ----AGQ-GTI--GLEILEQVP---DLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGV 198
PLN02550 PLN02550
threonine dehydratase
 19-218 4.74e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 51.08  E-value: 4.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  19 TPLEYLPRLSDYLGREIFIKRDDVTPLAmgGNKLR----KLEFLAADALREGadtLITAGAiqSNHVRQTAAVAAKLGlh 94
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVF--SFKLRgaynMMAKLPKEQLDKG---VICSSA--GNHAQGVALSAQRLG-- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  95 CVALLENPMGTRAENYLTNGNrllldLFNTQVEMCDALTDPDAQLEElatRIEAQGyRPYVIPVGGSNALGALGYVesAL 174
Cdd:PLN02550 181 CDAVIAMPVTTPEIKWQSVER-----LGATVVLVGDSYDEAQAYAKQ---RALEEG-RTFIPPFDHPDVIAGQGTV--GM 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 515713023 175 EIAQQCEGAveLSSVVVASGSAGTHAGLAVGLEQLMPNVELIGV 218
Cdd:PLN02550 250 EIVRQHQGP--LHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGV 291
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 16-282 2.43e-06

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 49.04  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  16 GAPTPLEYLPRLSDYLGREIFIKRDDVtpLAMGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVRQTAAVAAKLGLH 94
Cdd:PRK13803 269 GRPTPLTEAKRLSDIYGARIYLKREDL--NHTGSHKINNALGQALLAKRMGKTRIIAeTGAGQ--HGVATATACALFGLK 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  95 CVALL-ENPMGTRAENYL------------TNGNRLLLDLFNtqvemcDALTDPDAQLEELATRI-EAQGYRPYVIPVgg 160
Cdd:PRK13803 345 CTIFMgEEDIKRQALNVErmkllganvipvLSGSKTLKDAVN------EAIRDWVASVPDTHYLIgSAVGPHPYPEMV-- 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 161 snalgalGYVESAL--EIAQQC-EGAVELSSVVVASGSAGTHA-GLAVG-LEQlmPNVELIGVTVSRKvADQLPKVAA-- 233
Cdd:PRK13803 417 -------AYFQSVIgeEAKEQLkEQTGKLPDAIIACVGGGSNAiGIFYHfLDD--PSVKLIGVEAGGK-GVNTGEHAAti 486

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023 234 ---------------LQQAVANSLELEA-KAGIqlwdDYfaPGYG----------------IPNDEGMAAVKLLAQLEGI 281
Cdd:PRK13803 487 kkgrkgvlhgsmtylMQDENGQILEPHSiSAGL----DY--PGIGpmhanlfetgraiytsVTDEEALDAFKLLAKLEGI 560


                 .
gi 515713023 282 L 282
Cdd:PRK13803 561 I 561
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 13-96 2.81e-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: 48.30  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  13 ELIGAPTPLEYLPRLSDYLGR-EIFIKRDDVTPLamGGNKLRKLEFLAADALREGADTLIT-AGAIQsnHVRQTAAVAAK 90
Cdd:cd06446   29 DYVGRPTPLYRAKRLSEYLGGaKIYLKREDLNHT--GAHKINNALGQALLAKRMGKKRVIAeTGAGQ--HGVATATACAL 104


                 ....*.
gi 515713023  91 LGLHCV 96
Cdd:cd06446  105 FGLECE 110
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
 15-96 2.81e-04

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 42.36  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  15 IGAPTPLEYLPRLSDYL-GREIFIKRDDvtpLAMGG-----NKLrkleflaADAL---REG-----ADTlitaGAIQsnH 80
Cdd:PRK04346  55 VGRPTPLYFAERLSEHLgGAKIYLKRED---LNHTGahkinNVL-------GQALlakRMGkkriiAET----GAGQ--H 118

                         90
                 ....*....|....*.
gi 515713023  81 VRQTAAVAAKLGLHCV 96
Cdd:PRK04346 119 GVATATAAALLGLECV 134
PRK13028 PRK13028
tryptophan synthase subunit beta; Provisional
 16-96 3.39e-04

tryptophan synthase subunit beta; Provisional


Pssm-ID: 183851  Cd Length: 402  Bit Score: 42.16  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  16 GAPTPLEYLPRLSDYL-GREIFIKRDDvtpLAMGGNklRKLEFLAADAL---REGADTLIT-AGAIQsnHVRQTAAVAAK 90
Cdd:PRK13028  60 GRPTPLYHAKRLSEELgGAQIYLKRED---LNHTGA--HKINNCLGQALlakRMGKKRLIAeTGAGQ--HGVATATAAAL 132


                 ....*.
gi 515713023  91 LGLHCV 96
Cdd:PRK13028 133 FGLECE 138
PLN02618 PLN02618
tryptophan synthase, beta chain
 15-96 9.21e-04

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 40.51  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515713023  15 IGAPTPLEYLPRLSDYLGR------EIFIKRDDVTplAMGGNKLRKLEFLAADALREGADTLITA-GAIQsnHVRQTAAV 87
Cdd:PLN02618  63 VGRETPLYFAERLTEHYKRadgegpEIYLKREDLN--HTGAHKINNAVAQALLAKRLGKKRIIAEtGAGQ--HGVATATV 138


                 ....*....
gi 515713023  88 AAKLGLHCV 96
Cdd:PLN02618 139 CARFGLECI 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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