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Conserved domains on  [gi|502791162|ref|WP_013026138|]
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MULTISPECIES: D-cysteine desulfhydrase [Pantoea]

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
 4-326 0e+00

D-cysteine desulfhydrase; Validated


:

Pssm-ID: 179673  Cd Length: 331  Bit Score: 535.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   4 HLIHQFPRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  84 TAAVAAKLGLKCVALLENPIATHSENYLTNGNRLMLDLMDVEVVMVDALTQPAAQLAEQAERLEAQGFRPYILPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 164 LGALGYVECAQEIAHQS-EGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 243 ALE---AKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*..
gi 502791162 320 ALFAYHP 326
Cdd:PRK03910 321 ALFAYAD 327
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-326 0e+00

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 535.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   4 HLIHQFPRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  84 TAAVAAKLGLKCVALLENPIATHSENYLTNGNRLMLDLMDVEVVMVDALTQPAAQLAEQAERLEAQGFRPYILPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 164 LGALGYVECAQEIAHQS-EGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 243 ALE---AKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*..
gi 502791162 320 ALFAYHP 326
Cdd:PRK03910 321 ALFAYAD 327
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 12-328 3.46e-166

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: 465.05  E-value: 3.46e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   12 IELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   92 GLKCVALLENPIATHSENYLTNGNRLMLDLMDVE--VVMVDALTQPAAQLAEQAERLEAQGFRPYILPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAEtrIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  170 VECAQEIAHQSEGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQLALEAKAP 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502791162  250 VTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREgPLLFVHTGGAPALFAYHPSV 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 8-326 8.90e-151

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: 426.13  E-value: 8.90e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   8 QFPRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQTAAV 87
Cdd:COG2515    1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  88 AAKLGLKCVALLENPiathsENYLTNGNRLMLDLMDVEVVMVDALT--QPAAQLAEQAERLEAQGFRPYILPVGGSNALG 165
Cdd:COG2515   81 AAKLGLKCVLVLRGE-----EPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 166 ALGYVECAQEIAHQS-EGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQLAL 244
Cdd:COG2515  156 ALGYVEAAAELAAQLaELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 245 EAKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGGAPALFAY 324
Cdd:COG2515  236 VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315


                 ..
gi 502791162 325 HP 326
Cdd:COG2515  316 AE 317
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 2.44e-136

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: 389.09  E-value: 2.44e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLG--RDIFIKRDDVTP-LAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQTAAVAAKLGLKC 95
Cdd:cd06449    1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  96 VALLENPIATHSENYLTNGNRLMLDLMDVEVVMVDAL--TQPAAQLAEQAERLEAQGFRPYILPVGGS-NALGALGYVEC 172
Cdd:cd06449   81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 173 AQEIAHQSEGV-VDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQLALEAKAP-V 250
Cdd:cd06449  161 VLEIAQQEEELgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEEdV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502791162 251 TLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGG 317
Cdd:cd06449  241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 2.40e-52

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: 174.42  E-value: 2.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   12 IELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLamGGNKLRKLEFLAADALRE-GADVLLTAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   91 LGLKCVALLENPIathsenylTNGNRLMLDLMDVEVVMVDALTQPAAQLaeqAERLEAQGFRPYILPvGGSNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVVPEDA--------PPGKLLLMRALGAEVVLVGGDYDEAVAA---ARELAAEGPGAYYIN-QYDNPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  171 ECAQEIAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVA------EQRPKVDALRQALATQLAL 244
Cdd:pfam00291 145 TIGLEILEQLGGDPD--AVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPAlarslaAGRPVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502791162  245 EAKAPVTLW---DDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPvYTGKAMAGLiDGINQNRFRREGPLLFVHTG 316
Cdd:pfam00291 223 GDEPGALALdllDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAAL-KLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 4-326 0e+00

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 535.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   4 HLIHQFPRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQ 83
Cdd:PRK03910   1 MNLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  84 TAAVAAKLGLKCVALLENPIATHSENYLTNGNRLMLDLMDVEVVMVDALTQPAAQLAEQAERLEAQGFRPYILPVGGSNA 163
Cdd:PRK03910  81 TAAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 164 LGALGYVECAQEIAHQS-EGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQL 242
Cdd:PRK03910 161 LGALGYVACALEIAQQLaEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 243 ALE---AKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGGAP 319
Cdd:PRK03910 241 GLPteiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGGNVLFIHTGGAP 320


                 ....*..
gi 502791162 320 ALFAYHP 326
Cdd:PRK03910 321 ALFAYAD 327
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 12-328 3.46e-166

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: 465.05  E-value: 3.46e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   12 IELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQTAAVAAKL 91
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   92 GLKCVALLENPIATHSENYLTNGNRLMLDLMDVE--VVMVDALTQPAAQLAEQAERLEAQGFRPYILPVGGSNALGALGY 169
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAEtrIESCEEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  170 VECAQEIAHQSEGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQLALEAKAP 249
Cdd:TIGR01275 161 VEAALEIAQQLESEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTVSAV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502791162  250 VTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREgPLLFVHTGGAPALFAYHPSV 328
Cdd:TIGR01275 241 IPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDK-PILFIHTGGIPGLFAYHDHL 318
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 8-326 8.90e-151

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: 426.13  E-value: 8.90e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   8 QFPRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQTAAV 87
Cdd:COG2515    1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  88 AAKLGLKCVALLENPiathsENYLTNGNRLMLDLMDVEVVMVDALT--QPAAQLAEQAERLEAQGFRPYILPVGGSNALG 165
Cdd:COG2515   81 AAKLGLKCVLVLRGE-----EPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 166 ALGYVECAQEIAHQS-EGVVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQLAL 244
Cdd:COG2515  156 ALGYVEAAAELAAQLaELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 245 EAKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGGAPALFAY 324
Cdd:COG2515  236 VSRADIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGSRVLFIHTGGLPGLFGY 315


                 ..
gi 502791162 325 HP 326
Cdd:COG2515  316 AE 317
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 19-317 2.44e-136

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: 389.09  E-value: 2.44e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLG--RDIFIKRDDVTP-LAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQTAAVAAKLGLKC 95
Cdd:cd06449    1 TPIQYLPRLSEHLGgkVEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  96 VALLENPIATHSENYLTNGNRLMLDLMDVEVVMVDAL--TQPAAQLAEQAERLEAQGFRPYILPVGGS-NALGALGYVEC 172
Cdd:cd06449   81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGfdIGIRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 173 AQEIAHQSEGV-VDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQALATQLALEAKAP-V 250
Cdd:cd06449  161 VLEIAQQEEELgFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKLAEEGLEVKEEdV 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502791162 251 TLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHTGG 317
Cdd:cd06449  241 VLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGSKVLFIHLGG 307
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 6-324 1.77e-84

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 258.42  E-value: 1.77e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   6 IHQFPRIELLGAPTPLEYLPRLSDYLGR--DIFIKRDDVTP-LAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVR 82
Cdd:PRK12390   3 LQKFPRYPLTFGPTPIHPLKRLSAHLGGkvELYAKREDCNSgLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHTR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  83 QTAAVAAKLGLKCVALLENPIATHSENYLTNGNRLMLDLMDVEVVMVDA-LTQPAAQLAEQA-ERLEAQGFRPYILPVGG 160
Cdd:PRK12390  83 QVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVPDgFDIGIRKSWEDAlEDVRAAGGKPYAIPAGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 161 S-NALGALGYVECAQEIAHQSEGV-VDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQAL 238
Cdd:PRK12390 163 SdHPLGGLGFVGFAEEVRAQEAELgFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRIARNT 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 239 ATQLALE---AKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDGINQNRFRREGPLLFVHT 315
Cdd:PRK12390 243 AELVELGrdiTEDDVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSKVLYAHL 322


                 ....*....
gi 502791162 316 GGAPALFAY 324
Cdd:PRK12390 323 GGVPALNAY 331
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 5-324 1.80e-77

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 240.18  E-value: 1.80e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   5 LIHQFPRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLAMGGNKLRKLEFLAADALREGADVLLTAGAIQSNHVRQT 84
Cdd:PRK14045   8 LLSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  85 AAVAAKLGLKCVALLEnpiathSENYLtNGNRLMLDLMDVEVVMVDA-----LTQPAAQLAEQaerLEAQGFRPYILPVG 159
Cdd:PRK14045  88 GLAAKKLGLDAVLVLR------GKEEL-KGNYLLDKIMGIETRVYEAkdsfeLMKYAEEVAEE---LKGEGRKPYIIPPG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 160 GSNALGALGYVECAQEIAHQSEGV-VDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVAEQRPKVDALRQAL 238
Cdd:PRK14045 158 GASPVGTLGYVRAVGEIATQVKKLgVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKT 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 239 ATQLALEAKAPVTLWDDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPVYTGKAMAGLIDginqnrFRREGPL----LFVH 314
Cdd:PRK14045 238 KELLGVKVKVQEPELYDYSFGEYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMD------LAKKGELgekiLFIH 311

                        330
                 ....*....|
gi 502791162 315 TGGAPALFAY 324
Cdd:PRK14045 312 TGGISGTFHY 321
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-316 2.40e-52

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: 174.42  E-value: 2.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   12 IELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTPLamGGNKLRKLEFLAADALRE-GADVLLTAGAiqSNHVRQTAAVAAK 90
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKEGeGGKTVVEASS--GNHGRALAAAAAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   91 LGLKCVALLENPIathsenylTNGNRLMLDLMDVEVVMVDALTQPAAQLaeqAERLEAQGFRPYILPvGGSNALGALGYV 170
Cdd:pfam00291  77 LGLKVTIVVPEDA--------PPGKLLLMRALGAEVVLVGGDYDEAVAA---ARELAAEGPGAYYIN-QYDNPLNIEGYG 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  171 ECAQEIAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQLLPETELVGVTVSRNVA------EQRPKVDALRQALATQLAL 244
Cdd:pfam00291 145 TIGLEILEQLGGDPD--AVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPAlarslaAGRPVPVPVADTIADGLGV 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502791162  245 EAKAPVTLW---DDYFAPRYGEPNEEGMEAIKLLARLEGIFLDPvYTGKAMAGLiDGINQNRFRREGPLLFVHTG 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 3.29e-34

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: 125.32  E-value: 3.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLGRDIFIKRDDVTPlaMGGNKLRKLEFLAADALREG---ADVLLTAGAiqSNHVRQTAAVAAKLGLKC 95
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNP--TGSFKDRGALNLILLAEEEGklpKGVIIESTG--GNTGIALAAAAARLGLKC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  96 VALLEnpiATHSEnyltnGNRLMLDLMDVEVVMVDAlTQPAAQlaEQAERLEAQGFRPYILPvGGSNALGALGYVECAQE 175
Cdd:cd00640   77 TIVMP---EGASP-----EKVAQMRALGAEVVLVPG-DFDDAI--ALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGLE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 176 IAHQSEGvVDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGVTvsrnvaeqrPKVDALrqalatqlaleakapvtlwdd 255
Cdd:cd00640  145 ILEQLGG-QKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVE---------PEVVTV--------------------- 193

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502791162 256 yfaprygePNEEGMEAIKLLARLEGIFLDPVyTGKAMAGLIDGInqNRFRREGPLLFVHTGG 317
Cdd:cd00640  194 --------SDEEALEAIRLLAREEGILVEPS-SAAALAAALKLA--KKLGKGKTVVVILTGG 244
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 10-316 6.71e-11

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: 62.52  E-value: 6.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  10 PRIELLGAPTPLEYLPRLSDYLGRDIFIKRDDVTP--------LAMGGNKlrkleflaadALREGADVLLTA--GaiqsN 79
Cdd:COG0498   58 KAVSLGEGGTPLVKAPRLADELGKNLYVKEEGHNPtgsfkdraMQVAVSL----------ALERGAKTIVCAssG----N 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  80 HVRQTAAVAAKLGLKCVALlenpiatHSENYLTNGNRLMLDLMDVEVVMV-----DALtqpaAQLAEQAERLEaqgfrpy 154
Cdd:COG0498  124 GSAALAAYAARAGIEVFVF-------VPEGKVSPGQLAQMLTYGAHVIAVdgnfdDAQ----RLVKELAADEG------- 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 155 ILPVGGSNALGALGYVECAQEIAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQL--------LPetELVGVtVSRNVAe 226
Cdd:COG0498  186 LYAVNSINPARLEGQKTYAFEIAEQLGRVPD--WVVVPTGNGGNILAGYKAFKELkelglidrLP--RLIAV-QATGCN- 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 227 qrPKVDALRQALATqlaLEAKAPVTLWD--DYFAPRYGE----------------PNEEGMEAIKLLARLEGIFLDPvYT 288
Cdd:COG0498  260 --PILTAFETGRDE---YEPERPETIAPsmDIGNPSNGEralfalresggtavavSDEEILEAIRLLARREGIFVEP-AT 333

                        330       340
                 ....*....|....*....|....*...
gi 502791162 289 GKAMAGLIDGINQNRFRREGPLLFVHTG 316
Cdd:COG0498  334 AVAVAGLRKLREEGEIDPDEPVVVLSTG 361
PLN02550 PLN02550
threonine dehydratase
 19-218 2.86e-08

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 54.93  E-value: 2.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLGRDIFIKRDDVTPLAmgGNKLRKLEFLAADALREGadvlLTAGAIQS---NHVRQTAAVAAKLGlkC 95
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVF--SFKLRGAYNMMAKLPKEQ----LDKGVICSsagNHAQGVALSAQRLG--C 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  96 VALLENPIATHSENYLTngnrlmLDLMDVEVVMVDALTQPAAQLAEQaeRLEAQGfRPYILPVGGSNALGALGYVecAQE 175
Cdd:PLN02550 182 DAVIAMPVTTPEIKWQS------VERLGATVVLVGDSYDEAQAYAKQ--RALEEG-RTFIPPFDHPDVIAGQGTV--GME 250

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 502791162 176 IAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQLLPETELVGV 218
Cdd:PLN02550 251 IVRQHQGPLH--AIFVPVGGGGLIAGIAAYVKRVRPEVKIIGV 291
PRK06815 PRK06815
threonine/serine dehydratase;
18-218 4.61e-08

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 53.54  E-value: 4.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  18 PTPLEYLPRLSDYLGRDIFIKRDDVTPlaMGGNKLR----KLEFLAADALREGadvLLTAGAiqSNHVRQTAAVAAKLGL 93
Cdd:PRK06815  20 VTPLEHSPLLSQHTGCEVYLKCEHLQH--TGSFKFRgasnKLRLLNEAQRQQG---VITASS--GNHGQGVALAAKLAGI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  94 KcvALLENPiathsenylTNGNRLMLDLM-----DVEVVMVDALTqpaaqlAEQAERLEA--QGfRPYILPVGGSNALGA 166
Cdd:PRK06815  93 P--VTVYAP---------EQASAIKLDAIralgaEVRLYGGDALN------AELAARRAAeqQG-KVYISPYNDPQVIAG 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502791162 167 LGyvECAQEIAHQSEgvvDFAAVLVASGSAGTHAGLAVGLEQLLPETELVGV 218
Cdd:PRK06815 155 QG--TIGMELVEQQP---DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGC 201
PRK12483 PRK12483
threonine dehydratase; Reviewed
 19-239 2.99e-07

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 51.72  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLGRDIFIKRDDVTPLAmgGNKLR----KLEFLAADALREGadvLLTAGAiqSNHVRQTAAVAAKLGLK 94
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVF--SFKIRgaynKMARLPAEQLARG---VITASA--GNHAQGVALAAARLGVK 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  95 CVALLenPIATHS---ENYLTNGNrlmldlmdvEVVMV-----DALTQpAAQLAEQaerleaQGFrPYILPVGGSNALGA 166
Cdd:PRK12483 111 AVIVM--PRTTPQlkvDGVRAHGG---------EVVLHgesfpDALAH-ALKLAEE------EGL-TFVPPFDDPDVIAG 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502791162 167 LGYVecAQEIAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQLLPETELVGVtvsrnvaeQRPKVDALRQALA 239
Cdd:PRK12483 172 QGTV--AMEILRQHPGPLD--AIFVPVGGGGLIAGIAAYVKYVRPEIKVIGV--------EPDDSNCLQAALA 232
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
19-252 3.28e-07

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 51.68  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLGRDIFIKRDDVTPLAmgGNKLR----KLEFLAADALREGadvLLTAGAiqSNHVRQTAAVAAKLGLK 94
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVF--SFKLRgaynKMAQLTEEQLARG---VITASA--GNHAQGVALSAARLGIK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  95 cvALLENPIATHSenyltngnrlmldlmdvevVMVDALTQPAAQL----------AEQAERLEAQGFRPYILPVGGSNAL 164
Cdd:PRK09224  94 --AVIVMPVTTPD-------------------IKVDAVRAFGGEVvlhgdsfdeaYAHAIELAEEEGLTFIHPFDDPDVI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 165 GALGYVecAQEIAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQLLPETELVGVtvsrnvaeQRPKVDALRQalatqlAL 244
Cdd:PRK09224 153 AGQGTI--AMEILQQHPHPLD--AVFVPVGGGGLIAGVAAYIKQLRPEIKVIGV--------EPEDSACLKA------AL 214


                 ....*...
gi 502791162 245 EAKAPVTL 252
Cdd:PRK09224 215 EAGERVDL 222
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 19-218 3.31e-06

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: 47.89  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLGRDIFIKRDDVTPlaMGGNKLRKLEFLAADALREGA----DVLL--TAG----AIqsnhvrqtAAVA 88
Cdd:cd01561    3 TPLVRLNRLSPGTGAEIYAKLEFFNP--GGSVKDRIALYMIEDAEKRGLlkpgTTIIepTSGntgiGL--------AMVA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  89 AKLGLKCvallenpIATHSENYlTNGNRLMLDLMDVEVVMVDALTQPAAQLA-EQAERLEAQGFRpYILPVGGSNALGAL 167
Cdd:cd01561   73 AAKGYRF-------IIVMPETM-SEEKRKLLRALGAEVILTPEAEADGMKGAiAKARELAAETPN-AFWLNQFENPANPE 143

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502791162 168 GYVEC-AQEIAHQSEGVVDfaAVLVASGSAGTHAGLAVGLEQLLPETELVGV 218
Cdd:cd01561  144 AHYETtAPEIWEQLDGKVD--AFVAGVGTGGTITGVARYLKEKNPNVRIVGV 193
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 11-96 9.01e-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: 46.76  E-value: 9.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  11 RIELLGAPTPLEYLPRLSDYLGR-DIFIKRDDVTPLamGGNKLRKLEFLAADALREGADVLLT-AGAIQsnHVRQTAAVA 88
Cdd:cd06446   27 YKDYVGRPTPLYRAKRLSEYLGGaKIYLKREDLNHT--GAHKINNALGQALLAKRMGKKRVIAeTGAGQ--HGVATATAC 102


                 ....*...
gi 502791162  89 AKLGLKCV 96
Cdd:cd06446  103 ALFGLECE 110
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 16-95 2.81e-05

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 45.57  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  16 GAPTPLEYLPRLSDYLGRDIFIKRDDVtpLAMGGNKLRKLEFLAADALREG-ADVLLTAGAIQsnHVRQTAAVAAKLGLK 94
Cdd:PRK13803 269 GRPTPLTEAKRLSDIYGARIYLKREDL--NHTGSHKINNALGQALLAKRMGkTRIIAETGAGQ--HGVATATACALFGLK 344


                 .
gi 502791162  95 C 95
Cdd:PRK13803 345 C 345
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 19-316 1.25e-04

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: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  19 TPLEYLPRLSDYLG-RDIFIKRDDVTPlaMGGNKLRKLEFLAADALREGADVLLTAGAiqSNHVRQTAAVAAKLGLKCVA 97
Cdd:cd01563   23 TPLVRAPRLGERLGgKNLYVKDEGLNP--TGSFKDRGMTVAVSKAKELGVKAVACAST--GNTSASLAAYAARAGIKCVV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  98 LLENPIAThsenyltnGNRLMLDLMDVEVVMVDALTQPAAQLAEQAerleAQGFRPYILPVggSNALGALGYVECAQEIA 177
Cdd:cd01563   99 FLPAGKAL--------GKLAQALAYGATVLAVEGNFDDALRLVREL----AEENWIYLSNS--LNPYRLEGQKTIAFEIA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 178 HQSEG-VVDfaAVLVASGSAGTHAGLAVGLEQLlpetELVGVTvsrnvaEQRPKVDALRQALATQLALEAKAPVTLWDDY 256
Cdd:cd01563  165 EQLGWeVPD--YVVVPVGNGGNITAIWKGFKEL----KELGLI------DRLPRMVGVQAEGAAPIVRAFKEGKDDIEPV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162 257 FAP-------RYGEP---------------------NEEGMEAIKLLARLEGIFLDPVyTGKAMAGLIDGINQNRFRREG 308
Cdd:cd01563  233 ENPetiataiRIGNPasgpkalravresggtavavsDEEILEAQKLLARTEGIFVEPA-SAASLAGLKKLREEGIIDKGE 311


                 ....*...
gi 502791162 309 PLLFVHTG 316
Cdd:cd01563  312 RVVVVLTG 319
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 19-307 3.70e-04

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 41.60  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   19 TPLEYLPRLSDYLG-RDIFIKRDDVTPlaMGGNKLRKLEFLAADALREGADVLLTAGAiqSNHVRQTAAVAAKLGLKCVA 97
Cdd:TIGR00260  23 TPLFRAPALAANVGiKNLYVKELGHNP--TLSFKDRGMAVALTKALELGNDTVLCAST--GNTGAAAAAYAGKAGLKVVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162   98 LLenPIATHSENYLTNGnrlmldLM-DVEVVMV----DALTQPAAQLAEQAE------------RLEAQGFRPY------ 154
Cdd:TIGR00260  99 LY--PAGKISLGKLAQA------LGyNAEVVAIdgnfDDAQRLVKQLFEDKPalglnsansipyRLEGQKTYAFeaveql 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  155 --------ILPVGGSNALGA----------LGYVECAQEIAHQSEGVVDFAAVLVASGSAGTHAGLAvgleqllpetelv 216
Cdd:TIGR00260 171 gweapdkvVVPVPNSGNFGAiwkgfkekkmLGLDSLPVKRGIQAEGAADIVRAFLEGGQWEPIETPE------------- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  217 gvTVSRNVAEQRPkVDALRqalatqlALEAkAPVTLWddyfaprYGEP--NEEGMEAIKLLARLEGIFLDPvYTGKAMAG 294
Cdd:TIGR00260 238 --TLSTAMDIGNP-ANWPR-------ALEA-FRRSNG-------YAEDlsDEEILEAIKLLAREEGYFVEP-HSAVAVAA 298

                         330
                  ....*....|...
gi 502791162  295 LIDGINQNRFRRE 307
Cdd:TIGR00260 299 LLKLVEKGTADPA 311
PRK13028 PRK13028
tryptophan synthase subunit beta; Provisional
 11-96 1.99e-03

tryptophan synthase subunit beta; Provisional


Pssm-ID: 183851  Cd Length: 402  Bit Score: 39.46  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  11 RIELLGAPTPLEYLPRLSDYL-GRDIFIKRDDvtpLAMGGNklRKLEFLAADAL---REGADVLLT-AGAIQsnHVRQTA 85
Cdd:PRK13028  55 LKHYVGRPTPLYHAKRLSEELgGAQIYLKRED---LNHTGA--HKINNCLGQALlakRMGKKRLIAeTGAGQ--HGVATA 127

                         90
                 ....*....|.
gi 502791162  86 AVAAKLGLKCV 96
Cdd:PRK13028 128 TAAALFGLECE 138
PLN02618 PLN02618
tryptophan synthase, beta chain
 15-96 7.96e-03

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 37.81  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791162  15 LGAPTPLEYLPRLSDYLGR------DIFIKRDDVTplAMGGNKLRKLEFLAADALREGADVLLTA-GAIQsnHVRQTAAV 87
Cdd:PLN02618  63 VGRETPLYFAERLTEHYKRadgegpEIYLKREDLN--HTGAHKINNAVAQALLAKRLGKKRIIAEtGAGQ--HGVATATV 138


                 ....*....
gi 502791162  88 AAKLGLKCV 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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