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Conserved domains on  [gi|1985673024|emb|CAE6900260|]
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D-cysteine desulfhydrase [Pseudomonas marincola]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 6-330 3.67e-180

D-cysteine desulfhydrase; Validated


:

Pssm-ID: 179673  Cd Length: 331  Bit Score: 501.28  E-value: 3.67e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   6 SLSKFTRLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQT 85
Cdd:PRK03910    2 NLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  86 AAIAARLGLKCLALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVANLDNADEQLQEAADRLRANGRKPYIVPIGGSNAL 165
Cdd:PRK03910   82 AAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 166 GALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLN 245
Cdd:PRK03910  162 GALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELLG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 246 IAVP-DALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGGSPA 323
Cdd:PRK03910  242 LPTEiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGgNVLFIHTGGAPA 321


                  ....*..
gi 1985673024 324 LFAYHPA 330
Cdd:PRK03910  322 LFAYADA 328
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 6-330 3.67e-180

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 501.28  E-value: 3.67e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   6 SLSKFTRLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQT 85
Cdd:PRK03910    2 NLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  86 AAIAARLGLKCLALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVANLDNADEQLQEAADRLRANGRKPYIVPIGGSNAL 165
Cdd:PRK03910   82 AAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 166 GALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLN 245
Cdd:PRK03910  162 GALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELLG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 246 IAVP-DALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGGSPA 323
Cdd:PRK03910  242 LPTEiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGgNVLFIHTGGAPA 321


                  ....*..
gi 1985673024 324 LFAYHPA 330
Cdd:PRK03910  322 LFAYADA 328
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 9-329 2.56e-142

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: 404.56  E-value: 2.56e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   9 KFTRLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTAAI 88
Cdd:COG2515     1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  89 AARLGLKCLALLENpiassDRNYQSNGNRLLLDLFTCEVEHVANLD--NADEQLQEAADRLRANGRKPYIVPIGGSNALG 166
Cdd:COG2515    81 AAKLGLKCVLVLRG-----EEPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 167 ALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLNI 246
Cdd:COG2515   156 ALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 247 AVPDalQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGGSPALF 325
Cdd:COG2515   236 VSRA--DIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGsRVLFIHTGGLPGLF 313


                  ....
gi 1985673024 326 AYHP 329
Cdd:COG2515   314 GYAE 317
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 13-329 4.98e-134

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: 383.77  E-value: 4.98e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  13 LPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTAAIAARL 92
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  93 GLKCLALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVA--NLDNADEQLQEAADRLRANGRKPYIVPIGGSNALGALGY 170
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETRIESceEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 171 VRAGLELAEQIKlTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLNIAVpd 250
Cdd:TIGR01275 161 VEAALEIAQQLE-SEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTV-- 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985673024 251 ALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATGPVLFLHTGGSPALFAYHP 329
Cdd:TIGR01275 238 SAVIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDKPILFIHTGGIPGLFAYHD 316
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 20-320 4.67e-115

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: 335.16  E-value: 4.67e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGT--DVWVKRDDITP-FALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTAAIAARLGLKC 96
Cdd:cd06449     1 TPIQYLPRLSEHLGGkvEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  97 LALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVANLDNA--DEQLQEAADRLRANGRKPYIVPIGGS-NALGALGYVRA 173
Cdd:cd06449    81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFDIgiRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 174 GLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRT--AELLNIAVPDa 251
Cdd:cd06449   161 VLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKlaEEGLEVKEED- 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 252 lqIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGG 320
Cdd:cd06449   240 --VVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGsKVLFIHLGG 307
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-319 2.04e-51

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: 172.11  E-value: 2.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  19 PTPLEKLERLSSQLGTDVWVKRDDITPFalGGNKVRKLEFLAADAL-AQNADTLVTAGAiqSNHVRQTAAIAARLGLKCL 97
Cdd:pfam00291   7 PTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKeGEGGKTVVEASS--GNHGRALAAAAARLGLKVT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  98 ALLENPIassdrnyqSNGNRLLLDLFTCEVEHVanlDNADEQLQEAADRLRANGRKPYIVPiGGSNALGALGYVRAGLEL 177
Cdd:pfam00291  83 IVVPEDA--------PPGKLLLMRALGAEVVLV---GGDYDEAVAAARELAAEGPGAYYIN-QYDNPLNIEGYGTIGLEI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 178 AEQIkltGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLNIA-------VPD 250
Cdd:pfam00291 151 LEQL---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIAdglgvgdEPG 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985673024 251 ALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPvYTGKAFAGLLDGIANQQFATGPVLFLHTG 319
Cdd:pfam00291 228 ALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAALKLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
 6-330 3.67e-180

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 501.28  E-value: 3.67e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   6 SLSKFTRLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQT 85
Cdd:PRK03910    2 NLARFPRLELAGLPTPLEPLPRLSAALGPDIYIKRDDLTGLALGGNKTRKLEFLLADALAQGADTLITAGAIQSNHARQT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  86 AAIAARLGLKCLALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVANLDNADEQLQEAADRLRANGRKPYIVPIGGSNAL 165
Cdd:PRK03910   82 AAAAAKLGLKCVLLLENPVPTEAENYLANGNVLLDDLFGAEIHVVPAGTDMDAQLEELAEELRAQGRRPYVIPVGGSNAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 166 GALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLN 245
Cdd:PRK03910  162 GALGYVACALEIAQQLAEGGVDFDAVVVASGSGGTHAGLAAGLAALGPDIPVIGVTVSRSAAEQEPKVAKLAQATAELLG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 246 IAVP-DALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGGSPA 323
Cdd:PRK03910  242 LPTEiPRADIRLWDDYVGPGYGVPTDEMLEAVKLLARTEGILLDPVYTGKAMAGLIDLIRQGRFKKGgNVLFIHTGGAPA 321


                  ....*..
gi 1985673024 324 LFAYHPA 330
Cdd:PRK03910  322 LFAYADA 328
Acd COG2515
1-aminocyclopropane-1-carboxylate deaminase/D-cysteine desulfhydrase, PLP-dependent ACC family ...
 9-329 2.56e-142

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: 404.56  E-value: 2.56e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   9 KFTRLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTAAI 88
Cdd:COG2515     1 RFPRLPLAFLPTPLQPLPRLSAALGVELWIKRDDLTGPAIGGNKTRKLEYLLADALAQGADTLVTFGGAQSNHARATAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  89 AARLGLKCLALLENpiassDRNYQSNGNRLLLDLFTCEVEHVANLD--NADEQLQEAADRLRANGRKPYIVPIGGSNALG 166
Cdd:COG2515    81 AAKLGLKCVLVLRG-----EEPTPLNGNLLLDRLLGAELHFVSRGEyrDRDEAMEAVAAELRARGGKPYVIPEGGSNPLG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 167 ALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLNI 246
Cdd:COG2515   156 ALGYVEAAAELAAQLAELGVDFDYIVVASGSGGTLAGLVAGLALLGSDTRVIGISVLKGADFLRERVAELARATAALLGL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 247 AVPDalQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGGSPALF 325
Cdd:COG2515   236 VSRA--DIELDDDYHGGGYGKPTPELIEAIRLFARTEGILLDPVYTGKAMAGLIDLIRKGRFPPGsRVLFIHTGGLPGLF 313


                  ....
gi 1985673024 326 AYHP 329
Cdd:COG2515   314 GYAE 317
ACC_deam_rel TIGR01275
pyridoxal phosphate-dependent enzymes, D-cysteine desulfhydrase family; This model represents ...
 13-329 4.98e-134

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: 383.77  E-value: 4.98e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  13 LPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTAAIAARL 92
Cdd:TIGR01275   1 LELIGAPTPIQYLPRLSDYLGREIYIKRDDLTGLAMGGNKIRKLEFLLADALRKGADTVITAGAIQSNHARATAAVAAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  93 GLKCLALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVA--NLDNADEQLQEAADRLRANGRKPYIVPIGGSNALGALGY 170
Cdd:TIGR01275  81 GLHCVLLLRNPIGTTAENYLLNGNLLLDDLFGAETRIESceEYTDIDAQLEELAERLEKEGFKPYVIPVGGSNSLGALGY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 171 VRAGLELAEQIKlTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLNIAVpd 250
Cdd:TIGR01275 161 VEAALEIAQQLE-SEVKFDSIVVASGSGGTIAGLSLGLSHLMPDVELVGVTVSRFVADQTDKFVNLVQAIAEGLELTV-- 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985673024 251 ALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATGPVLFLHTGGSPALFAYHP 329
Cdd:TIGR01275 238 SAVIPLWDDYFGPGYGVPTSEGMEIVKKVASLEGIILDPVYTGKAFYGLIDGIRKKEFGDKPILFIHTGGIPGLFAYHD 316
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
 20-320 4.67e-115

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: 335.16  E-value: 4.67e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGT--DVWVKRDDITP-FALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTAAIAARLGLKC 96
Cdd:cd06449     1 TPIQYLPRLSEHLGGkvEIYAKRDDCNSgLAFGGNKIRKLEYLLPDALAKGADTLVTVGGIQSNHTRQVAAVAAKLGLKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  97 LALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVANLDNA--DEQLQEAADRLRANGRKPYIVPIGGS-NALGALGYVRA 173
Cdd:cd06449    81 VLVQENWVPYSDAVYDRVGNILLSRIMGADVRLVSAGFDIgiRKSFEEAAEEVEAKGGKPYVIPAGGSeHPLGGLGYVGF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 174 GLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRT--AELLNIAVPDa 251
Cdd:cd06449   161 VLEIAQQEEELGFKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQVLRIAQAKlaEEGLEVKEED- 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 252 lqIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATG-PVLFLHTGG 320
Cdd:cd06449   240 --VVLDDDYAAPEYGIPNDETIEAIKLCARLEGIITDPVYEGKSMQGMIDLVRNGEFKEGsKVLFIHLGG 307
PRK12390 PRK12390
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 6-327 1.64e-85

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 183494  Cd Length: 337  Bit Score: 261.12  E-value: 1.64e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   6 SLSKFTRLPLVNTPTPLEKLERLSSQLG--TDVWVKRDDITP-FALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHV 82
Cdd:PRK12390    2 NLQKFPRYPLTFGPTPIHPLKRLSAHLGgkVELYAKREDCNSgLAFGGNKTRKLEYLVPDALAQGADTLVSIGGVQSNHT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  83 RQTAAIAARLGLKCLALLENPIASSDRNYQSNGNRLLLDLFTCEVEHVAnlDNAD----EQLQEAADRLRANGRKPYIVP 158
Cdd:PRK12390   82 RQVAAVAAHLGMKCVLVQENWVNYEDAVYDRVGNILLSRIMGADVRLVP--DGFDigirKSWEDALEDVRAAGGKPYAIP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 159 IGGS-NALGALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLL 237
Cdd:PRK12390  160 AGASdHPLGGLGFVGFAEEVRAQEAELGFKFDYIVVCSVTGSTQAGMVVGFAADGRARRVIGIDASAKPEQTRAQVLRIA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 238 QRTAELLNIA--VPDAlQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDGIANQQFATGP-VL 314
Cdd:PRK12390  240 RNTAELVELGrdITED-DVVLDERYAGPEYGLPNEGTLEAIRLCARLEGMLTDPVYEGKSMHGMIDLVRKGEFPEGSkVL 318

                         330
                  ....*....|...
gi 1985673024 315 FLHTGGSPALFAY 327
Cdd:PRK12390  319 YAHLGGVPALNAY 331
PRK14045 PRK14045
1-aminocyclopropane-1-carboxylate deaminase; Provisional
 7-327 6.58e-80

1-aminocyclopropane-1-carboxylate deaminase; Provisional


Pssm-ID: 172537 [Multi-domain]  Cd Length: 329  Bit Score: 246.34  E-value: 6.58e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024   7 LSKFTRLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITPFALGGNKVRKLEFLAADALAQNADTLVTAGAIQSNHVRQTA 86
Cdd:PRK14045    9 LSKFPRVELIPWETPIQYLPNISRELGADVYVKRDDLTGLGIGGNKIRKLEYLLGDALSRGADVVITVGAVHSNHAFVTG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  87 AIAARLGLKCLALLENpiassdrNYQSNGNRLLLDLFTCEVEhVANLDNADEQL---QEAADRLRANGRKPYIVPIGGSN 163
Cdd:PRK14045   89 LAAKKLGLDAVLVLRG-------KEELKGNYLLDKIMGIETR-VYEAKDSFELMkyaEEVAEELKGEGRKPYIIPPGGAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 164 ALGALGYVRAGLELAEQIKLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAEL 243
Cdd:PRK14045  161 PVGTLGYVRAVGEIATQVKKLGVRFDSIVVAVGSGGTLAGLSLGLAILNAEWRVVGIAVGSFGEKMKEKVKNLVKKTKEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 244 LNIAVpDALQIELWDGYFApRYGEPNAATLQAISLLAATEGLLLDPVYTGKAFAGLLDgIANQQFATGPVLFLHTGGSPA 323
Cdd:PRK14045  241 LGVKV-KVQEPELYDYSFG-EYGKITKEVAKLIRSVGTMEGLILDPVYTGKAFYGLMD-LAKKGELGEKILFIHTGGISG 317


                  ....
gi 1985673024 324 LFAY 327
Cdd:PRK14045  318 TFHY 321
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 19-319 2.04e-51

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: 172.11  E-value: 2.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  19 PTPLEKLERLSSQLGTDVWVKRDDITPFalGGNKVRKLEFLAADAL-AQNADTLVTAGAiqSNHVRQTAAIAARLGLKCL 97
Cdd:pfam00291   7 PTPLVRLPRLSKELGVDVYLKLESLNPT--GSFKDRGALNLLLRLKeGEGGKTVVEASS--GNHGRALAAAAARLGLKVT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  98 ALLENPIassdrnyqSNGNRLLLDLFTCEVEHVanlDNADEQLQEAADRLRANGRKPYIVPiGGSNALGALGYVRAGLEL 177
Cdd:pfam00291  83 IVVPEDA--------PPGKLLLMRALGAEVVLV---GGDYDEAVAAARELAAEGPGAYYIN-QYDNPLNIEGYGTIGLEI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 178 AEQIkltGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQRPKVEGLLQRTAELLNIA-------VPD 250
Cdd:pfam00291 151 LEQL---GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIAdglgvgdEPG 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985673024 251 ALQIELWDGYFAPRYGEPNAATLQAISLLAATEGLLLDPvYTGKAFAGLLDGIANQQFATGPVLFLHTG 319
Cdd:pfam00291 228 ALALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEP-SSAAALAALKLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 20-320 5.70e-32

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: 119.54  E-value: 5.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGTDVWVKRDDITPFalGGNKVRKLEFLAADALAQ---NADTLVTAGAiqSNHVRQTAAIAARLGLKC 96
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPT--GSFKDRGALNLILLAEEEgklPKGVIIESTG--GNTGIALAAAAARLGLKC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  97 LALLENpiassdrnYQSNGNRLLLDLFTCEVEHV-ANLDNAdeqlQEAADRLRANGRKPYIVPiGGSNALGALGYVRAGL 175
Cdd:cd00640    77 TIVMPE--------GASPEKVAQMRALGAEVVLVpGDFDDA----IALAKELAEEDPGAYYVN-QFDNPANIAGQGTIGL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 176 ELAEQikLTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTvsrtdaaqrPKVegllqrtaellnIAVPDalqie 255
Cdd:cd00640   144 EILEQ--LGGQKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVE---------PEV------------VTVSD----- 195

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985673024 256 lwdgyfaprygepnAATLQAISLLAATEGLLLDPVyTGKAFAGLLDGiANQQFATGPVLFLHTGG 320
Cdd:cd00640   196 --------------EEALEAIRLLAREEGILVEPS-SAAALAAALKL-AKKLGKGKTVVVILTGG 244
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 20-301 1.49e-09

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: 57.91  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGTDVWVKRDDITPFalGGNKVRKLEFLAADALAQNA----DTLV--TAG----AIqsnhvrqtAAIA 89
Cdd:cd01561     3 TPLVRLNRLSPGTGAEIYAKLEFFNPG--GSVKDRIALYMIEDAEKRGLlkpgTTIIepTSGntgiGL--------AMVA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  90 ARLGLKCLALLenPiassdrNYQSNGNRLLLDLFTCEVEHVANLDNAD-EQLQEAADRLRANGRKpYIVPIGGSNALGAL 168
Cdd:cd01561    73 AAKGYRFIIVM--P------ETMSEEKRKLLRALGAEVILTPEAEADGmKGAIAKARELAAETPN-AFWLNQFENPANPE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 169 GYVRA-GLELAEQiklTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGV------TVSRTDAAQRpKVEGL-LQRT 240
Cdd:cd01561   144 AHYETtAPEIWEQ---LDGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVdpvgsvLFSGGPPGPH-KIEGIgAGFI 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985673024 241 AELLNIAVPD-ALQIELWDGYFAPRYgepnaatlqaislLAATEGLLLDPVyTGKAFAGLLD 301
Cdd:cd01561   220 PENLDRSLIDeVVRVSDEEAFAMARR-------------LAREEGLLVGGS-SGAAVAAALK 267
PLN02550 PLN02550
threonine dehydratase
 20-227 1.65e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 52.62  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGTDVWVKRDDITP---FALGGnkvrkleflAADALAQNADTLVTAGAIQS---NHVRQTAAIAARLG 93
Cdd:PLN02550  110 SPLQLAKKLSERLGVKVLLKREDLQPvfsFKLRG---------AYNMMAKLPKEQLDKGVICSsagNHAQGVALSAQRLG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  94 lkCLALLENPIASSDRNYQSngnrllLDLFTCEVEHVAnlDNADEQLQEAADRLRANGRKpYIVPIGGSNALGALGYVra 173
Cdd:PLN02550  181 --CDAVIAMPVTTPEIKWQS------VERLGATVVLVG--DSYDEAQAYAKQRALEEGRT-FIPPFDHPDVIAGQGTV-- 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985673024 174 GLELAEQIKltgEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDA 227
Cdd:PLN02550  248 GMEIVRQHQ---GPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANA 298
PRK06815 PRK06815
threonine/serine dehydratase;
19-220 2.26e-06

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 48.54  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  19 PTPLEKLERLSSQLGTDVWVKRDDITPfaLGGNKVR----KLEFLAAdalAQNADTLVTAGAiqSNHVRQTAAIAARLGL 94
Cdd:PRK06815   20 VTPLEHSPLLSQHTGCEVYLKCEHLQH--TGSFKFRgasnKLRLLNE---AQRQQGVITASS--GNHGQGVALAAKLAGI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  95 KclALLENPIASS----DRNYQSNGNRLLLDLFTCEVEhvanldnadeqlqEAADRLRANGRKPYIVPIGGSNALGALGY 170
Cdd:PRK06815   93 P--VTVYAPEQASaiklDAIRALGAEVRLYGGDALNAE-------------LAARRAAEQQGKVYISPYNDPQVIAGQGT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1985673024 171 VraGLELAEQIkltgEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGV 220
Cdd:PRK06815  158 I--GMELVEQQ----PDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGC 201
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
20-95 3.60e-06

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 48.21  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGTDVWVKRDDITP---FALGG--NKVRKlefLAADALAQNadtLVTAGAiqSNHVRQTAAIAARLGL 94
Cdd:PRK09224   21 TPLEKAPKLSARLGNQVLLKREDLQPvfsFKLRGayNKMAQ---LTEEQLARG---VITASA--GNHAQGVALSAARLGI 92


                  .
gi 1985673024  95 K 95
Cdd:PRK09224   93 K 93
PRK12483 PRK12483
threonine dehydratase; Reviewed
 20-95 1.32e-05

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 46.71  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGTDVWVKRDDITP-FALggnKVR----KLEFLAADALAQNadtLVTAGAiqSNHVRQTAAIAARLGL 94
Cdd:PRK12483   38 TPLQRAPNLSARLGNQVLLKREDLQPvFSF---KIRgaynKMARLPAEQLARG---VITASA--GNHAQGVALAAARLGV 109


                  .
gi 1985673024  95 K 95
Cdd:PRK12483  110 K 110
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 20-300 2.56e-05

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: 45.58  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  20 TPLEKLERLSSQLGTDVWVKRdditpfaLGGN-----KVRKLEFLAADALAQNADTLVTA--GaiqsNHVRQTAAIAARL 92
Cdd:COG0498    67 TPLVKAPRLADELGKNLYVKE-------EGHNptgsfKDRAMQVAVSLALERGAKTIVCAssG----NGSAALAAYAARA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  93 GLKCLALL-ENPIassdrnyqSNGNR---LLLDLFTCEVEhvANLDNADEQLQEAADRLRangrkpyIVPIGGSNALGAL 168
Cdd:COG0498   136 GIEVFVFVpEGKV--------SPGQLaqmLTYGAHVIAVD--GNFDDAQRLVKELAADEG-------LYAVNSINPARLE 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 169 GYVRAGLELAEQIkltGEQFSAVVLASGSAGTHSGLALA--------LEYALPgtRVVGV------TVSRTDAAQRPKVE 234
Cdd:COG0498   199 GQKTYAFEIAEQL---GRVPDWVVVPTGNGGNILAGYKAfkelkelgLIDRLP--RLIAVqatgcnPILTAFETGRDEYE 273

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985673024 235 GLLQRT-AELLNIAVP-------DALQIELWDGYFAprygePNAATLQAISLLAATEGLLLDPvYTGKAFAGLL 300
Cdd:COG0498   274 PERPETiAPSMDIGNPsngeralFALRESGGTAVAV-----SDEEILEAIRLLARREGIFVEP-ATAVAVAGLR 341
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 19-230 4.95e-05

Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440784 [Multi-domain]  Cd Length: 327  Bit Score: 44.26  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  19 PTPLEKLERLSSQLGTDVWVKRDDITP---F-ALGG-NKVRKlefLAADALAQnadTLVTA--GaiqsNHVRQTAAIAAR 91
Cdd:COG1171    24 RTPLLRSPTLSERLGAEVYLKLENLQPtgsFkLRGAyNALAS---LSEEERAR---GVVAAsaG----NHAQGVAYAARL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  92 LGLKCLallenpI-----ASSDRnyqsngnrllldlftceVEHVANL--------DNADEQLQEAADRLRANGRK----- 153
Cdd:COG1171    94 LGIPAT------IvmpetAPAVK-----------------VAATRAYgaevvlhgDTYDDAEAAAAELAEEEGATfvhpf 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985673024 154 --PYIVpiggsnalgaLGYVRAGLELAEQIkltgEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGVTVSRTDAAQR 230
Cdd:COG1171   151 ddPDVI----------AGQGTIALEILEQL----PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYR 215
PRK08639 PRK08639
threonine dehydratase; Validated
 12-220 1.20e-04

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 43.64  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  12 RLPLVNTPTPLEKLERLSSQLGTDVWVKRDDITP---FALGG--NKVRKLeflaadALAQNADTLVTAGAiqSNHVrQTA 86
Cdd:PRK08639   18 RLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPvrsYKLRGayNAISQL------SDEELAAGVVCASA--GNHA-QGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  87 AIAAR-LGLKclALLENPIASS----DRnyqsngnrllLDLFTCE-VEHVANLDNADEQLQEAADRLRANGRkPYIVPIG 160
Cdd:PRK08639   89 AYACRhLGIP--GVIFMPVTTPqqkiDQ----------VRFFGGEfVEIVLVGDTFDDSAAAAQEYAEETGA-TFIPPFD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024 161 GSNALGALGYVraGLELAEQIKlTGEQFSAVVLASGSAGTHSGLALALEYALPGTRVVGV 220
Cdd:PRK08639  156 DPDVIAGQGTV--AVEILEQLE-KEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGV 212
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 19-96 1.91e-03

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: 39.44  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985673024  19 PTPLEKLERLSSQL-GTDVWVKRDDITPfaLGGNKVRkleflaaDALAQ-------NADTLVT-AGAIQsnHVRQTAAIA 89
Cdd:cd06446    34 PTPLYRAKRLSEYLgGAKIYLKREDLNH--TGAHKIN-------NALGQallakrmGKKRVIAeTGAGQ--HGVATATAC 102


                  ....*..
gi 1985673024  90 ARLGLKC 96
Cdd:cd06446   103 ALFGLEC 109
 
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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