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Conserved domains on  [gi|1330027541|ref|WP_102280711|]
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cysteine synthase A [Vibrio lentus]

Protein Classification

cysteine synthase A( domain architecture ID 10793448)

cysteine synthase A (CysK/CysB/CysE) catalyzes the conversion of O-succinyl-L-serine/O-acetyl-L-serine into cysteine, the last step in the cysteine biosynthesis pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10717 PRK10717
cysteine synthase A; Provisional
 6-325 0e+00

cysteine synthase A; Provisional


:

Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 518.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALV 85
Cdd:PRK10717    3 IFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  86 AKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVEN-----ENYWWADQFENLSNYRAHY 160
Cdd:PRK10717   83 AAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELvasepNGAIWANQFDNPANREAHY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 161 LNTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFLRNGQYQSTGSSFTEGIGIMRTV 240
Cdd:PRK10717  163 ETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQGRIT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 241 ENFRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYSKLHNEAFLK 320
Cdd:PRK10717  243 ANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLR 322


                  ....*
gi 1330027541 321 EKEIQ 325
Cdd:PRK10717  323 EKGLP 327
 
Name Accession Description Interval E-value
PRK10717 PRK10717
cysteine synthase A; Provisional
 6-325 0e+00

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 518.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALV 85
Cdd:PRK10717    3 IFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  86 AKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVEN-----ENYWWADQFENLSNYRAHY 160
Cdd:PRK10717   83 AAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELvasepNGAIWANQFDNPANREAHY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 161 LNTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFLRNGQYQSTGSSFTEGIGIMRTV 240
Cdd:PRK10717  163 ETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQGRIT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 241 ENFRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYSKLHNEAFLK 320
Cdd:PRK10717  243 ANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLR 322


                  ....*
gi 1330027541 321 EKEIQ 325
Cdd:PRK10717  323 EKGLP 327
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 6-312 1.47e-130

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


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 374.77  E-value: 1.47e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALV 85
Cdd:COG0031     3 IYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  86 AKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYLNTGP 165
Cdd:COG0031    83 AAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA--EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 166 EIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSflrnGqyQSTGSSFTEGIGIMRTVENFRQ 245
Cdd:COG0031   161 EIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLS----G--GEPGPHKIEGIGAGFVPKILDP 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330027541 246 AKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYSK 312
Cdd:COG0031   235 SLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 15-308 1.25e-128

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: 369.54  E-value: 1.25e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALVAKSLGYKML 94
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  95 VVMPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYLNTGPEIWQQTQGN 174
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 175 IDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFlrngqyQSTGSSFTEGIGIMRTVENFRQAKINRAITL 254
Cdd:cd01561   161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVVRV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330027541 255 PDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAER 308
Cdd:cd01561   235 SDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGER 288
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 11-311 4.86e-82

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 251.52  E-value: 4.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  11 SELIGDTDLVRINSLSEISGcEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALVAKSLG 90
Cdd:TIGR01139   2 SELIGNTPLVRLNRIEGCNA-NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  91 YKMLVVMPRGQAQEKERMISLYNAELLLVDPC---PFANPEhfyhtAKRIGVENENYWW-ADQFENLSNYRAHYLNTGPE 166
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAegmKGAIAK-----AEEIAASTPNSYFmLQQFENPANPEIHRKTTGPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 167 IWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIysfLRNGQyqsTGSSFTEGIGIMRTVENFRQA 246
Cdd:TIGR01139 156 IWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV---LSGGK---PGPHKIQGIGAGFIPKNLNRS 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330027541 247 KINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYS 311
Cdd:TIGR01139 230 VIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 10-304 2.66e-69

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: 218.72  E-value: 2.66e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  10 LSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAgklKPGMTIVEGTAGNAGIGLALVAKSL 89
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  90 GYKMLVVMPRGQAQEKERMISLYNAELLLVDpcpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAhYLNTGPEIWQ 169
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVG----GDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEILE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 170 QTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSG-IYSFLRNGQYQ--STGSSFTEGIGIMRTVENF--- 243
Cdd:pfam00291 153 QLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPaLARSLAAGRPVpvPVADTIADGLGVGDEPGALald 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330027541 244 -RQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYA-AARMGKGKTIVTFSCD 304
Cdd:pfam00291 233 lLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
PRK10717 PRK10717
cysteine synthase A; Provisional
 6-325 0e+00

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 518.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALV 85
Cdd:PRK10717    3 IFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  86 AKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVEN-----ENYWWADQFENLSNYRAHY 160
Cdd:PRK10717   83 AAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNNYVKGAGRLAEELvasepNGAIWANQFDNPANREAHY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 161 LNTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFLRNGQYQSTGSSFTEGIGIMRTV 240
Cdd:PRK10717  163 ETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQGRIT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 241 ENFRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYSKLHNEAFLK 320
Cdd:PRK10717  243 ANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLR 322


                  ....*
gi 1330027541 321 EKEIQ 325
Cdd:PRK10717  323 EKGLP 327
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 6-312 1.47e-130

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


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 374.77  E-value: 1.47e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALV 85
Cdd:COG0031     3 IYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  86 AKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYLNTGP 165
Cdd:COG0031    83 AAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA--EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 166 EIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSflrnGqyQSTGSSFTEGIGIMRTVENFRQ 245
Cdd:COG0031   161 EIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLS----G--GEPGPHKIEGIGAGFVPKILDP 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330027541 246 AKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYSK 312
Cdd:COG0031   235 SLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 15-308 1.25e-128

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: 369.54  E-value: 1.25e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALVAKSLGYKML 94
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  95 VVMPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYLNTGPEIWQQTQGN 174
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILTPEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 175 IDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFlrngqyQSTGSSFTEGIGIMRTVENFRQAKINRAITL 254
Cdd:cd01561   161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSG------GPPGPHKIEGIGAGFIPENLDRSLIDEVVRV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330027541 255 PDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAER 308
Cdd:cd01561   235 SDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGER 288
PLN02356 PLN02356
phosphateglycerate kinase
 1-321 3.14e-94

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 286.89  E-value: 3.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   1 MSSAQIANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGI 80
Cdd:PLN02356   38 LSKKKPRNGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAI 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  81 GLALVAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVENENY---------------- 144
Cdd:PLN02356  118 SLATVAPAYGCKCHVVIPDDVAIEKSQILEALGATVERVRPVSITHKDHYVNIARRRALEANELaskrrkgsetdgihle 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 145 -----------------------WWADQFENLSNYRAHYLNTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPN 201
Cdd:PLN02356  198 ktngciseeekenslfsssctggFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPN 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 202 LETWLVDPNGSGIYSFLRNG-----------QYQSTGSSFTEGIGIMRTVENFRQAKINRAITLPDQDLVTISRLVAEHD 270
Cdd:PLN02356  278 IKCFLIDPPGSGLFNKVTRGvmytreeaegrRLKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKND 357

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330027541 271 GILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYSKLHNEAFLKE 321
Cdd:PLN02356  358 GLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQ 408
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 11-311 4.86e-82

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 251.52  E-value: 4.86e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  11 SELIGDTDLVRINSLSEISGcEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALVAKSLG 90
Cdd:TIGR01139   2 SELIGNTPLVRLNRIEGCNA-NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  91 YKMLVVMPRGQAQEKERMISLYNAELLLVDPC---PFANPEhfyhtAKRIGVENENYWW-ADQFENLSNYRAHYLNTGPE 166
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAegmKGAIAK-----AEEIAASTPNSYFmLQQFENPANPEIHRKTTGPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 167 IWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIysfLRNGQyqsTGSSFTEGIGIMRTVENFRQA 246
Cdd:TIGR01139 156 IWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV---LSGGK---PGPHKIQGIGAGFIPKNLNRS 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330027541 247 KINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCDLAERSYS 311
Cdd:TIGR01139 230 VIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 6-345 9.86e-81

cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273464 [Multi-domain]  Cd Length: 455  Bit Score: 253.18  E-value: 9.86e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALV 85
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  86 AKSLGYKMLVVMPRGQAQEKERMISLYNAElLLVDP--CPFANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYLNT 163
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAE-IVRTPtaAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 164 GPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSgIYSFLRNGQYQSTGSSFTEGIGimrtvENF 243
Cdd:TIGR01137 160 GPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEELNQTGRTPYKVEGIG-----YDF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 244 RQAKINRA-----ITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGK-GKTIVTFSCDlAERSY-SKLHNE 316
Cdd:TIGR01137 234 IPTVLDRKvvdewIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQeGQRCVVLLPD-SIRNYmTKFLND 312

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1330027541 317 AFLKEKEIqLNKENLS---QLWSRYQAEDGSM 345
Cdd:TIGR01137 313 EWMLDNGF-LDDEDLTvkdVLWWHARVKDLHL 343
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 17-304 1.03e-71

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: 223.16  E-value: 1.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLkPGMTIVEGTAGNAGIGLALVAKSLGYKMLVV 96
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  97 MPRGQAQEKERMISLYNAELLLVDpcpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYlNTGPEIWQQTQG-NI 175
Cdd:cd00640    80 MPEGASPEKVAQMRALGAEVVLVP----GDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 176 DALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPngsgiysflrngqyqstgssftegigimrtvenfrqakinRAITLP 255
Cdd:cd00640   155 DAVVVPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------EVVTVS 194

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1330027541 256 DQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGKTIVTFSCD 304
Cdd:cd00640   195 DEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTG 243
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 10-304 2.66e-69

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: 218.72  E-value: 2.66e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  10 LSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAgklKPGMTIVEGTAGNAGIGLALVAKSL 89
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  90 GYKMLVVMPRGQAQEKERMISLYNAELLLVDpcpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAhYLNTGPEIWQ 169
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVG----GDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEILE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 170 QTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSG-IYSFLRNGQYQ--STGSSFTEGIGIMRTVENF--- 243
Cdd:pfam00291 153 QLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPaLARSLAAGRPVpvPVADTIADGLGVGDEPGALald 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330027541 244 -RQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYA-AARMGKGKTIVTFSCD 304
Cdd:pfam00291 233 lLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGELKGGDRVVVVLTG 295
cysM PRK11761
cysteine synthase CysM;
8-308 2.60e-65

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 208.57  E-value: 2.60e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   8 NNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALVAK 87
Cdd:PRK11761    4 PTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  88 SLGYKMLVVMPRGQAQEKERMISLYNAELLLVDpcpfanpehfyhtaKRIGVE-----------NENYWWADQFENLSNY 156
Cdd:PRK11761   84 IKGYRMKLIMPENMSQERRAAMRAYGAELILVP--------------KEQGMEgardlalqmqaEGEGKVLDQFANPDNP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 157 RAHYLNTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPN-GSGIysflrngqyqstgssftegIG 235
Cdd:PRK11761  150 LAHYETTGPEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEeGSSI-------------------PG 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 236 IMRTVEN-----FRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSslnvAGALYAAARMGK---GKTIVTFSCDLAE 307
Cdd:PRK11761  211 IRRWPEEylpkiFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSS----GGAVAAALRIARenpNAVIVAIICDRGD 286


                  .
gi 1330027541 308 R 308
Cdd:PRK11761  287 R 287
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 10-311 8.46e-64

cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]


Pssm-ID: 130208 [Multi-domain]  Cd Length: 290  Bit Score: 204.38  E-value: 8.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  10 LSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTIVEGTAGNAGIGLALVAKSL 89
Cdd:TIGR01138   2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  90 GYKMLVVMPRGQAQEKERMISLYNAELLLVDPcpfanpEHFYHTAKRIGVENENYW---WADQFENLSNYRAHYLNTGPE 166
Cdd:TIGR01138  82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTK------EEGMEGARDLALELANRGegkLLDQFNNPDNPYAHYTSTGPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 167 IWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDP-NGSGIYSFLRngqyqsTGSSFTEGIgimrtvenFRQ 245
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPeEGSSIPGIRR------WPTEYLPGI--------FDA 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330027541 246 AKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMGKGkTIVTFSCDLAERSYS 311
Cdd:TIGR01138 222 SLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDA-VVVAIICDRGDRYLS 286
PLN02565 PLN02565
cysteine synthase
 5-323 1.14e-59

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 194.76  E-value: 1.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   5 QIANNLSELIGDTDLVRINSLSEisGCE--ILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTI-VEGTAGNAGIG 81
Cdd:PLN02565    4 SIAKDVTELIGKTPLVYLNNVVD--GCVarIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  82 LALVAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYL 161
Cdd:PLN02565   82 LAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPA--KGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 162 NTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFLRNGQY--QSTGSSFTEGIgimrt 239
Cdd:PLN02565  160 TTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHkiQGIGAGFIPGV----- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 240 venFRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAAR-MGKGKTIVTFSCDLAERSYSKLHNEAF 318
Cdd:PLN02565  235 ---LDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLFESV 311


                  ....*
gi 1330027541 319 LKEKE 323
Cdd:PLN02565  312 KKEAE 316
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 1-323 6.09e-53

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 178.62  E-value: 6.09e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   1 MSSAQIANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPG-MTIVEGTAGNAG 79
Cdd:PLN02556   44 LPGTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGkTTLIEPTSGNMG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  80 IGLALVAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANPEhfYHTAKRIGVENENYWWADQFENLSNYRAH 159
Cdd:PLN02556  124 ISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGT--VKKAYELLESTPDAFMLQQFSNPANTQVH 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 160 YLNTGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFLRNGQYQSTGS--SFTEGIGIM 237
Cdd:PLN02556  202 FETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNgvGFKPDILDM 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 238 RTVEnfrqakinRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALyAAARM--GKGKTIVTFSCDLAERSYSKLHN 315
Cdd:PLN02556  282 DVME--------KVLEVSSEDAVNMARELALKEGLMVGISSGANTVAAL-RLAKMpeNKGKLIVTVHPSFGERYLSSVLF 352


                  ....*...
gi 1330027541 316 EAFLKEKE 323
Cdd:PLN02556  353 QELRKEAE 360
PLN00011 PLN00011
cysteine synthase
 6-323 1.27e-52

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 176.73  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLseISGC--EILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGM-TIVEGTAGNAGIGL 82
Cdd:PLN00011    7 IKNDVTELIGNTPMVYLNNI--VDGCvaRIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKsTLIEATAGNTGIGL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  83 ALVAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCpfANPEHFYHTAKRIGVENENYWWADQFENLSNYRAHYLN 162
Cdd:PLN00011   85 ACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQS--IGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 163 TGPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSflrNGQyqsTGSSFTEGIGIMRTVEN 242
Cdd:PLN00011  163 TGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLS---GGQ---PGPHLIQGIGSGIIPFN 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 243 FRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAAR-MGKGKTIVTFSCDLAERSYSKLHNEAFLKE 321
Cdd:PLN00011  237 LDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVIFPSGGERYLSTKLFESVRYE 316


                  ..
gi 1330027541 322 KE 323
Cdd:PLN00011  317 AE 318
PLN03013 PLN03013
cysteine synthase
 6-291 9.58e-51

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 174.58  E-value: 9.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   6 IANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTI-VEGTAGNAGIGLAL 84
Cdd:PLN03013  113 IADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAF 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  85 VAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANPEhfYHTAKRIGVENENYWWADQFENLSNYRAHYLNTG 164
Cdd:PLN03013  193 IAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGA--VQKAEEILKNTPDAYMLQQFDNPANPKIHYETTG 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 165 PEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSFLRNGQYQstgssfTEGIGIMRTVENFR 244
Cdd:PLN03013  271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHK------IQGIGAGFIPKNLD 344

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1330027541 245 QAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAAR 291
Cdd:PLN03013  345 QKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKR 391
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 7-299 3.78e-24

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


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 100.25  E-value: 3.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   7 ANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPgmtIVEGTAGNAGIGLALVA 86
Cdd:cd01562     8 AARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKG---VVAASAGNHAQGVAYAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  87 KSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPcpfaNPEHFYHTAKRIgVENENYWWADQFENLsnyraHYLN---- 162
Cdd:cd01562    85 KLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGE----DFDEAEAKAREL-AEEEGLTFIHPFDDP-----DVIAgqgt 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 163 TGPEIWQQTqGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGS-GIYSFLRNGQYQS--TGSSFTEGIGIMRT 239
Cdd:cd01562   155 IGLEILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGApAMAQSLAAGKPVTlpEVDTIADGLAVKRP 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330027541 240 -VENFR--QAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMgKGKTIV 299
Cdd:cd01562   234 gELTFEiiRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDL-KGKKVV 295
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 17-303 1.16e-20

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: 90.87  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDR----AALQLVMDAVEAGklkpgmtIVEGTAGNAGIGLALVAKSLGYK 92
Cdd:COG1171    25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRgaynALASLSEEERARG-------VVAASAGNHAQGVAYAARLLGIP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  93 MLVVMPRGQAQEKERMISLYNAELLLVDPcpfaNPEHFYHTAKRIgVENENywwadqfenlsnyrAHYLN---------- 162
Cdd:COG1171    98 ATIVMPETAPAVKVAATRAYGAEVVLHGD----TYDDAEAAAAEL-AEEEG--------------ATFVHpfddpdviag 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 163 ---TGPEIWQQtQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGS-GIYSFLRNGQYQS--TGSSFTEGIGI 236
Cdd:COG1171   159 qgtIALEILEQ-LPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAaAMYRSLAAGEPVTlpGVDTIADGLAV 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 237 MRTVE-NFR--QAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMgKGKTIVTFSC 303
Cdd:COG1171   238 GRPGElTFEilRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERL-KGKRVVVVLS 306
PRK06815 PRK06815
threonine/serine dehydratase;
17-303 2.14e-20

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 90.14  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQlVMDAVEAGKLKPGmtIVEGTAGNAGIGLALVAKSLGYKMLVV 96
Cdd:PRK06815   21 TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASN-KLRLLNEAQRQQG--VITASSGNHGQGVALAAKLAGIPVTVY 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  97 MPRGQAQEKERMISLYNAELLLVDPCPFANPEHFYHTAKRIGVEnenYwwadqfenLSNYR-----AHYLNTGPEIWQQt 171
Cdd:PRK06815   98 APEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKV---Y--------ISPYNdpqviAGQGTIGMELVEQ- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 172 QGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDP-NGSGIYSFLRNGQY-----QSTGSSFTEGiGIMRTVENFR- 244
Cdd:PRK06815  166 QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPaNSPSLYTSLEAGEIvevaeQPTLSDGTAG-GVEPGAITFPl 244

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 245 -QAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMgKGKTIVTFSC 303
Cdd:PRK06815  245 cQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY-QGKKVAVVLC 303
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 15-190 1.30e-14

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: 73.40  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRINSLSEISG-CEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKlkpgMTIVEGTAGNAGIGLALVAKSLGYKM 93
Cdd:cd01563    21 GNTPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  94 LVVMPRGQAQEKERMISLYNAELLLVDpcpfANPEHFYHTAKRIGvenENYWWAdqFENLSN-YRAHYLNT-GPEIWQQT 171
Cdd:cd01563    97 VVFLPAGKALGKLAQALAYGATVLAVE----GNFDDALRLVRELA---EENWIY--LSNSLNpYRLEGQKTiAFEIAEQL 167

                         170       180
                  ....*....|....*....|
gi 1330027541 172 QGNI-DALVSVVGTGGTIAG 190
Cdd:cd01563   168 GWEVpDYVVVPVGNGGNITA 187
PRK12483 PRK12483
threonine dehydratase; Reviewed
 16-299 4.81e-13

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 69.83  E-value: 4.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  16 DTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAAL----QLVMDAVEAGklkpgmtIVEGTAGNAGIGLALVAKSLGY 91
Cdd:PRK12483   37 ETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYnkmaRLPAEQLARG-------VITASAGNHAQGVALAAARLGV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  92 KMLVVMPRGQAQEKERMISLYNAELLLVDPcpfANPEHFYHTAKRigVENENYWWADQFENlSNYRAHYLNTGPEIWQQT 171
Cdd:PRK12483  110 KAVIVMPRTTPQLKVDGVRAHGGEVVLHGE---SFPDALAHALKL--AEEEGLTFVPPFDD-PDVIAGQGTVAMEILRQH 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 172 QGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGS-GIYSFLRNGQYQSTGS--SFTEGIGIMRT-VENFR--Q 245
Cdd:PRK12483  184 PGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSnCLQAALAAGERVVLGQvgLFADGVAVAQIgEHTFElcR 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330027541 246 AKINRAITLPDQDLVTISRLVAEHDGILLGSSSSLNVAGALYAAARMG-KGKTIV 299
Cdd:PRK12483  264 HYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKKYAEREGiEGQTLV 318
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 15-120 5.42e-13

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: 69.46  E-value: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRaALQLVM-DAVEAGKLkpgmTIVEGTAGNAGIGLALVAKSLGYKM 93
Cdd:COG0498    65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDR-AMQVAVsLALERGAK----TIVCASSGNGSAALAAYAARAGIEV 139

                          90       100
                  ....*....|....*....|....*...
gi 1330027541  94 LVVMPRGQ-AQEKERMISLYNAELLLVD 120
Cdd:COG0498   140 FVFVPEGKvSPGQLAQMLTYGAHVIAVD 167
PRK06608 PRK06608
serine/threonine dehydratase;
1-324 5.00e-12

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 65.95  E-value: 5.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   1 MSSAQIANN-LSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPgmTIVEGTAGNAG 79
Cdd:PRK06608    7 PQNIAAAHNrIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  80 IGLALVAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVDPCPFANpehfyhtaKRIGVENEN-YWWADQFENLSNY-- 156
Cdd:PRK06608   85 QAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAE--------EKAKEDEEQgFYYIHPSDSDSTIag 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 157 --RAHYlntgpEIWQQTQGNIDALVSVVGTGGTIAGNshYLSEQ--QPNLETWLVDP-NGSGIYSFLRNGQ---YQSTGS 228
Cdd:PRK06608  157 agTLCY-----EALQQLGFSPDAIFASCGGGGLISGT--YLAKEliSPTSLLIGSEPlNANDAYLSLKNNKiyrLNYSPN 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 229 SFTEGIGIM----RTVENFRqaKINRAITLPDQD-------LVTISRLVAEhdgillgSSSSLN-VAGALYAAARMGKGK 296
Cdd:PRK06608  230 TIADGLKTLsvsaRTFEYLK--KLDDFYLVEEYEiyywtawLTHLLKVICE-------PSSAINmVAVVNWLKTQSKPQK 300

                         330       340
                  ....*....|....*....|....*....
gi 1330027541 297 TIVTFS-CDLAERSYSKLHNEAFLKEKEI 324
Cdd:PRK06608  301 LLVILSgGNIDPILYNELWKEDYLTIPPK 329
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
10-118 8.15e-11

bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 62.45  E-value: 8.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  10 LSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKpgmTIVEGTAGNAGIGLALVAKSL 89
Cdd:PRK08638   21 LAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRK---GVVACSAGNHAQGVALSCALL 97

                          90       100
                  ....*....|....*....|....*....
gi 1330027541  90 GYKMLVVMPRGQAQEKERMISLYNAELLL 118
Cdd:PRK08638   98 GIDGKVVMPKGAPKSKVAATCGYGAEVVL 126
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 17-328 1.81e-10

threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130197 [Multi-domain]  Cd Length: 380  Bit Score: 61.68  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKlKPGmtIVEGTAGNAGIGLALVAKSLGYKMLVV 96
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQR-QRG--VVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  97 MPRGQAQEKERMISLYNAELLLVDpcpfANPEHFYHTAKRIGvENENYWWADQFENlSNYRAHYLNTGPEIWQQTqGNID 176
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVILHG----DDYDEAYAFATSLA-EEEGRVFVHPFDD-EFVMAGQGTIGLEIMEDI-PDVD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 177 ALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGS-GIYSFLRNGQYQS--TGSSFTEGIGIMRTVE-NFRQAK--INR 250
Cdd:TIGR01127 151 TVIVPVGGGGLISGVASAAKQINPNVKVIGVEAEGApSMYESLREGKIKAveSVRTIADGIAVKKPGDlTFNIIKeyVDD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 251 AITLPDQDLVTISRLVAEHDGILLGSSSSLNVAgALYAAARMGKGKTIVTFSC----DLA----------ERSYSKLHNE 316
Cdd:TIGR01127 231 VVTVDEEEIANAIYLLLERHKILAEGAGAAGVA-ALLEQKVDVKGKKIAVVLSggniDLNllnkiiekglVKSGRKVRIE 309

                         330
                  ....*....|..
gi 1330027541 317 AFLKEKEIQLNK 328
Cdd:TIGR01127 310 TVLPDRPGALYH 321
PRK08197 PRK08197
threonine synthase; Validated
 15-120 4.47e-10

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 60.40  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRINSLSEISGC-EILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGMTivegTAGNAGIGLALVAKSLGYKM 93
Cdd:PRK08197   78 GMTPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMP----TNGNAGAAWAAYAARAGIRA 153

                          90       100
                  ....*....|....*....|....*..
gi 1330027541  94 LVVMPRGQAQEKERMISLYNAELLLVD 120
Cdd:PRK08197  154 TIFMPADAPEITRLECALAGAELYLVD 180
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 17-190 4.64e-10

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


Pssm-ID: 107209  Cd Length: 316  Bit Score: 60.01  E-value: 4.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPgMTIVEGTAGNAGIGLALVAKSLGYKMLVV 96
Cdd:cd06448     2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  97 MPrgqAQEKERMIS---LYNAELLLVDPCPFANPEHFYHTAkrigVENENYW-WADQFENlsnyrahylntgPEIWQ--- 169
Cdd:cd06448    81 VP---ESTKPRVVEklrDEGATVVVHGKVWWEADNYLREEL----AENDPGPvYVHPFDD------------PLIWEghs 141

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1330027541 170 ----------QTQGNIDALVSVVGTGGTIAG 190
Cdd:cd06448   142 smvdeiaqqlQSQEKVDAIVCSVGGGGLLNG 172
PRK06381 PRK06381
threonine synthase; Validated
 15-120 1.04e-09

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 58.95  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRINSLSEISGC-EILLKCEHQNPGGSIKDRAALQLVMDAVEAGKlkpgMTIVEGTAGNAGIGLALVAKSLGYKM 93
Cdd:PRK06381   14 GGTPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89

                          90       100
                  ....*....|....*....|....*..
gi 1330027541  94 LVVMPRGQAQEKERMISLYNAELLLVD 120
Cdd:PRK06381   90 VIFIPRSYSNSRVKEMEKYGAEIIYVD 116
PRK08246 PRK08246
serine/threonine dehydratase;
32-190 7.84e-09

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 56.12  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  32 EILLKCEHQNPGGSIKDRAALQLVMDAVEagklkPGMTIVEGTAGNAGIGLALVAKSLGYKMLVVMPRGQAQEKERMISL 111
Cdd:PRK08246   38 PVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 112 YNAELLLVdpcpfanPEHfYHTAkrigvenenywwadqfenLSNYRAHYLNTG---------PEI----------WQQTQ 172
Cdd:PRK08246  113 LGAEVVVV-------GAE-YADA------------------LEAAQAFAAETGallchaydqPEVlagagtlgleIEEQA 166

                         170
                  ....*....|....*...
gi 1330027541 173 GNIDALVSVVGTGGTIAG 190
Cdd:PRK08246  167 PGVDTVLVAVGGGGLIAG 184
PRK06110 PRK06110
threonine dehydratase;
25-117 2.56e-08

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 54.62  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  25 LSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPGmtIVEGTAGNAGIGLALVAKSLGYKMLVVMPRGQAQE 104
Cdd:PRK06110   30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVE 107

                          90
                  ....*....|...
gi 1330027541 105 KERMISLYNAELL 117
Cdd:PRK06110  108 KNAAMRALGAELI 120
PLN02550 PLN02550
threonine dehydratase
 25-285 2.91e-08

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 55.31  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  25 LSEISGCEILLKCEHQNPGGSIKDRAALQLvMDAVEAGKLKPGmtIVEGTAGNAGIGLALVAKSLGYKMLVVMPRGQAQE 104
Cdd:PLN02550  118 LSERLGVKVLLKREDLQPVFSFKLRGAYNM-MAKLPKEQLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEI 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 105 KERMISLYNAELLLVDPcpfANPEHFYHTAKRigVENENYWWADQFENlSNYRAHYLNTGPEIWQQTQGNIDALVSVVGT 184
Cdd:PLN02550  195 KWQSVERLGATVVLVGD---SYDEAQAYAKQR--ALEEGRTFIPPFDH-PDVIAGQGTVGMEIVRQHQGPLHAIFVPVGG 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 185 GGTIAGNSHYLSEQQPNLETWLVDPNGSGIYSF-LRNGQY----QSTGssFTEGIGImRTV--ENFRQAK-INRAITLPD 256
Cdd:PLN02550  269 GGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALsLHHGERvmldQVGG--FADGVAV-KEVgeETFRLCReLVDGVVLVS 345

                         250       260       270
                  ....*....|....*....|....*....|
gi 1330027541 257 QDLVTIS-RLVAEHDGILLGSSSSLNVAGA 285
Cdd:PLN02550  346 RDAICASiKDMFEEKRSILEPAGALALAGA 375
PRK08639 PRK08639
threonine dehydratase; Validated
 7-211 1.29e-07

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 52.89  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541   7 ANNLSELIGDTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAAL----QLVMDAVEAGklkpgmtIVEGTAGNAGIGL 82
Cdd:PRK08639   16 AKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYnaisQLSDEELAAG-------VVCASAGNHAQGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  83 ALVAKSLGYKMLVVMPRG---QAQEKERMISLYNAELLLV----DPCpfanpehfYHTAKRIgVENENYWWADQFENlsn 155
Cdd:PRK08639   89 AYACRHLGIPGVIFMPVTtpqQKIDQVRFFGGEFVEIVLVgdtfDDS--------AAAAQEY-AEETGATFIPPFDD--- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330027541 156 yrahyLNT-------GPEIWQQ--TQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNG 211
Cdd:PRK08639  157 -----PDViagqgtvAVEILEQleKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
PRK08329 PRK08329
threonine synthase; Validated
 22-190 3.72e-07

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 51.37  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  22 INSLSEISgCEILLKCEHQNPGGSIKDRAALqlvmdaVEAGKLKP-GMT-IVEGTAGNAGIGLALVAKSLGYKMLVVMPR 99
Cdd:PRK08329   64 ITPTVKRS-IKVYFKLDYLQPTGSFKDRGTY------VTVAKLKEeGINeVVIDSSGNAALSLALYSLSEGIKVHVFVSY 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 100 GQAQEKERMISLYNAELLLVDpcpfanpehfyhtAKRIGVENEnywwADQFENLSN--YRAHYLN---------TGPEIW 168
Cdd:PRK08329  137 NASKEKISLLSRLGAELHFVE-------------GDRMEVHEE----AVKFSKRNNipYVSHWLNpyflegtktIAYEIY 199

                         170       180
                  ....*....|....*....|..
gi 1330027541 169 QQTqGNIDALVSVVGTGGTIAG 190
Cdd:PRK08329  200 EQI-GVPDYAFVPVGSGTLFLG 220
eutB PRK07476
threonine dehydratase; Provisional
 17-99 3.74e-07

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 51.12  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKpgmTIVEGTAGNAGIGLALVAKSLGYKMLVV 96
Cdd:PRK07476   20 TPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERAR---GVVTASTGNHGRALAYAARALGIRATIC 96


                  ...
gi 1330027541  97 MPR 99
Cdd:PRK07476   97 MSR 99
PRK07334 PRK07334
threonine dehydratase; Provisional
 16-100 6.42e-06

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 47.58  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  16 DTDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKpgmTIVEGTAGNAGIGLALVAKSLGYKMLV 95
Cdd:PRK07334   23 RTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERAR---GVIAMSAGNHAQGVAYHAQRLGIPATI 99


                  ....*
gi 1330027541  96 VMPRG 100
Cdd:PRK07334  100 VMPRF 104
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
17-212 1.05e-05

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 47.06  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAA----LQLVMDAVEAGklkpgmtIVEGTAGNAGIGLALVAKSLGYK 92
Cdd:PRK09224   21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAynkmAQLTEEQLARG-------VITASAGNHAQGVALSAARLGIK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  93 MLVVMPRGQAQEKERMISLYNAELLLVDpcpfANPEHFYHTAKRIgVENENYWW----------ADQfenlsnyrahylN 162
Cdd:PRK09224   94 AVIVMPVTTPDIKVDAVRAFGGEVVLHG----DSFDEAYAHAIEL-AEEEGLTFihpfddpdviAGQ------------G 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330027541 163 T-GPEIWQQTQGNIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGS 212
Cdd:PRK09224  157 TiAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
PLN02970 PLN02970
serine racemase
 24-213 1.53e-05

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 46.21  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  24 SLSEISGCEILLKCEHQNPGGSIKDRAA----LQLVMDAVEAGklkpgmtIVEGTAGNAGIGLALVAKSLGYKMLVVMPR 99
Cdd:PLN02970   35 SLDALAGRSLFFKCECFQKGGAFKFRGAcnaiFSLSDDQAEKG-------VVTHSSGNHAAALALAAKLRGIPAYIVVPK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 100 GQAQEKERMISLYNAELLLVDPcpfaNPEHFYHTAKRIGVE---------NENYWWADQFenlsnyrahylNTGPEIWQQ 170
Cdd:PLN02970  108 NAPACKVDAVIRYGGIITWCEP----TVESREAVAARVQQEtgavlihpyNDGRVISGQG-----------TIALEFLEQ 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1330027541 171 TQGnIDALVSVVGTGGTIAGNSHYLSEQQPNLETWLVDPNGSG 213
Cdd:PLN02970  173 VPE-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGAD 214
PRK08813 PRK08813
threonine dehydratase; Provisional
 33-105 2.66e-05

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 45.39  E-value: 2.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330027541  33 ILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKPgmtIVEGTAGNAGIGLALVAKSLGYKMLVVMPRGQAQEK 105
Cdd:PRK08813   50 VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTK 119
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 53-120 6.59e-05

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 44.48  E-value: 6.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330027541  53 QLVMDAVEAGKLKP---GMTIVEGTAGNAGIGLALVAKSLGYKMLVVMPRGQAQEKERMISLYNAELLLVD 120
Cdd:PRK08206   99 ELSFEELTSGEVREklgDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITD 169
PRK05638 PRK05638
threonine synthase; Validated
 15-117 2.24e-04

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 42.88  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  15 GDTDLVRiNSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKpgmtIVEGTAGNAGIGLALVAKSLGYKML 94
Cdd:PRK05638   65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANG----FIVASDGNAAASVAAYSARAGKEAF 139

                          90       100
                  ....*....|....*....|...
gi 1330027541  95 VVMPRGQAQEKERMISLYNAELL 117
Cdd:PRK05638  140 VVVPRKVDKGKLIQMIAFGAKII 162
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
24-121 3.84e-03

threo-3-hydroxy-L-aspartate ammonia-lyase;


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 38.85  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  24 SLSEISGCEILLKCEHQNPGGSIKDRAA----LQLVMDAVEAGklkpgmtIVEGTAGNAGIGLALVAKSLGYKMLVVMPR 99
Cdd:PRK07048   32 TADARTGAQVFFKCENFQRMGAFKFRGAynalSQFSPEQRRAG-------VVTFSSGNHAQAIALSARLLGIPATIVMPQ 104

                          90       100
                  ....*....|....*....|..
gi 1330027541 100 GQAQEKERMISLYNAELLLVDP 121
Cdd:PRK07048  105 DAPAAKVAATRGYGGEVVTYDR 126
D-Ser-dehyd cd06447
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 27-109 5.38e-03

D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.


Pssm-ID: 107208  Cd Length: 404  Bit Score: 38.48  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  27 EISGcEILLKCEHQNP-GGSIKDRAALQLVMD-----AVEAGKLKPG-----------------MTIVEGTAGNAGIGLA 83
Cdd:cd06447    72 PIKG-RLLLKADSHLPiSGSIKARGGIYEVLKhaeklALEHGLLTLEddysklasekfrklfsqYSIAVGSTGNLGLSIG 150

                          90       100
                  ....*....|....*....|....*.
gi 1330027541  84 LVAKSLGYKMLVVMPRGQAQEKERMI 109
Cdd:cd06447   151 IMAAALGFKVTVHMSADAKQWKKDKL 176
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 17-299 8.29e-03

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 37.87  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  17 TDLVRINSLSEISGCEILLKCEHQNPGGSIKDRAALQLVMDAVEAGKLKpgmTIVEGTAGNAGIGLALVAKSLGYKMLVV 96
Cdd:PRK13803  272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKINNALGQALLAKRMGKTR---IIAETGAGQHGVATATACALFGLKCTIF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541  97 MP----RGQAQEKERMISLyNAELLLVDPCPfanpehfyHTAKRIGVENENYWWAdqfenlSNYRAHYL---NTGP---- 165
Cdd:PRK13803  349 MGeediKRQALNVERMKLL-GANVIPVLSGS--------KTLKDAVNEAIRDWVA------SVPDTHYLigsAVGPhpyp 413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 166 ----------------EIWQQTQGNIDALVSVVGTGGTIAGN-SHYLSEQQPNLETwlVDPNGSGI-------------- 214
Cdd:PRK13803  414 emvayfqsvigeeakeQLKEQTGKLPDAIIACVGGGSNAIGIfYHFLDDPSVKLIG--VEAGGKGVntgehaatikkgrk 491

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330027541 215 ------YSFL---RNGQYQ-----STGSSFTeGIGIMRTveNFRQAKINRAITLPDQDLVTISRLVAEHDGILLGSSSSL 280
Cdd:PRK13803  492 gvlhgsMTYLmqdENGQILephsiSAGLDYP-GIGPMHA--NLFETGRAIYTSVTDEEALDAFKLLAKLEGIIPALESSH 568

                         330
                  ....*....|....*....
gi 1330027541 281 NVAGALYAAARMGKGKTIV 299
Cdd:PRK13803  569 ALAYLKEGRKKFKKKDIVI 587
 
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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