NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488617769|ref|WP_002554618|]
View 

MULTISPECIES: cysteine synthase CysM [Pseudomonas]

Protein Classification

cysteine synthase CysM( domain architecture ID 10793608)

cysteine synthase B (CysM) catalyzes the biosynthesis of cysteine and it can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product

EC:  2.5.1.47
Gene Ontology:  GO:0004124|GO:0030170

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
cysM PRK11761
cysteine synthase CysM;
3-298 0e+00

cysteine synthase CysM;


:

Pssm-ID: 236972  Cd Length: 296  Bit Score: 645.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   3 LQYQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAM 82
Cdd:PRK11761   1 MAYPTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  83 AAAIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEI 162
Cdd:PRK11761  81 IAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 163 WRQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHEYLPKIYQSDRVDRIIDMGQTEAE 242
Cdd:PRK11761 161 WRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDVSQQEAE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488617769 243 DTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIICDRGDRYLSTGIYDS 298
Cdd:PRK11761 241 NTMRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAIICDRGDRYLSTGVFPA 296
 
Name Accession Description Interval E-value
cysM PRK11761
cysteine synthase CysM;
3-298 0e+00

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 645.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   3 LQYQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAM 82
Cdd:PRK11761   1 MAYPTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  83 AAAIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEI 162
Cdd:PRK11761  81 IAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 163 WRQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHEYLPKIYQSDRVDRIIDMGQTEAE 242
Cdd:PRK11761 161 WRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDVSQQEAE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488617769 243 DTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIICDRGDRYLSTGIYDS 298
Cdd:PRK11761 241 NTMRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAIICDRGDRYLSTGVFPA 296
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
7-296 0e+00

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: 511.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    7 TIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAI 86
Cdd:TIGR01138   1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   87 KGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEIWRQT 166
Cdd:TIGR01138  81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  167 GGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHEYLPKIYQSDRVDRIIDMGQTEAEDTMR 246
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPGIRRWPTEYLPGIFDASLVDRVLDIHQRDAENTMR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 488617769  247 RLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIICDRGDRYLSTGIY 296
Cdd:TIGR01138 241 ELAVREGIFCGVSSGGAVAAALRLARELPDAVVVAIICDRGDRYLSTGVF 290
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
5-293 8.43e-164

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: 457.20  E-value: 8.43e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAA 84
Cdd:COG0031    4 YDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  85 AIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAE-GRGKVLDQFANGDNPEAHYTSTGPEIW 163
Cdd:COG0031   84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAEtPGAFWPNQFENPANPEAHYETTGPEIW 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 164 RQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPG-------IRRWPHEYLPKIYQSDRVDRIIDM 236
Cdd:COG0031  164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGgepgphkIEGIGAGFVPKILDPSLIDEVITV 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488617769 237 GQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLST 293
Cdd:COG0031  244 SDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLgPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
13-292 4.26e-136

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: 386.48  E-value: 4.26e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAIKGYRMI 92
Cdd:cd01561    1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  93 LIMPDNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAERMQAEGRGKV-LDQFANGDNPEAHYTSTGPEIWRQTGGT 169
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTpeAEADGMKGAIAKARELAAETPNAFwLNQFENPANPEAHYETTAPEIWEQLDGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 170 VTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPME----------GASIPGIRRWpheYLPKIYQSDRVDRIIDMGQT 239
Cdd:cd01561  161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGsvlfsggppgPHKIEGIGAG---FIPENLDRSLIDEVVRVSDE 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488617769 240 EAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLS 292
Cdd:cd01561  238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTILPDSGERYLS 291
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
8-285 5.10e-77

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: 236.82  E-value: 5.10e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAElrgQIHPGDTLIEATSGNTGIALAMAAAIK 87
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   88 GYRMILIMPDNSSAERKAAMTAYGAELISVskDEGMEGARDLAERMQAEGRGKV-LDQFANGDNPEAhYTSTGPEIWRQT 166
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV--GGDYDEAVAAARELAAEGPGAYyINQYDNPLNIEG-YGTIGLEILEQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  167 GGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIP---------------------GIRRWPHEYLPKIY 225
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALArslaagrpvpvpvadtiadglGVGDEPGALALDLL 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617769  226 QsDRVDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGA-LRISREV-ENAVIVAIICD 285
Cdd:pfam00291 235 D-EYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELkGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
cysM PRK11761
cysteine synthase CysM;
3-298 0e+00

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 645.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   3 LQYQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAM 82
Cdd:PRK11761   1 MAYPTLEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  83 AAAIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEI 162
Cdd:PRK11761  81 IAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAEGEGKVLDQFANPDNPLAHYETTGPEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 163 WRQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHEYLPKIYQSDRVDRIIDMGQTEAE 242
Cdd:PRK11761 161 WRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDVSQQEAE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488617769 243 DTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIICDRGDRYLSTGIYDS 298
Cdd:PRK11761 241 NTMRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAIICDRGDRYLSTGVFPA 296
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
7-296 0e+00

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: 511.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    7 TIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAI 86
Cdd:TIGR01138   1 TIEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   87 KGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEIWRQT 166
Cdd:TIGR01138  81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLLDQFNNPDNPYAHYTSTGPEIWQQT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  167 GGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHEYLPKIYQSDRVDRIIDMGQTEAEDTMR 246
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPGIRRWPTEYLPGIFDASLVDRVLDIHQRDAENTMR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 488617769  247 RLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIICDRGDRYLSTGIY 296
Cdd:TIGR01138 241 ELAVREGIFCGVSSGGAVAAALRLARELPDAVVVAIICDRGDRYLSTGVF 290
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
5-293 8.43e-164

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: 457.20  E-value: 8.43e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAA 84
Cdd:COG0031    4 YDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  85 AIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAE-GRGKVLDQFANGDNPEAHYTSTGPEIW 163
Cdd:COG0031   84 AAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAEtPGAFWPNQFENPANPEAHYETTGPEIW 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 164 RQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPG-------IRRWPHEYLPKIYQSDRVDRIIDM 236
Cdd:COG0031  164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLSGgepgphkIEGIGAGFVPKILDPSLIDEVITV 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488617769 237 GQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLST 293
Cdd:COG0031  244 SDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLgPGKTIVTILPDSGERYLST 301
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
8-296 2.51e-162

cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273463  Cd Length: 299  Bit Score: 453.28  E-value: 2.51e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAIK 87
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   88 GYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAE-GRGKVLDQFANGDNPEAHYTSTGPEIWRQT 166
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAEtNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  167 GGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPG-------IRRWPHEYLPKIYQSDRVDRIIDMGQT 239
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGgepgphkIQGIGAGFIPKILDLSLIDEVITVSDE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488617769  240 EAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVEN--AVIVAIICDRGDRYLSTGIY 296
Cdd:TIGR01136 241 DAIETARRLAREEGILVGISSGAAVAAALKLAKRLENadKVIVAILPDTGERYLSTGLF 299
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
13-292 4.26e-136

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: 386.48  E-value: 4.26e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAIKGYRMI 92
Cdd:cd01561    1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  93 LIMPDNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAERMQAEGRGKV-LDQFANGDNPEAHYTSTGPEIWRQTGGT 169
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTpeAEADGMKGAIAKARELAAETPNAFwLNQFENPANPEAHYETTAPEIWEQLDGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 170 VTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPME----------GASIPGIRRWpheYLPKIYQSDRVDRIIDMGQT 239
Cdd:cd01561  161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGsvlfsggppgPHKIEGIGAG---FIPENLDRSLIDEVVRVSDE 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488617769 240 EAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLS 292
Cdd:cd01561  238 EAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLgPGKTIVTILPDSGERYLS 291
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
8-296 5.36e-114

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: 330.87  E-value: 5.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    8 IADCVGNTPLVRLQRMAGNTSNtLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAIK 87
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNAN-VFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   88 GYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAE--GRGKVLDQFANGDNPEAHYTSTGPEIWRQ 165
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAAStpNSYFMLQQFENPANPEIHRKTTGPEIWRD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  166 TGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHE-------YLPKIYQSDRVDRIIDMGQ 238
Cdd:TIGR01139 160 TDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKiqgigagFIPKNLNRSVIDEVITVSD 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488617769  239 TEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVE-NAVIVAIICDRGDRYLSTGIY 296
Cdd:TIGR01139 240 EEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEpDKLIVVILPSTGERYLSTPLF 298
PRK10717 PRK10717
cysteine synthase A; Provisional
5-293 8.32e-96

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 285.60  E-value: 8.32e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAA 84
Cdd:PRK10717   4 FEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  85 AIKGYRMILIMPDNSSAERKAAMTAYGAELISV------SKDEGMEGARDLAERMQAEGRGKVL--DQFANGDNPEAHYT 156
Cdd:PRK10717  84 AARGYKTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPNGAIwaNQFDNPANREAHYE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 157 STGPEIWRQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPM---------------EGASIP---GIRRwph 218
Cdd:PRK10717 164 TTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTgsalysyyktgelkaEGSSITegiGQGR--- 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488617769 219 eyLPKIYQSDRVDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLST 293
Cdd:PRK10717 241 --ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELgPGHTIVTILCDSGERYQSK 314
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
6-292 1.25e-88

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: 271.67  E-value: 1.25e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    6 QTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAA 85
Cdd:TIGR01137   3 DNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   86 IKGYRMILIMPDNSSAERKAAMTAYGAELI---SVSKDEGMEGARDLAERMQAEGRGKV-LDQFANGDNPEAHYTSTGPE 161
Cdd:TIGR01137  83 IKGYKCIIVLPEKMSSEKVDVLRALGAEIVrtpTAAAFDSPESHIGVAKRLVREIPGAHiLDQYRNPSNPLAHYDTTGPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  162 IWRQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQP-----MEGASIPGIRRWPHE-------YLPKIYQSDR 229
Cdd:TIGR01137 163 ILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPegsilAQPEELNQTGRTPYKvegigydFIPTVLDRKV 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488617769  230 VDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV--ENAVIVAIICDRGDRYLS 292
Cdd:TIGR01137 243 VDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDElqEGQRCVVLLPDSIRNYMT 307
PLN02565 PLN02565
cysteine synthase
8-298 1.28e-87

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 264.86  E-value: 1.28e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDT-LIEATSGNTGIALAMAAAI 86
Cdd:PLN02565   9 VTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESvLIEPTSGNTGIGLAFMAAA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  87 KGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEG-RGKVLDQFANGDNPEAHYTSTGPEIWRQ 165
Cdd:PLN02565  89 KGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTpNSYILQQFENPANPKIHYETTGPEIWKG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 166 TGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHE-------YLPKIYQSDRVDRIIDMGQ 238
Cdd:PLN02565 169 TGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKiqgigagFIPGVLDVDLLDEVVQVSS 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617769 239 TEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENA--VIVAIICDRGDRYLSTGIYDS 298
Cdd:PLN02565 249 DEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAgkLIVVIFPSFGERYLSSVLFES 310
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
8-297 6.47e-85

2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274872 [Multi-domain]  Cd Length: 304  Bit Score: 257.13  E-value: 6.47e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAIK 87
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   88 GYRMILIMPDNSSAERKAAMTAYGAELISVS-KDE--GMEGAR-DLAERMQAEGRGKV-LDQFANGDNPEAHYTSTGPEI 162
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTePDEtgGYLGTRiARVRELLASIPDAYwPNQYANPDNPRAHYHGTGREI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  163 WRQTgGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGL---------QPMEGASIPGI---RRwpheylPKIYQSDRV 230
Cdd:TIGR03945 161 ARAF-PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVdavgsvifgGPPGRRHIPGLgasVV------PELLDESLI 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488617769  231 DRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLSTgIYD 297
Cdd:TIGR03945 234 DDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIpEGSTVVAILPDRGERYLDT-VYN 300
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
15-286 5.04e-80

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: 242.42  E-value: 5.04e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  15 TPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIhPGDTLIEATSGNTGIALAMAAAIKGYRMILI 94
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  95 MPDNSSAERKAAMTAYGAELISVskDEGMEGARDLAERMQAEGRG-KVLDQFANGDNPEAHYTsTGPEIWRQTGG-TVTH 172
Cdd:cd00640   80 MPEGASPEKVAQMRALGAEVVLV--PGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGT-IGLEILEQLGGqKPDA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 173 FVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPmegasipgirrwpheylpkiyQSDRVDriidmgQTEAEDTMRRLAREE 252
Cdd:cd00640  157 VVVPVGGGGNIAGIARALKELLPNVKVIGVEP---------------------EVVTVS------DEEALEAIRLLAREE 209
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488617769 253 GIFCGVSSGGSVAGALRISREV-ENAVIVAIICDR 286
Cdd:cd00640  210 GILVEPSSAAALAAALKLAKKLgKGKTVVVILTGG 244
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
8-285 5.10e-77

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: 236.82  E-value: 5.10e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769    8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAElrgQIHPGDTLIEATSGNTGIALAMAAAIK 87
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   88 GYRMILIMPDNSSAERKAAMTAYGAELISVskDEGMEGARDLAERMQAEGRGKV-LDQFANGDNPEAhYTSTGPEIWRQT 166
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV--GGDYDEAVAAARELAAEGPGAYyINQYDNPLNIEG-YGTIGLEILEQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  167 GGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIP---------------------GIRRWPHEYLPKIY 225
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALArslaagrpvpvpvadtiadglGVGDEPGALALDLL 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617769  226 QsDRVDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGA-LRISREV-ENAVIVAIICD 285
Cdd:pfam00291 235 D-EYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELkGGDRVVVVLTG 295
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
12-297 6.58e-75

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 233.70  E-value: 6.58e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  12 VGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDT-LIEATSGNTGIALAMAAAIKGYR 90
Cdd:PLN02556  57 IGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMAAMKGYK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  91 MILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGA-RDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEIWRQTGGT 169
Cdd:PLN02556 137 MILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTvKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQ 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 170 VTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHE-------YLPKIYQSDRVDRIIDMGQTEAE 242
Cdd:PLN02556 217 VDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHitgngvgFKPDILDMDVMEKVLEVSSEDAV 296
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488617769 243 DTMRRLAREEGIFCGVSSGGSVAGALRISREVEN--AVIVAIICDRGDRYLSTGIYD 297
Cdd:PLN02556 297 NMARELALKEGLMVGISSGANTVAALRLAKMPENkgKLIVTVHPSFGERYLSSVLFQ 353
PLN00011 PLN00011
cysteine synthase
8-298 1.09e-74

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 231.82  E-value: 1.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPG-DTLIEATSGNTGIALAMAAAI 86
Cdd:PLN00011  11 VTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  87 KGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAERMQAEGRGK-VLDQFANGDNPEAHYTSTGPEIWRQ 165
Cdd:PLN00011  91 RGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGyIPQQFENPANPEIHYRTTGPEIWRD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 166 TGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPH-------EYLPKIYQSDRVDRIIDMGQ 238
Cdd:PLN00011 171 SAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHliqgigsGIIPFNLDLTIVDEIIQVTG 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617769 239 TEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENA--VIVAIICDRGDRYLSTGIYDS 298
Cdd:PLN00011 251 EEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAgkLIVVIFPSGGERYLSTKLFES 312
PLN03013 PLN03013
cysteine synthase
8-298 7.93e-71

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 225.04  E-value: 7.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDT-LIEATSGNTGIALAMAAAI 86
Cdd:PLN03013 117 VSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSvLVEPTSGNTGIGLAFIAAS 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  87 KGYRMILIMPDNSSAERKAAMTAYGAELISVSKDEGMEGARDLAER-MQAEGRGKVLDQFANGDNPEAHYTSTGPEIWRQ 165
Cdd:PLN03013 197 RGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEiLKNTPDAYMLQQFDNPANPKIHYETTGPEIWDD 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 166 TGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGASIPGIRRWPHE-------YLPKIYQSDRVDRIIDMGQ 238
Cdd:PLN03013 277 TKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKiqgigagFIPKNLDQKIMDEVIAISS 356
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617769 239 TEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENA-VIVAIICDRGDRYLSTGIYDS 298
Cdd:PLN03013 357 EEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAgKLIAVSLFASGRDIYTPRCSS 417
PLN02356 PLN02356
phosphateglycerate kinase
8-298 1.11e-42

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 151.68  E-value: 1.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPGDTLIEATSGNTGIALAMAAAIK 87
Cdd:PLN02356  47 LIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  88 GYRMILIMPDNSSAERKAAMTAYGAEL--------------ISVSKDEGMEgARDLAE--RMQAEGRGKVL--------- 142
Cdd:PLN02356 127 GCKCHVVIPDDVAIEKSQILEALGATVervrpvsithkdhyVNIARRRALE-ANELASkrRKGSETDGIHLektngcise 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 143 ------------------DQFANGDNPEAHYTSTGPEIWRQTGGTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQP 204
Cdd:PLN02356 206 eekenslfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDP 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 205 -------------------MEGASIP----------GIRRWPHEYLpkIYQSDRVDRIIDMgqtEAEDTMRRLAREEGIF 255
Cdd:PLN02356 286 pgsglfnkvtrgvmytreeAEGRRLKnpfdtitegiGINRLTQNFL--MAKLDGAFRGTDK---EAVEMSRYLLKNDGLF 360
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 488617769 256 CGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLSTgIYDS 298
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSLgPGHTIVTILCDSGMRHLSK-FHDP 403
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
13-284 3.04e-24

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: 99.98  E-value: 3.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRLQRMA-GNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQihpgDTLIEATSGNTGIALAMAAAIKGYRM 91
Cdd:cd01563   21 GNTPLVRAPRLGeRLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  92 ILIMPDNSSAERKAAMTAYGAELISVskdegmEGARDLAERMQAEGRGKVLDQFANGDNPEAH--YTSTGPEIWRQTGGT 169
Cdd:cd01563   97 VVFLPAGKALGKLAQALAYGATVLAV------EGNFDDALRLVRELAEENWIYLSNSLNPYRLegQKTIAFEIAEQLGWE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 170 V-THFVSSMGTTGTIMGTSRYLKEQ------NPEVQIVGLQPmEGAS---------------------------IPGIRR 215
Cdd:cd01563  171 VpDYVVVPVGNGGNITAIWKGFKELkelgliDRLPRMVGVQA-EGAApivrafkegkddiepvenpetiatairIGNPAS 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617769 216 WPhEYLPKIYQSDrvDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREV---ENAVIVAIIC 284
Cdd:cd01563  250 GP-KALRAVRESG--GTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGiidKGERVVVVLT 318
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
12-283 4.94e-23

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: 97.58  E-value: 4.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  12 VGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIhpgdTLIEATSGNTGIALAMAAAIKGYRM 91
Cdd:COG0498   64 EGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  92 ILIMP-DNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAERmqaEGRGkvldqFANGDNP---EAhYTSTGPEIWRQ 165
Cdd:COG0498  140 FVFVPeGKVSPGQLAQMLTYGAHVIAVdgNFDDAQRLVKELAAD---EGLY-----AVNSINParlEG-QKTYAFEIAEQ 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 166 TGGTVTHFVSSMGTTGTI--------MGTSRYLKEQNPevQIVGLQPmEGASiPGIRRWphEYLPKIYQSDRVDRI---I 234
Cdd:COG0498  211 LGRVPDWVVVPTGNGGNIlagykafkELKELGLIDRLP--RLIAVQA-TGCN-PILTAF--ETGRDEYEPERPETIapsM 284
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488617769 235 DMGQ---------------------TEAE--DTMRRLAREEGIFCGVSSGGSVAGALRISREVE---NAVIVAII 283
Cdd:COG0498  285 DIGNpsngeralfalresggtavavSDEEilEAIRLLARREGIFVEPATAVAVAGLRKLREEGEidpDEPVVVLS 359
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
6-284 1.32e-22

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: 95.49  E-value: 1.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   6 QTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITR--AELRGQihpgdTLIEATSGNTGIALAMA 83
Cdd:COG1171   16 ARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASlsEEERAR-----GVVAASAGNHAQGVAYA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  84 AAIKGYRMILIMPDNSSAERKAAMTAYGAELISVskDEGMEGARDLAERMQAEgRGKVLDQ-FangDNPE--AHYTSTGP 160
Cdd:COG1171   91 ARLLGIPATIVMPETAPAVKVAATRAYGAEVVLH--GDTYDDAEAAAAELAEE-EGATFVHpF---DDPDviAGQGTIAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 161 EIWRQTGGtVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQP------------------------MEGASIPGIRRW 216
Cdd:COG1171  165 EILEQLPD-LDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPegaaamyrslaagepvtlpgvdtiADGLAVGRPGEL 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488617769 217 PHEYLpkiyqSDRVDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIIC 284
Cdd:COG1171  244 TFEIL-----RDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLS 306
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
5-284 1.42e-21

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: 92.16  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMI---TRAELRGQIhpgdtlIEATSGNTGIALA 81
Cdd:cd01562    8 AARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLlslSEEERAKGV------VAASAGNHAQGVA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  82 MAAAIKGYRMILIMPDNSSAERKAAMTAYGAELISVskDEGMEGARDLAERMQAEGRGKVLDQFangDNPE--AHYTSTG 159
Cdd:cd01562   82 YAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLTFIHPF---DDPDviAGQGTIG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 160 PEIWRQTGGTVTHFVS-SMGttGTIMGTSRYLKEQNPEVQIVGLQPmEGA-----SIPGIRRWPHEYLPKI--------- 224
Cdd:cd01562  157 LEILEQVPDLDAVFVPvGGG--GLIAGIATAVKALSPNTKVIGVEP-EGApamaqSLAAGKPVTLPEVDTIadglavkrp 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488617769 225 ------YQSDRVDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIIC 284
Cdd:cd01562  234 geltfeIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLS 299
PRK06815 PRK06815
threonine/serine dehydratase;
5-286 1.55e-19

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 86.67  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITR--AELRGQihpgdTLIEATSGNTGIALAM 82
Cdd:PRK06815  11 HQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLlnEAQRQQ-----GVITASSGNHGQGVAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  83 AAAIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKDegMEGArDLAERMQAEGRGKVLDQFANGDNPEAHYTSTGPEI 162
Cdd:PRK06815  86 AAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGD--ALNA-ELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMEL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 163 WRQTGGTVTHFVsSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEGA----SIPGIRRWPHEYLPKIyqSD---------- 228
Cdd:PRK06815 163 VEQQPDLDAVFV-AVGGGGLISGIATYLKTLSPKTEIIGCWPANSPslytSLEAGEIVEVAEQPTL--SDgtaggvepga 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488617769 229 --------RVDRIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVIVAIICDR 286
Cdd:PRK06815 240 itfplcqqLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGK 305
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
11-269 6.14e-15

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 73.96  E-value: 6.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   11 CVGNTPLVRLQRMAGN-TSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQihpgDTLIEATSGNTGIALAMAAAIKGY 89
Cdd:TIGR00260  19 GEGVTPLFRAPALAANvGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   90 RMILIMPDNSSAERKAAMT-AYGAELISVSK--DEGMEGARDLAERMQAEGRGKVLDQFAngdNPEAHYTsTGPEIWRQT 166
Cdd:TIGR00260  95 KVVVLYPAGKISLGKLAQAlGYNAEVVAIDGnfDDAQRLVKQLFEDKPALGLNSANSIPY---RLEGQKT-YAFEAVEQL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  167 GGTV-THFVSSMGTTGTIMGTSRYLKEQNpEVQIVGLQPM-----EGASiPGIRRW-------PHEYLPKIYQS------ 227
Cdd:TIGR00260 171 GWEApDKVVVPVPNSGNFGAIWKGFKEKK-MLGLDSLPVKrgiqaEGAA-DIVRAFleggqwePIETPETLSTAmdignp 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488617769  228 ---DRVDRIIDMGQTEAED--------TMRRLAREEGIFCGVSSGGSVAGALR 269
Cdd:TIGR00260 249 anwPRALEAFRRSNGYAEDlsdeeileAIKLLAREEGYFVEPHSAVAVAALLK 301
PRK06381 PRK06381
threonine synthase; Validated
13-133 2.25e-13

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 69.35  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRLQRMAGN-TSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQihpgDTLIEATSGNTGIALAMAAAIKGYRM 91
Cdd:PRK06381  14 GGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488617769  92 ILIMPDNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAERM 133
Cdd:PRK06381  90 VIFIPRSYSNSRVKEMEKYGAEIIYVdgKYEEAVERSRKFAKEN 133
PRK12483 PRK12483
threonine dehydratase; Reviewed
15-204 3.30e-11

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 63.66  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  15 TPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPA---LSMITRAEL-RGqihpgdtLIEATSGNTGIALAMAAAIKGYR 90
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAynkMARLPAEQLaRG-------VITASAGNHAQGVALAAARLGVK 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  91 MILIMPDNSSAERKAAMTAYGAELisVSKDEGMEGARDLAERMQAEGRGKVLDQFangDNPE--AHYTSTGPEIWRQTGG 168
Cdd:PRK12483 111 AVIVMPRTTPQLKVDGVRAHGGEV--VLHGESFPDALAHALKLAEEEGLTFVPPF---DDPDviAGQGTVAMEILRQHPG 185
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488617769 169 TVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQP 204
Cdd:PRK12483 186 PLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEP 221
PRK06608 PRK06608
serine/threonine dehydratase;
5-207 6.07e-11

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 62.10  E-value: 6.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVR---LQRMAGNTsntLLLKLEGNNPAGSVKDRPALSmiTRAELRGQIHPGDTLIEATSGNTGIALA 81
Cdd:PRK06608  14 HNRIKQYLHLTPIVHsesLNEMLGHE---IFFKVESLQKTGAFKVRGVLN--HLLELKEQGKLPDKIVAYSTGNHGQAVA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  82 MAAAIKGYRMILIMPDNSSAERKAAMTAYGAELI-SVSKDEGMEGARdlaermQAEGRGKVLDQFANGDNPEAHYTSTGP 160
Cdd:PRK06608  89 YASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVIlTNTRQEAEEKAK------EDEEQGFYYIHPSDSDSTIAGAGTLCY 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488617769 161 EIWRQTGGTVTHFVSSMGTTGTIMGTsrYLKEQ--NPEVQIVGLQPMEG 207
Cdd:PRK06608 163 EALQQLGFSPDAIFASCGGGGLISGT--YLAKEliSPTSLLIGSEPLNA 209
PRK05638 PRK05638
threonine synthase; Validated
13-280 5.03e-10

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 59.83  E-value: 5.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRlQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRaelrGQIHPGDTLIEATSGNTGIALAMAAAIKGYRMI 92
Cdd:PRK05638  65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSY----GLPYAANGFIVASDGNAAASVAAYSARAGKEAF 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  93 LIMPDNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAermqaegRGKVLDQFANGDN---PEAHYTsTGPEIWRQTG 167
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRYgeSVDEAIEYAEELA-------RLNGLYNVTPEYNiigLEGQKT-IAFELWEEIN 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 168 GTvtHFVSSMGTTGTIM----GTSRYLK----EQNPE---VQIVGLQPMeGASIPGIRRWPHE------YLPKIYQSDRV 230
Cdd:PRK05638 212 PT--HVIVPTGSGSYLYsiykGFKELLEigviEEIPKliaVQTERCNPI-ASEILGNKTKCNEtkalglYVKNPVMKEYV 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488617769 231 DRIID-MGQT------EAEDTMRRLAREEGIFCGVSSGGSVAGALRISRE-----VENAVIV 280
Cdd:PRK05638 289 SEAIKeSGGTavvvneEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyiekGDKVVLV 350
PRK06110 PRK06110
threonine dehydratase;
33-139 5.94e-10

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 59.24  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  33 LKLEGNNPAGSVKDRPALSMITRAELRGQIHPGdtLIEATSGNTGIALAMAAAIKGYRMILIMPDNSSAERKAAMTAYGA 112
Cdd:PRK06110  40 VKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGA 117
                         90       100
                 ....*....|....*....|....*..
gi 488617769 113 ELISVSKDegMEGARDLAERMqAEGRG 139
Cdd:PRK06110 118 ELIEHGED--FQAAREEAARL-AAERG 141
PLN02550 PLN02550
threonine dehydratase
31-204 1.06e-09

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 59.16  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  31 LLLKLEGNNPAGSVKDRPALSMITRAElRGQIHPGdtLIEATSGNTGIALAMAAAIKGYRMILIMPDNSSAERKAAMTAY 110
Cdd:PLN02550 126 VLLKREDLQPVFSFKLRGAYNMMAKLP-KEQLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 111 GAELISV--SKDEGMEGARdlaERMQAEGRgKVLDQFangDNPE--AHYTSTGPEIWRQTGGTVTHFVSSMGTTGTIMGT 186
Cdd:PLN02550 203 GATVVLVgdSYDEAQAYAK---QRALEEGR-TFIPPF---DHPDviAGQGTVGMEIVRQHQGPLHAIFVPVGGGGLIAGI 275
                        170
                 ....*....|....*...
gi 488617769 187 SRYLKEQNPEVQIVGLQP 204
Cdd:PLN02550 276 AAYVKRVRPEVKIIGVEP 293
PRK08197 PRK08197
threonine synthase; Validated
13-273 5.04e-09

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 56.55  E-value: 5.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRLQRMAGNTS-NTLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHpgdtLIEATSGNTGIALAMAAAIKGYRM 91
Cdd:PRK08197  78 GMTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRA 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  92 ILIMPDNSSAERKAAMTAYGAELISVskdegmEGARDLAERMQAEGRGKV--LDqfangdnpeahyTST----------- 158
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYLV------DGLISDAGKIVAEAVAEYgwFD------------VSTlkepyriegkk 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 159 --GPEIWRQTGGTVTH--FVSSMGTTGTI--------MGTSRYLKEQNPE---VQIVGLQPMEGASIPGIRR---WPHEY 220
Cdd:PRK08197 216 tmGLELAEQLGWRLPDviLYPTGGGVGLIgiwkafdeLEALGWIGGKRPRlvaVQAEGCAPIVKAWEEGKEEsefWEDAH 295
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617769 221 -------LPK----------IYQSDRVDRIIDMGQTEAEdtMRRLAREEGIF-CgvSSGGSVAGALRISRE 273
Cdd:PRK08197 296 tvafgirVPKalgdflvldaVRETGGCAIAVSDDAILAA--QRELAREEGLFaC--PEGAATFAAARQLRE 362
PRK06450 PRK06450
threonine synthase; Validated
13-128 1.56e-08

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 55.13  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  13 GNTPLVRlqrmagntSNTLLLKLEGNNPAGSVKDRPALSMITR-AELR-GQIHpgdtliEATSGNTGIALAMAAAIKGYR 90
Cdd:PRK06450  57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYlAEKGiKQIS------EDSSGNAGASIAAYGAAAGIE 122
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488617769  91 MILIMPDNSSAERKAAMTAYGAELISVskdegmEGARD 128
Cdd:PRK06450 123 VKIFVPETASGGKLKQIESYGAEVVRV------RGSRE 154
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
15-203 3.30e-08

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 53.97  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  15 TPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPA---LSMITRAELRGQIhpgdtlIEATSGNTGIALAMAAAIKGYRM 91
Cdd:PRK08638  28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKGV------VACSAGNHAQGVALSCALLGIDG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  92 ILIMPDNSSAERKAAMTAYGAELISVSK--DEGMEGARDLAERmqaEGRgKVLDQFangDNPE--AHYTSTGPEIWRQTg 167
Cdd:PRK08638 102 KVVMPKGAPKSKVAATCGYGAEVVLHGDnfNDTIAKVEEIVEE---EGR-TFIPPY---DDPKviAGQGTIGLEILEDL- 173
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488617769 168 GTVTHFVSSMGTTGTIMGTSRYLKEQNPEVQIVGLQ 203
Cdd:PRK08638 174 WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQ 209
PLN02569 PLN02569
threonine synthase
10-120 2.29e-07

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 51.74  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  10 DCV----GNTPLVRLQRMAGNTS--NTLLLKLEGNNPAGSVKDR---PALSMITRaeLRGQIHPGDTLIEATSGNTGIAL 80
Cdd:PLN02569 125 DIVslfeGNSNLFWAERLGKEFLgmNDLWVKHCGISHTGSFKDLgmtVLVSQVNR--LRKMAKPVVGVGCASTGDTSAAL 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488617769  81 AMAAAIKGYRMILIMPDNS-SAERKAAMTAYGAELISVSKD 120
Cdd:PLN02569 203 SAYCAAAGIPSIVFLPADKiSIAQLVQPIANGALVLSIDTD 243
PRK08246 PRK08246
serine/threonine dehydratase;
5-132 2.66e-07

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 51.11  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVRLqRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELrgqihPGDTLIEATSGNTGIALAMAA 84
Cdd:PRK08246  14 AQRIAPHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAA 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488617769  85 AIKGYRMILIMPDNSSAERKAAMTAYGAELISVSKD--EGMEGARDLAER 132
Cdd:PRK08246  88 AALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEyaDALEAAQAFAAE 137
PRK08813 PRK08813
threonine dehydratase; Provisional
15-279 3.12e-07

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 51.17  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  15 TPLVRLQRMAgntsntLLLKLEGNNPAGSVKDRPALSMITRAELRGQIHPgdtLIEATSGNTGIALAMAAAIKGYRMILI 94
Cdd:PRK08813  40 TPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRLGVQAITV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  95 MPDNSSAERKAAMTAYGAELIS--VSKDEGMEGARDLAERMQAegrgKVLDQFangDNPE--AHYTSTGPEIWRQTGGTV 170
Cdd:PRK08813 111 MPHGAPQTKIAGVAHWGATVRQhgNSYDEAYAFARELADQNGY----RFLSAF---DDPDviAGQGTVGIELAAHAPDVV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 171 thfVSSMGTTGTIMGTSRYLKEQNpeVQIVGLQpMEG---------------ASIP----GIRRWPHEYLPKIYQSDRVD 231
Cdd:PRK08813 184 ---IVPIGGGGLASGVALALKSQG--VRVVGAQ-VEGvdsmarairgdlreiAPVAtladGVKVKIPGFLTRRLCSSLLD 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488617769 232 RIIDMGQTEAEDTMRRLAREEGIFCGVSSGGSVAGALRISREVENAVI 279
Cdd:PRK08813 258 DVVIVREAELRETLVRLALEEHVIAEGAGALALAAGRRVSGKRKCAVV 305
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
67-115 2.26e-06

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 48.34  E-value: 2.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488617769  67 TLIEATSGNTGIALAMAAAIKGYRMILIMPDNSSAERKAAMTAYGAELI 115
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECI 166
PRK08329 PRK08329
threonine synthase; Validated
15-120 2.38e-06

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 48.28  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  15 TPLVRLqrmagntSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQihpgDTLIEATSGNTGIALAMAAAIKGYRMILI 94
Cdd:PRK08329  65 TPTVKR-------SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
                         90       100
                 ....*....|....*....|....*.
gi 488617769  95 MPDNSSAERKAAMTAYGAELISVSKD 120
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFVEGD 159
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
6-207 2.94e-06

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 48.09  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   6 QTIADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDR---PALSMITRAELRGQIhpgdtlIEATSGNTGIALAM 82
Cdd:PRK07048  16 ARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRgayNALSQFSPEQRRAGV------VTFSSGNHAQAIAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  83 AAAIKGYRMILIMPDNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAERmqaegRGKVLdqFANGDNPE--AHYTST 158
Cdd:PRK07048  90 SARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYdrYTEDREEIGRRLAEE-----RGLTL--IPPYDHPHviAGQGTA 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488617769 159 GPEIWRQTGGTVTHFVsSMGTTGTIMGTSRYLKEQNPEVQIVGLQPMEG 207
Cdd:PRK07048 163 AKELFEEVGPLDALFV-CLGGGGLLSGCALAARALSPGCKVYGVEPEAG 210
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
15-204 6.15e-06

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 47.44  E-value: 6.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  15 TPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMI---TRAEL-RGqihpgdtLIEATSGNTGIALAMAAAIKGYR 90
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMaqlTEEQLaRG-------VITASAGNHAQGVALSAARLGIK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  91 MILIMPDNSSAERKAAMTAYGAE--LISVSKDEGMEGARDLAERmqaEGRGKVldqfANGDNPE--AHYTSTGPEIWRQT 166
Cdd:PRK09224  94 AVIVMPVTTPDIKVDAVRAFGGEvvLHGDSFDEAYAHAIELAEE---EGLTFI----HPFDDPDviAGQGTIAMEILQQH 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 488617769 167 GGTVTH-FVSsMGTTGTIMGTSRYLKEQNPEVQIVGLQP 204
Cdd:PRK09224 167 PHPLDAvFVP-VGGGGLIAGVAAYIKQLRPEIKVIGVEP 204
eutB PRK07476
threonine dehydratase; Provisional
8-131 9.06e-06

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 46.50  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   8 IADCVGNTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPA----LSMITRAELRGqihpgdtLIEATSGNTGIALAMA 83
Cdd:PRK07476  13 IAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGAtnalLSLSAQERARG-------VVTASTGNHGRALAYA 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488617769  84 AAIKGYRMILIMPDNSSAERKAAMTAYGAELISV--SKDEGMEGARDLAE 131
Cdd:PRK07476  86 ARALGIRATICMSRLVPANKVDAIRALGAEVRIVgrSQDDAQAEVERLVR 135
PLN02970 PLN02970
serine racemase
5-209 2.00e-03

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 39.28  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769   5 YQTIADCVGNTPLVR---LQRMAGNTsntLLLKLEGNNPAGSVKDRPA----LSMITRAELRGqihpgdtLIEATSGNTG 77
Cdd:PLN02970  18 RKRIAPFIHRTPVLTsssLDALAGRS---LFFKCECFQKGGAFKFRGAcnaiFSLSDDQAEKG-------VVTHSSGNHA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  78 IALAMAAAIKGYRMILIMPDNSSAERKAAMTAYGAELISVskDEGMEGARDLAERMQAEgRGKVLdqfangdnpeAHYTS 157
Cdd:PLN02970  88 AALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWC--EPTVESREAVAARVQQE-TGAVL----------IHPYN 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617769 158 TGPEIWRQtgGTVT-HFVSSM----------GTTGTIMGTSRYLKEQNPEVQIVGLQPmEGAS 209
Cdd:PLN02970 155 DGRVISGQ--GTIAlEFLEQVpeldviivpiSGGGLISGIALAAKAIKPSIKIIAAEP-KGAD 214
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
14-132 2.49e-03

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: 38.82  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769  14 NTPLVRLQRMAGNTSNTLLLKLEGNNPAGSVKDRPALSMITRAELRGQ---IHpgdtLIEATSGNTGIALAMAAAIKGYR 90
Cdd:cd06448    1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLnecVH----VVCSSGGNAGLAAAYAARKLGVP 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488617769  91 MILIMPDNSSAERKAAMTAYGAELI---SVSKDEGMEGARDLAER 132
Cdd:cd06448   77 CTIVVPESTKPRVVEKLRDEGATVVvhgKVWWEADNYLREELAEN 121
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
176-293 4.62e-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: 38.29  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617769 176 SMGTTGTIMGTSRYLKeQNPEVQIVglqpmEGASIPGIRRWP-----HEYLpkiYQSDRVDrIIDMGQTEAEDTMRRLAR 250
Cdd:cd06446  251 FGGTAGVLHGLKMYTL-QDEDGQIV-----PPHSISAGLDYPgvgpeHAYL---KDSGRVE-YVAVTDEEALEAFKLLAR 320
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488617769 251 EEGIFCGVSSGGSVAGALRISREV-ENAVIVAIICDRGDRYLST 293
Cdd:cd06446  321 TEGIIPALESSHAIAYAIKLAKKLgKEKVIVVNLSGRGDKDLQT 364
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH