NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578830008|ref|XP_006721628|]
View 

serine racemase isoform X1 [Homo sapiens]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
5-320 1.51e-154

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.


The actual alignment was detected with superfamily member PLN02970:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 328  Bit Score: 436.42  E-value: 1.51e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   5 YCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSS 84
Cdd:PLN02970   7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  85 GNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQG 164
Cdd:PLN02970  84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 165 TIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI 244
Cdd:PLN02970 164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIIT-LPVTNTIADGLRASL 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSP--EVKNICIVLSGGNVDLT 320
Cdd:PLN02970 243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLG 320
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
5-320 1.51e-154

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 436.42  E-value: 1.51e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   5 YCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSS 84
Cdd:PLN02970   7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  85 GNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQG 164
Cdd:PLN02970  84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 165 TIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI 244
Cdd:PLN02970 164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIIT-LPVTNTIADGLRASL 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSP--EVKNICIVLSGGNVDLT 320
Cdd:PLN02970 243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLG 320
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
9-318 2.48e-142

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: 404.56  E-value: 2.48e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   9 FADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHG 88
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE---EERAKGVVAASAGNHA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  89 QALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562   78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 169 EVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIGLN 247
Cdd:cd01562  158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVT-LPEVDTIADGLAvKRPGEL 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578830008 248 TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVD 318
Cdd:cd01562  237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
7-320 1.63e-122

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: 355.11  E-value: 1.63e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGN 86
Cdd:COG1171    6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERAR---GVVAASAGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTI 166
Cdd:COG1171   83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIG 245
Cdd:COG1171  163 ALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 246 LNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVDLT 320
Cdd:COG1171  242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPD 313
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
19-314 1.20e-86

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: 262.63  E-value: 1.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   19 IRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   99 GIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEG-IMVHPNQEPAVIAGQGTIALEVLNQV-PL 176
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  177 VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI--GLNTWPIIRD 254
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  255 LVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEvKNICIVLSG 314
Cdd:pfam00291 237 YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
26-321 3.49e-79

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: 246.58  E-value: 3.49e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpdALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  106 VPQTAPDCKKLAIQAYGASIV-YCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYA-FATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  185 GGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVK-SSIGLNTWPIIRDLVDDIFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIK-AVESVRTIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008  264 EDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDLTS 321
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNL 290
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
5-320 1.51e-154

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 436.42  E-value: 1.51e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   5 YCISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSS 84
Cdd:PLN02970   7 YAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVVTHSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  85 GNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQG 164
Cdd:PLN02970  84 GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 165 TIALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI 244
Cdd:PLN02970 164 TIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIIT-LPVTNTIADGLRASL 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSP--EVKNICIVLSGGNVDLT 320
Cdd:PLN02970 243 GDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVDLG 320
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
9-318 2.48e-142

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: 404.56  E-value: 2.48e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   9 FADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHG 88
Cdd:cd01562    1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE---EERAKGVVAASAGNHA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  89 QALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562   78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 169 EVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIGLN 247
Cdd:cd01562  158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVT-LPEVDTIADGLAvKRPGEL 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578830008 248 TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVD 318
Cdd:cd01562  237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
7-320 1.63e-122

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: 355.11  E-value: 1.63e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGN 86
Cdd:COG1171    6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERAR---GVVAASAGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTI 166
Cdd:COG1171   83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVK-SSIG 245
Cdd:COG1171  163 ALEILEQLPDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 246 LNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQtvsPEVKNICIVLSGGNVDLT 320
Cdd:COG1171  242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPD 313
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
7-320 2.10e-109

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 321.58  E-value: 2.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGN 86
Cdd:PRK07048   6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSP---EQRRAGVVTFSSGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTI 166
Cdd:PRK07048  83 HAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVKS-SIG 245
Cdd:PRK07048 163 AKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIV-HIDTPRTIADGAQTqHLG 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 246 LNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDLT 320
Cdd:PRK07048 242 NYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALR---GKVPLKGKRVGVIISGGNVDLA 313
PRK06608 PRK06608
serine/threonine dehydratase;
8-318 6.03e-88

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 267.79  E-value: 6.03e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   8 SFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDalERKPKAVVTHSSGNH 87
Cdd:PRK06608   6 NPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQ--GKLPDKIVAYSTGNH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  88 GQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKrvTEETEGIMVHPNQEPAVIAGQGTIA 167
Cdd:PRK06608  84 GQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKE--DEEQGFYYIHPSDSDSTIAGAGTLC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 168 LEVLNQVPL-VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNLYPPETIADGVKS-SIG 245
Cdd:PRK06608 162 YEALQQLGFsPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPNTIADGLKTlSVS 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578830008 246 LNTWPIIRDLvDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPevKNICIVLSGGNVD 318
Cdd:PRK06608 242 ARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKP--QKLLVILSGGNID 311
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
19-314 1.20e-86

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: 262.63  E-value: 1.20e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   19 IRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   99 GIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEG-IMVHPNQEPAVIAGQGTIALEVLNQV-PL 176
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  177 VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI--GLNTWPIIRD 254
Cdd:pfam00291 158 PDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDE 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  255 LVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEvKNICIVLSG 314
Cdd:pfam00291 237 YVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
PRK06815 PRK06815
threonine/serine dehydratase;
9-319 3.38e-83

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 254.62  E-value: 3.38e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   9 FADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGNHG 88
Cdd:PRK06815   4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQ---GVITASSGNHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  89 QALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIAL 168
Cdd:PRK06815  81 QGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 169 EVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSSI--GL 246
Cdd:PRK06815 161 ELVEQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVE-VAEQPTLSDGTAGGVepGA 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 247 NTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQhfqtvSPEV--KNICIVLSGGNVDL 319
Cdd:PRK06815 240 ITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKL-----APRYqgKKVAVVLCGKNIVL 309
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
26-321 3.49e-79

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: 246.58  E-value: 3.49e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpdALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  106 VPQTAPDCKKLAIQAYGASIV-YCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYA-FATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  185 GGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVK-SSIGLNTWPIIRDLVDDIFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIK-AVESVRTIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008  264 EDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDLTS 321
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNL 290
PRK07334 PRK07334
threonine dehydratase; Provisional
7-318 3.40e-74

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 234.40  E-value: 3.40e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGN 86
Cdd:PRK07334   5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTE---EERARGVIAMSAGN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIV-YCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK07334  82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVlHGETLDEARA-HARELAEEEGLTFVHPYDDPAVIAGQGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQsKLKGKLMPNlyPPETIADG--VKsS 243
Cdd:PRK07334 161 VALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYA-AIKGVALPC--GGSTIAEGiaVK-Q 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578830008 244 IGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLS--QHFQTvspevKNICIVLSGGNVD 318
Cdd:PRK07334 237 PGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAypERFRG-----RKVGLVLSGGNID 308
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
7-324 1.97e-73

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 230.39  E-value: 1.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPdalERKPKAVVTHSSGN 86
Cdd:PRK08638   9 VAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTD---AEKRKGVVACSAGN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIV-YCEPSDESRENVAKRVTEETEgIMVHPNQEPAVIAGQGT 165
Cdd:PRK08638  86 HAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVlHGDNFNDTIAKVEEIVEEEGR-TFIPPYDDPKVIAGQGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVKSSI- 244
Cdd:PRK08638 165 IGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEIT-THRTTGTLADGCDVSRp 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 245 GLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVlSGGNVDLT--SS 322
Cdd:PRK08638 244 GNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAII-SGGNVDLSrvSQ 322

                 ..
gi 578830008 323 IT 324
Cdd:PRK08638 323 IT 324
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
26-315 6.15e-72

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: 6.15e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpDALERKPKAVVTH-SSGNHGQALTYAAKLEGIPAYI 104
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLA--EEEGKLPKGVIIEsTGGNTGIALAAAAARLGLKCTI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 105 VVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEG-IMVHPNQEPAVIAGQGTIALEVLNQVP--LVDALV 181
Cdd:cd00640   79 VMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQLGgqKPDAVV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 182 VPVGGGGMLAGIAITVKALKPSVKVYAAEPsnaddcyqsklkgklmpnlyppetiadgvkssiglntwpiirdlvdDIFT 261
Cdd:cd00640  159 VPVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVT 192
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578830008 262 VTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTvsPEVKNICIVLSGG 315
Cdd:cd00640  193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL--GKGKTVVVILTGG 244
eutB PRK07476
threonine dehydratase; Provisional
7-319 1.81e-70

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 222.15  E-value: 1.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGN 86
Cdd:PRK07476   1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERAR---GVVTASTGN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPS-DESRENVAkRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK07476  78 HGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSqDDAQAEVE-RLVREEGLTMVPPFDDPRIIAGQGT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKlmP-NLYPPETIADGVKSSI 244
Cdd:PRK07476 157 IGLEILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAGR--PvQVEEVPTLADSLGGGI 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008 245 GLN---TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVLSGGNVDL 319
Cdd:PRK07476 235 GLDnryTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLA---GKIAARDGPIVVVVSGANIDM 309
PRK08246 PRK08246
serine/threonine dehydratase;
7-321 2.50e-62

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 200.95  E-value: 2.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSIlNQLTGRNLFFKCELFQKTGSFKIRGALNAVRS-LVPDAlerkpkAVVTHSSG 85
Cdd:PRK08246   5 ITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAaPVPAA------GVVAASGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  86 NHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK08246  78 NAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 166 IALEVLNQVPLVDALVVPVGGGGMLAGIAitvKALKPSVKVYAAEPSNADDCYQSKLKGKlmpnlyPPETIADGVKSS-- 243
Cdd:PRK08246 158 LGLEIEEQAPGVDTVLVAVGGGGLIAGIA---AWFEGRARVVAVEPEGAPTLHAALAAGE------PVDVPVSGIAADsl 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 244 ----IGLNTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEvkNICIVLSGGNVDL 319
Cdd:PRK08246 229 garrVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--RVAVVLCGANTDP 306

                 ..
gi 578830008 320 TS 321
Cdd:PRK08246 307 AT 308
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
7-319 1.24e-57

ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.


Pssm-ID: 132036 [Multi-domain]  Cd Length: 317  Bit Score: 188.91  E-value: 1.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008    7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpDALERKpKAVVTHSSGN 86
Cdd:TIGR02991   1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSL--SDTQRA-AGVVAASTGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASI-VYCEPSDESRENVaKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:TIGR02991  78 HGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVrIVGRSQDDAQEEV-ERLVADRGLTMLPPFDHPDIVAGQGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  166 IALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKlmPNLYPPE-TIADGVKSSI 244
Cdd:TIGR02991 157 LGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGR--PVLVAELpTLADSLGGGI 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008  245 GLN---TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPevknICIVLSGGNVDL 319
Cdd:TIGR02991 235 GLDnrvTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGP----CAVIVSGRNIDM 308
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
26-317 8.82e-55

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 186.50  E-value: 8.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK09224  21 TPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLAR---GVITASAGNHAQGVALSAARLGIKAVIV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 106 VPQTAPDCKKLAIQAYGASIV-YCEPSDESRENvAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVP 183
Cdd:PRK09224  98 MPVTTPDIKVDAVRAFGGEVVlHGDSFDEAYAH-AIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPhPLDAVFVP 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 184 VGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKlmpnlypPETI------ADG--VKsSIGLNTWPIIRDL 255
Cdd:PRK09224 177 VGGGGLIAGVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGE-------RVDLpqvglfADGvaVK-RIGEETFRLCQEY 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578830008 256 VDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAvLSQHFQTVSPEVKNICIVLSGGNV 317
Cdd:PRK09224 249 VDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAG-LKKYVAQHGIEGETLVAILSGANM 309
PRK12483 PRK12483
threonine dehydratase; Reviewed
26-318 1.32e-54

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 186.54  E-value: 1.32e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERkpkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLAR---GVITASAGNHAQGVALAAARLGVKAVIV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 106 VPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVPV 184
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPgPLDAIFVPV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 185 GGGGMLAGIAITVKALKPSVKVYAAEPSNAdDCYQSKLKGKLMPNLYPPETIADGVK-SSIGLNTWPIIRDLVDDIFTVT 263
Cdd:PRK12483 195 GGGGLIAGIAAYVKYVRPEIKVIGVEPDDS-NCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHYVDEVVTVS 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 264 EDEIKCATQLVWERMKLLIEPTAGVGVAAvLSQHFQTVSPEVKNICIVLSGGNVD 318
Cdd:PRK12483 274 TDELCAAIKDIYDDTRSITEPAGALAVAG-IKKYAEREGIEGQTLVAIDSGANVN 327
PRK08639 PRK08639
threonine dehydratase; Validated
7-318 3.05e-53

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 180.39  E-value: 3.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSSGN 86
Cdd:PRK08639   7 VSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELA---AGVVCASAGN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  87 HGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGAS----IVYCEPSDESrENVAKRVTEETEGIMVHPNQEPAVIAG 162
Cdd:PRK08639  84 HAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveiVLVGDTFDDS-AAAAQEYAEETGATFIPPFDDPDVIAG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 163 QGTIALEVLNQV---PLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKL--MPNLyppETIA 237
Cdd:PRK08639 163 QGTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPvtLEKI---DKFV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 238 DG--VKsSIGLNTWPIIRDLVDDIFTVTEDEIkCATQLvwermKLL------IEPtAGVGVAAVLSQHFQTVspEVKNIC 309
Cdd:PRK08639 240 DGaaVA-RVGDLTFEILKDVVDDVVLVPEGAV-CTTIL-----ELYnkegivAEP-AGALSIAALELYKDEI--KGKTVV 309

                 ....*....
gi 578830008 310 IVLSGGNVD 318
Cdd:PRK08639 310 CVISGGNND 318
PLN02550 PLN02550
threonine dehydratase
24-318 1.02e-40

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 150.46  E-value: 1.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  24 HLTPVLTSSI--------------LNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALErkpKAVVTHSSGNHGQ 89
Cdd:PLN02550  94 YLTNILSAKVydvaiesplqlakkLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLD---KGVICSSAGNHAQ 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  90 ALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALE 169
Cdd:PLN02550 171 GVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGME 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 170 VLNQVP-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMpNLYPPETIADGVK-SSIGLN 247
Cdd:PLN02550 251 IVRQHQgPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERV-MLDQVGGFADGVAvKEVGEE 329
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578830008 248 TWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVlSQHFQTVSPEVKNICIVLSGGNVD 318
Cdd:PLN02550 330 TFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGA-EAYCKYYGLKDENVVAITSGANMN 399
PRK08813 PRK08813
threonine dehydratase; Provisional
7-320 2.09e-38

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 139.76  E-value: 2.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   7 ISFADVEKAHINIRDSIHLTPVLTSSILNqltgrnLFFKCELFQKTGSFKIRGALNAVRSlvpdALER-KPKAVVTHSSG 85
Cdd:PRK08813  21 VSVADVLAAQARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLA----GLERgDERPVICASAG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  86 NHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGT 165
Cdd:PRK08813  91 NHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 166 IALEVLNQVPlvDALVVPVGGGGMLAGIAITVKAlkPSVKVYAAEPSNADDCYQSkLKGKLMpNLYPPETIADGVKSSI- 244
Cdd:PRK08813 171 VGIELAAHAP--DVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARA-IRGDLR-EIAPVATLADGVKVKIp 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578830008 245 GLNTWPIIRDLVDDIFTVTEDEIK-CATQLVWERmKLLIEPTAGVGVAAvlsqhFQTVSPEVKniCIVLSGGNVDLT 320
Cdd:PRK08813 245 GFLTRRLCSSLLDDVVIVREAELReTLVRLALEE-HVIAEGAGALALAA-----GRRVSGKRK--CAVVSGGNIDAT 313
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
9-294 5.34e-37

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: 136.87  E-value: 5.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   9 FADVEKAhINIRDSIhlTPVLTSSILNQLTGRNLFFKcELFQ-KTGSFKIRGAlnAVrsLVPDALERKPKAVVTHSSGNH 87
Cdd:COG0498   53 FDDEEKA-VSLGEGG--TPLVKAPRLADELGKNLYVK-EEGHnPTGSFKDRAM--QV--AVSLALERGAKTIVCASSGNG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  88 GQAL-TYAAKlEGIPAYIVVPQT-APDCKKLAIQAYGASIVYCEPS-DEsRENVAKRVTEETEGIMVHpNQEPAVIAGQG 164
Cdd:COG0498  125 SAALaAYAAR-AGIEVFVFVPEGkVSPGQLAQMLTYGAHVIAVDGNfDD-AQRLVKELAADEGLYAVN-SINPARLEGQK 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 165 TIALEV---LNQVPlvDALVVPVGGGGMLAGIAitvKALK-----------PsvKVYAAEPSNADDCYQSKLKGKLMPNL 230
Cdd:COG0498  202 TYAFEIaeqLGRVP--DWVVVPTGNGGNILAGY---KAFKelkelglidrlP--RLIAVQATGCNPILTAFETGRDEYEP 274
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578830008 231 YPPETIADGVksSIG--LNTWPIIRDLVD---DIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVL 294
Cdd:COG0498  275 ERPETIAPSM--DIGnpSNGERALFALREsggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLR 341
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
26-312 6.75e-37

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: 134.18  E-value: 6.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRslvpDALER---KPKA-VVTHSSGNHGQALTYAAKLEGIP 101
Cdd:cd01561    3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIE----DAEKRgllKPGTtIIEPTSGNTGIGLAMVAAAKGYR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 102 AYIVVPQTAPDCKKLAIQAYGASIVYCEPSD----ESRENVAKRVTEETEGImVHPNQ--EPA-VIAGQGTIALEVLNQV 174
Cdd:cd01561   79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEadgmKGAIAKARELAAETPNA-FWLNQfeNPAnPEAHYETTAPEIWEQL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 175 P-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADdcyqsklkgkLMPNLYPPETIADGvkssIGLNTWPII- 252
Cdd:cd01561  158 DgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSV----------LFSGGPPGPHKIEG----IGAGFIPENl 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578830008 253 -RDLVDDIFTVTEDE-IKCATQLVwERMKLLIEPTAGVGVAAVLsqHFQTVSPEVKNICIVL 312
Cdd:cd01561  224 dRSLIDEVVRVSDEEaFAMARRLA-REEGLLVGGSSGAAVAAAL--KLAKRLGPGKTIVTIL 282
PRK06110 PRK06110
threonine dehydratase;
8-332 1.38e-36

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 133.97  E-value: 1.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   8 SFADVEKAHINIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVpdALERKPKAVVTHSSGNH 87
Cdd:PRK06110   4 TLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLA--RRGPRVRGVISATRGNH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  88 GQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIV-YCEPSDESRENvAKRVTEETEGIMVhPNQEPAVIAGQGTI 166
Cdd:PRK06110  82 GQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIeHGEDFQAAREE-AARLAAERGLHMV-PSFHPDLVRGVATY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 167 ALEVLNQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKLKGKLMPNlypP--ETIADGVKSSI 244
Cdd:PRK06110 160 ALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTT---PvaTTLADGMACRT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 245 GL-NTWPIIRDLVDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQTvspEVKNICIVLSGGNVDLTSSI 323
Cdd:PRK06110 237 PDpEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERL---AGKRVGLVLSGGNIDRAVFA 313

                 ....*....
gi 578830008 324 TWVKQAERP 332
Cdd:PRK06110 314 RVLAGAAAE 322
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
26-316 2.39e-34

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: 128.19  E-value: 2.39e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSLVPDALERKPkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:cd06448    2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECV-HVVCSSGGNAGLAAAYAARKLGVPCTIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 106 VPQTAPDCKKLAIQAYGASIV-----YCEPSDESRENVAKRvteETEGIMVHPNQEPAVIAGQGTIALEVLNQVPL---V 177
Cdd:cd06448   81 VPESTKPRVVEKLRDEGATVVvhgkvWWEADNYLREELAEN---DPGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 178 DALVVPVGGGGMLAGIaitVKALK----PSVKVYAAEPSNADDCYQSKLKGKLMPnLYPPETIADGVKSS-IGLNTW--- 249
Cdd:cd06448  158 DAIVCSVGGGGLLNGI---VQGLErngwGDIPVVAVETEGAHSLNASLKAGKLVT-LPKITSVATSLGAKtVSSQALeya 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 250 ---PIIRDLVDDIFTVTedeikcATQLVWERMKLLIEPTAGVGVAAVLSQHFQTVSPEVK-----NICIVLSGGN 316
Cdd:cd06448  234 qehNIKSEVVSDRDAVQ------ACLRFADDERILVEPACGAALAVVYSGKILDLQLEVLltpldNVVVVVCGGS 302
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
26-294 3.80e-33

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: 125.01  E-value: 3.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSIL-NQLTGRNLFFKCELFQKTGSFKIRGALNAVRSlvpdALERKPKAVVTHSSGNHGQAL-TYAAKlEGIPAY 103
Cdd:cd01563   23 TPLVRAPRLgERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSK----AKELGVKAVACASTGNTSASLaAYAAR-AGIKCV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 104 IVVPQTAPDCKKLAIQAYGASIVycePSDESRENVAKRVTEETE--GIMVHPNQEPAVIAGQGTIALEVLNQ----VPlv 177
Cdd:cd01563   98 VFLPAGKALGKLAQALAYGATVL---AVEGNFDDALRLVRELAEenWIYLSNSLNPYRLEGQKTIAFEIAEQlgweVP-- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 178 DALVVPVGGGGMLAGIAITVKALKPS------VKVYAAEPSNADDCYQSKLKGKLMPNLYP-PETIADGVKssIGlN--T 248
Cdd:cd01563  173 DYVVVPVGNGGNITAIWKGFKELKELglidrlPRMVGVQAEGAAPIVRAFKEGKDDIEPVEnPETIATAIR--IG-NpaS 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578830008 249 WPIIRDLVD----DIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVL 294
Cdd:cd01563  250 GPKALRAVResggTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
18-266 2.53e-30

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: 116.69  E-value: 2.53e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  18 NIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRgalnAVRSLVPDALER---KP-KAVVTHSSGNHGQALTY 93
Cdd:COG0031    6 SILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR----IALSMIEDAEKRgllKPgGTIVEATSGNTGIGLAM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  94 AAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSD--ESRENVAKRVTEETEGiMVHPNQ--EPA-VIAGQGTIAL 168
Cdd:COG0031   82 VAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEgmKGAIDKAEELAAETPG-AFWPNQfeNPAnPEAHYETTGP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 169 EVLNQVPL-VDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNA-----DDCYQSKLKGklmpnlyppetiadgvks 242
Cdd:COG0031  161 EIWEQTDGkVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSpllsgGEPGPHKIEG------------------ 222
                        250       260
                 ....*....|....*....|....*.
gi 578830008 243 sIGLNTWP--IIRDLVDDIFTVTEDE 266
Cdd:COG0031  223 -IGAGFVPkiLDPSLIDEVITVSDEE 247
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
33-318 3.19e-24

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: 100.92  E-value: 3.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008   33 ILNQLTGRNLFFKCELFQKTGSFKIRGalnaVRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPD 112
Cdd:TIGR00260  31 LAANVGIKNLYVKELGHNPTLSFKDRG----MAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKIS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  113 CKKLAIQ-AYGASIVYCEPSDESRENVAKRVTEETEGIMVHP-NQEPAVIAGQGTIALEVLNQVP--LVDALVVPVGGGG 188
Cdd:TIGR00260 107 LGKLAQAlGYNAEVVAIDGNFDDAQRLVKQLFEDKPALGLNSaNSIPYRLEGQKTYAFEAVEQLGweAPDKVVVPVPNSG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  189 MLAGIAITVKALK-------PsvKVYAAEPSNADDCYQSKLKGKlmpNLYP---PETIA---DGVKSSIGLNTWPIIRDL 255
Cdd:TIGR00260 187 NFGAIWKGFKEKKmlgldslP--VKRGIQAEGAADIVRAFLEGG---QWEPietPETLStamDIGNPANWPRALEAFRRS 261
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830008  256 VDDIFTVTEDEIKCATQLVWERMKLLIEPTAGVGVAAVLSQHFQ-TVSPEVKNICIVLSGGNVD 318
Cdd:TIGR00260 262 NGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKgTADPAERVVCALTGNGLKD 325
PRK08329 PRK08329
threonine synthase; Validated
24-319 2.73e-20

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 90.27  E-value: 2.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  24 HLTPVLTSSILnqlTGRNLFFKCELFQKTGSFKIRGALNAVRSLvpdaLERKPKAVVTHSSGNHGQALTYAAKLEGIPAY 103
Cdd:PRK08329  59 HLTPPITPTVK---RSIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGINEVVIDSSGNAALSLALYSLSEGIKVH 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 104 IVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVP 183
Cdd:PRK08329 132 VFVSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVPDYAFVP 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 184 VGGGGMLAGIAITVKALK--------PSVKVYAAEPSNAdDCYQSKLKGKL-----MPNlyPP--ETIADGVKSSIGLnt 248
Cdd:PRK08329 212 VGSGTLFLGIWKGFKELHemgeiskmPKLVAVQAEGYES-LCKRSKSENKLadgiaIPE--PPrkEEMLRALEESNGF-- 286
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578830008 249 wpiirdlvddIFTVTEDEIKCAtqLVW-ERMKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSGGNVDL 319
Cdd:PRK08329 287 ----------CISVGEEETRAA--LHWlRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLKN 346
PRK05638 PRK05638
threonine synthase; Validated
26-314 1.49e-18

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 86.02  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLtGRNLFFKCELFQKTGSFKIRGALNAVRslvpDALERKPKAVVTHSSGNHGQALT-YAAKlEGIPAYI 104
Cdd:PRK05638  67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVS----YGLPYAANGFIVASDGNAAASVAaYSAR-AGKEAFV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 105 VVPQTAPDCKKLAIQAYGAS-IVYCEPSDESREnVAKRVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQV-PlvDALVV 182
Cdd:PRK05638 141 VVPRKVDKGKLIQMIAFGAKiIRYGESVDEAIE-YAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEInP--THVIV 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 183 PVGGGGMLAGI------AITVKALKPSVKVYAAEPSNADDCYQS------KLKGKLMPNLYppetIADGVKSSIGLNtwp 250
Cdd:PRK05638 218 PTGSGSYLYSIykgfkeLLEIGVIEEIPKLIAVQTERCNPIASEilgnktKCNETKALGLY----VKNPVMKEYVSE--- 290
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830008 251 IIRDLVDDIFTVTEDEIKCATQLVWERmKLLIEPTAGVGVAAVLSQHFQTVSPEVKNICIVLSG 314
Cdd:PRK05638 291 AIKESGGTAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTG 353
PRK10717 PRK10717
cysteine synthase A; Provisional
18-211 7.31e-17

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 79.91  E-value: 7.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  18 NIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRslvpDALER---KP-KAVVTHSSGNHGQALTY 93
Cdd:PRK10717   6 DVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIW----DAEKRgllKPgGTIVEGTAGNTGIGLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  94 AAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESREN----VAKRVTEEtegiMVHPNQEPAVIAGQ------ 163
Cdd:PRK10717  82 VAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNnyvkGAGRLAEE----LVASEPNGAIWANQfdnpan 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578830008 164 -----GTIALEVLNQVP-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEP 211
Cdd:PRK10717 158 reahyETTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADP 211
PRK06381 PRK06381
threonine synthase; Validated
26-193 1.70e-16

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 78.98  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVLTSSILNQLTG-RNLFFKCELFQKTGSFKIRGALNAVRslvpDALERKPKAVVTHSSGNHGQALTYAAKLEGIPAYI 104
Cdd:PRK06381  16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVR----RAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 105 VVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAKRVTEETEGIMVHPNQEPAVIA--GQGTIALEVLNQVPLV-DALV 181
Cdd:PRK06381  92 FIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSVNSVVDieAYSAIAYEIYEALGDVpDAVA 171
                        170
                 ....*....|..
gi 578830008 182 VPVGGGGMLAGI 193
Cdd:PRK06381 172 VPVGNGTTLAGI 183
PRK06450 PRK06450
threonine synthase; Validated
19-314 8.76e-15

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 74.00  E-value: 8.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  19 IRDSIHLTPVLTSSIlnqlTGRNLFFKCELFQKTGSFKIRGAlnavRSLVPDALERKPKAVVTHSSGNHGQALTYAAKLE 98
Cdd:PRK06450  48 IKHFISLGEGRTPLI----KKGNIWFKLDFLNPTGSYKDRGS----VTLISYLAEKGIKQISEDSSGNAGASIAAYGAAA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  99 GIPAYIVVPQTAPDCKKLAIQAYGASIVYCEpsdESRENVAKrVTEETEGIMVHPNQEPAVIAGQGTIALEVLNQ----V 174
Cdd:PRK06450 120 GIEVKIFVPETASGGKLKQIESYGAEVVRVR---GSREDVAK-AAENSGYYYASHVLQPQFRDGIRTLAYEIAKDldwkI 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 175 PlvDALVVPVGGGGMLAGIAITVKALKPS------VKVYAAEPSNADDCYqSKLKGKlmpNLYPPE---TIADGVKSsig 245
Cdd:PRK06450 196 P--NYVFIPVSAGTLLLGVYSGFKHLLDSgvisemPKIVAVQTEQVSPLC-AKFKGI---SYTPPDkvtSIADALVS--- 266
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578830008 246 lnTWPIIRDLVDDIF-------TVTEDEIKCAtqlvWE---RMKLLIEPTAGVGVAAvlsqhFQTVSPEvkNICIVLSG 314
Cdd:PRK06450 267 --TRPFLLDYMVKALseygeciVVSDNEIVEA----WKelaKKGLLVEYSSATVYAA-----YKKYSVN--DSVLVLTG 332
PRK08197 PRK08197
threonine synthase; Validated
25-201 1.08e-14

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 74.27  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  25 LTPVLTSSILNQLTG-RNLFFKCELFQKTGSFKIRGALNAVRSlvpdALERKPKAVVTHSSGNHGQAL-TYAAKLeGIPA 102
Cdd:PRK08197  79 MTPLLPLPRLGKALGiGRLWVKDEGLNPTGSFKARGLAVGVSR----AKELGVKHLAMPTNGNAGAAWaAYAARA-GIRA 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 103 YIVVPQTAPDCKKLAIQAYGASIVYCEP--SDESREnVAKRVTEetEGIM-VHPNQEPAVIAGQGTIALEVLNQ----VP 175
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAELYLVDGliSDAGKI-VAEAVAE--YGWFdVSTLKEPYRIEGKKTMGLELAEQlgwrLP 230
                        170       180
                 ....*....|....*....|....*.
gi 578830008 176 lvDALVVPVGGGGMLAGIaitVKALK 201
Cdd:PRK08197 231 --DVILYPTGGGVGLIGI---WKAFD 251
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
53-295 1.69e-14

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 73.76  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  53 GSFKIRGALNAV------------RSLVPDAL---ERKPKA----VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDC 113
Cdd:PRK08206  74 NAFKALGGAYAVarllaeklgldiSELSFEELtsgEVREKLgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 114 KKLAIQAYGASIV-----YcepsDES-REnvAKRVTEETEGIMVhpnQEPA----------VIAGQGTIALEVLNQVPlv 177
Cdd:PRK08206 154 RVDAIRALGAECIitdgnY----DDSvRL--AAQEAQENGWVVV---QDTAwegyeeiptwIMQGYGTMADEAVEQLK-- 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 178 DALVVP--------VGG--GGMLAGIAITVKALKPSVKVyaAEPSNADDCYQSKLKGKLmpnlyppeTIADGVKSSI--G 245
Cdd:PRK08206 223 EMGVPPthvflqagVGSlaGAVLGYFAEVYGEQRPHFVV--VEPDQADCLYQSAVDGKP--------VAVTGDMDTImaG 292
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008 246 LN-------TWPIIRDLVDDIFTVTEDEIKCAtqlvwerMKLLIEPTAG-----------VGVAAVLS 295
Cdd:PRK08206 293 LAcgepnplAWEILRNCADAFISCPDEVAALG-------MRILANPLGGdppivsgesgaVGLGALAA 353
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
18-294 5.57e-10

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 59.97  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  18 NIRDS----IHLTPVLtssILNQLT---GRNLFFKCELFQKTGSFKIRGALnavrSLVPDALERK-----PKAVVTHSSG 85
Cdd:PLN02556  48 KIKTDasqlIGKTPLV---YLNKVTegcGAYIAAKQEMFQPTSSIKDRPAL----AMIEDAEKKNlitpgKTTLIEPTSG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  86 NHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENVAK--RVTEET-EGIMVHPNQEPA-VIA 161
Cdd:PLN02556 121 NMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKayELLESTpDAFMLQQFSNPAnTQV 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 162 GQGTIALEVL-NQVPLVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKlkgklmPNlyPPETIADGV 240
Cdd:PLN02556 201 HFETTGPEIWeDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGK------PG--PHHITGNGV 272
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578830008 241 kssiGLNTWPIIRDLVDDIFTVT-EDEIKCATQLVWERmKLLIEPTAGVGVAAVL 294
Cdd:PLN02556 273 ----GFKPDILDMDVMEKVLEVSsEDAVNMARELALKE-GLMVGISSGANTVAAL 322
PLN02356 PLN02356
phosphateglycerate kinase
21-211 8.65e-09

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 56.54  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  21 DSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNavrsLVPDALERK---PKAVVTH-SSGNHGQALTYAAK 96
Cdd:PLN02356  49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVK----IIEEALESGqlfPGGVVTEgSAGSTAISLATVAP 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  97 LEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEP----------------SDESRENVAKR---------VTEETEGIMV 151
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVRPvsithkdhyvniarrrALEANELASKRrkgsetdgiHLEKTNGCIS 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 152 HPNQEPAVIAG---------------------QGTiALEVLNQVPL-VDALVVPVGGGGMLAGIAITVKALKPSVKVYAA 209
Cdd:PLN02356 205 EEEKENSLFSSsctggffadqfenlanfrahyEGT-GPEIWEQTQGnLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLI 283

                 ..
gi 578830008 210 EP 211
Cdd:PLN02356 284 DP 285
PLN02569 PLN02569
threonine synthase
52-192 5.73e-08

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 54.05  E-value: 5.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  52 TGSFKIRGALNAVrSLVpDALERKPK---AVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLaIQ--AYGASIV 126
Cdd:PLN02569 162 TGSFKDLGMTVLV-SQV-NRLRKMAKpvvGVGCASTGDTSAALSAYCAAAGIPSIVFLPADKISIAQL-VQpiANGALVL 238
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 127 YCEPSDESRENVAKRVTEETEgIMVHPNQEPAVIAGQGTIALEVLNQ----VPlvDALVVPVGGGGMLAG 192
Cdd:PLN02569 239 SIDTDFDGCMRLIREVTAELP-IYLANSLNSLRLEGQKTAAIEILQQfdweVP--DWVIVPGGNLGNIYA 305
PLN03013 PLN03013
cysteine synthase
18-294 5.22e-06

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 47.85  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  18 NIRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALnavrSLVPDALERK-----PKAVVTHSSGNHGQALT 92
Cdd:PLN03013 116 NVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGY----SMVTDAEQKGfispgKSVLVEPTSGNTGIGLA 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  93 YAAKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCEPSDESRENV--AKRVTEET-EGIMVHPNQEPAVIAGQ-GTIAL 168
Cdd:PLN03013 192 FIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVqkAEEILKNTpDAYMLQQFDNPANPKIHyETTGP 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 169 EVLNQVP-LVDALVVPVGGGGMLAGIAITVKALKPSVKVYAAEPSNADDCYQSKlkgklmPNLYPPETIADGVkssIGLN 247
Cdd:PLN03013 272 EIWDDTKgKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGK------PGPHKIQGIGAGF---IPKN 342
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578830008 248 twpIIRDLVDDIFTVTEDE-IKCATQLVWERmKLLIEPTAGVGVAAVL 294
Cdd:PLN03013 343 ---LDQKIMDEVIAISSEEaIETAKQLALKE-GLMVGISSGAAAAAAI 386
cysM PRK11761
cysteine synthase CysM;
19-150 9.86e-06

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 46.40  E-value: 9.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  19 IRDSIHLTPVLTSSILNQLTGRNLFFKCELFQKTGSFKIRGALNAVRSlvpdALER---KPKAV-VTHSSGNHGQALTYA 94
Cdd:PRK11761   6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQ----AEKRgeiKPGDTlIEATSGNTGIALAMI 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578830008  95 AKLEGIPAYIVVPQTAPDCKKLAIQAYGASIVYCePSDESRE---NVAKRVTEETEGIM 150
Cdd:PRK11761  82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILV-PKEQGMEgarDLALQMQAEGEGKV 139
PLN00011 PLN00011
cysteine synthase
45-323 9.92e-06

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 46.53  E-value: 9.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  45 KCELFQKTGSFKIRGALNAVRSLVPDALERKPKA-VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPDCKKLAIQAYGA 123
Cdd:PLN00011  37 KLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKStLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALGA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 124 SIVYCEPSDESR---ENVAKRVTEETEGIMVHPNQEPAVIAGQ-GTIALEVL-NQVPLVDALVVPVGGGGMLAGIAITVK 198
Cdd:PLN00011 117 EVHLTDQSIGLKgmlEKAEEILSKTPGGYIPQQFENPANPEIHyRTTGPEIWrDSAGKVDILVAGVGTGGTATGVGKFLK 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008 199 ALKPSVKVYAAEPSnaddcyQSKLKGKLMPNLYPPETIADG-VKSSIGLNtwpiirdLVDDIFTVTEDEIKCATQLVWER 277
Cdd:PLN00011 197 EKNKDIKVCVVEPV------ESAVLSGGQPGPHLIQGIGSGiIPFNLDLT-------IVDEIIQVTGEEAIETAKLLALK 263
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578830008 278 MKLLIEPTAGVGVAAVLSqhfQTVSPEVKNICIVL---SGGNVDLTSSI 323
Cdd:PLN00011 264 EGLLVGISSGAAAAAALK---VAKRPENAGKLIVVifpSGGERYLSTKL 309
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
26-206 4.20e-04

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 41.64  E-value: 4.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  26 TPVltsSILNQLTgRNLFFKCELFQK----TGSFKIRGalNAVRSL---VPDALERKPKAVVT----HSsgNHGQALTYA 94
Cdd:cd06449    1 TPI---QYLPRLS-EHLGGKVEIYAKrddcNSGLAFGG--NKIRKLeylLPDALAKGADTLVTvggiQS--NHTRQVAAV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830008  95 AKLEGIPAYIV----VPQTAPDCKK----LAIQAYGASIVYCEPS-----DESRENVAKRVTEE-------TEGIMVHPn 154
Cdd:cd06449   73 AAKLGLKCVLVqenwVPYSDAVYDRvgniLLSRIMGADVRLVSAGfdigiRKSFEEAAEEVEAKggkpyviPAGGSEHP- 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578830008 155 qepavIAGQGTI--ALEVLNQVPLV----DALVVPVGGGGMLAGIAITVKALKPSVKV 206
Cdd:cd06449  152 -----LGGLGYVgfVLEIAQQEEELgfkfDSIVVCSVTGSTHAGLSVGLAALGRQRRV 204
 
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