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Conserved domains on  [gi|1852860284|ref|NP_001371183|]
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serine dehydratase-like [Mus musculus]

Protein Classification

serine/threonine dehydratase family protein( domain architecture ID 10157824)

serine/threonine dehydratase family protein such as L-serine dehydratase/L-threonine deaminase, a pyridoxal-5'-phosphate (PLP)-dependent enzyme that catalyzes dehydration of L-Ser/Thr to yield pyruvate/ketobutyrate and ammonia

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 17-326 1.38e-147

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: 417.86  E-value: 1.38e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  17 VTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRG---CRHLVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:cd06448     1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLTGKVW-DEANVKAQELATRD-GWVNVSPFDHPLIWEGHASLVRELKESLGT--PPGAV 169
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 170 VLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKECEVLS 249
Cdd:cd06448   161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852860284 250 EVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgRLSSALASVVVIVCGGNNISSQQLQELKIQL 326
Cdd:cd06448   241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 17-326 1.38e-147

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: 417.86  E-value: 1.38e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  17 VTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRG---CRHLVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:cd06448     1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLTGKVW-DEANVKAQELATRD-GWVNVSPFDHPLIWEGHASLVRELKESLGT--PPGAV 169
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 170 VLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKECEVLS 249
Cdd:cd06448   161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852860284 250 EVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgRLSSALASVVVIVCGGNNISSQQLQELKIQL 326
Cdd:cd06448   241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 4-313 1.70e-65

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: 209.12  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284   4 ALAERVgaEPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAA 79
Cdd:COG1171    13 AAAARI--AGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynaLASLSEEERARG---VVAASAGNHAQGV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  80 AYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELK 159
Cdd:COG1171    88 AYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEIL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 160 ESLGTPpgavvlavggggllagvTAGLLEVG------------WQHVP---IVAMETRGAHSFNSALQAGRPVTLPDITS 224
Cdd:COG1171   168 EQLPDL-----------------DAVFVPVGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSLAAGEPVTLPGVDT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 225 VAKSLGAKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssala 302
Cdd:COG1171   231 IADGLAVGRPGELTFEILRDLvdDIVT--VSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------ 299

                         330
                  ....*....|.
gi 1852860284 303 SVVVIVCGGNN 313
Cdd:COG1171   300 RVVVVLSGGNI 310
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-310 7.93e-59

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: 190.98  E-value: 7.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  12 EPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQmAKRGC--RHLVCSSGGNAGIAAAYSARKLGIP 89
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEggKTVVEASSGNHGRALAAAAARLGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  90 VTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA-TRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGA 168
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 169 VVLAVGGGGLLAGVTAGLLEvGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAK-TVAARTLECAKECEV 247
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852860284 248 LSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwRLQAEGRLSSAlASVVVIVCG 310
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLTG 295
PRK08246 PRK08246
serine/threonine dehydratase;
4-312 2.04e-41

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 146.25  E-value: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284   4 ALAERVGaePFHRVTPLLESwALSQVAGMPVFLKYENVQIAGSFKIRGIghFCQQMAKR-GCRHLVCSSGGNAGIAAAYS 82
Cdd:PRK08246   12 AAAQRIA--PHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGA--FNRLLAAPvPAAGVVAASGGNAGLAVAYA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  83 ARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESL 162
Cdd:PRK08246   87 AAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 163 GTPPGAvvlavggggllagvtagLLEVG----------W--QHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLG 230
Cdd:PRK08246  167 PGVDTV-----------------LVAVGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 231 AKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgrlssalaSVVVIVCG 310
Cdd:PRK08246  230 ARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCG 301


                  ..
gi 1852860284 311 GN 312
Cdd:PRK08246  302 AN 303
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 18-312 4.76e-41

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: 147.20  E-value: 4.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSEDQRQRG---VVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVVLAV 173
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 174 GGGGLLAGVTA--GLLEvgwqHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKEC--EVLS 249
Cdd:TIGR01127 158 GGGLISGVASAakQINP----NVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYvdDVVT 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852860284 250 evVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalaSVVVIVCGGN 312
Cdd:TIGR01127 234 --VDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQ---KVDVKGK------KIAVVLSGGN 285
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 17-326 1.38e-147

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: 417.86  E-value: 1.38e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  17 VTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRG---CRHLVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:cd06448     1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLTGKVW-DEANVKAQELATRD-GWVNVSPFDHPLIWEGHASLVRELKESLGT--PPGAV 169
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 170 VLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKECEVLS 249
Cdd:cd06448   161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852860284 250 EVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgRLSSALASVVVIVCGGNNISSQQLQELKIQL 326
Cdd:cd06448   241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 4-313 1.70e-65

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: 209.12  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284   4 ALAERVgaEPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAA 79
Cdd:COG1171    13 AAAARI--AGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynaLASLSEEERARG---VVAASAGNHAQGV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  80 AYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELK 159
Cdd:COG1171    88 AYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIALEIL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 160 ESLGTPpgavvlavggggllagvTAGLLEVG------------WQHVP---IVAMETRGAHSFNSALQAGRPVTLPDITS 224
Cdd:COG1171   168 EQLPDL-----------------DAVFVPVGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSLAAGEPVTLPGVDT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 225 VAKSLGAKTVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssala 302
Cdd:COG1171   231 IADGLAVGRPGELTFEILRDLvdDIVT--VSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKGK------ 299

                         330
                  ....*....|.
gi 1852860284 303 SVVVIVCGGNN 313
Cdd:COG1171   300 RVVVVLSGGNI 310
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 12-313 3.79e-59

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: 192.32  E-value: 3.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  12 EPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLG 87
Cdd:cd01562    12 KPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  88 IPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPpg 167
Cdd:cd01562    89 IPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGLEILEQVPDL-- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 168 avvlavggggllagvTAGLLEVG---------------WQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAK 232
Cdd:cd01562   167 ---------------DAVFVPVGgggliagiatavkalSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTIADGLAVK 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 233 TVAARTLECAKEC--EVLSevVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalaSVVVIVCG 310
Cdd:cd01562   232 RPGELTFEIIRKLvdDVVT--VSEDEIAAAMLLLFEREKLVAEPAGALALAALLSG---KLDLKGK------KVVVVLSG 300


                  ...
gi 1852860284 311 GNN 313
Cdd:cd01562   301 GNI 303
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 12-310 7.93e-59

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: 190.98  E-value: 7.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  12 EPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQmAKRGC--RHLVCSSGGNAGIAAAYSARKLGIP 89
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEggKTVVEASSGNHGRALAAAAARLGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  90 VTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA-TRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGA 168
Cdd:pfam00291  81 VTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAaEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 169 VVLAVGGGGLLAGVTAGLLEvGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAK-TVAARTLECAKECEV 247
Cdd:pfam00291 161 VVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALALDLLDEYVG 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852860284 248 LSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwRLQAEGRLSSAlASVVVIVCG 310
Cdd:pfam00291 240 EVVTVSDEEALEAMRLLARREGIVVEPSSAAALAAL------KLALAGELKGG-DRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 18-311 4.61e-49

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: 164.23  E-value: 4.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRG---CRHLVCSSGGNAGIAAAYSARKLGIPVTIVL 94
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGklpKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  95 PEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA-TRDGWVNVSPFDHPLIWEGHASLVRELKEslgtppgavvlav 173
Cdd:cd00640    81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAeEDPGAYYVNQFDNPANIAGQGTIGLEILE------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 174 ggggllagvtagllEVGWQHVPIVAMETRGAHSFN---SALQAGRPVTlpditsvakslgaKTVAArtlecakecEVLSE 250
Cdd:cd00640   148 --------------QLGGQKPDAVVVPVGGGGNIAgiaRALKELLPNV-------------KVIGV---------EPEVV 191

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852860284 251 VVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILwRLQAEGRlssalasVVVIVCGG 311
Cdd:cd00640   192 TVSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAK-KLGKGKT-------VVVILTGG 244
PRK08246 PRK08246
serine/threonine dehydratase;
4-312 2.04e-41

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 146.25  E-value: 2.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284   4 ALAERVGaePFHRVTPLLESwALSQVAGMPVFLKYENVQIAGSFKIRGIghFCQQMAKR-GCRHLVCSSGGNAGIAAAYS 82
Cdd:PRK08246   12 AAAQRIA--PHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGA--FNRLLAAPvPAAGVVAASGGNAGLAVAYA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  83 ARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESL 162
Cdd:PRK08246   87 AAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 163 GTPPGAvvlavggggllagvtagLLEVG----------W--QHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLG 230
Cdd:PRK08246  167 PGVDTV-----------------LVAVGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLG 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 231 AKTVAARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGILWRLQAEgrlssalaSVVVIVCG 310
Cdd:PRK08246  230 ARRVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCG 301


                  ..
gi 1852860284 311 GN 312
Cdd:PRK08246  302 AN 303
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 18-312 4.76e-41

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: 147.20  E-value: 4.76e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGalnkIANLSEDQRQRG---VVAASAGNHAQGVAYAAKKFGIKAVIV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVVLAV 173
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 174 GGGGLLAGVTA--GLLEvgwqHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKEC--EVLS 249
Cdd:TIGR01127 158 GGGLISGVASAakQINP----NVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYvdDVVT 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852860284 250 evVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalaSVVVIVCGGN 312
Cdd:TIGR01127 234 --VDEEEIANAIYLLLERHKILAEGAGAAGVAALLEQ---KVDVKGK------KIAVVLSGGN 285
eutB PRK07476
threonine dehydratase; Provisional
 16-312 1.58e-31

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 120.46  E-value: 1.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  16 RVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGC-RHLVCSSGGNAGIAAAYSARKLGIPVTIVL 94
Cdd:PRK07476   18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERaRGVVTASTGNHGRALAYAARALGIRATICM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  95 PE---GTSVQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESL--------- 162
Cdd:PRK07476   98 SRlvpANKVDAIRAL---GAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEILEALpdvatvlvp 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 163 --GTPPGAVVLAVGGGGLLAGVTAGllevgwqhvpiVAMEtRGAhSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLE 240
Cdd:PRK07476  175 lsGGGLASGVAAAVKAIRPAIRVIG-----------VSME-RGA-AMHASLAAGRPVQVEEVPTLADSLGGGIGLDNRYT 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852860284 241 CAKECEVLSEVV--EDREAVSAVQRFLDDERMLVEPACGAALAAIYsgilwrlqaEGRLSSALASVVVIVCGGN 312
Cdd:PRK07476  242 FAMCRALLDDVVllDEAEIAAGIRHAYREERLVVEGAGAVGIAALL---------AGKIAARDGPIVVVVSGAN 306
PRK08639 PRK08639
threonine dehydratase; Validated
 18-323 1.12e-30

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 119.91  E-value: 1.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRG-CRHLVCSSGGNAGIAAAYSARKLGIPVTIVLPE 96
Cdd:PRK08639   26 TPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEElAAGVVCASAGNHAQGVAYACRHLGIPGVIFMPV 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  97 GT---SVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVVLAV 173
Cdd:PRK08639  106 TTpqqKIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKEGSPDYVFV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 174 GGGGllagvtAGLL--------EVGWQhVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKec 245
Cdd:PRK08639  186 PVGG------GGLIsgvttylkERSPK-TKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVDGAAVARVGDLTFEILK-- 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 246 EVLSEVV---EDReAVSAVQRFLDDERMLVEPAcGA----ALAAIYSGIlwrlqaEGRlssalaSVVVIVCGGNN-ISsq 317
Cdd:PRK08639  257 DVVDDVVlvpEGA-VCTTILELYNKEGIVAEPA-GAlsiaALELYKDEI------KGK------TVVCVISGGNNdIE-- 320


                  ....*.
gi 1852860284 318 QLQELK 323
Cdd:PRK08639  321 RMPEIK 326
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
16-312 2.31e-27

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 111.77  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  16 RVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLGIPVT 91
Cdd:PRK09224   19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARG---VITASAGNHAQGVALSAARLGIKAV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  92 IVLPEGT---SVQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGA 168
Cdd:PRK09224   96 IVMPVTTpdiKVDAVRAF---GGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 169 VVLAVGGGGLLAGVTAGLLEVgWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKecEVL 248
Cdd:PRK09224  173 VFVPVGGGGLIAGVAAYIKQL-RPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLFADGVAVKRIGEETFRLCQ--EYV 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852860284 249 SEVVE-DREAV-SAVQRFLDDERMLVEPAcGA-ALAAI--YSGilwRLQAEGRlssalaSVVVIVCGGN 312
Cdd:PRK09224  250 DDVITvDTDEIcAAIKDVFEDTRSIAEPA-GAlALAGLkkYVA---QHGIEGE------TLVAILSGAN 308
PRK06815 PRK06815
threonine/serine dehydratase;
13-321 4.73e-27

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 108.24  E-value: 4.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  13 PFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLGI 88
Cdd:PRK06815   16 PQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAAKLAGI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  89 PVTIVLPEGTS---VQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLgtP 165
Cdd:PRK06815   93 PVTVYAPEQASaikLDAIRAL---GAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMELVEQQ--P 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 166 PGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAK-SLGAKTVAARTLECAKE 244
Cdd:PRK06815  168 DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDgTAGGVEPGAITFPLCQQ 247

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852860284 245 CEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAiysgiLWRLQAE--GRlssalaSVVVIVCGGnNISSQQLQE 321
Cdd:PRK06815  248 LIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-----ALKLAPRyqGK------KVAVVLCGK-NIVLEKYLE 314
PRK07334 PRK07334
threonine dehydratase; Provisional
 18-312 6.23e-25

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 103.82  E-value: 6.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIghfCQQMA-------KRGcrhLVCSSGGNAGIAAAYSARKLGIPV 90
Cdd:PRK07334   24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGA---LNKLLllteeerARG---VIAMSAGNHAQGVAYHAQRLGIPA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  91 TIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKE------SLGT 164
Cdd:PRK07334   98 TIVMPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEMLEdapdldTLVV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 165 PpgavvlavgggGLLAGVTAGLLEVGWQHVP---IVAMETRgahSFNSALQAGRPVTLPDITS-VAKSLGAKTVAARTLE 240
Cdd:PRK07334  178 P-----------IGGGGLISGMATAAKALKPdieIIGVQTE---LYPSMYAAIKGVALPCGGStIAEGIAVKQPGQLTLE 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852860284 241 CAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAIysgilwrLQAEGRLssALASVVVIVCGGN 312
Cdd:PRK07334  244 IVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAAL-------LAYPERF--RGRKVGLVLSGGN 306
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 16-312 1.58e-24

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: 101.47  E-value: 1.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  16 RVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQM-AKRGCRHLVCSSGGNAGIAAAYSARKLGIPVTIVL 94
Cdd:TIGR02991  18 EETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLsDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  95 PEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVVLAVG 174
Cdd:TIGR02991  98 SELVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTLGLEVVEQMPDLATVLVPLSG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 175 GGGLLAGVTAGLLEVGWQHVPIVAMEtRGAhSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKECEVLSEVV-- 252
Cdd:TIGR02991 178 GGLASGVAMAVKAARPDTRVIGVSME-RGA-AMKASLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMCKALLDEIVlv 255

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 253 EDREAVSAVQRFLDDERMLVEPACGAALAAIYSGilwRLQAEGRlssalasVVVIVCGGN 312
Cdd:TIGR02991 256 SEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAG---KIKNPGP-------CAVIVSGRN 305
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
13-162 6.94e-24

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 99.81  E-value: 6.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  13 PFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLGI 88
Cdd:PRK08638   23 GRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGI 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852860284  89 PVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESL 162
Cdd:PRK08638  100 DGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTIGLEILEDL 173
PLN02970 PLN02970
serine racemase
 12-312 1.41e-23

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 98.98  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  12 EPFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLG 87
Cdd:PLN02970   22 APFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKG---VVTHSSGNHAAALALAAKLRG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  88 IPVTIVLPEGTSVQVVRRLEGEGAEVqltgkVWDEANV-----KAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESL 162
Cdd:PLN02970   99 IPAYIVVPKNAPACKVDAVIRYGGII-----TWCEPTVesreaVAARVQQETGAVLIHPYNDGRVISGQGTIALEFLEQV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 163 gtPPGAVVLAVGGGGLLAGVTAGLLEVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKtVAARTLECA 242
Cdd:PLN02970  174 --PELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LGDLTWPVV 250

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852860284 243 KecEVLSEV--VEDREAVSAVQRFLDDERMLVEPACGAALAAIYSGiLWRLQAEGRLSSalaSVVVIVCGGN 312
Cdd:PLN02970  251 R--DLVDDVitVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSD-SFRSNPAWKGCK---NVGIVLSGGN 316
PRK06608 PRK06608
serine/threonine dehydratase;
13-322 2.39e-23

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 98.30  E-value: 2.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  13 PFHRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCR--HLVCSSGGNAGIAAAYSARKLGIPV 90
Cdd:PRK06608   19 QYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpdKIVAYSTGNHGQAVAYASKLFGIKT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  91 TIVLPEGTSVQVVRRLEGEGAEVQLTgKVWDEANVKAQElATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVV 170
Cdd:PRK06608   99 RIYLPLNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYEALQQLGFSPDAIF 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 171 LAVGGggllagvtAGLL-------EVGWQHVPIVAMETRGAHSFNSALQAGRPVTLPDI-TSVAKSLGAKTVAARTLECA 242
Cdd:PRK06608  177 ASCGG--------GGLIsgtylakELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSpNTIADGLKTLSVSARTFEYL 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 243 KECEVLSEvVEDREAVSAVQRFLDDERMLVEPACGAALAAIYSgilWrLQAEgrlsSALASVVVIVCGGnNISSQQLQEL 322
Cdd:PRK06608  249 KKLDDFYL-VEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVN---W-LKTQ----SKPQKLLVILSGG-NIDPILYNEL 318
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 18-310 3.81e-23

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: 97.66  E-value: 3.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMP-VFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIA-AAYSARKlGIPVTIVLP 95
Cdd:cd01563    23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTGNTSASlAAYAARA-GIKCVVFLP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  96 EGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELAtRDGWVNVSPFDHPLIWEGHASLVRELKESLG--TP-----Pga 168
Cdd:cd01563   102 AGKALGKLAQALAYGATVLAVEGNFDDALRLVRELA-EENWIYLSNSLNPYRLEGQKTIAFEIAEQLGweVPdyvvvP-- 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 169 vvlavggggllaGVTAGLL-----------EVGW-QHVP-IVAMETRGA----HSFNSALQAGRPVTLPDitSVAKSL-- 229
Cdd:cd01563   179 ------------VGNGGNItaiwkgfkelkELGLiDRLPrMVGVQAEGAapivRAFKEGKDDIEPVENPE--TIATAIri 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 230 GAKTVAARTLECAKECEVLSEVVEDREAVSAvQRFLD-DERMLVEPACGAALAAiysgiLWRLQAEGRLSSAlASVVVIV 308
Cdd:cd01563   245 GNPASGPKALRAVRESGGTAVAVSDEEILEA-QKLLArTEGIFVEPASAASLAG-----LKKLREEGIIDKG-ERVVVVL 317


                  ..
gi 1852860284 309 CG 310
Cdd:cd01563   318 TG 319
PRK12483 PRK12483
threonine dehydratase; Reviewed
 16-283 2.13e-21

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 94.48  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  16 RVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAAAYSARKLGIPVT 91
Cdd:PRK12483   36 RETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLARG---VITASAGNHAQGVALAAARLGVKAV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  92 IVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVVL 171
Cdd:PRK12483  113 IVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPLDAIFV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 172 AVGGGGLLAGVTAGLLEVGwQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKecEVLSEV 251
Cdd:PRK12483  193 PVGGGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGEHTFELCR--HYVDEV 269

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1852860284 252 --VEDREAVSAVQRFLDDERMLVEPACGAALAAI 283
Cdd:PRK12483  270 vtVSTDELCAAIKDIYDDTRSITEPAGALAVAGI 303
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
4-163 5.41e-21

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 91.62  E-value: 5.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284   4 ALAERVgAEPFHRvTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRG----IGHFCQQMAKRGcrhLVCSSGGNAGIAA 79
Cdd:PRK07048   13 AAAARL-AGVAHR-TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAG---VVTFSSGNHAQAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  80 AYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELK 159
Cdd:PRK07048   88 ALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKELF 167


                  ....
gi 1852860284 160 ESLG 163
Cdd:PRK07048  168 EEVG 171
PLN02550 PLN02550
threonine dehydratase
 18-281 1.08e-20

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 92.68  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGC-RHLVCSSGGNAGIAAAYSARKLGIPVTIVLPE 96
Cdd:PLN02550  110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLdKGVICSSAGNHAQGVALSAQRLGCDAVIAMPV 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  97 GT---SVQVVRRLegeGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTPPGAVVLAV 173
Cdd:PLN02550  190 TTpeiKWQSVERL---GATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIFVPV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 174 GGGGLLAGVTAGLLEVGwQHVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKECeVLSEVVE 253
Cdd:PLN02550  267 GGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCREL-VDGVVLV 344

                         250       260
                  ....*....|....*....|....*....
gi 1852860284 254 DREAV-SAVQRFLDDERMLVEPACGAALA 281
Cdd:PLN02550  345 SRDAIcASIKDMFEEKRSILEPAGALALA 373
PRK06110 PRK06110
threonine dehydratase;
26-312 6.91e-20

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 88.51  E-value: 6.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  26 LSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRG--CRHLVCSSGGNAGIAAAYSARKLGIPVTIVLPEGTSVQVV 103
Cdd:PRK06110   30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGprVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 104 RRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFdHPLIWEGHASLVRELKESLgTPPGAVVLAVGGGGLLAGVT 183
Cdd:PRK06110  110 AAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALELFRAV-PDLDVVYVPIGMGSGICGAI 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 184 AGLLEVGWQhVPIVAMETRGAHSFNSALQAGRPVTLPDITSVAKSLGAKTVAARTLECAKECevLSEV--VEDREAVSAV 261
Cdd:PRK06110  188 AARDALGLK-TRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAG--ADRIvrVTDDEVAAAM 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1852860284 262 QRFLDDERMLVEPACGAALAAIysgilwrLQAEGRLssALASVVVIVCGGN 312
Cdd:PRK06110  265 RAYFTDTHNVAEGAGAAALAAA-------LQERERL--AGKRVGLVLSGGN 306
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 15-310 5.54e-18

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: 83.71  E-value: 5.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  15 HRVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIA-AAYSARKlGIPVTIV 93
Cdd:COG0498    64 EGGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAAlAAYAARA-GIEVFVF 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEG-TSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFdHPLIWEGHASLVRELKESLGTPPgavvla 172
Cdd:COG0498   143 VPEGkVSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLGRVPdwvvvp 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 173 vggggllagvTAG------LLEVGW-QHVP-IVAMETRGAHSFNSALQAGRPVTLPDitsvakslGAKTVA--------- 235
Cdd:COG0498   222 t---gnggniLAGykafkeLKELGLiDRLPrLIAVQATGCNPILTAFETGRDEYEPE--------RPETIApsmdignps 290

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852860284 236 --ARTLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAiysgiLWRLQAEGRLSSAlASVVVIVCG 310
Cdd:COG0498   291 ngERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAG-----LRKLREEGEIDPD-EPVVVLSTG 361
PRK08813 PRK08813
threonine dehydratase; Provisional
 34-158 1.12e-15

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 76.59  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  34 VFLKYENVQIAGSFKIRGIGHFCQQMAKRG-CRHLVCSSGGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAE 112
Cdd:PRK08813   50 VWLKLENLQRTGSYKVRGALNALLAGLERGdERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1852860284 113 VQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVREL 158
Cdd:PRK08813  130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIEL 175
PRK08197 PRK08197
threonine synthase; Validated
 18-310 3.95e-14

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 72.34  E-value: 3.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMP-VFLKYENVQIAGSFKIRGIGhFCQQMAKR-GCRHLVCSSGGNAGIA-AAYSARKlGIPVTIVL 94
Cdd:PRK08197   80 TPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGLA-VGVSRAKElGVKHLAMPTNGNAGAAwAAYAARA-GIRATIFM 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  95 PEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLG--TP-----Pg 167
Cdd:PRK08197  158 PADAPEITRLECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGwrLPdvilyP- 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 168 avvlavggggllagvTAG-------------LLEVGW--QHVP-IVAMETRGAHSFNSALQAGR--------PVTLPDIT 223
Cdd:PRK08197  237 ---------------TGGgvgligiwkafdeLEALGWigGKRPrLVAVQAEGCAPIVKAWEEGKeesefwedAHTVAFGI 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 224 SVAKSLGAKTVaartLECAKECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAiysgiLWRLQAEGRLSSAlAS 303
Cdd:PRK08197  302 RVPKALGDFLV----LDAVRETGGCAIAVSDDAILAAQRELAREEGLFACPEGAATFAA-----ARQLRESGWLKGD-ER 371


                  ....*..
gi 1852860284 304 VVVIVCG 310
Cdd:PRK08197  372 VVLFNTG 378
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 16-307 3.74e-12

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: 66.25  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  16 RVTPLLESWALSQ-VAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIAAAYSARKLGIPVTIVL 94
Cdd:TIGR00260  21 GVTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  95 PEG--TSVQVVRRLeGEGAEV-QLTGKvWDEANVKAQELATRD-GWVNVSPFDHPLIWEGHASLVRELKESLGTP-PGAV 169
Cdd:TIGR00260 101 PAGkiSLGKLAQAL-GYNAEVvAIDGN-FDDAQRLVKQLFEDKpALGLNSANSIPYRLEGQKTYAFEAVEQLGWEaPDKV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 170 VLAVGGGGLLAGVTAGLLE---VGWQHVPI-VAMETRGAHSFNSALQAGR---PVTLPDITSVAKSLGAKTVAARTLECA 242
Cdd:TIGR00260 179 VVPVPNSGNFGAIWKGFKEkkmLGLDSLPVkRGIQAEGAADIVRAFLEGGqwePIETPETLSTAMDIGNPANWPRALEAF 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852860284 243 KECEVLSEVVEDREAVSAVQRFLDDERMLVEPACGAALAAiysgiLWRLQAEGRLSSALASVVVI 307
Cdd:TIGR00260 259 RRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAA-----LLKLVEKGTADPAERVVCAL 318
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 18-282 1.57e-11

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: 64.07  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGC----RHLVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:cd01561     3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLT---GKVWDEANV-KAQELA-TRDGWVNVSPFDHPLIWEGH-----ASLVRELKESL- 162
Cdd:cd01561    83 MPETMSEEKRKLLRALGAEVILTpeaEADGMKGAIaKARELAaETPNAFWLNQFENPANPEAHyettaPEIWEQLDGKVd 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 163 ---------GTppgavvlavggggllagvTAGLLEVGWQHVP---IVAMETRGAHSFNSALQAGRPVT------LPDITs 224
Cdd:cd01561   163 afvagvgtgGT------------------ITGVARYLKEKNPnvrIVGVDPVGSVLFSGGPPGPHKIEgigagfIPENL- 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 225 vakslgaktvaartlecakECEVLSEV--VEDREAVSAVQRFLDDERMLVEPACGAALAA 282
Cdd:cd01561   224 -------------------DRSLIDEVvrVSDEEAFAMARRLAREEGLLVGGSSGAAVAA 264
PRK06381 PRK06381
threonine synthase; Validated
 18-166 2.20e-11

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 63.57  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGM-PVFLKYENVQIAGSFKIR-GIGHFCQQMaKRGCRHLVCSSGGNAGIAAAYSARKLGIPVTIVLP 95
Cdd:PRK06381   16 TPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRiAEAHVRRAM-RLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIP 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852860284  96 EGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFD-HPLI-WEGHASLVRELKESLGTPP 166
Cdd:PRK06381   95 RSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSvNSVVdIEAYSAIAYEIYEALGDVP 167
PRK05638 PRK05638
threonine synthase; Validated
 18-163 2.84e-10

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 60.98  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESwALSQVAGMPVFLKYENVQIAGSFKIR----GIGHFCQQMAKRgcrhLVCSSGGNAGIA-AAYSARKlGIPVTI 92
Cdd:PRK05638   67 TPLIRA-RISEKLGENVYIKDETRNPTGSFRDRlatvAVSYGLPYAANG----FIVASDGNAAASvAAYSARA-GKEAFV 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852860284  93 VLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLG 163
Cdd:PRK05638  141 VVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEIN 211
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 18-151 5.02e-10

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: 59.68  E-value: 5.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRgIGHFcqqMAKRGCR--------HLVCSSGGNAGIAAAYSARKLGIP 89
Cdd:COG0031    14 TPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDR-IALS---MIEDAEKrgllkpggTIVEATSGNTGIGLAMVAAAKGYR 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852860284  90 VTIVLPEGTSVQVVRRLEGEGAEVQLTGKV--WDEANVKAQELA-TRDGWVNVSPFDHPLIWEGH 151
Cdd:COG0031    90 LILVMPETMSKERRALLRAYGAEVVLTPGAegMKGAIDKAEELAaETPGAFWPNQFENPANPEAH 154
PRK08329 PRK08329
threonine synthase; Validated
 17-165 1.49e-08

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 55.22  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  17 VTPLLEswalsqvAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIA-AAYSARKlGIPVTIVLP 95
Cdd:PRK08329   64 ITPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSlALYSLSE-GIKVHVFVS 135

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  96 EGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGTP 165
Cdd:PRK08329  136 YNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGVP 205
PRK06450 PRK06450
threonine synthase; Validated
 34-282 6.13e-07

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 50.50  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  34 VFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRHLVCSSGGNAGIA-AAYSARKlGIPVTIVLPEGTSVQVVRRLEGEGAE 112
Cdd:PRK06450   67 IWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASiAAYGAAA-GIEVKIFVPETASGGKLKQIESYGAE 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 113 V-QLTGKVWDeanvkAQELATRDGWVNVSPFDHPLIWEGHASLVRELKESLGT-PPgavvlavggGGLLAGVTAG--LLE 188
Cdd:PRK06450  146 VvRVRGSRED-----VAKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKDLDWkIP---------NYVFIPVSAGtlLLG 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284 189 V--GWQH---------VP-IVAMETRGAHSFNSALQaGRPVTLPD-ITSVAKSLgaktVAARTLECAKECEVLSE----- 250
Cdd:PRK06450  212 VysGFKHlldsgviseMPkIVAVQTEQVSPLCAKFK-GISYTPPDkVTSIADAL----VSTRPFLLDYMVKALSEygeci 286

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1852860284 251 VVEDREAVSAvQRFLDDERMLVEPACGAALAA 282
Cdd:PRK06450  287 VVSDNEIVEA-WKELAKKGLLVEYSSATVYAA 317
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-140 1.54e-05

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 46.02  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284   1 MEGALAERVGAE----PFHRVTPLLESWALSQVAGM-PVFLKYENVQIA-GSFKIRG----IGHFCQQMAKRGCRHL--- 67
Cdd:PRK08206   24 LSQEEAKKARAFhqsfPGYAPTPLVALPDLAAELGVgSILVKDESYRFGlNAFKALGgayaVARLLAEKLGLDISELsfe 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  68 ----------------VCSSGGNAGIAAAYSARKLGIPVTIVLPEGTSVQVVRRLEGEGAEVQLTGKVWDEANVKAQELA 131
Cdd:PRK08206  104 eltsgevreklgditfATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGNYDDSVRLAAQEA 183


                  ....*....
gi 1852860284 132 TRDGWVNVS 140
Cdd:PRK08206  184 QENGWVVVQ 192
cysM PRK11761
cysteine synthase CysM;
18-118 1.31e-03

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 39.86  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRH----LVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:PRK11761   13 TPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKpgdtLIEATSGNTGIALAMIAAIKGYRMKLI 92

                          90       100
                  ....*....|....*....|....*
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLTGK 118
Cdd:PRK11761   93 MPENMSQERRAAMRAYGAELILVPK 117
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 16-113 3.57e-03

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 39.02  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  16 RVTPLLESWALSQVAGMPVFLKYENVQIAGSFKIR---GIGHFCQQMAKrgcRHLVCSSG-GNAGIAAAYSARKLGIPVT 91
Cdd:PRK13803  270 RPTPLTEAKRLSDIYGARIYLKREDLNHTGSHKINnalGQALLAKRMGK---TRIIAETGaGQHGVATATACALFGLKCT 346

                          90       100
                  ....*....|....*....|....*
gi 1852860284  92 IVLPE---GTSVQVVRRLEGEGAEV 113
Cdd:PRK13803  347 IFMGEediKRQALNVERMKLLGANV 371
PRK10717 PRK10717
cysteine synthase A; Provisional
 18-116 7.39e-03

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 37.53  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852860284  18 TPLLESWALSQVAGMPVFLKYENVQIAGSFKIRGIGHFCQQMAKRGCRH----LVCSSGGNAGIAAAYSARKLGIPVTIV 93
Cdd:PRK10717   14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKpggtIVEGTAGNTGIGLALVAAARGYKTVIV 93

                          90       100
                  ....*....|....*....|...
gi 1852860284  94 LPEGTSVQVVRRLEGEGAEVQLT 116
Cdd:PRK10717   94 MPETQSQEKKDLLRALGAELVLV 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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