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Conserved domains on  [gi|74731799|sp|Q96GA7|]
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RecName: Full=Serine dehydratase-like; AltName: Full=L-serine deaminase; AltName: Full=L-serine dehydratase/L-threonine deaminase; Short=SDHL; AltName: Full=L-threonine dehydratase; Short=TDH; AltName: Full=Serine dehydratase 2; Short=SDH 2

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

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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) ...
 17-326 1.34e-138

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 cd06448:

Pssm-ID: 444852  Cd Length: 316  Bit Score: 395.13  E-value: 1.34e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG---CRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  94 LPESTSLQVVQRLQGEGAEVQLTGKVW-DEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRT--PPGAL 169
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 170 VLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHS 249
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74731799 250 EVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgCLPPSLTSVVVIVCGGNNINSRELQALKTHL 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 1.34e-138

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: 395.13  E-value: 1.34e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG---CRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  94 LPESTSLQVVQRLQGEGAEVQLTGKVW-DEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRT--PPGAL 169
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 170 VLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHS 249
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74731799 250 EVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgCLPPSLTSVVVIVCGGNNINSRELQALKTHL 326
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 13-325 3.71e-51

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: 172.14  E-value: 3.71e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  13 PFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSggnagiaaayaaRKLGI 88
Cdd:COG1171  20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynaLASLSEEERARG---VVAASagnhaqgvayaaRLLGI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  89 PATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL-------VQELKAV 161
Cdd:COG1171  97 PATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIaleileqLPDLDAV 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 162 LrTPpgalvlavggggllagvvaglleVG------------WQHVP---IIAMETHGAHCFNAAITAGKLVTLPDITSVA 226
Cdd:COG1171 177 F-VP-----------------------VGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 227 KSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGllrRLQAEGclppslTSVVV 306
Cdd:COG1171 233 DGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKG------KRVVV 303

                       330
                ....*....|....*....
gi 74731799 307 IVCGGnNINSRELQALKTH 325
Cdd:COG1171 304 VLSGG-NIDPDRLAEILER 321
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 18-310 5.09e-45

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: 155.16  E-value: 5.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEmAKKGC--RHLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    96 ESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAvg 174
Cdd:pfam00291  87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGpGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVP-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   175 gggllagvvaglleVG---------------WQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAK-TVAARA 238
Cdd:pfam00291 165 --------------VGgggliagiarglkelGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALA 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74731799   239 LECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEGclppsltSVVVIVCG 310
Cdd:pfam00291 231 LDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD-------RVVVVLTG 295
ilvA_2Cterm TIGR01124
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ...
 16-312 5.36e-30

threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130194 [Multi-domain]  Cd Length: 499  Bit Score: 119.07  E-value: 5.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPAT 91
Cdd:TIGR01124  16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGaynkMAQLSPEQKARG---VIAASAGNHAQGVAFSAARLGLKAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    92 IVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVL 171
Cdd:TIGR01124  93 IVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   172 AVGGGGLLAGVVAGLLEVGWQhVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE-CMQVckIHSE 250
Cdd:TIGR01124 173 PVGGGGLAAGVAALIKQLMPE-IKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRlCQQY--LDDI 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74731799   251 VVEDTEAV-SAVQQLLDDERMLVEPACGAALAaiysGLLRRLQAEGCLPPSLtsvVVIVCGGN 312
Cdd:TIGR01124 250 VTVDTDEVcAAIKDLFEDTRAVAEPAGALALA----GLKKYVALHGIRGQTL---VAILSGAN 305
PRK08246 PRK08246
serine/threonine dehydratase;
13-312 1.68e-26

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 106.58  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   13 PFHVVTPLLESwALSQVAGMPVFLKCENVQPSGSFKIRGIGHFcQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATI 92
Cdd:PRK08246  19 PHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   93 VLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLa 172
Cdd:PRK08246  97 FVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVA- 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  173 vggggllagvvaglleVG----------W--QHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE 240
Cdd:PRK08246 176 ----------------VGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFA 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74731799  241 CMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgclppsltSVVVIVCGGN 312
Cdd:PRK08246 240 LARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGAN 303
 
Name Accession Description Interval E-value
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 17-326 1.34e-138

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: 395.13  E-value: 1.34e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG---CRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd06448   1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGlneCVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  94 LPESTSLQVVQRLQGEGAEVQLTGKVW-DEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRT--PPGAL 169
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHGKVWwEADNYLREELAENDpGPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqeKVDAI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 170 VLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHS 249
Cdd:cd06448 161 VCSVGGGGLLNGIVQGLERNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQALEYAQEHNIKS 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74731799 250 EVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgCLPPSLTSVVVIVCGGNNINSRELQALKTHL 326
Cdd:cd06448 241 EVVSDRDAVQACLRFADDERILVEPACGAALAVVYSGKILDLQLE-VLLTPLDNVVVVVCGGSNITLEQLKEYKKQL 316
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 13-325 3.71e-51

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: 172.14  E-value: 3.71e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  13 PFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSggnagiaaayaaRKLGI 88
Cdd:COG1171  20 GVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGaynaLASLSEEERARG---VVAASagnhaqgvayaaRLLGI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  89 PATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL-------VQELKAV 161
Cdd:COG1171  97 PATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTIaleileqLPDLDAV 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 162 LrTPpgalvlavggggllagvvaglleVG------------WQHVP---IIAMETHGAHCFNAAITAGKLVTLPDITSVA 226
Cdd:COG1171 177 F-VP-----------------------VGgggliagvaaalKALSPdirVIGVEPEGAAAMYRSLAAGEPVTLPGVDTIA 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 227 KSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGllrRLQAEGclppslTSVVV 306
Cdd:COG1171 233 DGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAG---KERLKG------KRVVV 303

                       330
                ....*....|....*....
gi 74731799 307 IVCGGnNINSRELQALKTH 325
Cdd:COG1171 304 VLSGG-NIDPDRLAEILER 321
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 6-313 1.94e-47

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: 161.89  E-value: 1.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   6 AEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAY 81
Cdd:cd01562   6 AAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGaynkLLSLSEEERAKG---VVAASAGNHAQGVAY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  82 AARKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL------- 154
Cdd:cd01562  83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIgleileq 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 155 VQELKAVL------------------RTPpgalvlavggggllagvvagllevgwqHVPIIAMETHGAHCFNAAITAGKL 216
Cdd:cd01562 163 VPDLDAVFvpvggggliagiatavkaLSP---------------------------NTKVIGVEPEGAPAMAQSLAAGKP 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 217 VTLPDITSVAKSLGAKTVAARALEcmqVCKIH-SEV--VEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQA 293
Cdd:cd01562 216 VTLPEVDTIADGLAVKRPGELTFE---IIRKLvDDVvtVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGK 292

                       330       340
                ....*....|....*....|
gi 74731799 294 egclppsltSVVVIVCGGNN 313
Cdd:cd01562 293 ---------KVVVVLSGGNI 303
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 18-310 5.09e-45

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: 155.16  E-value: 5.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEmAKKGC--RHLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLR-LKEGEggKTVVEASSGNHGRALAAAAARLGLKVTIVVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    96 ESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAvg 174
Cdd:pfam00291  87 EDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGpGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVP-- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   175 gggllagvvaglleVG---------------WQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAK-TVAARA 238
Cdd:pfam00291 165 --------------VGgggliagiarglkelGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGdEPGALA 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74731799   239 LECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEGclppsltSVVVIVCG 310
Cdd:pfam00291 231 LDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGGD-------RVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 18-311 1.04e-38

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: 137.26  E-value: 1.04e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQ---EMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVL 94
Cdd:cd00640   1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILlaeEEGKLPKGVIIESTGGNTGIALAAAAARLGLKCTIVM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  95 PESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD-GWENVPPFDHPLIWKGHASLVQELKAvlrtppgalvlav 173
Cdd:cd00640  81 PEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDpGAYYVNQFDNPANIAGQGTIGLEILE------------- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 174 ggggllagvvagllEVGWQHVPII--AMETHGAHcfnAAITAGKLVTLPDItsvakslgaKTVAARAlecmqvckiHSEV 251
Cdd:cd00640 148 --------------QLGGQKPDAVvvPVGGGGNI---AGIARALKELLPNV---------KVIGVEP---------EVVT 192

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 252 VEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSglLRRLQAEGclppslTSVVVIVCGG 311
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALK--LAKKLGKG------KTVVVILTGG 244
ilvA_2Cterm TIGR01124
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ...
 16-312 5.36e-30

threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 130194 [Multi-domain]  Cd Length: 499  Bit Score: 119.07  E-value: 5.36e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPAT 91
Cdd:TIGR01124  16 QETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGaynkMAQLSPEQKARG---VIAASAGNHAQGVAFSAARLGLKAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    92 IVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVL 171
Cdd:TIGR01124  93 IVMPETTPDIKVDAVRGFGGEVVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEILRQVANPLDAVFV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   172 AVGGGGLLAGVVAGLLEVGWQhVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE-CMQVckIHSE 250
Cdd:TIGR01124 173 PVGGGGLAAGVAALIKQLMPE-IKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFRlCQQY--LDDI 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74731799   251 VVEDTEAV-SAVQQLLDDERMLVEPACGAALAaiysGLLRRLQAEGCLPPSLtsvVVIVCGGN 312
Cdd:TIGR01124 250 VTVDTDEVcAAIKDLFEDTRAVAEPAGALALA----GLKKYVALHGIRGQTL---VAILSGAN 305
PRK08246 PRK08246
serine/threonine dehydratase;
13-312 1.68e-26

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 106.58  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   13 PFHVVTPLLESwALSQVAGMPVFLKCENVQPSGSFKIRGIGHFcQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATI 92
Cdd:PRK08246  19 PHIRRTPVLEA-DGAGFGPAPVWLKLEHLQHTGSFKARGAFNR-LLAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   93 VLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLa 172
Cdd:PRK08246  97 FVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQAPGVDTVLVA- 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  173 vggggllagvvaglleVG----------W--QHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALE 240
Cdd:PRK08246 176 ----------------VGgggliagiaaWfeGRARVVAVEPEGAPTLHAALAAGEPVDVPVSGIAADSLGARRVGEIAFA 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74731799  241 CMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSGLLRRLQAEgclppsltSVVVIVCGGN 312
Cdd:PRK08246 240 LARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--------RVAVVLCGAN 303
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
16-312 2.60e-25

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 105.61  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPAT 91
Cdd:PRK09224  19 QETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGaynkMAQLTEEQLARG---VITASAGNHAQGVALSAARLGIKAV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   92 IVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVL 171
Cdd:PRK09224  96 IVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAMEILQQHPHPLDAVFV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  172 AVGGGGLLAGVVAGLLEVgWQHVPIIAMETHGAHCFNAAITAGKLVTLPDItsvakSLGAKTVAARAL--ECMQVCKIH- 248
Cdd:PRK09224 176 PVGGGGLIAGVAAYIKQL-RPEIKVIGVEPEDSACLKAALEAGERVDLPQV-----GLFADGVAVKRIgeETFRLCQEYv 249

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74731799  249 SEVVE-DTEAV-SAVQQLLDDERMLVEPAcGA-ALAaiysGLLRRLQAEGCLPPSLtsvVVIVCGGN 312
Cdd:PRK09224 250 DDVITvDTDEIcAAIKDVFEDTRSIAEPA-GAlALA----GLKKYVAQHGIEGETL---VAILSGAN 308
PRK12483 PRK12483
threonine dehydratase; Reviewed
 18-283 3.66e-23

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 99.87  E-value: 3.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGaynkMARLPAEQLARG---VITASAGNHAQGVALAAARLGVKAVIV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALVLAV 173
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPGPLDAIFVPV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  174 GGGGLLAGVVAGLLEVGwQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAAralECMQVCKIH-SEVV 252
Cdd:PRK12483 195 GGGGLIAGIAAYVKYVR-PEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGE---HTFELCRHYvDEVV 270

                        250       260       270
                 ....*....|....*....|....*....|...
gi 74731799  253 E-DTEAV-SAVQQLLDDERMLVEPACGAALAAI 283
Cdd:PRK12483 271 TvSTDELcAAIKDIYDDTRSITEPAGALAVAGI 303
eutB PRK07476
threonine dehydratase; Provisional
 16-158 5.55e-23

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 96.96  E-value: 5.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   16 VVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGC-RHLVCSSGGNAGIAAAYAARKLGIPATIVL 94
Cdd:PRK07476  18 RRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERaRGVVTASTGNHGRALAYAARALGIRATICM 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74731799   95 PESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK07476  98 SRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTIGLEI 161
PRK08639 PRK08639
threonine dehydratase; Validated
 15-313 6.20e-22

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 95.26  E-value: 6.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   15 HVV--TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGI 88
Cdd:PRK08639  21 DVVpeTPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGaynaISQLSDEELAAG---VVCASAGNHAQGVAYACRHLGI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   89 PATIVLPESTSLQVVQRLQ---GEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTP 165
Cdd:PRK08639  98 PGVIFMPVTTPQQKIDQVRffgGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVIAGQGTVAVEILEQLEKE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  166 PGALVLAVGgggllagvvaglleVGW------------QHVP---IIAMETHGAHCFNAAITAGKLVTLPDI------TS 224
Cdd:PRK08639 178 GSPDYVFVP--------------VGGgglisgvttylkERSPktkIIGVEPAGAASMKAALEAGKPVTLEKIdkfvdgAA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  225 VAKsLGAKTVAaralecmqVCKihsEVVEDTEAV------SAVQQLLDDERMLVEPACGAALAAiysglLRRLQAEgcLP 298
Cdd:PRK08639 244 VAR-VGDLTFE--------ILK---DVVDDVVLVpegavcTTILELYNKEGIVAEPAGALSIAA-----LELYKDE--IK 304

                        330
                 ....*....|....*
gi 74731799  299 PSltSVVVIVCGGNN 313
Cdd:PRK08639 305 GK--TVVCVISGGNN 317
PRK06815 PRK06815
threonine/serine dehydratase;
8-323 5.33e-20

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 88.60  E-value: 5.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    8 HAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAA 83
Cdd:PRK06815  11 HQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGasnkLRLLNEAQRQQG---VITASSGNHGQGVALAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   84 RKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELkaVLR 163
Cdd:PRK06815  88 KLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGMEL--VEQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  164 TPPGALVLAVGGGGLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLV------TLPDITSVAKSLGAKTVAAr 237
Cdd:PRK06815 166 QPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVevaeqpTLSDGTAGGVEPGAITFPL- 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  238 aleCMQVCKiHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiYSGLLRRLQAEgclppsltSVVVIVCGGNNINSR 317
Cdd:PRK06815 245 ---CQQLID-QKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAA-ALKLAPRYQGK--------KVAVVLCGKNIVLEK 311


                 ....*.
gi 74731799  318 ELQALK 323
Cdd:PRK06815 312 YLEAVS 317
PLN02970 PLN02970
serine racemase
 5-312 1.06e-19

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 88.20  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    5 VAEHAKQEPFHVVTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAA 80
Cdd:PLN02970  15 REARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGacnaIFSLSDDQAEKG---VVTHSSGNHAAALA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   81 YAARKLGIPATIVLPESTSLQVVQRLQGEGAEVqltgkVWDEANLR-----AQELAKRDGWENVPPFDHPLIWKGHASL- 154
Cdd:PLN02970  92 LAAKLRGIPAYIVVPKNAPACKVDAVIRYGGII-----TWCEPTVEsreavAARVQQETGAVLIHPYNDGRVISGQGTIa 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  155 ------VQELKAVLrtppgalvlavggggllagvvaglleVGWQ-----------------HVPIIAMETHGAHCFNAAI 211
Cdd:PLN02970 167 lefleqVPELDVII--------------------------VPISggglisgialaakaikpSIKIIAAEPKGADDAAQSK 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  212 TAGKLVTLPDITSVAK----SLGAKTVA-ARALecmqVCKIhsEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAIYSG 286
Cdd:PLN02970 221 AAGEIITLPVTNTIADglraSLGDLTWPvVRDL----VDDV--ITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSD 294

                        330       340
                 ....*....|....*....|....*..
gi 74731799  287 LLR-RLQAEGClppslTSVVVIVCGGN 312
Cdd:PLN02970 295 SFRsNPAWKGC-----KNVGIVLSGGN 316
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
18-154 1.24e-19

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 87.87  E-value: 1.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK08638  28 TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGafnkLSSLTDAEKRKG---VVACSAGNHAQGVALSCALLGIDGKVV 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74731799   94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASL 154
Cdd:PRK08638 105 MPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVIAGQGTI 165
PLN02550 PLN02550
threonine dehydratase
 18-281 9.52e-19

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 86.90  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGaynmMAKLPKEQLDKG---VICSSAGNHAQGVALSAQRLGCDAVIA 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   94 LPEST---SLQVVQRLqgeGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKAVLRTPPGALV 170
Cdd:PLN02550 187 MPVTTpeiKWQSVERL---GATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGPLHAIF 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  171 LAVGGGGLLAGVVAGLLEVGwQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAAralECMQVCK--IH 248
Cdd:PLN02550 264 VPVGGGGLIAGIAAYVKRVR-PEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGE---ETFRLCRelVD 339

                        250       260       270
                 ....*....|....*....|....*....|....
gi 74731799  249 SEVVEDTEAVSA-VQQLLDDERMLVEPACGAALA 281
Cdd:PLN02550 340 GVVLVSRDAICAsIKDMFEEKRSILEPAGALALA 373
PRK07334 PRK07334
threonine dehydratase; Provisional
 18-158 1.61e-18

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 85.33  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK07334  24 TPCVHSRTLSQITGAEVWLKFENLQFTASFKERGalnkLLLLTEEERARG---VIAMSAGNHAQGVAYHAQRLGIPATIV 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74731799   94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK07334 101 MPRFTPTVKVERTRGFGAEVVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTVALEM 165
PRK06608 PRK06608
serine/threonine dehydratase;
18-157 4.17e-17

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 80.59  E-value: 4.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCR--HLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:PRK06608  24 TPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQGKLpdKIVAYSTGNHGQAVAYASKLFGIKTRIYLP 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74731799   96 ESTSLQVVQRLQGEGAEVQLTgKVWDEANLRAQElAKRDGWENVPPFDHPLIWKGHASLVQE 157
Cdd:PRK06608 104 LNTSKVKQQAALYYGGEVILT-NTRQEAEEKAKE-DEEQGFYYIHPSDSDSTIAGAGTLCYE 163
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
 18-312 4.31e-17

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: 80.28  E-value: 4.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEM-AKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPE 96
Cdd:TIGR02991  20 TPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLsDTQRAAGVVAASTGNHGRALAYAAAEEGVRATICMSE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    97 STSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLvqELKAVLRTPPGALVLAVGGG 176
Cdd:TIGR02991 100 LVPQNKVDEIRRLGAEVRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTL--GLEVVEQMPDLATVLVPLSG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   177 GLLAGVVAGLLEVGWQHVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHSEVVEDTE 256
Cdd:TIGR02991 178 GGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADSLGGGIGLDNRVTFAMCKALLDEIVLVSE 257

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 74731799   257 A--VSAVQQLLDDERMLVEPACGAALAAIYSGllrRLQAEGclppsltSVVVIVCGGN 312
Cdd:TIGR02991 258 AeiAAGIRHAYAEEREIVEGAGAVGIAALLAG---KIKNPG-------PCAVIVSGRN 305
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
18-158 5.04e-17

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 80.45  E-value: 5.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRG----IGHFCQEMAKKGcrhLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:PRK07048  25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGaynaLSQFSPEQRRAG---VVTFSSGNHAQAIALSARLLGIPATIV 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74731799   94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK07048 102 MPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTAAKEL 166
PRK06110 PRK06110
threonine dehydratase;
26-312 8.29e-14

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 70.79  E-value: 8.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   26 LSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKG--CRHLVCSSGGNAGIAAAYAARKLGIPATIVLPESTSLQVV 103
Cdd:PRK06110  30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGprVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  104 QRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFdHPLIWKGHASLVQELkavLRTPPGALVLAVGGGGLLAGVV 183
Cdd:PRK06110 110 AAMRALGAELIEHGEDFQAAREEAARLAAERGLHMVPSF-HPDLVRGVATYALEL---FRAVPDLDVVYVPIGMGSGICG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  184 AGLLE--VGWQhVPIIAMETHGAHCFNAAITAGKLVTLPDITSVAKSLGAKTVAARALECMQVCKIHSEVVEDTEAVSAV 261
Cdd:PRK06110 186 AIAARdaLGLK-TRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAM 264

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74731799  262 QQLLDDERMLVEPACGAALAAIysgLLRRLQAEGclppslTSVVVIVCGGN 312
Cdd:PRK06110 265 RAYFTDTHNVAEGAGAAALAAA---LQERERLAG------KRVGLVLSGGN 306
PRK08813 PRK08813
threonine dehydratase; Provisional
 34-160 2.33e-11

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 63.88  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   34 VFLKCENVQPSGSFKIRG-IGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPESTSLQVVQRLQGEGAE 112
Cdd:PRK08813  50 VWLKLENLQRTGSYKVRGaLNALLAGLERGDERPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGAT 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 74731799  113 VQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQELKA 160
Cdd:PRK08813 130 VRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGTVGIELAA 177
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 18-310 5.99e-11

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: 62.61  E-value: 5.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  18 TPLLESWALSQVAGMP-VFLKCENVQPSGSFKIRGIG---HFCQEMakkGCRHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd01563  23 TPLVRAPRLGERLGGKnLYVKDEGLNPTGSFKDRGMTvavSKAKEL---GVKAVACASTGNTSASLAAYAARAGIKCVVF 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  94 LPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRD---------------------------GWEnVPpfDH-- 144
Cdd:cd01563 100 LPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENwiylsnslnpyrlegqktiafeiaeqlGWE-VP--DYvv 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 145 -PL--------IWKGhaslVQELKavlrtppgalvlavggggllagvvagllEVGW-QHVP-IIAMETHGAHCFNAAITA 213
Cdd:cd01563 177 vPVgnggnitaIWKG----FKELK----------------------------ELGLiDRLPrMVGVQAEGAAPIVRAFKE 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 214 GKLVTLP--DITSVAKSL--GAKTVAARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiysglLR 289
Cdd:cd01563 225 GKDDIEPveNPETIATAIriGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAG-----LK 299

                       330       340
                ....*....|....*....|.
gi 74731799 290 RLQAEGCLPPSLTsVVVIVCG 310
Cdd:cd01563 300 KLREEGIIDKGER-VVVVLTG 319
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 17-307 2.24e-08

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: 54.82  E-value: 2.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  17 VTPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPE 96
Cdd:COG0498  66 GTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPE 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  97 S-TSLqvVQRLQ--GEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFdHPL--------------------------- 146
Cdd:COG0498 146 GkVSP--GQLAQmlTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPArlegqktyafeiaeqlgrvpdwvvvpt 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 147 --------IWKGhaslVQELKavlrtppgalvlavggggllagvvagllEVGW-QHVP-IIAMETHGAHCFNAAITAGKL 216
Cdd:COG0498 223 gnggnilaGYKA----FKELK----------------------------ELGLiDRLPrLIAVQATGCNPILTAFETGRD 270

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799 217 VTLPDitsvakslGAKTVA-----------ARALECMQVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiys 285
Cdd:COG0498 271 EYEPE--------RPETIApsmdignpsngERALFALRESGGTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAG--- 339

                       330       340
                ....*....|....*....|..
gi 74731799 286 glLRRLQAEGCLPPSLTSVVVI 307
Cdd:COG0498 340 --LRKLREEGEIDPDEPVVVLS 359
PRK08197 PRK08197
threonine synthase; Validated
 11-136 8.43e-06

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 46.92  E-value: 8.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   11 QEPFHVV------TPLLESWALSQVAGMP-VFLKCENVQPSGSFKIRGIGhFCQEMAKK-GCRHLVCSSGGNAGIAAAYA 82
Cdd:PRK08197  67 RDPEHIVslgegmTPLLPLPRLGKALGIGrLWVKDEGLNPTGSFKARGLA-VGVSRAKElGVKHLAMPTNGNAGAAWAAY 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 74731799   83 ARKLGIPATIVLPESTSLQVVQRLQGEGAEVQLT-GKVWDEANLRAQELAKRdGW 136
Cdd:PRK08197 146 AARAGIRATIFMPADAPEITRLECALAGAELYLVdGLISDAGKIVAEAVAEY-GW 199
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 17-318 8.71e-06

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: 46.61  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    17 VTPLLESWALSQ-VAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLP 95
Cdd:TIGR00260  22 VTPLFRAPALAAnVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    96 E-STSL-QVVQRLqGEGAEV-QLTGKvWDEANLRAQELAKRD-GWE----NVPPFdHPLIWKGHA-SLVQELKAVLRTPP 166
Cdd:TIGR00260 102 AgKISLgKLAQAL-GYNAEVvAIDGN-FDDAQRLVKQLFEDKpALGlnsaNSIPY-RLEGQKTYAfEAVEQLGWEAPDKV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   167 GALVLAVGGGGLLAGVVAGLLEVGWQHVPI-IAMETHGAHCF-NAAITAGKLVTLPDITSVAKSL--GAKTVAARALECM 242
Cdd:TIGR00260 179 VVPVPNSGNFGAIWKGFKEKKMLGLDSLPVkRGIQAEGAADIvRAFLEGGQWEPIETPETLSTAMdiGNPANWPRALEAF 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74731799   243 QVCKIHSEVVEDTEAVSAVQQLLDDERMLVEPACGAALAAiysglLRRLQAEGCLPPSLTSVVVIVcgGNNINSRE 318
Cdd:TIGR00260 259 RRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAA-----LLKLVEKGTADPAERVVCALT--GNGLKDPE 327
PRK05638 PRK05638
threonine synthase; Validated
 18-158 1.54e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 46.34  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESwALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPES 97
Cdd:PRK05638  67 TPLIRA-RISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRK 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74731799   98 TSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFDHPLIWKGHASLVQEL 158
Cdd:PRK05638 146 VDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFEL 206
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 18-151 1.60e-03

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: 39.80  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799  18 TPLLESWALSQVAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGC----RHLVCSSGGNAGIAAAYAARKLGIPATIV 93
Cdd:cd01561   3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLlkpgTTIIEPTSGNTGIGLAMVAAAKGYRFIIV 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74731799  94 LPESTSLQVVQRLQGEGAEVQLTGKVWDE----ANLRAQELAKR-DGWENVPPFDHPLIWKGH 151
Cdd:cd01561  83 MPETMSEEKRKLLRALGAEVILTPEAEADgmkgAIAKARELAAEtPNAFWLNQFENPANPEAH 145
PRK08329 PRK08329
threonine synthase; Validated
 4-135 6.64e-03

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 37.88  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799    4 PVAEHAKQEPFHVVTPLLEswalsqvAGMPVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAA 83
Cdd:PRK08329  51 PVDEEFLPHLTPPITPTVK-------RSIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYS 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74731799   84 RKLGIPATIVLPESTSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDG 135
Cdd:PRK08329 124 LSEGIKVHVFVSYNASKEKISLLSRLGAELHFVEGDRMEVHEEAVKFSKRNN 175
PRK06381 PRK06381
threonine synthase; Validated
 18-166 7.91e-03

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 37.76  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74731799   18 TPLLESWALSQVAGM-PVFLKCENVQPSGSFKIRGIGHFCQEMAKKGCRHLVCSSGGNAGIAAAYAARKLGIPATIVLPE 96
Cdd:PRK06381  16 TPLLRARKLEEELGLrKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPR 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74731799   97 STSLQVVQRLQGEGAEVQLTGKVWDEANLRAQELAKRDGWENVPPFD-HPLI-WKGHASLVQELKAVLRTPP 166
Cdd:PRK06381  96 SYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYDANPGSvNSVVdIEAYSAIAYEIYEALGDVP 167
 
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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