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Conserved domains on  [gi|284793947|pdb|3HMK|B]
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Chain B, Serine racemase

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) ...
1-322 2.70e-144

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


The actual alignment was detected with superfamily member PLN02970:

Pssm-ID: 444852 [Multi-domain]  Cd Length: 328  Bit Score: 410.61  E-value: 2.70e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         1 MDAQYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEgkpKAVV 80
Cdd:PLN02970   3 ASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        81 THSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVI 160
Cdd:PLN02970  80 THSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       161 AGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGV 240
Cdd:PLN02970 160 SGQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       241 KSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSP--EVKNICIVLSGGNVD 318
Cdd:PLN02970 239 RASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVD 318

                 ....
3HMK_B       319 LTSL 322
Cdd:PLN02970 319 LGVL 322
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
1-322 2.70e-144

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 410.61  E-value: 2.70e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         1 MDAQYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEgkpKAVV 80
Cdd:PLN02970   3 ASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        81 THSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVI 160
Cdd:PLN02970  80 THSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       161 AGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGV 240
Cdd:PLN02970 160 SGQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       241 KSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSP--EVKNICIVLSGGNVD 318
Cdd:PLN02970 239 RASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVD 318

                 ....
3HMK_B       319 LTSL 322
Cdd:PLN02970 319 LGVL 322
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
9-318 7.15e-124

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: 357.57  E-value: 7.15e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        9 FADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGNHG 88
Cdd:cd01562   1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE---EERAKGVVAASAGNHA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562  78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      169 EVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLN 247
Cdd:cd01562 158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVD-TIADGLAvKRPGEL 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3HMK_B      248 TWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQtvsPEVKNICIVLSGGNVD 318
Cdd:cd01562 237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
7-327 1.16e-107

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: 317.36  E-value: 1.16e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        7 ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGN 86
Cdd:COG1171   6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSE---EERARGVVAASAGN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTI 166
Cdd:COG1171  83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      167 ALEVLNQVPLVDALvvpvggggmvagIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVK-SSIG 245
Cdd:COG1171 163 ALEILEQLPDLDAVfvpvggggliagVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      246 LNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQtvsPEVKNICIVLSGGNVDLTSLSWV 325
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPDRLAEI 318

                ..
3HMK_B      326 KQ 327
Cdd:COG1171 319 LE 320
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
26-314 2.34e-72

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: 226.04  E-value: 2.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        106 VPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEG-ILVHPNQEPAVIAGQGTIALEVLNQV-PLVDALVVP 183
Cdd:pfam00291  85 VPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        184 VGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GLNTWPIIRDLVDDVFT 261
Cdd:pfam00291 165 VGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDEYVGEVVT 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
3HMK_B        262 VTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPEvKNICIVLSG 314
Cdd:pfam00291 244 VSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
26-325 2.78e-68

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: 218.46  E-value: 2.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        106 VPQTAPNCKKLAIQAYGASIV-YSEPSDESREnVAQRIIQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYA-FATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        185 GGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLNTWPIIRDLVDDVFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVR-TIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
3HMK_B        264 EDEIKYATQLVWERMKLLIEPTAGVGLAAVLSqhfQTVSPEVKNICIVLSGGNVDLTSLSWV 325
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNLLNKI 294
 
Name Accession Description Interval E-value
PLN02970 PLN02970
serine racemase
1-322 2.70e-144

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 410.61  E-value: 2.70e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         1 MDAQYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEgkpKAVV 80
Cdd:PLN02970   3 ASEKYAADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAE---KGVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        81 THSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVI 160
Cdd:PLN02970  80 THSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       161 AGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHpPETIADGV 240
Cdd:PLN02970 160 SGQGTIALEFLEQVPELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPV-TNTIADGL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       241 KSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSP--EVKNICIVLSGGNVD 318
Cdd:PLN02970 239 RASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAAALSDSFRSNPAwkGCKNVGIVLSGGNVD 318

                 ....
3HMK_B       319 LTSL 322
Cdd:PLN02970 319 LGVL 322
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
9-318 7.15e-124

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: 357.57  E-value: 7.15e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        9 FADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGNHG 88
Cdd:cd01562   1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSE---EERAKGVVAASAGNHA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:cd01562  78 QGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      169 EVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLN 247
Cdd:cd01562 158 EILEQVPDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVD-TIADGLAvKRPGEL 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3HMK_B      248 TWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQtvsPEVKNICIVLSGGNVD 318
Cdd:cd01562 237 TFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLD---LKGKKVVVVLSGGNID 304
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
7-327 1.16e-107

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: 317.36  E-value: 1.16e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        7 ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGN 86
Cdd:COG1171   6 PTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSE---EERARGVVAASAGN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTI 166
Cdd:COG1171  83 HAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQGTI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      167 ALEVLNQVPLVDALvvpvggggmvagIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVK-SSIG 245
Cdd:COG1171 163 ALEILEQLPDLDAVfvpvggggliagVAAALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVT-LPGVDTIADGLAvGRPG 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      246 LNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQtvsPEVKNICIVLSGGNVDLTSLSWV 325
Cdd:COG1171 242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKER---LKGKRVVVVLSGGNIDPDRLAEI 318

                ..
3HMK_B      326 KQ 327
Cdd:COG1171 319 LE 320
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
7-323 2.19e-97

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 291.15  E-value: 2.19e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         7 ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGN 86
Cdd:PRK07048   6 PTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSP---EQRRAGVVTFSSGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK07048  83 HAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGRRLAEERGLTLIPPYDHPHVIAGQGTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       167 ALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADGVKS-SIG 245
Cdd:PRK07048 163 AKELFEEVGPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIV-HIDTPRTIADGAQTqHLG 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3HMK_B       246 LNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSqhfQTVSPEVKNICIVLSGGNVDLTSLS 323
Cdd:PRK07048 242 NYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALR---GKVPLKGKRVGVIISGGNVDLARFA 316
PRK06608 PRK06608
serine/threonine dehydratase;
8-323 1.04e-75

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 236.21  E-value: 1.04e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         8 SFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGK-PKAVVTHSSGN 86
Cdd:PRK06608   6 NPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKE---QGKlPDKIVAYSTGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRiiQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK06608  83 HGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKED--EEQGFYYIHPSDSDSTIAGAGTL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       167 ALEVLNQVPL-VDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPETIADGVKS-SI 244
Cdd:PRK06608 161 CYEALQQLGFsPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLNYSPNTIADGLKTlSV 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3HMK_B       245 GLNTWPIIRDLvDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPevKNICIVLSGGNVDLTSLS 323
Cdd:PRK06608 241 SARTFEYLKKL-DDFYLVEEYEIYYWTAWLTHLLKVICEPSSAINMVAVVNWLKTQSKP--QKLLVILSGGNIDPILYN 316
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
26-314 2.34e-72

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: 226.04  E-value: 2.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:pfam00291   8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        106 VPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEG-ILVHPNQEPAVIAGQGTIALEVLNQV-PLVDALVVP 183
Cdd:pfam00291  85 VPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEGPGaYYINQYDNPLNIEGYGTIGLEILEQLgGDPDAVVVP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        184 VGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GLNTWPIIRDLVDDVFT 261
Cdd:pfam00291 165 VGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVP-VPVADTIADGLGVGDepGALALDLLDEYVGEVVT 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
3HMK_B        262 VTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPEvKNICIVLSG 314
Cdd:pfam00291 244 VSDEEALEAMRLLARREGIVVEPSSAAALAALKLALAGELKGG-DRVVVVLTG 295
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
26-325 2.78e-68

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: 218.46  E-value: 2.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:TIGR01127   1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANL---SEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        106 VPQTAPNCKKLAIQAYGASIV-YSEPSDESREnVAQRIIQETEGILVHPNQEPAVIAGQGTIALEVLNQVPLVDALVVPV 184
Cdd:TIGR01127  78 MPESAPPSKVKATKSYGAEVIlHGDDYDEAYA-FATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDIPDVDTVIVPV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        185 GGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTIADGVK-SSIGLNTWPIIRDLVDDVFTVT 263
Cdd:TIGR01127 157 GGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVR-TIADGIAvKKPGDLTFNIIKEYVDDVVTVD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
3HMK_B        264 EDEIKYATQLVWERMKLLIEPTAGVGLAAVLSqhfQTVSPEVKNICIVLSGGNVDLTSLSWV 325
Cdd:TIGR01127 236 EEEIANAIYLLLERHKILAEGAGAAGVAALLE---QKVDVKGKKIAVVLSGGNIDLNLLNKI 294
PRK06815 PRK06815
threonine/serine dehydratase;
9-322 4.17e-67

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 213.40  E-value: 4.17e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         9 FADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRgLIPDtlEGKPKAVVTHSSGNHG 88
Cdd:PRK06815   4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLR-LLNE--AQRQQGVITASSGNHG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        89 QALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTIAL 168
Cdd:PRK06815  81 QGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       169 EVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSSI--GL 246
Cdd:PRK06815 161 ELVEQQPDLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVE-VAEQPTLSDGTAGGVepGA 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3HMK_B       247 NTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQhfqtvSPEV--KNICIVLSGGNVDLTSL 322
Cdd:PRK06815 240 ITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKL-----APRYqgKKVAVVLCGKNIVLEKY 312
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
1-323 1.59e-62

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 202.27  E-value: 1.59e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         1 MDAQYD--ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTLEGKPKA 78
Cdd:PRK08638   1 MHITYDlpVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSL---TDAEKRKG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        79 VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YSEPSDESRENVAQRIiqETEG-ILVHPNQE 156
Cdd:PRK08638  78 VVACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVlHGDNFNDTIAKVEEIV--EEEGrTFIPPYDD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       157 PAVIAGQGTIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPNLHPPeTI 236
Cdd:PRK08638 156 PKVIAGQGTIGLEILEDLWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTG-TL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       237 ADGVKSSI-GLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPEVKNICIVlSGG 315
Cdd:PRK08638 235 ADGCDVSRpGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKLDQYIQNKKVVAII-SGG 313

                 ....*...
3HMK_B       316 NVDLTSLS 323
Cdd:PRK08638 314 NVDLSRVS 321
PRK07334 PRK07334
threonine dehydratase; Provisional
7-318 7.71e-59

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 194.73  E-value: 7.71e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         7 ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGN 86
Cdd:PRK07334   5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTE---EERARGVIAMSAGN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YSEPSDESRENVAQriIQETEG-ILVHPNQEPAVIAGQG 164
Cdd:PRK07334  82 HAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVlHGETLDEARAHARE--LAEEEGlTFVHPYDDPAVIAGQG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       165 TIALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQsKLKGELTPNLHppETIADG--VKs 242
Cdd:PRK07334 160 TVALEMLEDAPDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYA-AIKGVALPCGG--STIAEGiaVK- 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3HMK_B       243 SIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLS--QHFQTvspevKNICIVLSGGNVD 318
Cdd:PRK07334 236 QPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAypERFRG-----RKVGLVLSGGNID 308
eutB PRK07476
threonine dehydratase; Provisional
7-319 2.18e-57

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 188.64  E-value: 2.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         7 ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPdtlEGKPKAVVTHSSGN 86
Cdd:PRK07476   1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSA---QERARGVVTASTGN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTI 166
Cdd:PRK07476  78 HGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       167 ALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGeltpnlHP-----PETIADGVK 241
Cdd:PRK07476 158 GLEILEALPDVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMERGAAMHASLAAG------RPvqveeVPTLADSLG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       242 SSIGLN---TWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSqhfQTVSPEVKNICIVLSGGNVD 318
Cdd:PRK07476 232 GGIGLDnryTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLA---GKIAARDGPIVVVVSGANID 308

                 .
3HMK_B       319 L 319
Cdd:PRK07476 309 M 309
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
26-315 3.39e-54

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: 177.71  E-value: 3.39e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDtLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:cd00640   1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEE-GKLPKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      106 VPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEG-ILVHPNQEPAVIAGQGTIALEVLNQVP--LVDALVV 182
Cdd:cd00640  80 MPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKELAEEDPGaYYVNQFDNPANIAGQGTIGLEILEQLGgqKPDAVVV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      183 PVGGGGMVAGIAITIKTLKPSVKVYAAEPsnaddcyqsklkgeltpnlhppetiadgvkssiglntwpiirdlvdDVFTV 262
Cdd:cd00640 160 PVGGGGNIAGIARALKELLPNVKVIGVEP----------------------------------------------EVVTV 193
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
3HMK_B      263 TEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTvsPEVKNICIVLSGG 315
Cdd:cd00640 194 SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKL--GKGKTVVVILTGG 244
PRK08246 PRK08246
serine/threonine dehydratase;
7-322 3.01e-51

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 172.06  E-value: 3.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         7 ISFADVEKAHLNIQDSVHLTPVLTSSIlNQIAGRNLFFKCELFQKTGSFKIRGALNAIR-GLIPdtlegkPKAVVTHSSG 85
Cdd:PRK08246   5 ITRSDVRAAAQRIAPHIRRTPVLEADG-AGFGPAPVWLKLEHLQHTGSFKARGAFNRLLaAPVP------AAGVVAASGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        86 NHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGT 165
Cdd:PRK08246  78 NAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       166 IALEVLNQVPLVDALVVPVGGGGMVAGIAitiKTLKPSVKVYAAEPSNADDCYQSKLKGEltpnlhPPETIADGVKSS-- 243
Cdd:PRK08246 158 LGLEIEEQAPGVDTVLVAVGGGGLIAGIA---AWFEGRARVVAVEPEGAPTLHAALAAGE------PVDVPVSGIAADsl 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       244 ----IGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPEvkNICIVLSGGNVDL 319
Cdd:PRK08246 229 garrVGEIAFALARAHVVTSVLVSDEAIIAARRALWEELRLAVEPGAATALAALLSGAYVPAPGE--RVAVVLCGANTDP 306

                 ...
3HMK_B       320 TSL 322
Cdd:PRK08246 307 ATL 309
ectoine_eutB TIGR02991
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ...
7-319 1.06e-46

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: 160.79  E-value: 1.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B          7 ISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTLEGKPKAVVTHSSGN 86
Cdd:TIGR02991   1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSL---SDTQRAAGVVAASTGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         87 HGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASI-VYSEPSDESRENVaQRIIQETEGILVHPNQEPAVIAGQGT 165
Cdd:TIGR02991  78 HGRALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAEVrIVGRSQDDAQEEV-ERLVADRGLTMLPPFDHPDIVAGQGT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        166 IALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSkLKGELTPNLHPPETIADGVKSSIG 245
Cdd:TIGR02991 157 LGLEVVEQMPDLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKAS-LQAGRPVLVAELPTLADSLGGGIG 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3HMK_B        246 LN---TWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTVSPevknICIVLSGGNVDL 319
Cdd:TIGR02991 236 LDnrvTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGP----CAVIVSGRNIDM 308
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
39-330 3.41e-42

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 152.99  E-value: 3.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        39 GRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEgkpKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAI 118
Cdd:PRK09224  34 GNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLA---RGVITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       119 QAYGASIV-----YSEPSDESREnvaqriIQETEG-ILVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVPVGGGGMVA 191
Cdd:PRK09224 111 RAFGGEVVlhgdsFDEAYAHAIE------LAEEEGlTFIHPFDDPDVIAGQGTIAMEILQQHPhPLDAVFVPVGGGGLIA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       192 GIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADG--VKsSIGLNTWPIIRDLVDDVFTVTEDEIKY 269
Cdd:PRK09224 185 GVAAYIKQLRPEIKVIGVEPEDSACLKAALEAGERV-DLPQVGLFADGvaVK-RIGEETFRLCQEYVDDVITVDTDEICA 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
3HMK_B       270 ATQLVWERMKLLIEPTAGVGLAAvLSQHFQTVSPEVKNICIVLSGGNVDLTSLSWVkqAER 330
Cdd:PRK09224 263 AIKDVFEDTRSIAEPAGALALAG-LKKYVAQHGIEGETLVAILSGANMNFDRLRYV--AER 320
PRK12483 PRK12483
threonine dehydratase; Reviewed
26-330 3.09e-41

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 150.72  E-value: 3.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEgkpKAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLA---RGVITASAGNHAQGVALAAARLGVKAVIV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       106 VPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGTIALEVLNQVP-LVDALVVPV 184
Cdd:PRK12483 115 MPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVAMEILRQHPgPLDAIFVPV 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       185 GGGGMVAGIAITIKTLKPSVKVYAAEPSNAdDCYQSKLKGELTPNLHPPETIADGVK-SSIGLNTWPIIRDLVDDVFTVT 263
Cdd:PRK12483 195 GGGGLIAGIAAYVKYVRPEIKVIGVEPDDS-NCLQAALAAGERVVLGQVGLFADGVAvAQIGEHTFELCRHYVDEVVTVS 273
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3HMK_B       264 EDEIKYATQLVWERMKLLIEPTAGVGLAAvLSQHFQTVSPEVKNICIVLSGGNVDLTSLSWVkqAER 330
Cdd:PRK12483 274 TDELCAAIKDIYDDTRSITEPAGALAVAG-IKKYAEREGIEGQTLVAIDSGANVNFDRLRHV--AER 337
PRK08639 PRK08639
threonine dehydratase; Validated
1-330 2.87e-36

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 135.32  E-value: 2.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         1 MDAQYDISFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdTLEGKPKAVV 80
Cdd:PRK08639   1 MTVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQL---SDEELAAGVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        81 THSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGAS----IVYSEPSDESrENVAQRIIQETEGILVHPNQE 156
Cdd:PRK08639  78 CASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEfveiVLVGDTFDDS-AAAAQEYAEETGATFIPPFDD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       157 PAVIAGQGTIALEVLNQV---PLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTPnLHPP 233
Cdd:PRK08639 157 PDVIAGQGTVAVEILEQLekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVT-LEKI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       234 ETIADG--VKSsIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPtAGVGLAAVLSQHFQTVspEVKNICIV 311
Cdd:PRK08639 236 DKFVDGaaVAR-VGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEP-AGALSIAALELYKDEI--KGKTVVCV 311
                        330
                 ....*....|....*....
3HMK_B       312 LSGGNVDLTSLSWVKqaER 330
Cdd:PRK08639 312 ISGGNNDIERMPEIK--ER 328
PRK08813 PRK08813
threonine dehydratase; Provisional
7-333 7.09e-32

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 122.04  E-value: 7.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         7 ISFADVEKAHLNIQDSVHLTPVltssilnQIAGR-NLFFKCELFQKTGSFKIRGALNAirgLIPDTLEGKPKAVVTHSSG 85
Cdd:PRK08813  21 VSVADVLAAQARLRRYLSPTPL-------HYAERfGVWLKLENLQRTGSYKVRGALNA---LLAGLERGDERPVICASAG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        86 NHGQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENVAQRIIQETEGILVHPNQEPAVIAGQGT 165
Cdd:PRK08813  91 NHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQGT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       166 IALEVLNQVPlvDALVVPVGGGGMVAGIAITIKTlkPSVKVYAAEPSNADDCYQSkLKGELTpNLHPPETIADGVKSSI- 244
Cdd:PRK08813 171 VGIELAAHAP--DVVIVPIGGGGLASGVALALKS--QGVRVVGAQVEGVDSMARA-IRGDLR-EIAPVATLADGVKVKIp 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       245 GLNTWPIIRDLVDDVFTVTEDEIKYA-TQLVWERmKLLIEPTAGVGLAAvlsqhFQTVSPEVKniCIVLSGGNVDLTSLS 323
Cdd:PRK08813 245 GFLTRRLCSSLLDDVVIVREAELRETlVRLALEE-HVIAEGAGALALAA-----GRRVSGKRK--CAVVSGGNIDATVLA 316
                        330
                 ....*....|
3HMK_B       324 WVKQAERPAP 333
Cdd:PRK08813 317 TLLSEVRPRP 326
PLN02550 PLN02550
threonine dehydratase
24-327 2.67e-30

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 120.80  E-value: 2.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        24 HLTPVLTSSI--------------LNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEgkpKAVVTHSSGNHGQ 89
Cdd:PLN02550  94 YLTNILSAKVydvaiesplqlakkLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLD---KGVICSSAGNHAQ 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        90 ALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPS-DESRENVAQRIIQETEgILVHPNQEPAVIAGQGTIAL 168
Cdd:PLN02550 171 GVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSyDEAQAYAKQRALEEGR-TFIPPFDHPDVIAGQGTVGM 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       169 EVLNQVP-LVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGELTpNLHPPETIADGVK-SSIGL 246
Cdd:PLN02550 250 EIVRQHQgPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERV-MLDQVGGFADGVAvKEVGE 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       247 NTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVlSQHFQTVSPEVKNICIVLSGGNVDLTSLSWVK 326
Cdd:PLN02550 329 ETFRLCRELVDGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGA-EAYCKYYGLKDENVVAITSGANMNFDRLRIVT 407

                 .
3HMK_B       327 Q 327
Cdd:PLN02550 408 E 408
PRK06110 PRK06110
threonine dehydratase;
8-325 2.12e-28

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 112.01  E-value: 2.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         8 SFADVEKAHLNIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDtlEGKPKAVVTHSSGNH 87
Cdd:PRK06110   4 TLAELEAAAAVVYAAMPPTPQYRWPLLAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARR--GPRVRGVISATRGNH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        88 GQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIV-YSEPSDESRENvAQRIIQETEGILVhPNQEPAVIAGQGTI 166
Cdd:PRK06110  82 GQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIeHGEDFQAAREE-AARLAAERGLHMV-PSFHPDLVRGVATY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       167 ALEVLNQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKLKGEL--TPNlhpPETIADGVKSSI 244
Cdd:PRK06110 160 ALELFRAVPDLDVVYVPIGMGSGICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVvtTPV---ATTLADGMACRT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       245 GL-NTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQTvspEVKNICIVLSGGNVDLTSLS 323
Cdd:PRK06110 237 PDpEALEVIRAGADRIVRVTDDEVAAAMRAYFTDTHNVAEGAGAAALAAALQERERL---AGKRVGLVLSGGNIDRAVFA 313

                 ..
3HMK_B       324 WV 325
Cdd:PRK06110 314 RV 315
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
26-312 6.17e-26

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: 104.90  E-value: 6.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-PDTlegkpkAVVTHSSGNHGQALTYAAKLEG 99
Cdd:cd01561   3 TPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIedaekRGLLkPGT------TIIEPTSGNTGIGLAMVAAAKG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      100 IPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSD----ESRENVAQRIIQETEGIlVHPNQ--EPA-VIAGQGTIALEVLN 172
Cdd:cd01561  77 YRFIIVMPETMSEEKRKLLRALGAEVILTPEAEadgmKGAIAKARELAAETPNA-FWLNQfeNPAnPEAHYETTAPEIWE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      173 QVP-LVDALvvpvggggmvagIA-------IT-----IKTLKPSVKVYAAEPSNADdcyqsklkgeLTPNLHPPETIADG 239
Cdd:cd01561 156 QLDgKVDAF------------VAgvgtggtITgvaryLKEKNPNVRIVGVDPVGSV----------LFSGGPPGPHKIEG 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3HMK_B      240 vkssIGLNTWPII--RDLVDDVFTVTEDE-IKYATQLVwERMKLLIEPTAGVGLAAVLsqHFQTVSPEVKNICIVL 312
Cdd:cd01561 214 ----IGAGFIPENldRSLIDEVVRVSDEEaFAMARRLA-REEGLLVGGSSGAAVAAAL--KLAKRLGPGKTIVTIL 282
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
26-316 8.20e-23

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: 96.60  E-value: 8.20e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLIPDTLEGKPkAVVTHSSGNHGQALTYAAKLEGIPAYIV 105
Cdd:cd06448   2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNECV-HVVCSSGGNAGLAAAYAARKLGVPCTIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      106 VPQTAPNCKKLAIQAYGASIVYS-----EPSDESRENVAQRIIqetEGILVHPNQEPAVIAGQGTIALEVLNQVPL---V 177
Cdd:cd06448  81 VPESTKPRVVEKLRDEGATVVVHgkvwwEADNYLREELAENDP---GPVYVHPFDDPLIWEGHSSMVDEIAQQLQSqekV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      178 DALVVPVGGGGMVAGIaitIKTLK----PSVKVYAAEPSNADDCYQSKLKGELTPnLHPPETIADGVKSS-IGLNTW--- 249
Cdd:cd06448 158 DAIVCSVGGGGLLNGI---VQGLErngwGDIPVVAVETEGAHSLNASLKAGKLVT-LPKITSVATSLGAKtVSSQALeya 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      250 ---PIIRDLVDD------VFTVTEDEikyatqlvwermKLLIEPTAGVGLAAVLSQHFQTVSPEVK-----NICIVLSGG 315
Cdd:cd06448 234 qehNIKSEVVSDrdavqaCLRFADDE------------RILVEPACGAALAVVYSGKILDLQLEVLltpldNVVVVVCGG 301

                .
3HMK_B      316 N 316
Cdd:cd06448 302 S 302
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
26-294 9.14e-23

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


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 97.58  E-value: 9.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       26 TPVLTSSILNQIAGRNLFFKcELFQ-KTGSFKIRG---ALNAIRGLipdtleGKpKAVVTHSSGNHGQAL-TYAAKlEGI 100
Cdd:COG0498  67 TPLVKAPRLADELGKNLYVK-EEGHnPTGSFKDRAmqvAVSLALER------GA-KTIVCASSGNGSAALaAYAAR-AGI 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      101 PAYIVVPQT-APNCKKLAIQAYGASIV-----YSEpsdesRENVAQRIIQETEGILVHpNQEPAVIAGQGTIALEV---L 171
Cdd:COG0498 138 EVFVFVPEGkVSPGQLAQMLTYGAHVIavdgnFDD-----AQRLVKELAADEGLYAVN-SINPARLEGQKTYAFEIaeqL 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      172 NQVP---------LVDALvvpvggggmvagiAI-----------TIKTLkPsvKVYAAEPSNADDCYQSKLKGELTPNLH 231
Cdd:COG0498 212 GRVPdwvvvptgnGGNIL-------------AGykafkelkelgLIDRL-P--RLIAVQATGCNPILTAFETGRDEYEPE 275
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3HMK_B      232 PPETIADGVksSIG--LNTWPIIRDLVD---DVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVL 294
Cdd:COG0498 276 RPETIAPSM--DIGnpSNGERALFALREsggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLR 341
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
26-294 1.10e-19

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: 88.03  E-value: 1.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       26 TPVLTSSILNQIAG-RNLFFKCELFQKTGSFKIRGALNAIRglipDTLEGKPKAVVTHSSGNHGQAL-TYAAKlEGIPAY 103
Cdd:cd01563  23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVS----KAKELGVKAVACASTGNTSASLaAYAAR-AGIKCV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      104 IVVPQTAPNCKKLAIQAYGASIVysePSDESRE---NVAQRIIQETEGILVHpNQEPAVIAGQGTIALEVLNQ------- 173
Cdd:cd01563  98 VFLPAGKALGKLAQALAYGATVL---AVEGNFDdalRLVRELAEENWIYLSN-SLNPYRLEGQKTIAFEIAEQlgwevpd 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      174 ---VPLVDALVVPVGGGGMVAGIAITIKTLKPsvKVYAAEPSNADDCYQSKLKG--ELTPNLHpPETIADGVKssIGlN- 247
Cdd:cd01563 174 yvvVPVGNGGNITAIWKGFKELKELGLIDRLP--RMVGVQAEGAAPIVRAFKEGkdDIEPVEN-PETIATAIR--IG-Np 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
3HMK_B      248 -TWPIIRDLVD----DVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVL 294
Cdd:cd01563 248 aSGPKALRAVResggTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLK 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
18-294 6.81e-18

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: 82.40  E-value: 6.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       18 NIQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-PDT--LEGkpkavvthSSGNHGQ 89
Cdd:COG0031   6 SILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIedaekRGLLkPGGtiVEA--------TSGNTGI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       90 ALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSD--ESRENVAQRIIQETEGIlVHPNQ--EPA-VIAGQG 164
Cdd:COG0031  78 GLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEgmKGAIDKAEELAAETPGA-FWPNQfeNPAnPEAHYE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B      165 TIALEVLNQVPL-VDALvvpvggggmvagIA-------IT-----IKTLKPSVKVYAAEPSNAddcyqSKLKGElTPNLH 231
Cdd:COG0031 157 TTGPEIWEQTDGkVDAF------------VAgvgtggtITgvgryLKERNPDIKIVAVEPEGS-----PLLSGG-EPGPH 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3HMK_B      232 PPETIADGVKSSIglntwpIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVL 294
Cdd:COG0031 219 KIEGIGAGFVPKI------LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAAL 275
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
33-318 3.14e-14

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: 72.41  E-value: 3.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B         33 ILNQIAGRNLFFKCELFQKTGSFKIRGALNAIRGLipdtLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPN 112
Cdd:TIGR00260  31 LAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKA----LELGNDTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAGKIS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        113 CKKLAIQ-AYGASIV-YSEPSDESRENVAQrIIQETEGILVHP-NQEPAVIAGQGTIALEVLNQVP------LVDALVVP 183
Cdd:TIGR00260 107 LGKLAQAlGYNAEVVaIDGNFDDAQRLVKQ-LFEDKPALGLNSaNSIPYRLEGQKTYAFEAVEQLGweapdkVVVPVPNS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        184 VGGGGMVAGIAITIKTLKPSVKVY-AAEPSNADDCYQSKLK-GELTPNLHPpETIA---DGVKSSIGLNTWPIIRDLVDD 258
Cdd:TIGR00260 186 GNFGAIWKGFKEKKMLGLDSLPVKrGIQAEGAADIVRAFLEgGQWEPIETP-ETLStamDIGNPANWPRALEAFRRSNGY 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
3HMK_B        259 VFTVTEDEIKYATQLVWERMKLLIEPTAGVGLAAVLSQHFQ-TVSPEVKNICIVLSGGNVD 318
Cdd:TIGR00260 265 AEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKgTADPAERVVCALTGNGLKD 325
PRK05638 PRK05638
threonine synthase; Validated
26-314 1.12e-13

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 71.38  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        26 TPVLTSSILNQIaGRNLFFKCELFQKTGSFKIRGALNAIRglipDTLEGKPKAVVTHSSGNHGQALT-YAAKlEGIPAYI 104
Cdd:PRK05638  67 TPLIRARISEKL-GENVYIKDETRNPTGSFRDRLATVAVS----YGLPYAANGFIVASDGNAAASVAaYSAR-AGKEAFV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       105 VVPQTAPNCKKLAIQAYGAS-IVYSEPSDESRENVAQRiiQETEGIL-VHPNQEPAVIAGQGTIALEVLNQ-------VP 175
Cdd:PRK05638 141 VVPRKVDKGKLIQMIAFGAKiIRYGESVDEAIEYAEEL--ARLNGLYnVTPEYNIIGLEGQKTIAFELWEEinpthviVP 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       176 LVDALVVPVGGGGMVAGIAITIKTLKPsvKVYAAEPSNADDCYQSKL--KGELTPNLHPPETIADGVKSSIGLNtwpIIR 253
Cdd:PRK05638 219 TGSGSYLYSIYKGFKELLEIGVIEEIP--KLIAVQTERCNPIASEILgnKTKCNETKALGLYVKNPVMKEYVSE---AIK 293
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
3HMK_B       254 DLVDDVFTVTEDEIKYATQLVWERmKLLIEPTAGVGLAAVLSQHFQTVSPEVKNICIVLSG 314
Cdd:PRK05638 294 ESGGTAVVVNEEEIMAGEKLLAKE-GIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTG 353
PRK08329 PRK08329
threonine synthase; Validated
24-319 4.13e-12

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 66.39  E-value: 4.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        24 HLTPVLTSSILNqiaGRNLFFKCELFQKTGSFKIRGALNAIRGLipdtLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAY 103
Cdd:PRK08329  59 HLTPPITPTVKR---SIKVYFKLDYLQPTGSFKDRGTYVTVAKL----KEEGINEVVIDSSGNAALSLALYSLSEGIKVH 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       104 IVVPQTAPNCKKLAIQAYGASIVYSepsDESRENVAQRIIQ--ETEGIL-VHPNQEPAVIAGQGTIALEVLNQVPLVDAL 180
Cdd:PRK08329 132 VFVSYNASKEKISLLSRLGAELHFV---EGDRMEVHEEAVKfsKRNNIPyVSHWLNPYFLEGTKTIAYEIYEQIGVPDYA 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       181 VVPVGGGGMVAGIAITIKTLK--------PSVKVYAAEPSNAdDCYQSKLKGELT-----PNlhPP--ETIADGVKSSIG 245
Cdd:PRK08329 209 FVPVGSGTLFLGIWKGFKELHemgeiskmPKLVAVQAEGYES-LCKRSKSENKLAdgiaiPE--PPrkEEMLRALEESNG 285
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3HMK_B       246 LntwpiirdlvddVFTVTEDEIKYAtqLVW-ERMKLLIEPTAGVGLAAVLSQHFQTVSPEVKNICIVLSGGNVDL 319
Cdd:PRK08329 286 F------------CISVGEEETRAA--LHWlRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLKN 346
PRK06450 PRK06450
threonine synthase; Validated
37-173 1.09e-10

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 62.06  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        37 IAGRNLFFKCELFQKTGSFKIRGAlnaiRGLIPDTLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNCKKL 116
Cdd:PRK06450  62 IKKGNIWFKLDFLNPTGSYKDRGS----VTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLK 137
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
3HMK_B       117 AIQAYGASIVYSEpsdESRENVaQRIIQETEGILVHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PRK06450 138 QIESYGAEVVRVR---GSREDV-AKAAENSGYYYASHVLQPQFRDGIRTLAYEIAKD 190
PRK06381 PRK06381
threonine synthase; Validated
26-174 2.69e-10

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 60.49  E-value: 2.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        26 TPVLTSSILNQIAG-RNLFFKCELFQKTGSFKIRGALNAIRglipDTLEGKPKAVVTHSSGNHGQALTYAAKLEGIPAYI 104
Cdd:PRK06381  16 TPLLRARKLEEELGlRKIYLKFEGANPTGTQKDRIAEAHVR----RAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVI 91
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3HMK_B       105 VVPQTAPNCKKLAIQAYGASIVYSEPSDEsrENVAQ-RIIQETEGIL-VHPNQEPAVIA--GQGTIALEVLNQV 174
Cdd:PRK06381  92 FIPRSYSNSRVKEMEKYGAEIIYVDGKYE--EAVERsRKFAKENGIYdANPGSVNSVVDieAYSAIAYEIYEAL 163
PRK08197 PRK08197
threonine synthase; Validated
25-173 4.96e-09

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 56.93  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        25 LTPVLTSSIL-NQIAGRNLFFKCELFQKTGSFKIRGALNAI-RGLipdtlEGKPKAVVTHSSGNHGQAL-TYAAKLeGIP 101
Cdd:PRK08197  79 MTPLLPLPRLgKALGIGRLWVKDEGLNPTGSFKARGLAVGVsRAK-----ELGVKHLAMPTNGNAGAAWaAYAARA-GIR 152
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3HMK_B       102 AYIVVPQTAPNCKKLAIQAYGASIVYSEP--SDESREnVAQRIiqETEGIL-VHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PRK08197 153 ATIFMPADAPEITRLECALAGAELYLVDGliSDAGKI-VAEAV--AEYGWFdVSTLKEPYRIEGKKTMGLELAEQ 224
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
53-295 6.60e-09

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 56.81  E-value: 6.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        53 GSFKIRGALNA------------IRGLIPDTL---EGKPKA----VVTHSSGNHGQALTYAAKLEGIPAYIVVPQTAPNC 113
Cdd:PRK08206  74 NAFKALGGAYAvarllaeklgldISELSFEELtsgEVREKLgditFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       114 KKLAIQAYGASIVYSEPS-DES-REnvAQRIIQETEGILVhpnQEPA----------VIAGQGTIALEVLNQVPlvdalv 181
Cdd:PRK08206 154 RVDAIRALGAECIITDGNyDDSvRL--AAQEAQENGWVVV---QDTAwegyeeiptwIMQGYGTMADEAVEQLK------ 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       182 vpvggggmvagiaitIKTLKPS-------------------VKVYAA--------EPSNADDCYQSKLKGELTPNLHPPE 234
Cdd:PRK08206 223 ---------------EMGVPPThvflqagvgslagavlgyfAEVYGEqrphfvvvEPDQADCLYQSAVDGKPVAVTGDMD 287
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3HMK_B       235 TI----ADGVKSSIGlntWPIIRDLVDDVFTVTEDEIKYAtqlvwerMKLLIEPTAG-----------VGLAAVLS 295
Cdd:PRK08206 288 TImaglACGEPNPLA---WEILRNCADAFISCPDEVAALG-------MRILANPLGGdppivsgesgaVGLGALAA 353
cysM PRK11761
cysteine synthase CysM;
19-150 4.27e-06

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 47.56  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        19 IQDSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLI-P-DTLegkpkavVTHSSGNHGQAL 91
Cdd:PRK11761   6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIvqaekRGEIkPgDTL-------IEATSGNTGIAL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
3HMK_B        92 TYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSePSDESRE---NVAQRIIQETEGIL 150
Cdd:PRK11761  79 AMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILV-PKEQGMEgarDLALQMQAEGEGKV 139
PRK10717 PRK10717
cysteine synthase A; Provisional
26-276 6.58e-06

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 47.16  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        26 TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdtlegKP-KAVVTHSSGNHGQALTYAAKLEG 99
Cdd:PRK10717  14 TPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIwdaekRGLL------KPgGTIVEGTAGNTGIGLALVAAARG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       100 IPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESREN----VAQRIIQEtegiLVHPNQEPAVIAGQ-----------G 164
Cdd:PRK10717  88 YKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANPNnyvkGAGRLAEE----LVASEPNGAIWANQfdnpanreahyE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       165 TIALEVLNQVP-LVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNAdDCYQSKLKGELTPnlhPPETIADGvkss 243
Cdd:PRK10717 164 TTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGS-ALYSYYKTGELKA---EGSSITEG---- 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
3HMK_B       244 IGLN--TWPIIRDLVDDVFTVTEDE-IKYATQLVWE 276
Cdd:PRK10717 236 IGQGriTANLEGAPIDDAIRIPDEEaLSTAYRLLEE 271
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
17-294 8.97e-05

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 43.80  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        17 LNIQDSVHL----TPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNAI-----RGLIpdtLEGKpKAVVTHSSGNH 87
Cdd:PLN02556  47 TKIKTDASQligkTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIedaekKNLI---TPGK-TTLIEPTSGNM 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        88 GQALTYAAKLEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRENV--AQRIIQET-EGILVHPNQEPA-VIAGQ 163
Cdd:PLN02556 123 GISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVkkAYELLESTpDAFMLQQFSNPAnTQVHF 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B       164 GTIALEVL-NQVPLVDALVVPVGGGGMVAGIAITIKTLKPSVKVYAAEPSNADDCYQSKlkgeltPNLHPPETIADGVKS 242
Cdd:PLN02556 203 ETTGPEIWeDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGK------PGPHHITGNGVGFKP 276
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
3HMK_B       243 SIglntwpIIRDLVDDVFTVT-EDEIKYATQLVWERmKLLIEPTAGVGLAAVL 294
Cdd:PLN02556 277 DI------LDMDVMEKVLEVSsEDAVNMARELALKE-GLMVGISSGANTVAAL 322
PLN02356 PLN02356
phosphateglycerate kinase
21-141 3.15e-04

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 42.29  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        21 DSVHLTPVLTSSILNQIAGRNLFFKCELFQKTGSFKIRGALNairgLIPDTLE-GK--PKAVVTH-SSGNHGQALTYAAK 96
Cdd:PLN02356  49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVK----IIEEALEsGQlfPGGVVTEgSAGSTAISLATVAP 124
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
3HMK_B        97 LEGIPAYIVVPQTAPNCKKLAIQAYGASIVYSEPSDESRE----NVAQR 141
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVRPVSITHKdhyvNIARR 173
PLN02569 PLN02569
threonine synthase
36-173 1.12e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 40.57  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3HMK_B        36 QIAGRN-LFFKCELFQKTGSFKIRG------ALNAIRGLipdtleGKP-KAVVTHSSGNHGQALTYAAKLEGIPAYIVVP 107
Cdd:PLN02569 145 EFLGMNdLWVKHCGISHTGSFKDLGmtvlvsQVNRLRKM------AKPvVGVGCASTGDTSAALSAYCAAAGIPSIVFLP 218
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3HMK_B       108 QTAPNCKKLAIQAYGASIVYSEPSDesrENVAQRIIQETEG---ILVHPNQEPAVIAGQGTIALEVLNQ 173
Cdd:PLN02569 219 ADKISIAQLVQPIANGALVLSIDTD---FDGCMRLIREVTAelpIYLANSLNSLRLEGQKTAAIEILQQ 284
 
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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