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Conserved domains on  [gi|489502016|ref|WP_003406912|]
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MULTISPECIES: O-phosphoserine sulfhydrylase [Mycobacterium]

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) ...
 7-306 8.15e-130

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 TIGR01136:

Pssm-ID: 444852  Cd Length: 299  Bit Score: 372.00  E-value: 8.15e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    7 LLQALGNTPLVGLQRLSPRWDDgrdgphvRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISL 86
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDA-------RVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYCGTG 166
Cdd:TIGR01136  74 AMVAAARGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  167 PELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGE-------GVYALRNMDEGFVPELYDPEILTA 238
Cdd:TIGR01136 154 PEIWRDTDgRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPvlsggepGPHKIQGIGAGFIPKILDLSLIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502016  239 RYSVGAVDAVRRTRELVHTEGIFAGISTGAVLHaaLGVGAGALAAGERADIALVVADAGWKYLSTGAY 306
Cdd:TIGR01136 234 VITVSDEDAIETARRLAREEGILVGISSGAAVA--AALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
 
Name Accession Description Interval E-value
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 7-306 8.15e-130

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


Pssm-ID: 273463  Cd Length: 299  Bit Score: 372.00  E-value: 8.15e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    7 LLQALGNTPLVGLQRLSPRWDDgrdgphvRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISL 86
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDA-------RVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYCGTG 166
Cdd:TIGR01136  74 AMVAAARGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  167 PELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGE-------GVYALRNMDEGFVPELYDPEILTA 238
Cdd:TIGR01136 154 PEIWRDTDgRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPvlsggepGPHKIQGIGAGFIPKILDLSLIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502016  239 RYSVGAVDAVRRTRELVHTEGIFAGISTGAVLHaaLGVGAGALAAGERADIALVVADAGWKYLSTGAY 306
Cdd:TIGR01136 234 VITVSDEDAIETARRLAREEGILVGISSGAAVA--AALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 1-303 5.84e-119

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: 344.34  E-value: 5.84e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   1 MTRYDSLLQALGNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSG 80
Cdd:COG0031    1 MRIYDSILELIGNTPLVRLNRLSP-------GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  81 NTGISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDS 160
Cdd:COG0031   74 NTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 161 HYCGTGPELLADLP-EITHFVAglgttgtlmgtgRFLREHVANVKIVAAEPRYG-------EGVYALRNMDEGFVPELYD 232
Cdd:COG0031  154 HYETTGPEIWEQTDgKVDAFVAgvgtggtitgvgRYLKERNPDIKIVAVEPEGSpllsggePGPHKIEGIGAGFVPKILD 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502016 233 PEILTARYSVGAVDAVRRTRELVHTEGIFAGISTGAVLHaalGVGAGALAAGERADIALVVADAGWKYLST 303
Cdd:COG0031  234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVA---AALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 12-302 1.80e-109

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: 319.84  E-value: 1.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISLAMAAR 91
Cdd:cd01561    1 GNTPLVRLNRLSP-------GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  92 LKGYRLICVMPENTSVERRQLLELYGAQIIF--SAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYCGTGPEL 169
Cdd:cd01561   74 AKGYRFIIVMPETMSEEKRKLLRALGAEVILtpEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 170 LADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYG-------EGVYALRNMDEGFVPELYDPEILTARYS 241
Cdd:cd01561  154 WEQLDgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSvlfsggpPGPHKIEGIGAGFIPENLDRSLIDEVVR 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502016 242 VGAVDAVRRTRELVHTEGIFAGISTGAVLHaalGVGAGALAAGERADIALVVADAGWKYLS 302
Cdd:cd01561  234 VSDEEAFAMARRLAREEGLLVGGSSGAAVA---AALKLAKRLGPGKTIVTILPDSGERYLS 291
cysM PRK11761
cysteine synthase CysM;
4-306 1.62e-83

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 254.03  E-value: 1.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   4 YDSLLQALGNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTG 83
Cdd:PRK11761   3 YPTLEDTIGNTPLVKLQRLPP-------DRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  84 ISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAAtNPSWVMLYQYGNPANTDSHYC 163
Cdd:PRK11761  76 IALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQA-EGEGKVLDQFANPDNPLAHYE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 164 GTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGEGVYALRNMDEGFVPELYDPEILTARYSV 242
Cdd:PRK11761 155 TTGPEIWRQTEgRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDV 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502016 243 GAVDAVRRTRELVHTEGIFAGISTGAVLHaalgVGAGALAAGERADIALVVADAGWKYLSTGAY 306
Cdd:PRK11761 235 SQQEAENTMRRLAREEGIFCGVSSGGAVA----AALRIARENPNAVIVAIICDRGDRYLSTGVF 294
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 7-271 6.05e-58

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: 188.67  E-value: 6.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    7 LLQALGNTPLVGLQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIEQAEAdglLRPGATILEPTSGNTGISL 86
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELG-------VDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRAL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSaaEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDShYCGTG 166
Cdd:pfam00291  71 AAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLV--GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  167 PELLADL-PEITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGEGVYALRN----------------MDEGFVPE 229
Cdd:pfam00291 148 LEILEQLgGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAagrpvpvpvadtiadgLGVGDEPG 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489502016  230 LYDPEILTAR----YSVGAVDAVRRTRELVHTEGIFAGISTGAVLH 271
Cdd:pfam00291 228 ALALDLLDEYvgevVTVSDEEALEAMRLLARREGIVVEPSSAAALA 273
 
Name Accession Description Interval E-value
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 7-306 8.15e-130

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


Pssm-ID: 273463  Cd Length: 299  Bit Score: 372.00  E-value: 8.15e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    7 LLQALGNTPLVGLQRLSPRWDDgrdgphvRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISL 86
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDA-------RVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYCGTG 166
Cdd:TIGR01136  74 AMVAAARGYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  167 PELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGE-------GVYALRNMDEGFVPELYDPEILTA 238
Cdd:TIGR01136 154 PEIWRDTDgRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPvlsggepGPHKIQGIGAGFIPKILDLSLIDE 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489502016  239 RYSVGAVDAVRRTRELVHTEGIFAGISTGAVLHaaLGVGAGALAAGERADIALVVADAGWKYLSTGAY 306
Cdd:TIGR01136 234 VITVSDEDAIETARRLAREEGILVGISSGAAVA--AALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 1-303 5.84e-119

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: 344.34  E-value: 5.84e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   1 MTRYDSLLQALGNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSG 80
Cdd:COG0031    1 MRIYDSILELIGNTPLVRLNRLSP-------GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  81 NTGISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDS 160
Cdd:COG0031   74 NTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 161 HYCGTGPELLADLP-EITHFVAglgttgtlmgtgRFLREHVANVKIVAAEPRYG-------EGVYALRNMDEGFVPELYD 232
Cdd:COG0031  154 HYETTGPEIWEQTDgKVDAFVAgvgtggtitgvgRYLKERNPDIKIVAVEPEGSpllsggePGPHKIEGIGAGFVPKILD 233

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502016 233 PEILTARYSVGAVDAVRRTRELVHTEGIFAGISTGAVLHaalGVGAGALAAGERADIALVVADAGWKYLST 303
Cdd:COG0031  234 PSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVA---AALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 12-302 1.80e-109

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: 319.84  E-value: 1.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISLAMAAR 91
Cdd:cd01561    1 GNTPLVRLNRLSP-------GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  92 LKGYRLICVMPENTSVERRQLLELYGAQIIF--SAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYCGTGPEL 169
Cdd:cd01561   74 AKGYRFIIVMPETMSEEKRKLLRALGAEVILtpEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 170 LADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYG-------EGVYALRNMDEGFVPELYDPEILTARYS 241
Cdd:cd01561  154 WEQLDgKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSvlfsggpPGPHKIEGIGAGFIPENLDRSLIDEVVR 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502016 242 VGAVDAVRRTRELVHTEGIFAGISTGAVLHaalGVGAGALAAGERADIALVVADAGWKYLS 302
Cdd:cd01561  234 VSDEEAFAMARRLAREEGLLVGGSSGAAVA---AALKLAKRLGPGKTIVTILPDSGERYLS 291
cysM PRK11761
cysteine synthase CysM;
4-306 1.62e-83

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 254.03  E-value: 1.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   4 YDSLLQALGNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTG 83
Cdd:PRK11761   3 YPTLEDTIGNTPLVKLQRLPP-------DRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  84 ISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAAtNPSWVMLYQYGNPANTDSHYC 163
Cdd:PRK11761  76 IALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQA-EGEGKVLDQFANPDNPLAHYE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 164 GTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGEGVYALRNMDEGFVPELYDPEILTARYSV 242
Cdd:PRK11761 155 TTGPEIWRQTEgRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEEGSSIPGIRRWPEEYLPKIFDASRVDRVLDV 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502016 243 GAVDAVRRTRELVHTEGIFAGISTGAVLHaalgVGAGALAAGERADIALVVADAGWKYLSTGAY 306
Cdd:PRK11761 235 SQQEAENTMRRLAREEGIFCGVSSGGAVA----AALRIARENPNAVIVAIICDRGDRYLSTGVF 294
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 11-303 3.95e-79

cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273465  Cd Length: 298  Bit Score: 243.04  E-value: 3.95e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   11 LGNTPLVGLQRLsprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISLAMAA 90
Cdd:TIGR01139   5 IGNTPLVRLNRI--------EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   91 RLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNP-SWVMLYQYGNPANTDSHYCGTGPEL 169
Cdd:TIGR01139  77 AARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPnSYFMLQQFENPANPEIHRKTTGPEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  170 LADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEP------RYGE-GVYALRNMDEGFVPELYDPEILTARYS 241
Cdd:TIGR01139 157 WRDTDgKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPaespvlSGGKpGPHKIQGIGAGFIPKNLNRSVIDEVIT 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502016  242 VGAVDAVRRTRELVHTEGIFAGISTGAVLhaaLGVGAGALAAGERADIALVVADAGWKYLST 303
Cdd:TIGR01139 237 VSDEEAIETARRLAAEEGILVGISSGAAV---AAALKLAKRPEPDKLIVVILPSTGERYLST 295
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 6-306 1.71e-71

cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]


Pssm-ID: 130208 [Multi-domain]  Cd Length: 290  Bit Score: 223.25  E-value: 1.71e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    6 SLLQALGNTPLVGLQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGIS 85
Cdd:TIGR01138   1 TIEQTVGNTPLVRLQRMGPENG-------SEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   86 LAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVmLYQYGNPANTDSHYCGT 165
Cdd:TIGR01138  74 LAMIAALKGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKL-LDQFNNPDNPYAHYTST 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  166 GPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGEGVYALRNMDEGFVPELYDPEILTARYSVGA 244
Cdd:TIGR01138 153 GPEIWQQTGgRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPEEGSSIPGIRRWPTEYLPGIFDASLVDRVLDIHQ 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489502016  245 VDAVRRTRELVHTEGIFAGISTGAVLhaalGVGAGALAAGERADIALVVADAGWKYLSTGAY 306
Cdd:TIGR01138 233 RDAENTMRELAVREGIFCGVSSGGAV----AAALRLARELPDAVVVAIICDRGDRYLSTGVF 290
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
 7-303 4.85e-66

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


Pssm-ID: 274872 [Multi-domain]  Cd Length: 304  Bit Score: 209.75  E-value: 4.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    7 LLQALGNTPLVGLQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISL 86
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDAP-------FRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIAL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQIIF---SAAEGGS-NTAVATAKELAATNPSWVMLYQYGNPANTDSHY 162
Cdd:TIGR03945  74 AMICAYKGLRFICVVDPNISPQNLKLLRAYGAEVEKvtePDETGGYlGTRIARVRELLASIPDAYWPNQYANPDNPRAHY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  163 CGTGPELLADLPEITHFVAGLGTTGTLMGTGRFLREHVANVKIVA------------AEPRYGEGVYALRnmdegfVPEL 230
Cdd:TIGR03945 154 HGTGREIARAFPTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAvdavgsvifggpPGRRHIPGLGASV------VPEL 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502016  231 YDPEILTARYSVGAVDAVRRTRELVHTEGIFAGISTGAVLhaaLGVGAGALAAGERADIALVVADAGWKYLST 303
Cdd:TIGR03945 228 LDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVV---AAIKRLLPRIPEGSTVVAILPDRGERYLDT 297
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 5-302 1.71e-61

cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]


Pssm-ID: 273464 [Multi-domain]  Cd Length: 455  Bit Score: 202.34  E-value: 1.71e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    5 DSLLQALGNTPLVGLQRLSPrwddgrdGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGI 84
Cdd:TIGR01137   3 DNILDLIGNTPLVRLNKVSK-------GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   85 SLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIF---SAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSH 161
Cdd:TIGR01137  76 GLALVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRtptAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  162 YCGTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEP------------RYGEGVYALRNMDEGFVP 228
Cdd:TIGR01137 156 YDTTGPEILEQCEgKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPegsilaqpeelnQTGRTPYKVEGIGYDFIP 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489502016  229 ELYDPEILTARYSVGAVDAVRRTRELVHTEGIFAGISTGAVLHAALGVGAGALAAGERadIALVVADAGWKYLS 302
Cdd:TIGR01137 236 TVLDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQR--CVVLLPDSIRNYMT 307
PRK10717 PRK10717
cysteine synthase A; Provisional
 1-268 1.04e-58

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 191.61  E-value: 1.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   1 MTRYDSLLQALGNTPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSG 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAS-------EATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  81 NTGISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSN------TAVATAKELAATNPS-WVMLYQYG 153
Cdd:PRK10717  74 NTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAAPYANpnnyvkGAGRLAEELVASEPNgAIWANQFD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 154 NPANTDSHYCGTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPrYGEGVYA-LRNMDE------- 224
Cdd:PRK10717 154 NPANREAHYETTGPEIWEQTDgKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADP-TGSALYSyYKTGELkaegssi 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489502016 225 ------GFVPE-LYDPEILTArYSVGAVDAVRRTRELVHTEGIFAGISTGA 268
Cdd:PRK10717 233 tegigqGRITAnLEGAPIDDA-IRIPDEEALSTAYRLLEEEGLCLGGSSGI 282
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 7-271 6.05e-58

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: 188.67  E-value: 6.05e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016    7 LLQALGNTPLVGLQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIEQAEAdglLRPGATILEPTSGNTGISL 86
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELG-------VDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRAL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSaaEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDShYCGTG 166
Cdd:pfam00291  71 AAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLV--GGDYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  167 PELLADL-PEITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGEGVYALRN----------------MDEGFVPE 229
Cdd:pfam00291 148 LEILEQLgGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAagrpvpvpvadtiadgLGVGDEPG 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489502016  230 LYDPEILTAR----YSVGAVDAVRRTRELVHTEGIFAGISTGAVLH 271
Cdd:pfam00291 228 ALALDLLDEYvgevVTVSDEEALEAMRLLARREGIVVEPSSAAALA 273
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 5-268 4.04e-56

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 186.32  E-value: 4.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   5 DSLLQALGNTPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATIL-EPTSGNTG 83
Cdd:PLN02556  51 TDASQLIGKTPLVYLNKVT-------EGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLiEPTSGNMG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  84 ISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYC 163
Cdd:PLN02556 124 ISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFE 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 164 GTGPELLAD-LPEITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGE-------GVYALRNMDEGFVPELYDPEI 235
Cdd:PLN02556 204 TTGPEIWEDtLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNvlnggkpGPHHITGNGVGFKPDILDMDV 283

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489502016 236 LTARYSVGAVDAVRRTRELVHTEGIFAGISTGA 268
Cdd:PLN02556 284 MEKVLEVSSEDAVNMARELALKEGLMVGISSGA 316
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 14-271 2.87e-55

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: 180.02  E-value: 2.87e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  14 TPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLrPGATILEPTSGNTGISLAMAARLK 93
Cdd:cd00640    1 TPLVRLKRLS-------KLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  94 GYRLICVMPENTSVERRQLLELYGAQIIfsAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYcGTGPELLADL 173
Cdd:cd00640   73 GLKCTIVMPEGASPEKVAQMRALGAEVV--LVPGDFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 174 PE--ITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYgegvyalrnmdegfvpelydpeiltarYSVGAVDAVRRT 251
Cdd:cd00640  150 GGqkPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPEV---------------------------VTVSDEEALEAI 202

                        250       260
                 ....*....|....*....|
gi 489502016 252 RELVHTEGIFAGISTGAVLH 271
Cdd:cd00640  203 RLLAREEGILVEPSSAAALA 222
PLN02565 PLN02565
cysteine synthase
 11-268 9.41e-53

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 175.88  E-value: 9.41e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  11 LGNTPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATIL-EPTSGNTGISLAMA 89
Cdd:PLN02565  13 IGKTPLVYLNNVV-------DGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLiEPTSGNTGIGLAFM 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  90 ARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYCGTGPEL 169
Cdd:PLN02565  86 AAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 170 L-ADLPEITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGE-------GVYALRNMDEGFVPELYDPEILTARYS 241
Cdd:PLN02565 166 WkGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAvlsggkpGPHKIQGIGAGFIPGVLDVDLLDEVVQ 245

                        250       260
                 ....*....|....*....|....*..
gi 489502016 242 VGAVDAVRRTRELVHTEGIFAGISTGA 268
Cdd:PLN02565 246 VSSDEAIETAKLLALKEGLLVGISSGA 272
PLN00011 PLN00011
cysteine synthase
 5-314 2.55e-48

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 164.41  E-value: 2.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   5 DSLLQALGNTPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPG-ATILEPTSGNTG 83
Cdd:PLN00011   9 NDVTELIGNTPMVYLNNIV-------DGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  84 ISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYC 163
Cdd:PLN00011  82 IGLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 164 GTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRY------GE-GVYALRNMDEGFVPELYDPEI 235
Cdd:PLN00011 162 TTGPEIWRDSAgKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVEsavlsgGQpGPHLIQGIGSGIIPFNLDLTI 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 236 LTARYSVGAVDAVRRTRELVHTEGIFAGISTGAvlhaALGVGAGALAAGERAD--IALVVADAGWKYLSTGAYAGSLDDA 313
Cdd:PLN00011 242 VDEIIQVTGEEAIETAKLLALKEGLLVGISSGA----AAAAALKVAKRPENAGklIVVIFPSGGERYLSTKLFESVRYEA 317


                 .
gi 489502016 314 E 314
Cdd:PLN00011 318 E 318
PLN03013 PLN03013
cysteine synthase
 5-268 6.56e-48

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 166.11  E-value: 6.56e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   5 DSLLQALGNTPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATIL-EPTSGNTG 83
Cdd:PLN03013 115 DNVSQLIGKTPMVYLNSIA-------KGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLvEPTSGNTG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  84 ISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGSNTAVATAKELAATNPSWVMLYQYGNPANTDSHYC 163
Cdd:PLN03013 188 IGLAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 164 GTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVKIVAAEPRYGE-------GVYALRNMDEGFVPELYDPEI 235
Cdd:PLN03013 268 TTGPEIWDDTKgKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDilsggkpGPHKIQGIGAGFIPKNLDQKI 347

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489502016 236 LTARYSVGAVDAVRRTRELVHTEGIFAGISTGA 268
Cdd:PLN03013 348 MDEVIAISSEEAIETAKQLALKEGLMVGISSGA 380
PLN02356 PLN02356
phosphateglycerate kinase
 7-266 5.30e-22

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 95.44  E-value: 5.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   7 LLQALGNTPLVGLQRLSprwddgrDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATILEPTSGNTGISL 86
Cdd:PLN02356  47 LIDAIGNTPLIRINSLS-------EATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  87 AMAARLKGYRLICVMPENTSVERRQLLELYGAQI---------------------IFSAAEGGSN---TAVATAKELAAT 142
Cdd:PLN02356 120 ATVAPAYGCKCHVVIPDDVAIEKSQILEALGATVervrpvsithkdhyvniarrrALEANELASKrrkGSETDGIHLEKT 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 143 N---------PSWVMLY--------QYGNPANTDSHYCGTGPELLADLP-EITHFVAGLGTTGTLMGTGRFLREHVANVK 204
Cdd:PLN02356 200 NgciseeekeNSLFSSSctggffadQFENLANFRAHYEGTGPEIWEQTQgNLDAFVAAAGTGGTLAGVSRFLQEKNPNIK 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 205 IVAAEP-------RYGEGVYALRNMDEGfvPELYDP----------EILTARYSVGAVD---------AVRRTRELVHTE 258
Cdd:PLN02356 280 CFLIDPpgsglfnKVTRGVMYTREEAEG--RRLKNPfdtitegigiNRLTQNFLMAKLDgafrgtdkeAVEMSRYLLKND 357


                 ....*...
gi 489502016 259 GIFAGIST 266
Cdd:PLN02356 358 GLFVGSSS 365
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 12-141 2.69e-14

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: 72.93  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGLQRLSPRWDDgrdgphvRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLrpgaTILEPTSGNTGISLAMAAR 91
Cdd:COG0498   65 GGTPLVKAPRLADELGK-------NLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAA 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489502016  92 LKGYRLICVMPEN-TSVERRQLLELYGAQIIfsAAEGGSNTAVATAKELAA 141
Cdd:COG0498  134 RAGIEVFVFVPEGkVSPGQLAQMLTYGAHVI--AVDGNFDDAQRLVKELAA 182
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 12-144 8.35e-14

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: 70.70  E-value: 8.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGLQRLSPRWDDGRdgphvrLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLlrpgATILEPTSGNTGISLAMAAR 91
Cdd:cd01563   21 GNTPLVRAPRLGERLGGKN------LYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAA 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489502016  92 LKGYRLICVMPENTSVERRQLLELYGAQIIfsAAEGGSNTAVATAKELAATNP 144
Cdd:cd01563   91 RAGIKCVVFLPAGKALGKLAQALAYGATVL--AVEGNFDDALRLVRELAEENW 141
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 14-181 3.24e-12

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: 66.21  E-value: 3.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  14 TPLVGLQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADgllRPGATILEPTSGNTGISLAMAARLK 93
Cdd:COG1171   25 TPLLRSPTLSERLG-------AEVYLKLENLQPTGSFKLRGAYNALASLSEE---ERARGVVAASAGNHAQGVAYAARLL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  94 GYRLICVMPENTSVERRQLLELYGAQIIFSaaegGSNT--AVATAKELAA---------TNPSWVMLYQygnpantdshy 162
Cdd:COG1171   95 GIPATIVMPETAPAVKVAATRAYGAEVVLH----GDTYddAEAAAAELAEeegatfvhpFDDPDVIAGQ----------- 159

                        170       180
                 ....*....|....*....|
gi 489502016 163 cGT-GPELLADLPEITHFVA 181
Cdd:COG1171  160 -GTiALEILEQLPDLDAVFV 178
PRK06381 PRK06381
threonine synthase; Validated
 36-162 8.30e-11

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 62.03  E-value: 8.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  36 RLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLlrpgATILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLEL 115
Cdd:PRK06381  32 KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEK 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489502016 116 YGAQIIFsaAEGGSNTAVATAKELAATNPswvmLYQyGNPANTDSHY 162
Cdd:PRK06381 108 YGAEIIY--VDGKYEEAVERSRKFAKENG----IYD-ANPGSVNSVV 147
PRK08197 PRK08197
threonine synthase; Validated
 12-122 4.30e-10

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 60.01  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGLQRLSPRWDDGRdgphvrLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLlrpgATILEPTSGNTGISLAMAAR 91
Cdd:PRK08197  78 GMTPLLPLPRLGKALGIGR------LWVKDEGLNPTGSFKARGLAVGVSRAKELGV----KHLAMPTNGNAGAAWAAYAA 147

                         90       100       110
                 ....*....|....*....|....*....|.
gi 489502016  92 LKGYRLICVMPENTSVERRQLLELYGAQIIF 122
Cdd:PRK08197 148 RAGIRATIFMPADAPEITRLECALAGAELYL 178
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 10-146 5.56e-09

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: 56.62  E-value: 5.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   10 ALGNTPLVGLQRLSPRWddGRDgphvRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLlrpgATILEPTSGNTGISLAMA 89
Cdd:TIGR00260  19 GEGVTPLFRAPALAANV--GIK----NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAY 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489502016   90 ARLKGYRLICVMPENtSVERRQLLE--LYGAQIIfsAAEGGSNTAVATAKELAATNPSW 146
Cdd:TIGR00260  89 AGKAGLKVVVLYPAG-KISLGKLAQalGYNAEVV--AIDGNFDDAQRLVKQLFEDKPAL 144
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 14-143 6.34e-09

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: 56.34  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  14 TPLVGLQRLSPRwddgrdgPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPgatILEPTSGNTGISLAMAARLK 93
Cdd:cd01562   18 TPLLTSPTLSEL-------LGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLL 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489502016  94 GYRLICVMPENTSVERRQLLELYGAQIIFSaaEGGSNTAVATAKELAATN 143
Cdd:cd01562   88 GIPATIVMPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEE 135
PRK06450 PRK06450
threonine synthase; Validated
 38-121 1.97e-07

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 51.66  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  38 WAKLEDRNPTGSIKDRPAVRMIEQAEADGLlrpgATILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLELYG 117
Cdd:PRK06450  68 WFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYG 143


                 ....
gi 489502016 118 AQII 121
Cdd:PRK06450 144 AEVV 147
PLN02970 PLN02970
serine racemase
 35-210 2.18e-07

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 51.60  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  35 VRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRpgaTILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLE 114
Cdd:PLN02970  42 RSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEK---GVVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016 115 LYGAQIIFSAAEGGSNTAVAtAKELAATNPSWVMLYQYGNPAntdshyCGTGP---ELLADLPEITHFVAGLGTTGTLMG 191
Cdd:PLN02970 119 RYGGIITWCEPTVESREAVA-ARVQQETGAVLIHPYNDGRVI------SGQGTialEFLEQVPELDVIIVPISGGGLISG 191

                        170
                 ....*....|....*....
gi 489502016 192 TGRFLREHVANVKIVAAEP 210
Cdd:PLN02970 192 IALAAKAIKPSIKIIAAEP 210
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 13-155 5.23e-07

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: 50.38  E-value: 5.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  13 NTPLVGLQRLSPRwddgrDGPHVrlWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPgATILEPTSGNTGISLAMAARL 92
Cdd:cd06448    1 KTPLIESTALSKT-----AGCNV--FLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARK 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502016  93 KGYRLICVMPENTSVERRQLLELYGAQIIFSAAEGGsNTAVATAKELAATNPSWVMLYQYGNP 155
Cdd:cd06448   73 LGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWW-EADNYLREELAENDPGPVYVHPFDDP 134
PRK06608 PRK06608
serine/threonine dehydratase;
40-166 7.83e-06

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 47.07  E-value: 7.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  40 KLEDRNPTGSIKDRPAVRMIEQAEADGllRPGATILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQ 119
Cdd:PRK06608  43 KVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGE 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489502016 120 IIFSAAEGGSNTAVATAKElaatnPSWVmlyqYGNPANTDSHYCGTG 166
Cdd:PRK06608 121 VILTNTRQEAEEKAKEDEE-----QGFY----YIHPSDSDSTIAGAG 158
PRK05638 PRK05638
threonine synthase; Validated
 12-143 1.75e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 45.96  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGlQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIeqaeADGLLRPGATILEPTSGNTGISLAMAAR 91
Cdd:PRK05638  65 GGTPLIR-ARISEKLG-------ENVYIKDETRNPTGSFRDRLATVAV----SYGLPYAANGFIVASDGNAAASVAAYSA 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489502016  92 LKGYRLICVMPENTSVERRQLLELYGAQIIFSaaEGGSNTAVATAKELAATN 143
Cdd:PRK05638 133 RAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARLN 182
PRK06110 PRK06110
threonine dehydratase;
38-141 3.63e-05

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 44.99  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  38 WAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGatILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLELYG 117
Cdd:PRK06110  39 WVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALG 116

                         90       100
                 ....*....|....*....|....*.
gi 489502016 118 AQIIfsaaEGGSN--TAVATAKELAA 141
Cdd:PRK06110 117 AELI----EHGEDfqAAREEAARLAA 138
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 78-148 4.85e-05

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 44.48  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  78 TSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIFSaaEGGSNTAVATAKELAATN-------------- 143
Cdd:PRK08206 123 TDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT--DGNYDDSVRLAAQEAQENgwvvvqdtawegye 200


                 ....*..
gi 489502016 144 --PSWVM 148
Cdd:PRK08206 201 eiPTWIM 207
PRK08329 PRK08329
threonine synthase; Validated
 35-122 1.12e-04

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 43.28  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  35 VRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLlrpgATILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLE 114
Cdd:PRK08329  72 IKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLS 147


                 ....*...
gi 489502016 115 LYGAQIIF 122
Cdd:PRK08329 148 RLGAELHF 155
ilvA_1Cterm TIGR01127
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ...
 32-225 2.05e-04

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: 42.81  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016   32 GPHVRLwaKLEDRNPTGSIKDRPAVRMIEQAEADGLLRpgaTILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQ 111
Cdd:TIGR01127  14 GSEVYL--KLENLQKTGSFKIRGALNKIANLSEDQRQR---GVVAASAGNHAQGVAYAAKKFGIKAVIVMPESAPPSKVK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  112 LLELYGAQIIFSAAEggSNTAVATAKELA---------ATNPSWVMLYQygnpantdshycGT-GPELLADLPEITHFVA 181
Cdd:TIGR01127  89 ATKSYGAEVILHGDD--YDEAYAFATSLAeeegrvfvhPFDDEFVMAGQ------------GTiGLEIMEDIPDVDTVIV 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489502016  182 GLGTTGTLMGTGRFLREHVANVKIVAAEPRYGEGVYAlrNMDEG 225
Cdd:TIGR01127 155 PVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYE--SLREG 196
PLN02569 PLN02569
threonine synthase
 12-105 2.33e-04

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 42.49  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  12 GNTPLVGLQRLSPRWDDGRDgphvrLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLL-RPGATILEPTSGNTGISLAMAA 90
Cdd:PLN02569 132 GNSNLFWAERLGKEFLGMND-----LWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYC 206

                         90
                 ....*....|....*
gi 489502016  91 RLKGYRLICVMPENT 105
Cdd:PLN02569 207 AAAGIPSIVFLPADK 221
eutB PRK07476
threonine dehydratase; Provisional
 14-112 2.54e-04

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 42.26  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  14 TPLVGLQRLSPRWDdgrdgphVRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRPGATIlepTSGNTGISLAMAARLK 93
Cdd:PRK07476  20 TPLVASASLSARAG-------VPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTA---STGNHGRALAYAARAL 89

                         90       100
                 ....*....|....*....|...
gi 489502016  94 GYR-LICV---MPENTSVERRQL 112
Cdd:PRK07476  90 GIRaTICMsrlVPANKVDAIRAL 112
PRK06815 PRK06815
threonine/serine dehydratase;
36-122 4.72e-04

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 41.22  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  36 RLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRpgaTILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLEL 115
Cdd:PRK06815  36 EVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQ---GVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRA 112


                 ....*..
gi 489502016 116 YGAQIIF 122
Cdd:PRK06815 113 LGAEVRL 119
PRK08246 PRK08246
serine/threonine dehydratase;
18-120 1.66e-03

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 39.55  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  18 GLQRLSPRWD-DGRDGPHVRLWAKLEDRNPTGSIKDRPAVRMIEQAEAdgllrPGATILEPTSGNTGISLAMAARLKGYR 96
Cdd:PRK08246  19 PHIRRTPVLEaDGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVP 93

                         90       100
                 ....*....|....*....|....
gi 489502016  97 LICVMPENTSVERRQLLELYGAQI 120
Cdd:PRK08246  94 ATVFVPETAPPAKVARLRALGAEV 117
PRK12483 PRK12483
threonine dehydratase; Reviewed
 14-105 2.58e-03

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 39.40  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  14 TPLVGLQRLSPRWDDgrdgphvRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRpgaTILEPTSGNTGISLAMAARLK 93
Cdd:PRK12483  38 TPLQRAPNLSARLGN-------QVLLKREDLQPVFSFKIRGAYNKMARLPAEQLAR---GVITASAGNHAQGVALAAARL 107

                         90
                 ....*....|..
gi 489502016  94 GYRLICVMPENT 105
Cdd:PRK12483 108 GVKAVIVMPRTT 119
PLN02550 PLN02550
threonine dehydratase
 35-121 4.09e-03

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 38.75  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  35 VRLWAKLEDRNPTGSIKDRPAVRMIEQAEADGLLRpgaTILEPTSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLE 114
Cdd:PLN02550 124 VKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDK---GVICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVE 200


                 ....*..
gi 489502016 115 LYGAQII 121
Cdd:PLN02550 201 RLGATVV 207
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 55-150 5.26e-03

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 37.97  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502016  55 AVRMIEQAEAdglLRPGATILEpTSGNTGISLAMA--ARLKGYRLICVM--PENTSVERRQLLELyGAQIIFSAAEggsN 130
Cdd:cd08290  134 AYRLLEDFVK---LQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVrdRPDLEELKERLKAL-GADHVLTEEE---L 205

                         90       100
                 ....*....|....*....|
gi 489502016 131 TAVATAKELAATNPSWVMLY 150
Cdd:cd08290  206 RSLLATELLKSAPGGRPKLA 225
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
78-122 8.25e-03

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 37.31  E-value: 8.25e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489502016  78 TSGNTGISLAMAARLKGYRLICVMPENTSVERRQLLELYGAQIIF 122
Cdd:PRK07048  79 SSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVT 123
 
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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