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Conserved domains on  [gi|15595596|ref|NP_249090|]
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cystathionine beta-synthase [Pseudomonas aeruginosa PAO1]

Protein Classification

CBS_like and CBS_pair_CBS domain-containing protein( domain architecture ID 12773407)

CBS_like and CBS_pair_CBS domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 9-311 3.79e-157

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: 446.80  E-value: 3.79e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   9 VLDLIGNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAK 87
Cdd:COG0031   7 ILELIGNTPLVRLNRLSPGPgAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  88 GYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDvgkGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTGPELW 167
Cdd:COG0031  87 GYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIW 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 168 AQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADLSSV 247
Cdd:COG0031 164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLL----SG--GEPGPHKIEGIGAGFVPKILDPSLI 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595596 248 RHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLSK 311
Cdd:COG0031 238 DEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 334-451 5.50e-42

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


:

Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 144.98  E-value: 5.50e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 334 DIIARRFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDAVSSAMNAAPETL 412
Cdd:cd04608   1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDeDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15595596 413 APGASLAQLQAVLDRGLVAIVADASG-FHGLITRFDLLNH 451
Cdd:cd04608  81 DLDTPLGALSRILERDHFALVVDGQGkVLGIVTRIDLLNY 120
 
Name Accession Description Interval E-value
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 9-311 3.79e-157

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: 446.80  E-value: 3.79e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   9 VLDLIGNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAK 87
Cdd:COG0031   7 ILELIGNTPLVRLNRLSPGPgAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  88 GYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDvgkGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTGPELW 167
Cdd:COG0031  87 GYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIW 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 168 AQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADLSSV 247
Cdd:COG0031 164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLL----SG--GEPGPHKIEGIGAGFVPKILDPSLI 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595596 248 RHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLSK 311
Cdd:COG0031 238 DEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 14-310 1.73e-137

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: 396.50  E-value: 1.73e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  14 GNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAKGYRVV 92
Cdd:cd01561   1 GNTPLVRLNRLSPGTgAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  93 LVVPDKMSTEKVLHLRAMGAEVHITRSDvGKGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTGPELWAQTGH 172
Cdd:cd01561  81 IVMPETMSEEKRKLLRALGAEVILTPEA-EADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 173 DLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADLSSVRHAYS 252
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLF----SG--GPPGPHKIEGIGAGFIPENLDRSLIDEVVR 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595596 253 ISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLS 310
Cdd:cd01561 234 VSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 5-452 2.85e-133

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: 391.86  E-value: 2.85e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     5 SRPAVLDLIGNTPLVRVTRFDTG-PCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALV 83
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGlKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    84 GRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTG 163
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   164 PELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAE-YSRSGTLGTPgsWAVEGIGEDFVPAIA 242
Cdd:TIGR01137 161 PEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQpEELNQTGRTP--YKVEGIGYDFIPTVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   243 DLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQ-KEPKRVVSFVCDTGTRYLSKIYNDQWMTDQ 321
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDElQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   322 GLL--QRKHYGDLRDIIARRFEEG--RVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPR 396
Cdd:TIGR01137 319 GFLddEDLTVKDVLWWHARVKDLHlpAPVTVHPTETVGDAIEILREYGFDQLPVVDeAGKVLGSVTLRELLSALFAGKAQ 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596   397 FRDAVSSAMNAAPETLAPGASLAQLQAVLDRGLVAIVADASGFHGLITRFDLLNHL 452
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKPIGVVTKIDLLSFL 454
PRK10717 PRK10717
cysteine synthase A; Provisional
 3-323 1.97e-121

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 357.25  E-value: 1.97e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    3 SDSRPAVLDLIGNTPLVRVTRF--DTGpCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGL 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAseATG-CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   81 ALVGRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSdVGKGHPEYYQDVAARLAQDI-----PGAFFADQFNNPANP 155
Cdd:PRK10717  80 ALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasepNGAIWANQFDNPANR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  156 LAHECGTGPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAEYSRSGTLGTPGSWAVEGIGE 235
Cdd:PRK10717 159 EAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  236 DFVPAIADLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLSKIYND 315
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNP 318


                 ....*...
gi 15595596  316 QWMTDQGL 323
Cdd:PRK10717 319 DFLREKGL 326
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 9-303 4.61e-80

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: 249.92  E-value: 4.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     9 VLDLIGNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERdgrLRPGGTIVEATAGNTGLGLALVGRAK 87
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELgVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    88 GYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGhpeyyQDVAARLAQDIPGAFFADQFNNPANPLAHEcGTGPELW 167
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEA-----VAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEIL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   168 AQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS-IMAEYSRSGTLGT--PGSWAVEGIGEDFVPAIADL 244
Cdd:pfam00291 152 EQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPvpVADTIADGLGVGDEPGALAL 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595596   245 SSVR----HAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAA-LRFCREQKEPKRVVSFVCD 303
Cdd:pfam00291 232 DLLDeyvgEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 334-451 5.50e-42

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 144.98  E-value: 5.50e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 334 DIIARRFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDAVSSAMNAAPETL 412
Cdd:cd04608   1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDeDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15595596 413 APGASLAQLQAVLDRGLVAIVADASG-FHGLITRFDLLNH 451
Cdd:cd04608  81 DLDTPLGALSRILERDHFALVVDGQGkVLGIVTRIDLLNY 120
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
333-457 8.23e-17

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 76.83  E-value: 8.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 333 RDIIARRfeegrVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDA------VSSAM 405
Cdd:COG3448   5 RDIMTRD-----VVTVSPDTTLREALELMREHGIRGLPVVDeDGRLVGIVTERDLLRALLPDRLDELEErlldlpVEDVM 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595596 406 NAAPETLAPGASLAQL-QAVLDRGLVAI-VADASG-FHGLITRFDLLNHLRRKLA 457
Cdd:COG3448  80 TRPVVTVTPDTPLEEAaELMLEHGIHRLpVVDDDGrLVGIVTRTDLLRALARLLE 134
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 345-387 8.98e-09

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 51.45  E-value: 8.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15595596   345 VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL 387
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDeDGKLVGIVTLKDLL 52
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 344-387 4.49e-07

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 46.35  E-value: 4.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 15595596    344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDIL 387
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDII 45
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
332-386 8.21e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 48.29  E-value: 8.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596  332 LRDIiarrfEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDI 386
Cdd:PRK14869  70 VRDL-----EIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDeEGKLLGLVSLSDL 120
 
Name Accession Description Interval E-value
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 9-311 3.79e-157

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: 446.80  E-value: 3.79e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   9 VLDLIGNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAK 87
Cdd:COG0031   7 ILELIGNTPLVRLNRLSPGPgAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAK 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  88 GYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDvgkGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTGPELW 167
Cdd:COG0031  87 GYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIW 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 168 AQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADLSSV 247
Cdd:COG0031 164 EQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLL----SG--GEPGPHKIEGIGAGFVPKILDPSLI 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595596 248 RHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLSK 311
Cdd:COG0031 238 DEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 14-310 1.73e-137

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: 396.50  E-value: 1.73e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  14 GNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAKGYRVV 92
Cdd:cd01561   1 GNTPLVRLNRLSPGTgAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  93 LVVPDKMSTEKVLHLRAMGAEVHITRSDvGKGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTGPELWAQTGH 172
Cdd:cd01561  81 IVMPETMSEEKRKLLRALGAEVILTPEA-EADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 173 DLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADLSSVRHAYS 252
Cdd:cd01561 160 KVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLF----SG--GPPGPHKIEGIGAGFIPENLDRSLIDEVVR 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595596 253 ISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLS 310
Cdd:cd01561 234 VSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 5-452 2.85e-133

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: 391.86  E-value: 2.85e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     5 SRPAVLDLIGNTPLVRVTRFDTG-PCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALV 83
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGlKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    84 GRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGHPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHECGTG 163
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   164 PELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAE-YSRSGTLGTPgsWAVEGIGEDFVPAIA 242
Cdd:TIGR01137 161 PEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQpEELNQTGRTP--YKVEGIGYDFIPTVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   243 DLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQ-KEPKRVVSFVCDTGTRYLSKIYNDQWMTDQ 321
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDElQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   322 GLL--QRKHYGDLRDIIARRFEEG--RVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPR 396
Cdd:TIGR01137 319 GFLddEDLTVKDVLWWHARVKDLHlpAPVTVHPTETVGDAIEILREYGFDQLPVVDeAGKVLGSVTLRELLSALFAGKAQ 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596   397 FRDAVSSAMNAAPETLAPGASLAQLQAVLDRGLVAIVADASGFHGLITRFDLLNHL 452
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKPIGVVTKIDLLSFL 454
PRK10717 PRK10717
cysteine synthase A; Provisional
 3-323 1.97e-121

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 357.25  E-value: 1.97e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    3 SDSRPAVLDLIGNTPLVRVTRF--DTGpCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGL 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRAseATG-CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   81 ALVGRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSdVGKGHPEYYQDVAARLAQDI-----PGAFFADQFNNPANP 155
Cdd:PRK10717  80 ALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasepNGAIWANQFDNPANR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  156 LAHECGTGPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAEYSRSGTLGTPGSWAVEGIGE 235
Cdd:PRK10717 159 EAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSYYKTGELKAEGSSITEGIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  236 DFVPAIADLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLSKIYND 315
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNP 318


                 ....*...
gi 15595596  316 QWMTDQGL 323
Cdd:PRK10717 319 DFLREKGL 326
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 9-310 8.01e-102

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: 305.74  E-value: 8.01e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     9 VLDLIGNTPLVRVTRFDTG-PCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAK 87
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    88 GYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVG-KGHpeyyQDVAARLAQDIPGAFFADQFNNPANPLAHECGTGPEL 166
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGmKGA----IDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   167 WAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPegsimaEYSRSGTLGTPGSWAVEGIGEDFVPAIADLSS 246
Cdd:TIGR01136 157 WRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP------AESPVLSGGEPGPHKIQGIGAGFIPKILDLSL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595596   247 VRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEP-KRVVSFVCDTGTRYLS 310
Cdd:TIGR01136 231 IDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLENAdKVIVAILPDTGERYLS 295
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 9-310 9.34e-101

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: 303.13  E-value: 9.34e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     9 VLDLIGNTPLVRVTRFDTGPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRAKG 88
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    89 YRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVG-KGHPEYYQDVAARlaqdIPGAFF-ADQFNNPANPLAHECGTGPEL 166
Cdd:TIGR01139  81 YKLILTMPETMSIERRKLLKAYGAELVLTPGAEGmKGAIAKAEEIAAS----TPNSYFmLQQFENPANPEIHRKTTGPEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   167 WAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADLSS 246
Cdd:TIGR01139 157 WRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVL----SG--GKPGPHKIQGIGAGFIPKNLNRSV 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595596   247 VRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLS 310
Cdd:TIGR01139 231 IDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
cysM PRK11761
cysteine synthase CysM;
7-310 2.24e-81

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 253.26  E-value: 2.24e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    7 PAVLDLIGNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGR 85
Cdd:PRK11761   4 PTLEDTIGNTPLVKLQRLPPDRgNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   86 AKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKghpEYYQDVAARLAQDIPGaFFADQFNNPANPLAHECGTGPE 165
Cdd:PRK11761  84 IKGYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGM---EGARDLALQMQAEGEG-KVLDQFANPDNPLAHYETTGPE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  166 LWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADP-EGSIMaeysrsgtlgtPG--SWAVEgigedFVPAIA 242
Cdd:PRK11761 160 IWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSSI-----------PGirRWPEE-----YLPKIF 223

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595596  243 DLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQkEPKRVVSFVCDTGTRYLS 310
Cdd:PRK11761 224 DASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLS 290
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 9-303 4.61e-80

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: 249.92  E-value: 4.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     9 VLDLIGNTPLVRVTRFDTGP-CTLYLKLESQNPGGSIKDRIGVAMIEAAERdgrLRPGGTIVEATAGNTGLGLALVGRAK 87
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELgVDVYLKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    88 GYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGhpeyyQDVAARLAQDIPGAFFADQFNNPANPLAHEcGTGPELW 167
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEA-----VAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEIL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   168 AQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS-IMAEYSRSGTLGT--PGSWAVEGIGEDFVPAIADL 244
Cdd:pfam00291 152 EQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPvpVADTIADGLGVGDEPGALAL 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595596   245 SSVR----HAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAA-LRFCREQKEPKRVVSFVCD 303
Cdd:pfam00291 232 DLLDeyvgEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 16-303 1.38e-73

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: 231.64  E-value: 1.38e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  16 TPLVRVTRF-DTGPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLrPGGTIVEATAGNTGLGLALVGRAKGYRVVLV 94
Cdd:cd00640   1 TPLVRLKRLsKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  95 VPDKMSTEKVLHLRAMGAEVHITRSDvgkghPEYYQDVAARLAQDIPGAFFADQFNNPANPLAHEcGTGPELWAQTGH-D 173
Cdd:cd00640  80 MPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 174 LDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEgsimaeysrsgtlgtpgswavegigedfvpaiadlssvrhAYSI 253
Cdd:cd00640 154 PDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------------------------------VVTV 193

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15595596 254 SDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCD 303
Cdd:cd00640 194 SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTG 243
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 9-310 2.74e-70

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: 224.79  E-value: 2.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     9 VLDLIGNTPLVRVTRF--DTGpCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALVGRA 86
Cdd:TIGR01138   2 IEQTVGNTPLVRLQRMgpENG-SEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    87 KGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKghpEYYQDVAARLAQDIPGAFFaDQFNNPANPLAHECGTGPEL 166
Cdd:TIGR01138  81 KGYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGM---EGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   167 WAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADP-EGSimaeysrsgtlgtpgswAVEGIG---EDFVPAIA 242
Cdd:TIGR01138 157 WQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPeEGS-----------------SIPGIRrwpTEYLPGIF 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595596   243 DLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQkEPKRVVSFVCDTGTRYLS 310
Cdd:TIGR01138 220 DASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLAREL-PDAVVVAIICDRGDRYLS 286
PLN02565 PLN02565
cysteine synthase
 9-312 9.63e-66

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 214.02  E-value: 9.63e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    9 VLDLIGNTPLVRVTRFDTGpCT--LYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTI-VEATAGNTGLGLALVGR 85
Cdd:PLN02565   9 VTELIGKTPLVYLNNVVDG-CVarIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   86 AKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVG-KGHPEYYQDVAARlaqdIPGAFFADQFNNPANPLAHECGTGP 164
Cdd:PLN02565  88 AKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGmKGAVQKAEEILAK----TPNSYILQQFENPANPKIHYETTGP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  165 ELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADP-EGSIMaeysrSGtlGTPGSWAVEGIGEDFVPAIAD 243
Cdd:PLN02565 164 EIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPvESAVL-----SG--GKPGPHKIQGIGAGFIPGVLD 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  244 LSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFC-REQKEPKRVVSFVCDTGTRYLSKI 312
Cdd:PLN02565 237 VDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAkRPENAGKLIVVIFPSFGERYLSSV 306
PLN00011 PLN00011
cysteine synthase
 9-310 2.50e-64

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 210.24  E-value: 2.50e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    9 VLDLIGNTPLVRVTRFDTGpCTLYL--KLESQNPGGSIKDRIGVAMIEAAERDGRLRPG-GTIVEATAGNTGLGLALVGR 85
Cdd:PLN00011  11 VTELIGNTPMVYLNNIVDG-CVARIaaKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   86 AKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVG-KGHPEYYQDVAARlaqdIPGAFFADQFNNPANPLAHECGTGP 164
Cdd:PLN00011  90 ARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGlKGMLEKAEEILSK----TPGGYIPQQFENPANPEIHYRTTGP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  165 ELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGSIMAeysrSGtlGTPGSWAVEGIGEDFVPAIADL 244
Cdd:PLN00011 166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVL----SG--GQPGPHLIQGIGSGIIPFNLDL 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595596  245 SSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFC-REQKEPKRVVSFVCDTGTRYLS 310
Cdd:PLN00011 240 TIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAkRPENAGKLIVVIFPSGGERYLS 306
PLN02356 PLN02356
phosphateglycerate kinase
 6-323 4.71e-62

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 207.54  E-value: 4.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    6 RPAVLDLIGNTPLVRVTRFD--TGpCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTIVEATAGNTGLGLALV 83
Cdd:PLN02356  44 RNGLIDAIGNTPLIRINSLSeaTG-CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   84 GRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSdVGKGHPEYYQDVAARLAQD------------------------ 139
Cdd:PLN02356 123 APAYGCKCHVVIPDDVAIEKSQILEALGATVERVRP-VSITHKDHYVNIARRRALEanelaskrrkgsetdgihlektng 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  140 ---------------IPGAFFADQFNNPANPLAHECGTGPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMV 204
Cdd:PLN02356 202 ciseeekenslfsssCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCF 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  205 LADPEGS---------IM--AEYSRSGTLGTPGSWAVEGIGEDFVPAIADLSSVRHAYSISDEESFAMARELLRVEGIPG 273
Cdd:PLN02356 282 LIDPPGSglfnkvtrgVMytREEAEGRRLKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFV 361

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 15595596  274 GSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLSKIYNDQWMTDQGL 323
Cdd:PLN02356 362 GSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
PLN03013 PLN03013
cysteine synthase
 9-310 6.81e-58

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 196.54  E-value: 6.81e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    9 VLDLIGNTPLVRVTRFDTG-PCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGTI-VEATAGNTGLGLALVGRA 86
Cdd:PLN03013 117 VSQLIGKTPMVYLNSIAKGcVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIAAS 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   87 KGYRVVLVVPDKMSTEKVLHLRAMGAEVHITrsDVGKGHPEYYQDvAARLAQDIPGAFFADQFNNPANPLAHECGTGPEL 166
Cdd:PLN03013 197 RGYRLILTMPASMSMERRVLLKAFGAELVLT--DPAKGMTGAVQK-AEEILKNTPDAYMLQQFDNPANPKIHYETTGPEI 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  167 WAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADP-EGSIMaeysrSGtlGTPGSWAVEGIGEDFVPAIADLS 245
Cdd:PLN03013 274 WDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPtESDIL-----SG--GKPGPHKIQGIGAGFIPKNLDQK 346

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595596  246 SVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQKEPKRVVSFVCDTGTRYLS 310
Cdd:PLN03013 347 IMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 6-316 1.59e-53

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 183.62  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    6 RPAVLDLIGNTPLVRVTRFDTGpCTLYL--KLESQNPGGSIKDRIGVAMIEAAERDGRLRPGGT-IVEATAGNTGLGLAL 82
Cdd:PLN02556  50 KTDASQLIGKTPLVYLNKVTEG-CGAYIaaKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAF 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   83 VGRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGHPeyyQDVAARLAQDIPGAFFADQFNNPANPLAHECGT 162
Cdd:PLN02556 129 MAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGT---VKKAYELLESTPDAFMLQQFSNPANTQVHFETT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  163 GPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADP-EGSIMaeysrSGtlGTPGSWAVEGIGEDFVPAI 241
Cdd:PLN02556 206 GPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPaESNVL-----NG--GKPGPHHITGNGVGFKPDI 278

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596  242 ADLSSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCRE-QKEPKRVVSFVCDTGTRYLSKIYNDQ 316
Cdd:PLN02556 279 LDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMpENKGKLIVTVHPSFGERYLSSVLFQE 354
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 334-451 5.50e-42

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 144.98  E-value: 5.50e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 334 DIIARRFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDAVSSAMNAAPETL 412
Cdd:cd04608   1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDeDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15595596 413 APGASLAQLQAVLDRGLVAIVADASG-FHGLITRFDLLNH 451
Cdd:cd04608  81 DLDTPLGALSRILERDHFALVVDGQGkVLGIVTRIDLLNY 120
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 14-305 2.44e-25

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: 105.75  E-value: 2.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  14 GNTPLVRVTRFDT--GPCTLYLKLESQNPGGSIKDR-IGVAMIEAAERDGRlrpggTIVEATAGNTGLGLALVGRAKGYR 90
Cdd:cd01563  21 GNTPLVRAPRLGErlGGKNLYVKDEGLNPTGSFKDRgMTVAVSKAKELGVK-----AVACASTGNTSASLAAYAARAGIK 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  91 VVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGHpeyyqDVAARLAQDIPGAffadqFNNPANPLAHEcGT---GPELW 167
Cdd:cd01563  96 CVVFLPAGKALGKLAQALAYGATVLAVEGNFDDAL-----RLVRELAEENWIY-----LSNSLNPYRLE-GQktiAFEIA 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 168 AQTGHDL-DAIVVGVGSSGTLTGLTRFFQkvqpELE----------MVLADPEG-SIMAEYSRSGT-------------- 221
Cdd:cd01563 165 EQLGWEVpDYVVVPVGNGGNITAIWKGFK----ELKelglidrlprMVGVQAEGaAPIVRAFKEGKddiepvenpetiat 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 222 ---LGTPGSW--AVEGIGEdfvpaiadlsSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFCREQ--KEP 294
Cdd:cd01563 241 airIGNPASGpkALRAVRE----------SGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGiiDKG 310

                       330
                ....*....|.
gi 15595596 295 KRVVSFVCDTG 305
Cdd:cd01563 311 ERVVVVLTGHG 321
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 14-302 2.27e-19

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: 89.49  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  14 GNTPLVRVTRF-DTGPCTLYLKLESQNPGGSIKDR---IGVAMieAAERDGRlrpggTIVEATAGNTGLGLALVGRAKGY 89
Cdd:COG0498  65 GGTPLVKAPRLaDELGKNLYVKEEGHNPTGSFKDRamqVAVSL--ALERGAK-----TIVCASSGNGSAALAAYAARAGI 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  90 RVVLVVP-DKMSTEKVLHLRAMGAEVHI---TRSDVgkghpeyyQDVAARLAQDiPGAFFAdqfnNPANPLAHEcGT--- 162
Cdd:COG0498 138 EVFVFVPeGKVSPGQLAQMLTYGAHVIAvdgNFDDA--------QRLVKELAAD-EGLYAV----NSINPARLE-GQkty 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 163 GPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQ--------PELEMVLADPEGSIMAEYSRsgtlgtpGSWAVEGIG 234
Cdd:COG0498 204 AFEIAEQLGRVPDWVVVPTGNGGNILAGYKAFKELKelglidrlPRLIAVQATGCNPILTAFET-------GRDEYEPER 276

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 235 EDFV-PAIADLSSVR-------------HAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALRFcREQKEPKRVVSF 300
Cdd:COG0498 277 PETIaPSMDIGNPSNgeralfalresggTAVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKL-REEGEIDPDEPV 355


                ..
gi 15595596 301 VC 302
Cdd:COG0498 356 VV 357
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 16-302 1.62e-17

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: 83.16  E-value: 1.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  16 TPLVRVTRFD--TGpCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRpggTIVEATAGNTGLGLALVGRAKGYRVVL 93
Cdd:COG1171  25 TPLLRSPTLSerLG-AEVYLKLENLQPTGSFKLRGAYNALASLSEEERAR---GVVAASAGNHAQGVAYAARLLGIPATI 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  94 VVPDKMSTEKVLHLRAMGAEVHItrsdvgkgHPEYYQD---VAARLAQDiPGAFFADQFNNPAnpLAHECGT-GPELWAQ 169
Cdd:COG1171 101 VMPETAPAVKVAATRAYGAEVVL--------HGDTYDDaeaAAAELAEE-EGATFVHPFDDPD--VIAGQGTiALEILEQ 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 170 TGhDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS-IMAEYSRSG---TLGTPGSWAvEGIGedfVPAIADLS 245
Cdd:COG1171 170 LP-DLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGAaAMYRSLAAGepvTLPGVDTIA-DGLA---VGRPGELT 244

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596 246 ------SVRHAYSISDEESFAMARELLRVEGI---PGGSSTgtllAAALRFCREQKEPKRVVSFVC 302
Cdd:COG1171 245 feilrdLVDDIVTVSEDEIAAAMRLLLERTKIvvePAGAAA----LAALLAGKERLKGKRVVVVLS 306
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 16-302 4.30e-17

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: 81.76  E-value: 4.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  16 TPLVRVTRFD--TGpCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPggtIVEATAGNTGLGLALVGRAKGYRVVL 93
Cdd:cd01562  18 TPLLTSPTLSelLG-AEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPATI 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  94 VVPDKMSTEKVLHLRAMGAEVHItrsdvgkgHPEYYQD---VAARLAQDiPGAFFADQFNNPANPLAHecGT-GPELWAQ 169
Cdd:cd01562  94 VMPETAPAAKVDATRAYGAEVVL--------YGEDFDEaeaKARELAEE-EGLTFIHPFDDPDVIAGQ--GTiGLEILEQ 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 170 TGhDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS-IMAEYSRSG---TLGTPGSWA----VEGIGEDFVPAI 241
Cdd:cd01562 163 VP-DLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGApAMAQSLAAGkpvTLPEVDTIAdglaVKRPGELTFEII 241

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596 242 ADLssVRHAYSISDEES-----FAMARELLRVEGipggssTGTLLAAALRFCREQKEPKRVVSFVC 302
Cdd:cd01562 242 RKL--VDDVVTVSEDEIaaamlLLFEREKLVAEP------AGALALAALLSGKLDLKGKKVVVVLS 299
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
333-457 8.23e-17

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 76.83  E-value: 8.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 333 RDIIARRfeegrVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDA------VSSAM 405
Cdd:COG3448   5 RDIMTRD-----VVTVSPDTTLREALELMREHGIRGLPVVDeDGRLVGIVTERDLLRALLPDRLDELEErlldlpVEDVM 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595596 406 NAAPETLAPGASLAQL-QAVLDRGLVAI-VADASG-FHGLITRFDLLNHLRRKLA 457
Cdd:COG3448  80 TRPVVTVTPDTPLEEAaELMLEHGIHRLpVVDDDGrLVGIVTRTDLLRALARLLE 134
PRK06381 PRK06381
threonine synthase; Validated
 14-307 8.55e-17

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 80.91  E-value: 8.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   14 GNTPLVRVTRFDT--GPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRlrpgGTIVEATAGNTGLGLALVGRAKGYRV 91
Cdd:PRK06381  14 GGTPLLRARKLEEelGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   92 VLVVPDKMSTEKVLHLRAMGAEVHITRSDvgkghpeyYQDVAARLAQdipgafFADQFN----NP--ANP-LAHE--CGT 162
Cdd:PRK06381  90 VIFIPRSYSNSRVKEMEKYGAEIIYVDGK--------YEEAVERSRK------FAKENGiydaNPgsVNSvVDIEaySAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  163 GPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELE------MVLADPEG------SIMAEYSRSGTLgTPGSWAV 230
Cdd:PRK06381 156 AYEIYEALGDVPDAVAVPVGNGTTLAGIYHGFRRLYDRGKtsrmprMIGVSTSGgnqiveSFKRGSSEVVDL-EVDEIRE 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  231 EGIGEDFVPAIA-----DLSSVR----HAYSISDEESFAMARELLRVEGI---PGGSSTgtlLAAALRFCREQKEPKRVV 298
Cdd:PRK06381 235 TAVNEPLVSYRSfdgdnALEAIYdshgYAFGFSDDEMVKYAELLRRMEGLnalPASASA---LAALVKYLKKNGVNDNVV 311


                 ....*....
gi 15595596  299 SFVcdTGTR 307
Cdd:PRK06381 312 AVI--TGRR 318
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
325-452 4.30e-16

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 76.85  E-value: 4.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 325 QRKHYGDLRDIIARRFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILLGVHADAPRFRDAVSSA 404
Cdd:COG2524  76 AEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRDLLDAPVSDI 155

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15595596 405 MNAAPETLAPGASLAQLQAVLDR---GLVAIVADASGFHGLITRFDLLNHL 452
Cdd:COG2524 156 MTRDVVTVSEDDSLEEALRLMLEhgiGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
345-457 1.01e-15

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 73.36  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPRFRDA-VSSAMNAAPETLAPGASLAQLQ 422
Cdd:COG0517  11 VVTVSPDATVREALELMSEKRIGGLPVVDEdGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTVSPDTSLEEAA 90

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15595596 423 AVLDR---GLVAIVADASGFHGLITRFDLLNHLRRKLA 457
Cdd:COG0517  91 ELMEEhkiRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 345-450 4.55e-15

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 71.12  E-value: 4.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPRFRDAVSSAMNAAPETLAPGASLAQ-LQ 422
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVDDdGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEaLE 83

                        90       100       110
                ....*....|....*....|....*....|
gi 15595596 423 AVLDRGL--VAIVADASGFHGLITRFDLLN 450
Cdd:cd02205  84 LMLEHGIrrLPVVDDDGKLVGIVTRRDILR 113
PRK06815 PRK06815
threonine/serine dehydratase;
17-211 1.27e-14

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 74.34  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   17 PLVRVTRFDTGP-------CTLYLKLESQNPGGSIKDRiGVA-----MIEAAERDGrlrpggtIVEATAGNTGLGLALVG 84
Cdd:PRK06815  16 PQVRVTPLEHSPllsqhtgCEVYLKCEHLQHTGSFKFR-GASnklrlLNEAQRQQG-------VITASSGNHGQGVALAA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   85 RAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHITRSDVGKGhpEYYqdvAARLAQDiPGAFFADQFNNPaNPLAHECGTGP 164
Cdd:PRK06815  88 KLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDALNA--ELA---ARRAAEQ-QGKVYISPYNDP-QVIAGQGTIGM 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15595596  165 ELWAQTGhDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS 211
Cdd:PRK06815 161 ELVEQQP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANS 206
PRK08246 PRK08246
serine/threonine dehydratase;
16-285 7.82e-14

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 71.91  E-value: 7.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   16 TPLVRVTRFDTGPCTLYLKLESQNPGGSIKDRIGVAMIEAAERdgrlrPGGTIVEATAGNTGLGLALVGRAKGYRVVLVV 95
Cdd:PRK08246  24 TPVLEADGAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVFV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   96 PDKMSTEKVLHLRAMGAEVHItrsdVGKGHPEYYQDVAARLAQDipGAFFADQFNNPANpLAHECGTGPELWAQTGhDLD 175
Cdd:PRK08246  99 PETAPPAKVARLRALGAEVVV----VGAEYADALEAAQAFAAET--GALLCHAYDQPEV-LAGAGTLGLEIEEQAP-GVD 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  176 AIVVGVGSSGTLTGLTRFFqkvQPELEMVLADPEGsiMAEYSRSGTLGTPGSWAVEGIGEDFVPA--IADLS------SV 247
Cdd:PRK08246 171 TVLVAVGGGGLIAGIAAWF---EGRARVVAVEPEG--APTLHAALAAGEPVDVPVSGIAADSLGArrVGEIAfalaraHV 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15595596  248 RHAYSISDEESFAMAREL---LRVEGIPGGSstgTLLAAAL 285
Cdd:PRK08246 246 VTSVLVSDEAIIAARRALweeLRLAVEPGAA---TALAALL 283
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 332-456 3.80e-13

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 66.01  E-value: 3.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 332 LRDIIARRfeegrVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDA-VSSAMNAAP 409
Cdd:COG2905   1 VKDIMSRD-----VVTVSPDATVREAARLMTEKGVGSLVVVDdDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPP 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15595596 410 ETLAPGASLAQ-LQAVLDRGL-VAIVADASGFHGLITRFDLLNHLRRKL 456
Cdd:COG2905  76 ITVSPDDSLAEaLELMEEHRIrHLPVVDDGKLVGIVSITDLLRALSEEL 124
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 2-286 1.39e-12

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 68.56  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596     2 TSDSRPAVLDLiGNTPLVRVTRF--DTGPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLrpggTIVEATAGNTGLG 79
Cdd:TIGR00260  10 VTEKDLVDLGE-GVTPLFRAPALaaNVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGND----TVLCASTGNTGAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    80 LALVGRAKGYRVVLVVP-DKMSTEKVLHLRAMGAEVHITRSDVgkghpeyyqDVAARLAQDIPGAFFADQFNN----PAN 154
Cdd:TIGR00260  85 AAAYAGKAGLKVVVLYPaGKISLGKLAQALGYNAEVVAIDGNF---------DDAQRLVKQLFEDKPALGLNSansiPYR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   155 PLAHECgTGPELWAQTGHDL-DAIVVGVGSSGTLTGLTRFFQkvqpELEMVLAD---------PEGS--IMAEYSRSGTL 222
Cdd:TIGR00260 156 LEGQKT-YAFEAVEQLGWEApDKVVVPVPNSGNFGAIWKGFK----EKKMLGLDslpvkrgiqAEGAadIVRAFLEGGQW 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   223 ---------------GTPGSW--AVEGIGEdfvpaiadlsSVRHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAAL 285
Cdd:TIGR00260 231 epietpetlstamdiGNPANWprALEAFRR----------SNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALL 300


                  .
gi 15595596   286 R 286
Cdd:TIGR00260 301 K 301
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 15-190 1.71e-11

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: 65.01  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  15 NTPLVRVTRFD-TGPCTLYLKLESQNPGGSIKDR-IGVAMIEAAERDGRLRPGgtIVEATAGNTGLGLALVGRAKGYRVV 92
Cdd:cd06448   1 KTPLIESTALSkTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  93 LVVPDKMSTEKVLHLRAMGAEVHITrsdvGKGHPEYYQDVAARLAQDIPGAFFADQFNNpanplahecgtgPELWA---- 168
Cdd:cd06448  79 IVVPESTKPRVVEKLRDEGATVVVH----GKVWWEADNYLREELAENDPGPVYVHPFDD------------PLIWEghss 142

                       170       180       190
                ....*....|....*....|....*....|.
gi 15595596 169 ---------QTGHDLDAIVVGVGSSGTLTGL 190
Cdd:cd06448 143 mvdeiaqqlQSQEKVDAIVCSVGGGGLLNGI 173
PRK08329 PRK08329
threonine synthase; Validated
 16-301 9.93e-11

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 62.92  E-value: 9.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   16 TPLVRVtrfdtgPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRlrpgGTIVEATAGNTGLGLALVGRAKGYRVVLVV 95
Cdd:PRK08329  65 TPTVKR------SIKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   96 PDKMSTEKVLHLRAMGAEVHITRSDVGKGHPEyyqdvAARLAQDiPGAFFADQFNNP-----ANPLAHecgtgpELWAQT 170
Cdd:PRK08329 135 SYNASKEKISLLSRLGAELHFVEGDRMEVHEE-----AVKFSKR-NNIPYVSHWLNPyflegTKTIAY------EIYEQI 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  171 GhDLDAIVVGVGSSGTLTGLTRFFQKVQ--------PELEMVLADPEGSIMAEYSRSGTLGtpgswavEGIG-------E 235
Cdd:PRK08329 203 G-VPDYAFVPVGSGTLFLGIWKGFKELHemgeiskmPKLVAVQAEGYESLCKRSKSENKLA-------DGIAipepprkE 274

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596  236 DFVPAIADLSSVrhAYSISDEESFAMARELLRVEGIPGGSSTGTLlaAALRFCREQKEPKRVVSFV 301
Cdd:PRK08329 275 EMLRALEESNGF--CISVGEEETRAALHWLRRMGFLVEPTSAVAL--AAYWKLLEEGLIEGGSKVL 336
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-387 1.10e-10

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 58.97  E-value: 1.10e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd04584  10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLL 52
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 343-433 2.37e-10

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 57.81  E-value: 2.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 343 GRVISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPRFRDA-VSSAMNAAPETLAPGASLAQ 420
Cdd:cd04623   2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVRKLALRGASSLDTpVSEIMTRDVVTCTPDDTVEE 81

                        90       100
                ....*....|....*....|....*
gi 15595596 421 LQA-----------VLDRG-LVAIV 433
Cdd:cd04623  82 CMAlmterrirhlpVVEDGkLVGIV 106
PRK12483 PRK12483
threonine dehydratase; Reviewed
 9-211 4.37e-10

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 61.74  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596    9 VLDLIGNTPLVRVTRFDTG-PCTLYLKLESQNPGGSIKDRIG---VAMIEAAERdgrlrpGGTIVEATAGNTGLGLALVG 84
Cdd:PRK12483  31 VYDVARETPLQRAPNLSARlGNQVLLKREDLQPVFSFKIRGAynkMARLPAEQL------ARGVITASAGNHAQGVALAA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   85 RAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHItrsdvgkgHPEYYQDVAARLA--QDIPGAFFADQFNNPaNPLAHECGT 162
Cdd:PRK12483 105 ARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVL--------HGESFPDALAHALklAEEEGLTFVPPFDDP-DVIAGQGTV 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 15595596  163 GPELWAQTGHDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS 211
Cdd:PRK12483 176 AMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
PRK06450 PRK06450
threonine synthase; Validated
 14-129 7.19e-10

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 60.13  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   14 GNTPLVRVTRFdtgpctlYLKLESQNPGGSIKDRIGVAMIEAAERDGRlrpgGTIVEATAGNTGLGLALVGRAKGYRVVL 93
Cdd:PRK06450  57 GRTPLIKKGNI-------WFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKI 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15595596   94 VVPDKMSTEKVLHLRAMGAE---VHITRSDVGKGHPE---YY 129
Cdd:PRK06450 126 FVPETASGGKLKQIESYGAEvvrVRGSREDVAKAAENsgyYY 167
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 345-387 4.41e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 54.35  E-value: 4.41e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15595596 345 VISVGPDDTLLTAFQRMRLAD-----VSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd17784  69 VATVHPDETLLEAIKKMDSNApdeeiINQLPVVDDGKLVGIISDGDII 116
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
333-454 5.83e-09

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 54.15  E-value: 5.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 333 RDIIARRfeegRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIlLGVHADAPrfrdaVSSAMNAAPET 411
Cdd:COG4109  19 EDIMTLE----DVATLSEDDTVEDALELLEKTGHSRFPVVDeNGRLVGIVTSKDI-LGKDDDTP-----IEDVMTKNPIT 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15595596 412 LAPGASLA---QLQAVLDRGLVAIVADASGFHGLITRFDLLNHLRR 454
Cdd:COG4109  89 VTPDTSLAsaaHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQK 134
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 345-387 8.98e-09

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 51.45  E-value: 8.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15595596   345 VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL 387
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDeDGKLVGIVTLKDLL 52
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 344-434 9.75e-09

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 53.19  E-value: 9.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILL-GVHADAPRFRDAVSSAMNAAPETLAPGASL---- 418
Cdd:cd04622   4 DVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVrAVAEGKDPNTTTVREVMTGDVVTCSPDDDVeeaa 83

                        90       100
                ....*....|....*....|....*
gi 15595596 419 ---AQLQ----AVLDRG--LVAIVA 434
Cdd:cd04622  84 rlmAEHQvrrlPVVDDDgrLVGIVS 108
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 332-450 9.92e-09

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 52.33  E-value: 9.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 332 LRDIIARRfeegrVISVGPDDTLLTAFQRMRLA-DVSQLPVLddgKLVGViDESDILLGVHADA-PRFRDavssamnaap 409
Cdd:COG3620   1 VRDLMSRD-----VVTVSPDDTLGEALRLMRKElGLSQLPVA---ELVGV-SQSDILRIESGKRdPTVST---------- 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595596 410 etlapgasLAQLQAVLDRGLVAI-VADASGFHGLITRFDLLN 450
Cdd:COG3620  62 --------LEKIAEALGKELSAVlVVDDGKLVGIITRRDLLK 95
PRK06110 PRK06110
threonine dehydratase;
29-114 1.33e-08

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 56.16  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   29 CTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRPGgtIVEATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEKVLHLR 108
Cdd:PRK06110  36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113


                 ....*.
gi 15595596  109 AMGAEV 114
Cdd:PRK06110 114 ALGAEL 119
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-387 1.39e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 53.19  E-value: 1.39e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd04584  84 VITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDIL 126
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-451 1.74e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 52.34  E-value: 1.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIlLGVHADapRFrdaVSSAMNAAPETLAPGASLAQLQAV 424
Cdd:cd04599   5 PITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDV-RRAHPN--RL---VADAMSRNVVTISPEASLWEAKEL 78

                        90       100
                ....*....|....*....|....*....
gi 15595596 425 LDRGLVA--IVADASGFHGLITRFDLLNH 451
Cdd:cd04599  79 MEEHGIErlVVVEEGRLVGIITKSTLYLE 107
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-451 2.46e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 51.80  E-value: 2.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD--GKLVGVIDESDILLGVH---ADAPrfrdaVSSAMNAAPETLAPGASLA 419
Cdd:cd17772   4 VISVEPDTTIAEAAELMTRYNINALPVVDGgtGRLVGIITRQVAEKAIYhglGDLP-----VSEYMTTEFATVTPDAPLS 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15595596 420 QLQAVL---DRGLVAIVaDASGFHGLITRFDLLNH 451
Cdd:cd17772  79 EIQEIIveqRQRLVPVV-EDGRLVGVITRTDLLNL 112
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 339-457 3.59e-08

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 55.47  E-value: 3.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   339 RFEEGRV---ISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILLGVHADAPrfrdaVSSAMNAAPETLAP- 414
Cdd:pfam00478  81 RSESGMItdpVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDLRFETDLSQP-----VSEVMTKENLVTAPe 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15595596   415 GASLAQLQAVLDR---GLVAIVADASGFHGLITRFDLLNHLRRKLA 457
Cdd:pfam00478 156 GTTLEEAKEILHKhkiEKLPVVDDNGRLVGLITIKDIEKAKEYPNA 201
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 345-387 3.69e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 51.28  E-value: 3.69e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd04629  72 VLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVL 114
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 345-449 4.67e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 51.56  E-value: 4.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPRFRDA-------------VSSAMNAAPE 410
Cdd:cd04632   4 VITVNEDDTIGKAINLLREHGISRLPVVDDnGKLVGIVTTYDIVDFVVRPGTKTRGGdrggekermldlpVYDIMSSPVV 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595596 411 TLAPGASLAQ-LQAVLDRGL--VAIVADASGFHGLITRFDLL 449
Cdd:cd04632  84 TVTRDATVADaVERMLENDIsgLVVTPDDNMVIGILTKTDVL 125
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-449 5.41e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 51.66  E-value: 5.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL----LGVHADAPRFRDA------------------- 400
Cdd:cd04586   5 VVTVTPDTSVREAARLLLEHRISGLPVVDdDGKLVGIVSEGDLLrreePGTEPRRVWWLDAllesperlaeeyvkahgrt 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595596 401 VSSAMNAAPETLAPGASLAQLQA-----------VLDRG-LVaivadasgfhGLITRFDLL 449
Cdd:cd04586  85 VGDVMTRPVVTVSPDTPLEEAARlmerhrikrlpVVDDGkLV----------GIVSRADLL 135
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 332-387 6.18e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 50.71  E-value: 6.18e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 332 LRDIIARRFEEGR-------------VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDIL 387
Cdd:cd02205  43 ERDILRALVEGGLaldtpvaevmtpdVITVSPDTDLEEALELMLEHGIRRLPVVDDdGKLVGIVTRRDIL 112
CBS COG0517
CBS domain [Signal transduction mechanisms];
333-387 6.33e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 51.02  E-value: 6.33e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 333 RDIIARRFEEGR--------------VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDIL 387
Cdd:COG0517  51 RDLRRALAAEGKdlldtpvsevmtrpPVTVSPDTSLEEAAELMEEHKIRRLPVVDDdGRLVGIITIKDLL 120
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-450 1.07e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 49.80  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILLGVH---ADAPrfrdaVSSAMNAAPETLAPGASLAQL 421
Cdd:cd04595   4 VKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDVDKAKHhglGHAP-----VKGYMSTNVITIDPDTSLEEA 78

                        90       100       110
                ....*....|....*....|....*....|..
gi 15595596 422 QAVL---DRGLVAIVADASgFHGLITRFDLLN 450
Cdd:cd04595  79 QELMvehDIGRLPVVEEGK-LVGIVTRSDVLR 109
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 333-387 1.38e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 49.87  E-value: 1.38e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595596 333 RDIIARRfeegrVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd04801  62 RDVMTKD-----VITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLM 111
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-451 1.38e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 49.73  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDI-----LLGVHADAPrfrdaVSSAMNAAPETLAPGASL 418
Cdd:cd04587   5 PPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLrnrvvAEGLDPDTP-----VSEIMTPPPVTIDADALV 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15595596 419 --AQLQ---------AVLDRGLVAivadasgfhGLITRFDLLNH 451
Cdd:cd04587  80 feALLLmlernihhlPVVDDGRVV---------GVVTATDLMRL 114
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 345-435 3.66e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 48.96  E-value: 3.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPRFRDAVSSAMNAAPETLAPGASLA---- 419
Cdd:cd17784   4 VITAKPNEGVVEAFEKMLKHKISALPVVDDeGKLIGIVTATDLGHNLILDKYELGTTVEEVMVKDVATVHPDETLLeaik 83

                        90       100
                ....*....|....*....|....*....
gi 15595596 420 -------------QLQAVLDRGLVAIVAD 435
Cdd:cd17784  84 kmdsnapdeeiinQLPVVDDGKLVGIISD 112
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-449 3.69e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 49.10  E-value: 3.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAPRFRDA---------------VSSAMNAA 408
Cdd:cd04600   5 VVTVTPDTSLEEAWRLLRRHRIKALPVVDrARRLVGIVTLADLLKHADLDPPRGLRGrlrrtlglrrdrpetVGDIMTRP 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15595596 409 PETLAPGASLAQLQAVL-DRGLVAI-VADASG-FHGLITRFDLL 449
Cdd:cd04600  85 VVTVRPDTPIAELVPLFsDGGLHHIpVVDADGrLVGIVTQSDLI 128
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 344-387 4.49e-07

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 46.35  E-value: 4.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 15595596    344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDIL 387
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDII 45
PRK05638 PRK05638
threonine synthase; Validated
 14-286 6.20e-07

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 51.35  E-value: 6.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   14 GNTPLVRVTRFDTGPCTLYLKLESQNPGGSIKDRIGVAMIEaaerDGRLRPGGTIVEATAGNTGLGLALVGRAKGYRVVL 93
Cdd:PRK05638  65 GGTPLIRARISEKLGENVYIKDETRNPTGSFRDRLATVAVS----YGLPYAANGFIVASDGNAAASVAAYSARAGKEAFV 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   94 VVPDKMSTEKVLHLRAMGAEVHITRSDVGKGhPEYyqdvAARLAQdIPGAFFADQFNNPANpLAHECGTGPELWAQTGHd 173
Cdd:PRK05638 141 VVPRKVDKGKLIQMIAFGAKIIRYGESVDEA-IEY----AEELAR-LNGLYNVTPEYNIIG-LEGQKTIAFELWEEINP- 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  174 lDAIVVGVGSSGTLTGLTRFFQKVQ--------PELEMVLADPEGSIMAEY----SRSGTLGTPGSWAVEGIGEDFVPAI 241
Cdd:PRK05638 213 -THVIVPTGSGSYLYSIYKGFKELLeigvieeiPKLIAVQTERCNPIASEIlgnkTKCNETKALGLYVKNPVMKEYVSEA 291

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15595596  242 ADLSSvrHAYSISDEESFAMARELLRVEGIPGGSSTGTLLAAALR 286
Cdd:PRK05638 292 IKESG--GTAVVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLK 334
PLN02970 PLN02970
serine racemase
 16-211 8.22e-07

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 50.83  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   16 TPLVRVTRFDT-GPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRpggTIVEATAGNTGLGLALVGRAKGYRVVLV 94
Cdd:PLN02970  28 TPVLTSSSLDAlAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEK---GVVTHSSGNHAAALALAAKLRGIPAYIV 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   95 VPDKMSTEKVLHLRAMGAEVHITRSDVgkghpEYYQDVAARLAQDiPGAFFADQFNNPanPLAHECGT-GPELWAQTgHD 173
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGGIITWCEPTV-----ESREAVAARVQQE-TGAVLIHPYNDG--RVISGQGTiALEFLEQV-PE 175

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15595596  174 LDAIVVGVGSSGTLTGLTRFFQKVQPELEMVLADPEGS 211
Cdd:PLN02970 176 LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
PLN02550 PLN02550
threonine dehydratase
 31-271 9.78e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 51.08  E-value: 9.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   31 LYLKLESQNPGGSIKDRIGVAMIEAAERDgRLRPGgtIVEATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEKVLHLRAM 110
Cdd:PLN02550 126 VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERL 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  111 GAEVHItrsdVGKGHPEyYQDVAARLAQDiPGAFFADQFNNPaNPLAHECGTGPELWAQTGHDLDAIVVGVGSSGTLTGL 190
Cdd:PLN02550 203 GATVVL----VGDSYDE-AQAYAKQRALE-EGRTFIPPFDHP-DVIAGQGTVGMEIVRQHQGPLHAIFVPVGGGGLIAGI 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  191 TRFFQKVQPELEMVLADP-EGSIMAEYSRSGtlgtpgswavEGIGEDFVPAIADLSSVRHAysisDEESFAMARELlrVE 269
Cdd:PLN02550 276 AAYVKRVRPEVKIIGVEPsDANAMALSLHHG----------ERVMLDQVGGFADGVAVKEV----GEETFRLCREL--VD 339


                 ..
gi 15595596  270 GI 271
Cdd:PLN02550 340 GV 341
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 344-450 1.06e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 47.43  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGV-----HADAPRfrdAVSSAMNAAPETLAPGAS 417
Cdd:cd04629   4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEqGRLVGFLSEQDCLKALleasyHCEPGG---TVADYMSTEVLTVSPDTS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15595596 418 ---LAQ--LQA------VLDRG-LVaivadasgfhGLITRFDLLN 450
Cdd:cd04629  81 ivdLAQlfLKNkprrypVVEDGkLV----------GQISRRDVLR 115
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 330-387 1.38e-06

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 47.22  E-value: 1.38e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595596 330 GDLRDIIARRFEE---GRVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd04631  67 GNIHEVLNVPISSimkRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDIL 127
eutB PRK07476
threonine dehydratase; Provisional
 16-139 1.65e-06

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 49.58  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   16 TPLVRVTRF-DTGPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRLRpggTIVEATAGNTGLGLALVGRAKGYRVVLV 94
Cdd:PRK07476  20 TPLVASASLsARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERAR---GVVTASTGNHGRALAYAARALGIRATIC 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15595596   95 VPDKMSTEKVLHLRAMGAEVHItrsdVGKGHPEYYQDVaARLAQD 139
Cdd:PRK07476  97 MSRLVPANKVDAIRALGAEVRI----VGRSQDDAQAEV-ERLVRE 136
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 344-451 2.97e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 45.86  E-value: 2.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL-LGVHADAPRFRDAVSSAMNAAPETLAPGASLAQLQ 422
Cdd:cd17776   4 DVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALhAGYATDDPFSEIPVRAVASRPLVTISPTATLREAA 83

                        90       100       110
                ....*....|....*....|....*....|.
gi 15595596 423 AVLDRGLVA--IVADASGFHGLITRFDLLNH 451
Cdd:cd17776  84 ERMVDEGVKklPVVDGLDLVGILTATDIIRA 114
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 331-387 3.28e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 46.03  E-value: 3.28e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595596 331 DLRDIIarrFEEG-------------RVISVGPDDTLLTAFQRMRLADVSQLPVLDD---GKLVGVIDESDIL 387
Cdd:cd04613  46 DVRGVL---FEEElwdlvvvkdlattDVITVTPDDDLYTALLKFTSTNLDQLPVVDDddpGKVLGMLSRRDVI 115
PRK06608 PRK06608
serine/threonine dehydratase;
31-208 5.09e-06

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 48.23  E-value: 5.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   31 LYLKLESQNPGGSIKDRIGVAMIEAAERDGRLrPGgTIVEATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEKVLHLRAM 110
Cdd:PRK06608  40 IFFKVESLQKTGAFKVRGVLNHLLELKEQGKL-PD-KIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYY 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  111 GAEVHITRSdvgkgHPEyyQDVAARLAQDiPGAFFADQFNNPANPlaheCGTGP---ELWAQTGHDLDAIVVGVGSSGTL 187
Cdd:PRK06608 118 GGEVILTNT-----RQE--AEEKAKEDEE-QGFYYIHPSDSDSTI----AGAGTlcyEALQQLGFSPDAIFASCGGGGLI 185

                        170       180
                 ....*....|....*....|.
gi 15595596  188 TGLTRFFQKVQPELEMVLADP 208
Cdd:PRK06608 186 SGTYLAKELISPTSLLIGSEP 206
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 344-387 6.71e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 44.79  E-value: 6.71e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd04595  65 NVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVL 108
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 346-450 6.74e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 44.82  E-value: 6.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 346 ISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILLGVHADAprfrdAVSSAMNAAPETLAPGASLAQ-LQA 423
Cdd:cd04583   5 VTITPERTLAQAIEIMREKRVDSLLVVDkDNVLLGIVDIEDINRNYRKAK-----KVGEIMERDVFTVKEDSLLRDtVDR 79

                        90       100
                ....*....|....*....|....*....
gi 15595596 424 VLDRGL--VAIVADASGFHGLITRFDLLN 450
Cdd:cd04583  80 ILKRGLkyVPVVDEQGRLVGLVTRASLVD 108
CBS_pair_bac cd17783
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 350-387 7.99e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341419 [Multi-domain]  Cd Length: 108  Bit Score: 44.49  E-value: 7.99e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15595596 350 PDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL 387
Cdd:cd17783   9 PTDSVEKALDWMEEFRVSQLPVVDNGQYLGLISEDDLL 46
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
332-386 8.21e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 48.29  E-value: 8.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596  332 LRDIiarrfEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDI 386
Cdd:PRK14869  70 VRDL-----EIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDeEGKLLGLVSLSDL 120
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 345-387 8.81e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 44.84  E-value: 8.81e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDIL 387
Cdd:cd17775  71 LITAREDDGLFEALERMREKGVRRLPVVDDdGELVGIVTLDDIL 114
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 344-449 9.48e-06

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 45.01  E-value: 9.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL--LGVHADAPRFRDA---------VSSAMNAAPETL 412
Cdd:cd17778   9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVkyFGSHEAKKRLTTGdideaystpVEEIMSKEVVTI 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15595596 413 APGASL---AQLQAVLDRGLVAIVADASGFHGLITRFDLL 449
Cdd:cd17778  89 EPDADIaeaARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 344-390 1.60e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 43.87  E-value: 1.60e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGV 390
Cdd:cd04597   6 KVEPLSPETSIKDAWNLMDENNLKTLPVTDDnGKLIGLLSISDIARTV 53
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 333-388 2.05e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 43.48  E-value: 2.05e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595596 333 RDIiaRRFEEGR---------VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILL 388
Cdd:cd04599  44 RDV--RRAHPNRlvadamsrnVVTISPEASLWEAKELMEEHGIERLVVVEEGRLVGIITKSTLYL 106
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 345-419 4.04e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 42.90  E-value: 4.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPRfRDAVSSAMNAAPETLAPGASLA 419
Cdd:cd09836   5 VVTVPPETTIREAAKLMAENNIGSVVVVDDdGKPVGIVTERDIVRAVAEGIDL-DTPVEEIMTKNLVTVSPDESIY 79
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 261-386 4.60e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 42.33  E-value: 4.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 261 MARELLRVEgIPGGSSTgtllaaALRFCreQKEPKRVVSFVCDTGTRYLskiyndqwmtdqGLLQRKhygdlrDIIARRF 340
Cdd:cd04638   1 MTKDVVTVT-LPGTRDD------VLEIL--KKKAISGVPVVKKETGKLV------------GIVTRK------DLLRNPD 53

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15595596 341 EEG-------RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDI 386
Cdd:cd04638  54 EEQiallmsrDPITISPDDTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVADL 106
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 345-388 4.80e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 42.31  E-value: 4.80e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILL 388
Cdd:cd04610   5 VITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLG 48
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 346-450 4.95e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 42.40  E-value: 4.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 346 ISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHADAPrfrdaVSSAM--NAAPETLAPGASLAQLQ 422
Cdd:cd04601   5 VTLSPDATVADVLELKAEYGISGVPVTEDgGKLVGIVTSRDIRFETDLSTP-----VSEVMtpDERLVTAPEGITLEEAK 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 15595596 423 AVLDR---GLVAIVADASGFHGLITRFDLLN 450
Cdd:cd04601  80 EILHKhkiEKLPIVDDNGELVGLITRKDIEK 110
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 329-386 8.42e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 41.84  E-value: 8.42e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15595596 329 YGDLRDIIARRfeegrVISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDI 386
Cdd:cd04605  60 KDSLEEIMTRN-----VITARPDEPIELAARKMEKHNISALPVVDDdRRVIGIITSDDI 113
PRK08813 PRK08813
threonine dehydratase; Provisional
 16-190 8.70e-05

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 44.62  E-value: 8.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   16 TPLVRVTRFDTgpctlYLKLESQNPGGSIKDRIGV-AMIEAAERdGRLRPggtIVEATAGNTGLGLALVGRAKGYRVVLV 94
Cdd:PRK08813  40 TPLHYAERFGV-----WLKLENLQRTGSYKVRGALnALLAGLER-GDERP---VICASAGNHAQGVAWSAYRLGVQAITV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   95 VPDKMSTEKVLHLRAMGAEVHitrsDVGKGHPEYYQdVAARLAQDiPGAFFADQFNNPaNPLAHECGTGPELwaqTGHDL 174
Cdd:PRK08813 111 MPHGAPQTKIAGVAHWGATVR----QHGNSYDEAYA-FARELADQ-NGYRFLSAFDDP-DVIAGQGTVGIEL---AAHAP 180

                        170
                 ....*....|....*.
gi 15595596  175 DAIVVGVGSSGTLTGL 190
Cdd:PRK08813 181 DVVIVPIGGGGLASGV 196
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 333-386 1.21e-04

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 41.25  E-value: 1.21e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595596 333 RDIIARRFEEGR--------------VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDI 386
Cdd:cd04622  44 RDIVVRAVAEGKdpntttvrevmtgdVVTCSPDDDVEEAARLMAEHQVRRLPVVDdDGRLVGIVSLGDL 112
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 367-452 1.21e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 41.72  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 367 SQLPVLD-DGKLVGVIDESDIL---LGV-HADAPRFRD-AVSSAMNAAPETLAPGASLAQ-LQAVLDRGLVAIVADASGF 439
Cdd:cd04643  31 SRIPVLDkDYKLVGLISLSMILdaiLGLeRIEFEKLSElKVEEVMNTDVPTVSPDDDLEEvLHLLVDHPFLCVVDEDGYF 110

                        90
                ....*....|....*.
gi 15595596 440 HGLITRFDLL---NHL 452
Cdd:cd04643 111 LGIITRREILkavNKL 126
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 351-387 1.26e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 42.27  E-value: 1.26e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 15595596 351 DDT-LLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL 387
Cdd:cd04614  11 DETpLPVALRAMRLANVPAAPVLDsEGKLVGIVTERDLI 49
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
16-204 2.02e-04

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 43.19  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   16 TPLVRvTRFDTGPC--TLYLKLESQNPGGSIKDRiGVA-----MIEAAERDGrlrpggtIVEATAGNTGLGLALVGRAKG 88
Cdd:PRK08638  28 TPLPR-SNYLSERCkgEIFLKLENMQRTGSFKIR-GAFnklssLTDAEKRKG-------VVACSAGNHAQGVALSCALLG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   89 YRVVLVVPDKMSTEKVLHLRAMGAEVHItrsdvgkgHPEYYQDVAARLAQDIP--GAFFADQFNNPaNPLAHECGTGPE- 165
Cdd:PRK08638  99 IDGKVVMPKGAPKSKVAATCGYGAEVVL--------HGDNFNDTIAKVEEIVEeeGRTFIPPYDDP-KVIAGQGTIGLEi 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15595596  166 ---LWaqtghDLDAIVVGVGSSGTLTGLTRFFQKVQPELEMV 204
Cdd:PRK08638 170 ledLW-----DVDTVIVPIGGGGLIAGIAVALKSINPTIHII 206
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 345-387 2.12e-04

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 41.37  E-value: 2.12e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDIL 387
Cdd:cd17774  79 LFSLRPDDSLWTAHQLMQQRRIRRLVVVGEqGELLGIVTQTSLL 122
CBS_pair_bac cd09834
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 345-451 2.62e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341404 [Multi-domain]  Cd Length: 118  Bit Score: 40.56  E-value: 2.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL--------LGVHA-------DAPRFRDAVSSAMNAA 408
Cdd:cd09834   4 VAYLYDDSTLRQALEKMEYHRYTAIPILNrDGKYVGTITEGDLLwyiknkpnLDLKDaekisikDIPRRRDNKPVNINAN 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15595596 409 PETLapgaslaqLQAVLDRGLVAIVADASGFHGLITRFDLLNH 451
Cdd:cd09834  84 MEDL--------LDLAMNQNFVPVVDDRGVFIGIVTRKDIIKY 118
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 16-298 2.68e-04

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 42.91  E-value: 2.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  16 TPLVRVTRFD--TGPCTLYLKLESQNPGGSIKdrIGVAMIEA--AERDGRLRpggTIVEATAGNTGLGLALVGRAKGYRV 91
Cdd:cd06446  35 TPLYRAKRLSeyLGGAKIYLKREDLNHTGAHK--INNALGQAllAKRMGKKR---VIAETGAGQHGVATATACALFGLEC 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  92 VlVVPDKMSTEK----VLHLRAMGAEVHITRSDVGK---GHPEYYQDVaarlAQDIPGAFF-----ADQFNNPANPLAHE 159
Cdd:cd06446 110 E-IYMGAVDVERqplnVFRMELLGAEVVPVPSGSGTlkdAISEAIRDW----VTNVEDTHYllgsvVGPHPYPNMVRDFQ 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 160 CGTGPELWAQ----TGHDLDAIV--VGVGS------------------------SGTLTG-----LTRFFQKVQPELEM- 203
Cdd:cd06446 185 SVIGEEAKKQilekEGELPDVVIacVGGGSnaaglfypfindkdvkligveaggCGLETGghaayLFGGTAGVLHGLKMy 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 204 VLADPEGSIMAEYSRSGTLGTPgswaveGIGedfvPAIADLSSVR--HAYSISDEESFAMARELLRVEGIPGGSSTGTLL 281
Cdd:cd06446 265 TLQDEDGQIVPPHSISAGLDYP------GVG----PEHAYLKDSGrvEYVAVTDEEALEAFKLLARTEGIIPALESSHAI 334

                       330
                ....*....|....*..
gi 15595596 282 AAALRFCREQKEPKRVV 298
Cdd:cd06446 335 AYAIKLAKKLGKEKVIV 351
PRK07334 PRK07334
threonine dehydratase; Provisional
 29-233 3.30e-04

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 42.96  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   29 CTLYLKLESQNPGGSIKDRiG----VAMIEAAERdgrlRPGgtIVEATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEKV 104
Cdd:PRK07334  38 AEVWLKFENLQFTASFKER-GalnkLLLLTEEER----ARG--VIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  105 LHLRAMGAEVHITrsdvGKGHPEYYQdVAARLAQDiPGAFFADQFNNPAnpLAHECGT-GPELWAQTGhDLDAIVVGVGS 183
Cdd:PRK07334 111 ERTRGFGAEVVLH----GETLDEARA-HARELAEE-EGLTFVHPYDDPA--VIAGQGTvALEMLEDAP-DLDTLVVPIGG 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15595596  184 SGTLTGLTRFFQKVQPELEMVLADPEG-SIMAEYSRSGTLGTPGSWAVEGI 233
Cdd:PRK07334 182 GGLISGMATAAKALKPDIEIIGVQTELyPSMYAAIKGVALPCGGSTIAEGI 232
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 332-387 4.19e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 40.73  E-value: 4.19e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15595596 332 LRDIIARRFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL 387
Cdd:cd04614  92 LPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSgEGDLAGMLRDVDLL 148
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 344-449 4.58e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 39.86  E-value: 4.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIllgvHADAPRFRDA--VSSAMNAAPETLAPGASLAQL 421
Cdd:cd04801   6 EVVTVTPEMTVSELLDRMFEEKHLGYPVVENGRLVGIVTLEDI----RKVPEVEREAtrVRDVMTKDVITVSPDADAMEA 81

                        90       100       110
                ....*....|....*....|....*....|
gi 15595596 422 QAVLDRGLVA--IVADASGFHGLITRFDLL 449
Cdd:cd04801  82 LKLMSQNNIGrlPVVEDGELVGIISRTDLM 111
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 346-427 4.98e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 39.74  E-value: 4.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 346 ISVGPDDTLLTAFQR-----MRLADVsqlpVLDDGKLVGVIDESDI----LLGVHADAPrfrdaVSSAMNAAPETLAPGA 416
Cdd:cd04607   5 VLVSPDTTIREAIEVidkgaLQIALV----VDENRKLLGTVTDGDIrrglLKGLSLDAP-----VEEVMNKNPITASPST 75

                        90
                ....*....|.
gi 15595596 417 SLAQLQAVLDR 427
Cdd:cd04607  76 SREELLALMRA 86
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 345-387 5.46e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 39.43  E-value: 5.46e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL 387
Cdd:cd09836  69 LVTVSPDESIYEAAELMREHNIRHLPVVDgGGKLVGVISIRDLA 112
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 310-387 5.70e-04

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 39.80  E-value: 5.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 310 SKIYNDQWMT-DQGLLQRkhygdlrdiiARRFEegRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIL 387
Cdd:cd04641  53 EKTYNNLDLTvGEALQHR----------SEDFE--GVHTCTLNDTLETIIDRIVKAEVHRLVVVDeEDRLEGIVSLSDIL 120
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 339-407 6.19e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 39.51  E-value: 6.19e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595596 339 RFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILLGVHADAPRFRDAVSSAMNA 407
Cdd:cd09833   1 RIVSTSLLTCSPDTPLADAAARMAERRCSSILIVENGEIVGIWTERDALKLDFSDPDAFRRPISEVMSS 69
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
29-211 1.20e-03

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 41.28  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   29 CTLYLKLESQNPGGSIKDRIGVAMI-----EAAERdgrlrpgGTIVeATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEK 103
Cdd:PRK09224  35 NQVLLKREDLQPVFSFKLRGAYNKMaqlteEQLAR-------GVIT-ASAGNHAQGVALSAARLGIKAVIVMPVTTPDIK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596  104 VLHLRAMGAEV--HitrsdvGKGHPEYYQDvAARLAQDiPGAFFADQFNNPAnPLAHEcGT-GPELWAQTGHDLDAIVVG 180
Cdd:PRK09224 107 VDAVRAFGGEVvlH------GDSFDEAYAH-AIELAEE-EGLTFIHPFDDPD-VIAGQ-GTiAMEILQQHPHPLDAVFVP 176

                        170       180       190
                 ....*....|....*....|....*....|.
gi 15595596  181 VGSSGTLTGLTRFFQKVQPELEMVLADPEGS 211
Cdd:PRK09224 177 VGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 345-450 2.41e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 37.51  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDILLGVHADAPRFRdaVSSAMNAAPETLAPGASLAQLQAV 424
Cdd:cd04588   4 LITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDIAKALAEGKENAK--VKDIMTKDVITIDKDEKIYDAIRL 81

                        90       100
                ....*....|....*....|....*....
gi 15595596 425 LDR---GLVAIVADASGFHGLITRFDLLN 450
Cdd:cd04588  82 MNKhniGRLIVVDDNGKPVGIITRTDILK 110
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 344-450 2.50e-03

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 37.98  E-value: 2.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 344 RVISVGPDDTLLTAFQRMRLADVSQLPVLDDGKLVGVIDESDIL--LG-------VHADAPR--FRDAVSSAMNAAPETL 412
Cdd:cd04631   9 NVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMryLGsgeafekLKTGNIHevLNVPISSIMKRDIITT 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15595596 413 APGASLAQL-QAVLDRGLVAI-VADASGFHGLITRFDLLN 450
Cdd:cd04631  89 TPDTDLGEAaELMLEKNIGALpVVDDGKLVGIITERDILR 128
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 333-386 6.30e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 36.96  E-value: 6.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595596 333 RDIIARRFEEGRV-ISVGPDDTLLTAFQRMRLADVSQLPVLDD------GKLVGVIDESDI 386
Cdd:cd04592  67 SSICTRNGGYCRGlWTCTPDMDLLTAKMLMEARGINQLPVVKRggeerrRRVVGLLDRDSI 127
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 67-117 6.77e-03

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 38.71  E-value: 6.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15595596   67 TIVEATAGNTGLGLALVGRAKGYRVVLVVPDKMSTEKVLHLRAMGAEVHIT 117
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT 168
PLN02569 PLN02569
threonine synthase
 14-114 7.48e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 38.64  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596   14 GNTPLVRVTRF---DTGPCTLYLKLESQNPGGSIKDRIGVAMIEAAERDGRL-RPGGTIVEATAGNTGLGLALVGRAKGY 89
Cdd:PLN02569 132 GNSNLFWAERLgkeFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGI 211

                         90       100
                 ....*....|....*....|....*.
gi 15595596   90 RVVLVVP-DKMSTEKVLHLRAMGAEV 114
Cdd:PLN02569 212 PSIVFLPaDKISIAQLVQPIANGALV 237
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 346-450 9.47e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 35.78  E-value: 9.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 346 ISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDIllgvhadAPRFRDAVSSAMNAAPETLAPGASLAQLQAV 424
Cdd:cd04594   5 IKVSAYDTVERALKIMRENNLLSLPVVDnDSNFLGAVYLRDI-------ENKSPGKVGKYVVRGSPYVTPTSSLEEAWEI 77

                        90       100
                ....*....|....*....|....*....
gi 15595596 425 LDRG---LVAIVaDASGFHGLITRFDLLN 450
Cdd:cd04594  78 MMRNksrWVAVV-EKGKFLGIITLDDLLE 105
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 323-388 9.49e-03

signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 36.44  E-value: 9.49e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595596 323 LLQRKHYGDLRDII---ARRFEEGRVISVGPDDTLLTAFQRMRLADVSQLPVLD-DGKLVGVIDESDILL 388
Cdd:cd17779  65 LVEKKHNGNLLAAInepVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDkDGKVIGIVTERDFLK 134
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 345-392 9.77e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 35.98  E-value: 9.77e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15595596 345 VISVGPDDTLLTAFQRMRLADVSQLPVLDD-GKLVGVIDESDILLGVHA 392
Cdd:cd17775   5 VVTASPDTSVLEAARLMRDHHVGSVVVVEEdGKPVGIVTDRDIVVEVVA 53
 
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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