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Conserved domains on  [gi|685917698|ref|WP_031654511|]
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MULTISPECIES: cystathionine beta-synthase [Mycobacterium]

Protein Classification

cystathionine beta-synthase( domain architecture ID 1002792)

cystathionine beta-synthase is a hydro-lyase that catalyzes the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine

CATH:  3.40.50.1100
EC:  4.2.1.22
Gene Ontology:  GO:0019344|GO:0004122|GO:0030170|GO:0020037|GO:0046872
PubMed:  32365821

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cysta_beta super family cl36831
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 3-458 0e+00

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]


The actual alignment was detected with superfamily member TIGR01137:

Pssm-ID: 273464 [Multi-domain]  Cd Length: 455  Bit Score: 711.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    3 IAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALV 82
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   83 AQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAVPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTG 162
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  163 PEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADPEGSVYSGG-----AGR-PYLVEGVGEDFWPAAYD 236
Cdd:TIGR01137 161 PEILEQCEGKLDMFVAGVGTGGTITGIARYLKE-SCPGCRIVGADPEGSILAQPeelnqTGRtPYKVEGIGYDFIPTVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  237 PSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDA-LIVVLLPDGGRGYMSKIFNDAWMSSYG 315
Cdd:TIGR01137 240 RKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGqRCVVLLPDSIRNYMTKFLNDEWMLDNG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  316 FLRSrldgstEQSTVGDVL----RRKSGALPALVHTHPSETVRDAIGILREYGVSQMPVVGaeppvMAGEVAGSVSEREL 391
Cdd:TIGR01137 320 FLDD------EDLTVKDVLwwhaRVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVD-----EAGKVLGSVTLREL 388

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685917698  392 LSAVFEGRAKLADAVSAHMSPPLRMIGAGELVSAAGKALRDWDALMVVEEGKPVGVITRYDLLGFLS 458
Cdd:TIGR01137 389 LSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKPIGVVTKIDLLSFLA 455
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 3-458 0e+00

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: 711.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    3 IAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALV 82
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   83 AQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAVPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTG 162
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  163 PEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADPEGSVYSGG-----AGR-PYLVEGVGEDFWPAAYD 236
Cdd:TIGR01137 161 PEILEQCEGKLDMFVAGVGTGGTITGIARYLKE-SCPGCRIVGADPEGSILAQPeelnqTGRtPYKVEGIGYDFIPTVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  237 PSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDA-LIVVLLPDGGRGYMSKIFNDAWMSSYG 315
Cdd:TIGR01137 240 RKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGqRCVVLLPDSIRNYMTKFLNDEWMLDNG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  316 FLRSrldgstEQSTVGDVL----RRKSGALPALVHTHPSETVRDAIGILREYGVSQMPVVGaeppvMAGEVAGSVSEREL 391
Cdd:TIGR01137 320 FLDD------EDLTVKDVLwwhaRVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVD-----EAGKVLGSVTLREL 388

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685917698  392 LSAVFEGRAKLADAVSAHMSPPLRMIGAGELVSAAGKALRDWDALMVVEEGKPVGVITRYDLLGFLS 458
Cdd:TIGR01137 389 LSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKPIGVVTKIDLLSFLA 455
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 1-304 2.03e-147

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: 422.15  E-value: 2.03e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLA 80
Cdd:COG0031    1 MRIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAvppHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVT 160
Cdd:COG0031   81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYET 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 161 TGPEIWADTEGKVTHFVagigtggtitgagRYLKEVSGGrVRIVGADPEGS-VYSGGAGRPYLVEGVGEDFWPAAYDPSV 239
Cdd:COG0031  158 TGPEIWEQTDGKVDAFVagvgtggtitgvgRYLKERNPD-IKIVAVEPEGSpLLSGGEPGPHKIEGIGAGFVPKILDPSL 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685917698 240 PDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSK 304
Cdd:COG0031  237 IDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 12-303 5.32e-125

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: 364.91  E-value: 5.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRRGYKCV 91
Cdd:cd01561    1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  92 FVCPDKVSEDKRNVLIAYGAEVVVCPTAvPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTGPEIWADTEG 171
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEA-EADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 172 KVTHFVAGIGTGGTITGAGRYLKEVSGGrVRIVGADPEGSV-YSGGAGRPYLVEGVGEDFWPAAYDPSVPDEIIAVSDSD 250
Cdd:cd01561  160 KVDAFVAGVGTGGTITGVARYLKEKNPN-VRIVGVDPVGSVlFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685917698 251 SFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMS 303
Cdd:cd01561  239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
PRK10717 PRK10717
cysteine synthase A; Provisional
 1-316 1.47e-101

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 306.79  E-value: 1.47e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLA 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPtAVPPHDPASYYSVSDRL-----VRDIDGAWKPDQYANPEGPA 155
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVP-AAPYANPNNYVKGAGRLaeelvASEPNGAIWANQFDNPANRE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 156 SHYVTTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEVSGGrVRIVGADPEGS-VYS---GG---AGRPYLVEGVGE 228
Cdd:PRK10717 160 AHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK-VKIVLADPTGSaLYSyykTGelkAEGSSITEGIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 229 DFWPAAYDPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSKIFND 308
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNP 318


                 ....*...
gi 685917698 309 AWMSSYGF 316
Cdd:PRK10717 319 DFLREKGL 326
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 7-296 8.68e-61

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: 200.23  E-value: 8.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    7 ISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEasgQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTavpphDPASYYSVSDRLVRDIDGAWKPDQYANPEGPAShYVTTGPEIW 166
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG-----DYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEIL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  167 ADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADPEGSV----------YSGGAGRPYLVEGVGEDFWPAAYD 236
Cdd:pfam00291 152 EQLGGDPDAVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPalarslaagrPVPVPVADTIADGLGVGDEPGALA 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685917698  237 PSV----PDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAA-LKVAEEAGPDALIVVLLPD 296
Cdd:pfam00291 231 LDLldeyVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 348-395 6.69e-05

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: 40.19  E-value: 6.69e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 685917698   348 HPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAV 395
Cdd:smart00116   6 SPDTTLEEALELLRENGIRRLPVVDEE-----GRLVGIVTRRDIIKAL 48
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 3-458 0e+00

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: 711.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    3 IAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALV 82
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   83 AQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAVPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTG 162
Cdd:TIGR01137  81 AAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  163 PEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADPEGSVYSGG-----AGR-PYLVEGVGEDFWPAAYD 236
Cdd:TIGR01137 161 PEILEQCEGKLDMFVAGVGTGGTITGIARYLKE-SCPGCRIVGADPEGSILAQPeelnqTGRtPYKVEGIGYDFIPTVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  237 PSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDA-LIVVLLPDGGRGYMSKIFNDAWMSSYG 315
Cdd:TIGR01137 240 RKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGqRCVVLLPDSIRNYMTKFLNDEWMLDNG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  316 FLRSrldgstEQSTVGDVL----RRKSGALPALVHTHPSETVRDAIGILREYGVSQMPVVGaeppvMAGEVAGSVSEREL 391
Cdd:TIGR01137 320 FLDD------EDLTVKDVLwwhaRVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVD-----EAGKVLGSVTLREL 388

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685917698  392 LSAVFEGRAKLADAVSAHMSPPLRMIGAGELVSAAGKALRDWDALMVVEEGKPVGVITRYDLLGFLS 458
Cdd:TIGR01137 389 LSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKPIGVVTKIDLLSFLA 455
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 1-304 2.03e-147

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: 422.15  E-value: 2.03e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLA 80
Cdd:COG0031    1 MRIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAvppHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVT 160
Cdd:COG0031   81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYET 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 161 TGPEIWADTEGKVTHFVagigtggtitgagRYLKEVSGGrVRIVGADPEGS-VYSGGAGRPYLVEGVGEDFWPAAYDPSV 239
Cdd:COG0031  158 TGPEIWEQTDGKVDAFVagvgtggtitgvgRYLKERNPD-IKIVAVEPEGSpLLSGGEPGPHKIEGIGAGFVPKILDPSL 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685917698 240 PDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSK 304
Cdd:COG0031  237 IDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 12-303 5.32e-125

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: 364.91  E-value: 5.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRRGYKCV 91
Cdd:cd01561    1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  92 FVCPDKVSEDKRNVLIAYGAEVVVCPTAvPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTGPEIWADTEG 171
Cdd:cd01561   81 IVMPETMSEEKRKLLRALGAEVILTPEA-EADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 172 KVTHFVAGIGTGGTITGAGRYLKEVSGGrVRIVGADPEGSV-YSGGAGRPYLVEGVGEDFWPAAYDPSVPDEIIAVSDSD 250
Cdd:cd01561  160 KVDAFVAGVGTGGTITGVARYLKEKNPN-VRIVGVDPVGSVlFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685917698 251 SFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMS 303
Cdd:cd01561  239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 7-303 2.94e-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: 307.29  E-value: 2.94e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    7 ISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVCP------TAVpphdpasyySVSDRLVRDIDGAWKPDQYANPEGPASHYVT 160
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPgeegmkGAI---------DKAEELAAETNKYVMLDQFENPANPEAHYKT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  161 TGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEVSgGRVRIVGADP-EGSVYSGGAGRPYLVEGVGEDFWPAAYDPSV 239
Cdd:TIGR01136 152 TGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQN-PNIQIVAVEPaESPVLSGGEPGPHKIQGIGAGFIPKILDLSL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685917698  240 PDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAG-PDALIVVLLPDGGRGYMS 303
Cdd:TIGR01136 231 IDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
PRK10717 PRK10717
cysteine synthase A; Provisional
 1-316 1.47e-101

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 306.79  E-value: 1.47e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLA 80
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPtAVPPHDPASYYSVSDRL-----VRDIDGAWKPDQYANPEGPA 155
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVP-AAPYANPNNYVKGAGRLaeelvASEPNGAIWANQFDNPANRE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 156 SHYVTTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEVSGGrVRIVGADPEGS-VYS---GG---AGRPYLVEGVGE 228
Cdd:PRK10717 160 AHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPK-VKIVLADPTGSaLYSyykTGelkAEGSSITEGIGQ 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 229 DFWPAAYDPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSKIFND 308
Cdd:PRK10717 239 GRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNP 318


                 ....*...
gi 685917698 309 AWMSSYGF 316
Cdd:PRK10717 319 DFLREKGL 326
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 7-303 3.83e-98

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: 296.59  E-value: 3.83e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    7 ISELIGGTPLVRLNYVVPDGaGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCN-ANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAVppHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTTGPEIW 166
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAE--GMKGAIAKAEEIAASTPNSYFMLQQFENPANPEIHRKTTGPEIW 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  167 ADTEGKVTHFVAGIGTGGTITGAGRYLKEVSgGRVRIVGADPEGS-VYSGGAGRPYLVEGVGEDFWPAAYDPSVPDEIIA 245
Cdd:TIGR01139 158 RDTDGKLDAFVAGVGTGGTITGVGEVLKEQK-PNIKIVAVEPAESpVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVIT 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 685917698  246 VSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMS 303
Cdd:TIGR01139 237 VSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
cysM PRK11761
cysteine synthase CysM;
7-303 2.53e-79

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 248.25  E-value: 2.53e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   7 ISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:PRK11761   6 LEDTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTAVP---PHDPAsyysvsDRLVRDIDGAwKPDQYANPEGPASHYVTTGP 163
Cdd:PRK11761  86 GYRMKLIMPENMSQERRAAMRAYGAELILVPKEQGmegARDLA------LQMQAEGEGK-VLDQFANPDNPLAHYETTGP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 164 EIWADTEGKVTHFVAGIGTGGTITGAGRYLKEVSgGRVRIVGADP-EGSVYSGGAGRPylvegvgEDFWPAAYDPSVPDE 242
Cdd:PRK11761 159 EIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQN-PAVQIVGLQPeEGSSIPGIRRWP-------EEYLPKIFDASRVDR 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685917698 243 IIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAgPDALIVVLLPDGGRGYMS 303
Cdd:PRK11761 231 VLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLS 290
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
 7-310 1.31e-75

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


Pssm-ID: 274872 [Multi-domain]  Cd Length: 304  Bit Score: 239.03  E-value: 1.31e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    7 ISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVcptaVPPHDPASYYSVS-----DRLVRDIDGAWKPDQYANPEGPASHYVTT 161
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEK----VTEPDETGGYLGTriarvRELLASIPDAYWPNQYANPDNPRAHYHGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  162 GPEIwADTEGKVTHFVAGIGTGGTITGAGRYLKEVsGGRVRIVGADPEGSVYSGGAGRPYLVEGVGEDFWPAAYDPSVPD 241
Cdd:TIGR03945 157 GREI-ARAFPTLDYLFVGVSTTGTLMGCSRRLRER-GPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLID 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685917698  242 EIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSKIFNDAW 310
Cdd:TIGR03945 235 DVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
PLN02565 PLN02565
cysteine synthase
 2-309 5.52e-68

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 220.18  E-value: 5.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   2 RIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTI-VEPTSGNTGVGLA 80
Cdd:PLN02565   4 SIAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCptavpphDPA----SYYSVSDRLVRDIDGAWKPDQYANPEGPAS 156
Cdd:PLN02565  84 FMAAAKGYKLIITMPASMSLERRIILLAFGAELVLT-------DPAkgmkGAVQKAEEILAKTPNSYILQQFENPANPKI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 157 HYVTTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADP-EGSVYSGGAGRPYLVEGVGEDFWPAAY 235
Cdd:PLN02565 157 HYETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKE-QNPDIKLYGVEPvESAVLSGGKPGPHKIQGIGAGFIPGVL 235

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685917698 236 DPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVA---EEAGpdALIVVLLPDGGRGYMSKIFNDA 309
Cdd:PLN02565 236 DVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAkrpENAG--KLIVVIFPSFGERYLSSVLFES 310
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 7-303 8.72e-67

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: 215.93  E-value: 8.72e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    7 ISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:TIGR01138   2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVcptAVPPHDPASYYSVSDRLVRDIDGAWKpDQYANPEGPASHYVTTGPEIW 166
Cdd:TIGR01138  82 GYRMKLLMPDNMSQERKAAMRAYGAELIL---VTKEEGMEGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEIW 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  167 ADTEGKVTHFVAGIGTGGTITGAGRYLKEVSGGrVRIVGADPEgsvysggagRPYLVEGVG---EDFWPAAYDPSVPDEI 243
Cdd:TIGR01138 158 QQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPP-VQIVGLQPE---------EGSSIPGIRrwpTEYLPGIFDASLVDRV 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  244 IAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAgPDALIVVLLPDGGRGYMS 303
Cdd:TIGR01138 228 LDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLAREL-PDAVVVAIICDRGDRYLS 286
PLN00011 PLN00011
cysteine synthase
 3-303 2.26e-65

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 213.33  E-value: 2.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   3 IAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPG-GTIVEPTSGNTGVGLAL 81
Cdd:PLN00011   7 IKNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLAC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  82 VAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPtavPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYVTT 161
Cdd:PLN00011  87 IGAARGYKVILVMPSTMSLERRIILRALGAEVHLTD---QSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 162 GPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADP-EGSVYSGGAGRPYLVEGVGEDFWPAAYDPSVP 240
Cdd:PLN00011 164 GPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKE-KNKDIKVCVVEPvESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIV 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685917698 241 DEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVA---EEAGpdALIVVLLPDGGRGYMS 303
Cdd:PLN00011 243 DEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAkrpENAG--KLIVVIFPSGGERYLS 306
PLN03013 PLN03013
cysteine synthase
 1-306 1.41e-62

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 209.25  E-value: 1.41e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTI-VEPTSGNTGVGL 79
Cdd:PLN03013 111 LNIADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  80 ALVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPtavPPHDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYV 159
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTD---PAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYE 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 160 TTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADP-EGSVYSGGAGRPYLVEGVGEDFWPAAYDPS 238
Cdd:PLN03013 268 TTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKE-KNPKTQVIGVEPtESDILSGGKPGPHKIQGIGAGFIPKNLDQK 346

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685917698 239 VPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVA---EEAGpdALIVVLLPDGGRGYMSKIF 306
Cdd:PLN03013 347 IMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAkrpENAG--KLIAVSLFASGRDIYTPRC 415
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 7-296 8.68e-61

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: 200.23  E-value: 8.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698    7 ISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEasgQLKPGGTIVEPTSGNTGVGLALVAQRR 86
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLK---EGEGGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   87 GYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTavpphDPASYYSVSDRLVRDIDGAWKPDQYANPEGPAShYVTTGPEIW 166
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG-----DYDEAVAAARELAAEGPGAYYINQYDNPLNIEG-YGTIGLEIL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  167 ADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADPEGSV----------YSGGAGRPYLVEGVGEDFWPAAYD 236
Cdd:pfam00291 152 EQLGGDPDAVVVPVGGGGLIAGIARGLKE-LGPDVRVIGVEPEGAPalarslaagrPVPVPVADTIADGLGVGDEPGALA 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685917698  237 PSV----PDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAA-LKVAEEAGPDALIVVLLPD 296
Cdd:pfam00291 231 LDLldeyVGEVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 14-297 5.73e-59

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: 193.89  E-value: 5.73e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  14 TPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGqLKPGGTIVEPTSGNTGVGLALVAQRRGYKCVFV 93
Cdd:cd00640    1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEG-KLPKGVIIESTGGNTGIALAAAAARLGLKCTIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  94 CPDKVSEDKRNVLIAYGAEVVVCPTavpphDPASYYSVSDRLVRDIDGAWKPDQYANPEGPASHYvTTGPEIWADTEG-K 172
Cdd:cd00640   80 MPEGASPEKVAQMRALGAEVVLVPG-----DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 173 VTHFVAGIGTGGTITGAGRYLKEVsGGRVRIVGADPegsvysggagrpylvegvgedfwpaaydpsvpdEIIAVSDSDSF 252
Cdd:cd00640  154 PDAVVVPVGGGGNIAGIARALKEL-LPNVKVIGVEP---------------------------------EVVTVSDEEAL 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 685917698 253 DMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDG 297
Cdd:cd00640  200 EAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 2-308 8.58e-57

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 192.10  E-value: 8.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   2 RIAQHISELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGT-IVEPTSGNTGVGLA 80
Cdd:PLN02556  48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCptavpphDPASYYSVSDR----LVRDIDGAWKPDQYANPEGPAS 156
Cdd:PLN02556 128 FMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLT-------DPTKGMGGTVKkayeLLESTPDAFMLQQFSNPANTQV 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 157 HYVTTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEvSGGRVRIVGADP-EGSVYSGGAGRPYLVEGVGEDFWPAAY 235
Cdd:PLN02556 201 HFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKS-KNPNVKIYGVEPaESNVLNGGKPGPHHITGNGVGFKPDIL 279

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685917698 236 DPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVA---EEAGpdALIVVLLPDGGRGYMSKIFND 308
Cdd:PLN02556 280 DMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAkmpENKG--KLIVTVHPSFGERYLSSVLFQ 353
PLN02356 PLN02356
phosphateglycerate kinase
 9-316 1.96e-43

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 158.23  E-value: 1.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   9 ELIGGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGGTIVEPTSGNTGVGLALVAQRRGY 88
Cdd:PLN02356  49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGC 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  89 KCVFVCPDKVSEDKRNVLIAYGAEVV-VCPTAVPPHD-----------PASYYSVSDRLVRDID---------------- 140
Cdd:PLN02356 129 KCHVVIPDDVAIEKSQILEALGATVErVRPVSITHKDhyvniarrralEANELASKRRKGSETDgihlektngciseeek 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 141 ----------GAWKPDQYANPEGPASHYVTTGPEIWADTEGKVTHFVAGIGTGGTITGAGRYLKEVSgGRVRIVGADPEG 210
Cdd:PLN02356 209 enslfsssctGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKN-PNIKCFLIDPPG 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 211 S-----VYSG-------GAGR----PY--LVEGVGEDFWPAAYDPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGM 272
Cdd:PLN02356 288 SglfnkVTRGvmytreeAEGRrlknPFdtITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAM 367

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 685917698 273 AVVAALKVAEEAGPDALIVVLLPDGGRGYMSKIFNDAWMSSYGF 316
Cdd:PLN02356 368 NCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 334-456 5.44e-32

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: 118.40  E-value: 5.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 334 LRRKSGALPALVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAKLADAVSAHMSPP 413
Cdd:cd04608    2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDED-----GRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQ 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 685917698 414 LRMIGAGELVSAAGKAL-RDWDALMVVEEGKPVGVITRYDLLGF 456
Cdd:cd04608   77 FKQVDLDTPLGALSRILeRDHFALVVDGQGKVLGIVTRIDLLNY 120
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 330-459 2.03e-17

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 77.95  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 330 VGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAKLADA-VSA 408
Cdd:COG2905    1 VKDIMSRD------VVTVSPDATVREAARLMTEKGVGSLVVVDDD-----GRLVGIITDRDLRRRVLAEGLDPLDTpVSE 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685917698 409 HMSPPLRMIGAGELVSAAGKALRDW--DALMVVEEGKPVGVITRYDLLGFLSE 459
Cdd:COG2905   70 VMTRPPITVSPDDSLAEALELMEEHriRHLPVVDDGKLVGIVSITDLLRALSE 122
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
243-454 1.99e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 74.92  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 243 IIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAGPDALIVVLLPDGGRGYMSKIFNDAWMSSYGFLRSRLD 322
Cdd:COG2524    1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 323 GSTEQSTVGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAeppvmaGEVAGSVSERELLSAVFEGRAKL 402
Cdd:COG2524   81 GLVLKMKVKDIMTKD------VITVSPDTTLEEALELMLEKGISGLPVVDD------GKLVGIITERDLLKALAEGRDLL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 685917698 403 ADAVSAHMSPPLRMIGAGELVSAAGKALR--DWDALMVVE-EGKPVGVITRYDLL 454
Cdd:COG2524  149 DAPVSDIMTRDVVTVSEDDSLEEALRLMLehGIGRLPVVDdDGKLVGIITRTDIL 203
CBS COG0517
CBS domain [Signal transduction mechanisms];
329-459 4.37e-15

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 71.82  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 329 TVGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVF-EGRAKLADAVS 407
Cdd:COG0517    2 KVKDIMTTD------VVTVSPDATVREALELMSEKRIGGLPVVDED-----GKLVGIVTDRDLRRALAaEGKDLLDTPVS 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 685917698 408 AHMSPPLRMIGAGELVSAAGKALRDWD--ALMVVEE-GKPVGVITRYDLLGFLSE 459
Cdd:COG0517   71 EVMTRPPVTVSPDTSLEEAAELMEEHKirRLPVVDDdGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 344-454 1.56e-14

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: 69.58  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 344 LVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAKLADAVSAHMSPPLRMIGAGELV 423
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDD-----GKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDL 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 685917698 424 SAAGKALRDWD--ALMVV-EEGKPVGVITRYDLL 454
Cdd:cd02205   79 EEALELMLEHGirRLPVVdDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
329-464 5.07e-14

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 68.74  E-value: 5.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 329 TVGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAK------L 402
Cdd:COG3448    3 TVRDIMTRD------VVTVSPDTTLREALELMREHGIRGLPVVDED-----GRLVGIVTERDLLRALLPDRLDeleerlL 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685917698 403 ADAVSAHMSPPLRMIGAGELVSAAGKALRDWD--ALMVV-EEGKPVGVITRYDLLGFLSEGAGRR 464
Cdd:COG3448   72 DLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGihRLPVVdDDGRLVGIVTRTDLLRALARLLEEE 136
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 12-115 7.31e-13

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: 69.16  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRL-NYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQlkpgGTIVEPTSGNTGVGLALVAQRRGYKC 90
Cdd:cd01563   21 GNTPLVRApRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96

                         90       100
                 ....*....|....*....|....*
gi 685917698  91 VFVCPDKVSEDKRNVLIAYGAEVVV 115
Cdd:cd01563   97 VVFLPAGKALGKLAQALAYGATVLA 121
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 330-454 7.34e-11

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: 58.49  E-value: 7.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 330 VGDVLRRKsgalpaLVHTHPSETVRDAIGILREY-GVSQMPVVgaeppvmagEVAGsVSERELlsavfegraklADAVSA 408
Cdd:COG3620    1 VRDLMSRD------VVTVSPDDTLGEALRLMRKElGLSQLPVA---------ELVG-VSQSDI-----------LRIESG 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 685917698 409 HMSPPLRMIGagELVSAAGKALrdwDALMVVEEGKPVGVITRYDLL 454
Cdd:COG3620   54 KRDPTVSTLE--KIAEALGKEL---SAVLVVDDGKLVGIITRRDLL 94
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 12-115 2.30e-10

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: 62.14  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLkpggTIVEPTSGNTGVGLALVAQRRGYKC- 90
Cdd:COG0498   65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEVf 140

                         90       100
                 ....*....|....*....|....*
gi 685917698  91 VFVCPDKVSEDKRNVLIAYGAEVVV 115
Cdd:COG0498  141 VFVPEGKVSPGQLAQMLTYGAHVIA 165
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-457 8.49e-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: 56.66  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 345 VHT-HPSETVRDAIGILREYGVSQMPVVGAeppvmaGEVAGSVSERELLSA---------VFEGRAKLAD-AVSAHMSPP 413
Cdd:cd04584   10 VVTvTPDTSLAEARELMKEHKIRHLPVVDD------GKLVGIVTDRDLLRAspskatslsIYELNYLLSKiPVKDIMTKD 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 685917698 414 LRMIGAGELVSAAGKALRDWD--ALMVVEEGKPVGVITRYDLLGFL 457
Cdd:cd04584   84 VITVSPDDTVEEAALLMLENKigCLPVVDGGKLVGIITETDILRAF 129
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-454 1.57e-09

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: 55.20  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 345 VHT-HPSETVRDAIGILREYGVSQMPVVGAeppvmaGEVAGSVSERELLSAVfegRAKLADA-VSAHMSPPLRMIGAGEL 422
Cdd:cd04595    4 VKTvSPDTTIEEARKIMLRYGHTGLPVVED------GKLVGIISRRDVDKAK---HHGLGHApVKGYMSTNVITIDPDTS 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 685917698 423 VSAAGKALRDWDA--LMVVEEGKPVGVITRYDLL 454
Cdd:cd04595   75 LEEAQELMVEHDIgrLPVVEEGKLVGIVTRSDVL 108
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 345-453 4.28e-09

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: 53.96  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 345 VHT-HPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFE-GRAKLADAVSAHMSPPLRMIGAGEL 422
Cdd:cd04623    4 VVTvSPDATVAEALRLLAEKNIGALVVVDDG-----GRLVGILSERDYVRKLALrGASSLDTPVSEIMTRDVVTCTPDDT 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685917698 423 VSAAGkalrdwdALM---------VVEEGKPVGVITRYDL 453
Cdd:cd04623   79 VEECM-------ALMterrirhlpVVEDGKLVGIVSIGDV 111
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 345-454 6.80e-09

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: 53.97  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 345 VHT-HPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSE---------------RELLSAVFEGRAKLA-DAVS 407
Cdd:cd04586    5 VVTvTPDTSVREAARLLLEHRISGLPVVDDD-----GKLVGIVSEgdllrreepgteprrVWWLDALLESPERLAeEYVK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685917698 408 AH-------MSPPLRMIGAGELVSAAGKAL--RDWDALMVVEEGKPVGVITRYDLL 454
Cdd:cd04586   80 AHgrtvgdvMTRPVVTVSPDTPLEEAARLMerHRIKRLPVVDDGKLVGIVSRADLL 135
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 12-114 1.01e-08

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 56.62  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   12 GGTPLVRLNYVV-PDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLkpggTIVEPTSGNTGVGLALVAQRRGYKC 90
Cdd:TIGR00260  21 GVTPLFRAPALAaNVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGND----TVLCASTGNTGAAAAAYAGKAGLKV 96

                          90       100
                  ....*....|....*....|....*
gi 685917698   91 VFVCP-DKVSEDKRNVLIAYGAEVV 114
Cdd:TIGR00260  97 VVLYPaGKISLGKLAQALGYNAEVV 121
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 347-458 1.18e-08

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: 52.91  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 347 THPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAkLADAVSAHMSPPLRMIGAGELVSAA 426
Cdd:cd09836    8 VPPETTIREAAKLMAENNIGSVVVVDDD-----GKPVGIVTERDIVRAVAEGID-LDTPVEEIMTKNLVTVSPDESIYEA 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685917698 427 GKALRDWDA--LMVVE-EGKPVGVITRYDLLGFLS 458
Cdd:cd09836   82 AELMREHNIrhLPVVDgGGKLVGVISIRDLARELS 116
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 2-293 2.04e-08

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: 55.81  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   2 RIAQHISEliggTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIA-VKMIEAAEASGQLkpggTIVEPTSGNTGVGLA 80
Cdd:COG1171   17 RIAGVVRR----TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAyNALASLSEEERAR----GVVAASAGNHAQGVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTavpphdpasYYSVSDRLVRdidgawkpdQYANPEG-----PA 155
Cdd:COG1171   89 YAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGD---------TYDDAEAAAA---------ELAEEEGatfvhPF 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 156 SH------YVTTGPEIWADTeGKVTH-FVAgigtggtitgagrylkeVSGG---------------RVRIVGADPEG--S 211
Cdd:COG1171  151 DDpdviagQGTIALEILEQL-PDLDAvFVP-----------------VGGGgliagvaaalkalspDIRVIGVEPEGaaA 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 212 VY-SGGAGRPYLVEG------------VGEDFWPAAYDpsVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAAL 278
Cdd:COG1171  213 MYrSLAAGEPVTLPGvdtiadglavgrPGELTFEILRD--LVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALL 290

                        330
                 ....*....|....*
gi 685917698 279 KVAEEAGPDALIVVL 293
Cdd:COG1171  291 AGKERLKGKRVVVVL 305
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 348-454 2.45e-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: 52.05  E-value: 2.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 348 HPSETVRDAIGILREYGVSQMPVVGAeppvmAGEVAGSVSERELLSAVFEGR--AKLADAVSAHMSPPLRMIGAGE-LVS 424
Cdd:cd04629    9 TPDTSILEAVELLLEHKISGAPVVDE-----QGRLVGFLSEQDCLKALLEASyhCEPGGTVADYMSTEVLTVSPDTsIVD 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685917698 425 AAgkalrdwdALM---------VVEEGKPVGVITRYDLL 454
Cdd:cd04629   84 LA--------QLFlknkprrypVVEDGKLVGQISRRDVL 114
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 ...
 343-454 5.13e-08

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: 50.89  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 343 ALVHTHPSETVRDAIGILREYGVSQMPVVGAEPPVmagevaGSVSERELLSAVFEGRAKLADAVSAHMSPPLRMIGAGEL 422
Cdd:cd04587    5 PPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLV------GIVTDRDLRNRVVAEGLDPDTPVSEIMTPPPVTIDADAL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 685917698 423 VSaagkalrdwDALM-----------VVEEGKPVGVITRYDLL 454
Cdd:cd04587   79 VF---------EALLlmlernihhlpVVDDGRVVGVVTATDLM 112
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 2-293 2.99e-07

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: 52.10  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   2 RIAQHISEliggTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASgQLKPGgtIVEPTSGNTGVGLAL 81
Cdd:cd01562   10 RIKPVVRR----TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEE-ERAKG--VVAASAGNHAQGVAY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  82 VAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCptavpPHDPASYYSVSDRLVRDIDGAWKPdqyanpegPASHYV-- 159
Cdd:cd01562   83 AAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLY-----GEDFDEAEAKARELAEEEGLTFIH--------PFDDPDvi 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 160 ----TTGPEIWADTEGKVTHFVAgigtggtitgagrylkeVSGG---------------RVRIVGADPEGS---VYSGGA 217
Cdd:cd01562  150 agqgTIGLEILEQVPDLDAVFVP-----------------VGGGgliagiatavkalspNTKVIGVEPEGApamAQSLAA 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 218 GRPYLVEG------------VGEDFWPAAYDpsVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEEAG 285
Cdd:cd01562  213 GKPVTLPEvdtiadglavkrPGELTFEIIRK--LVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLK 290


                 ....*...
gi 685917698 286 PDALIVVL 293
Cdd:cd01562  291 GKKVVVVL 298
PRK06608 PRK06608
serine/threonine dehydratase;
2-118 9.98e-07

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 50.54  E-value: 9.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   2 RIAQHISEliggTPLVR---LNYVVpdgAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGqlKPGGTIVEPTSGNTGVG 78
Cdd:PRK06608  16 RIKQYLHL----TPIVHsesLNEML---GHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 685917698  79 LALVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPT 118
Cdd:PRK06608  87 VAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNT 126
PRK08246 PRK08246
serine/threonine dehydratase;
2-119 1.31e-06

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 49.95  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   2 RIAQHISEliggTPLVRLNyVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEAsgqlkPGGTIVEPTSGNTGVGLAL 81
Cdd:PRK08246  16 RIAPHIRR----TPVLEAD-GAGFGPAPVWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAY 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685917698  82 VAQRRGYKC-VFVcPDKVSEDKRNVLIAYGAEVVVCPTA 119
Cdd:PRK08246  86 AAAALGVPAtVFV-PETAPPAKVARLRALGAEVVVVGAE 123
PRK06450 PRK06450
threonine synthase; Validated
 6-114 1.67e-06

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 49.73  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   6 HISELI----GGTPLVRlnyvvpdgAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQlkpgGTIVEPTSGNTGVGLAL 81
Cdd:PRK06450  47 YIKHFIslgeGRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAA 114

                         90       100       110
                 ....*....|....*....|....*....|...
gi 685917698  82 VAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVV 114
Cdd:PRK06450 115 YGAAAGIEVKIFVPETASGGKLKQIESYGAEVV 147
PRK06381 PRK06381
threonine synthase; Validated
 12-114 1.70e-06

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 49.70  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRLNYVVPD-GAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQlkpgGTIVEPTSGNTGVGLALVAQRRGYKC 90
Cdd:PRK06381  14 GGTPLLRARKLEEElGLRKIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKA 89

                         90       100
                 ....*....|....*....|....
gi 685917698  91 VFVCPDKVSEDKRNVLIAYGAEVV 114
Cdd:PRK06381  90 VIFIPRSYSNSRVKEMEKYGAEII 113
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
317-459 2.03e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 46.83  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 317 LRSRLDGSTEQSTVGDVLRRKSgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAvf 396
Cdd:COG4109    5 ISTSYDTFKEILLVEDIMTLED-----VATLSEDDTVEDALELLEKTGHSRFPVVDEN-----GRLVGIVTSKDILGK-- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685917698 397 eGRAKLADAVsahMSPPLRMIGAGELVSAAGKAL--RDWDALMVVEE-GKPVGVITRYDLLGFLSE 459
Cdd:COG4109   73 -DDDTPIEDV---MTKNPITVTPDTSLASAAHKMiwEGIELLPVVDDdGRLLGIISRQDVLKALQK 134
PRK08197 PRK08197
threonine synthase; Validated
 12-113 2.51e-06

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 49.61  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRLNYVVPD-GAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKpggtIVEPTSGNTGVGLALVAQRRGYKC 90
Cdd:PRK08197  78 GMTPLLPLPRLGKAlGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRA 153

                         90       100
                 ....*....|....*....|...
gi 685917698  91 VFVCPDKVSEDKRNVLIAYGAEV 113
Cdd:PRK08197 154 TIFMPADAPEITRLECALAGAEL 176
PRK05638 PRK05638
threonine synthase; Validated
 12-115 2.61e-06

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 49.43  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  12 GGTPLVRLNYVVPDGAgTVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQlkpGGTIVePTSGNTGVGLALVAQRRGYKCV 91
Cdd:PRK05638  65 GGTPLIRARISEKLGE-NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA---NGFIV-ASDGNAAASVAAYSARAGKEAF 139

                         90       100
                 ....*....|....*....|....
gi 685917698  92 FVCPDKVSEDKRNVLIAYGAEVVV 115
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIR 163
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 330-397 4.06e-06

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: 44.13  E-value: 4.06e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685917698  330 VGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFE 397
Cdd:pfam00571   1 VKDIMTKD------VVTVSPDTTLEEALELMREHGISRLPVVDED-----GKLVGIVTLKDLLRALLG 57
PRK06815 PRK06815
threonine/serine dehydratase;
1-283 4.51e-06

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 48.54  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISEliggTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMIEAAEASgQLKPGgtIVEPTSGNTGVGLA 80
Cdd:PRK06815  12 QRLRPQVRV----TPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEA-QRQQG--VITASSGNHGQGVA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  81 LVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVVCPTavpphDPASYYSVSDRLVRDiDGAWKPDQYANPEGPASHYvT 160
Cdd:PRK06815  85 LAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGG-----DALNAELAARRAAEQ-QGKVYISPYNDPQVIAGQG-T 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 161 TGPEIWADTEGKVTHFVAGIGTGGTITGAGrYLKEVSgGRVRIVGADPEGSV---YSGGAGRPYLVE-----------GV 226
Cdd:PRK06815 158 IGMELVEQQPDLDAVFVAVGGGGLISGIAT-YLKTLS-PKTEIIGCWPANSPslyTSLEAGEIVEVAeqptlsdgtagGV 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 685917698 227 GEDFWPAAYDPSVPDEIIAVSDSDSFDMTRRLAREEAMLVGGSCGMAVVAALKVAEE 283
Cdd:PRK06815 236 EPGAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPR 292
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 342-453 2.74e-05

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: 43.37  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 342 PALVHTHPSETVRDAIGILREYGVSQMPVVgaeppvMAGEVAGSVSERELLSAVFEGRAKLADAVSAHMSPPLRMIGAGE 421
Cdd:cd09833    5 TSLLTCSPDTPLADAAARMAERRCSSILIV------ENGEIVGIWTERDALKLDFSDPDAFRRPISEVMSSPVLTIPQDT 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 685917698 422 LVSAAGKALRDWDA--LMVV-EEGKPVGVITRYDL 453
Cdd:cd09833   79 TLGEAAVRFRQEGVrhLLVVdDDGRPVGIVSQTDV 113
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 348-395 6.69e-05

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: 40.19  E-value: 6.69e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 685917698   348 HPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAV 395
Cdd:smart00116   6 SPDTTLEEALELLRENGIRRLPVVDEE-----GRLVGIVTRRDIIKAL 48
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
330-463 2.15e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 42.56  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 330 VGDVLRRKSGALPALVHTHPSETVRDAIGILREYGVSqMPVVGAEPPVMAGEVAGSVSERELLSAVFEGRAKLADAVSAH 409
Cdd:COG2524   13 LPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAA-AAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDI 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685917698 410 MSPPLRMIGAGELVSAAGKALRD--WDALMVVEEGKPVGVITRYDLLGFLSEGAGR 463
Cdd:COG2524   92 MTKDVITVSPDTTLEEALELMLEkgISGLPVVDDGKLVGIITERDLLKALAEGRDL 147
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 345-454 4.37e-04

CBS domain protein; 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 39.99  E-value: 4.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 345 VHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAKLADAVSAHMSPPLRMIGAGELVS 424
Cdd:cd17771    7 VTCSPDTPLRAALETMHERRVGSMVVVDAN-----RRPVGIFTLRDLLSRVALPQIDLDAPISEVMTPDPVRLPPSASAF 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 685917698 425 AAGKAL--RDWDALMVVEEGKPVGVITRYDLL 454
Cdd:cd17771   82 EAALLMaeHGFRHVCVVDNGRLVGVVSERDLF 113
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 53-115 4.89e-04

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 42.17  E-value: 4.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685917698  53 EAAEASGQLkpggTIVEPTSGNTGVGLALVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVV 115
Cdd:PRK08206 109 EVREKLGDI----TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECII 167
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 348-454 5.93e-04

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: 39.32  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 348 HPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLsavFEgrAKLADAVSAHMSPPLRMIGAGELVSA-- 425
Cdd:cd04601    8 SPDATVADVLELKAEYGISGVPVTEDG-----GKLVGIVTSRDIR---FE--TDLSTPVSEVMTPDERLVTAPEGITLee 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 685917698 426 AGKALRDW--DALMVV-EEGKPVGVITRYDLL 454
Cdd:cd04601   78 AKEILHKHkiEKLPIVdDNGELVGLITRKDIE 109
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 349-454 6.38e-04

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: 39.62  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 349 PSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELLSAVFEGRAK-------------LADAVSAHMSPPLR 415
Cdd:cd04632    9 EDDTIGKAINLLREHGISRLPVVDDN-----GKLVGIVTTYDIVDFVVRPGTKtrggdrggekermLDLPVYDIMSSPVV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685917698 416 MIGAGELVSAAGKALRDWD--ALMVV-EEGKPVGVITRYDLL 454
Cdd:cd04632   84 TVTRDATVADAVERMLENDisGLVVTpDDNMVIGILTKTDVL 125
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 349-456 1.03e-03

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: 38.70  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 349 PSETVRDAIGILREYGVSQMPVVGAEPpvmaGEVAGSVSERELLSAVFEGRAKLadAVSAHMSPplrmigagELVSAAGK 428
Cdd:cd17772    9 PDTTIAEAAELMTRYNINALPVVDGGT----GRLVGIITRQVAEKAIYHGLGDL--PVSEYMTT--------EFATVTPD 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 685917698 429 A-LRDWDALM---------VVEEGKPVGVITRYDLLGF 456
Cdd:cd17772   75 ApLSEIQEIIveqrqrlvpVVEDGRLVGVITRTDLLNL 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 406-459 1.14e-03

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: 37.19  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 685917698  406 VSAHMSPPLRMIGAGELVSAAGKALRDWD--ALMVV-EEGKPVGVITRYDLLGFLSE 459
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGisRLPVVdEDGKLVGIVTLKDLLRALLG 57
PRK08329 PRK08329
threonine synthase; Validated
 29-113 1.49e-03

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 40.58  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  29 TVAAKVEYLNPGGSSKDRIAVKMIeaaeasGQLKPGGT--IVEPTSGNTGVGLALVAQRRGYKCVFVCPDKVSEDKRNVL 106
Cdd:PRK08329  73 KVYFKLDYLQPTGSFKDRGTYVTV------AKLKEEGIneVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLL 146


                 ....*..
gi 685917698 107 IAYGAEV 113
Cdd:PRK08329 147 SRLGAEL 153
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 349-454 2.04e-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: 37.90  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 349 PSETVRDAIGILREYGVSqmpvvGAepPVMA-GEVAGSVSERELLSAVFEGraKLADAVSAHMSPPLRMIGAGELVSAAG 427
Cdd:cd04588    9 PDATIKDAAKLLSENNIH-----GA--PVVDdGKLVGIVTLTDIAKALAEG--KENAKVKDIMTKDVITIDKDEKIYDAI 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 685917698 428 KALRDWDA--LMVV-EEGKPVGVITRYDLL 454
Cdd:cd04588   80 RLMNKHNIgrLIVVdDNGKPVGIITRTDIL 109
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
1-115 2.29e-03

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 40.10  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698   1 MRIAQHISEliggTPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDRIAVKMI----EAAEASGqlkpggtIVEPTSGNTG 76
Cdd:PRK08638  19 QRLAGRIRK----TPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLssltDAEKRKG-------VVACSAGNHA 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685917698  77 VGLALVAQRRGYKCVFVCPDKVSEDKRNVLIAYGAEVVV 115
Cdd:PRK08638  88 QGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVL 126
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 342-454 2.79e-03

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: 37.32  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 342 PALVHTHPSETVRDAIGILREYGVSQMPVVGAeppvmaGEVAGSVSERELLSAvFEGRAkLADAVSAH---MSPPLRMIG 418
Cdd:cd04599    3 RNPITISPLDSVARAAALMERQRIGGLPVVEN------GKLVGIITSRDVRRA-HPNRL-VADAMSRNvvtISPEASLWE 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 685917698 419 AGELVSAAGKalrdwDALMVVEEGKPVGVITRYDLL 454
Cdd:cd04599   75 AKELMEEHGI-----ERLVVVEEGRLVGIITKSTLY 105
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 14-115 4.80e-03

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: 38.82  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  14 TPLVRLNYVVPDGAGTVAAKVEYLNPGGSSKDR-IAVKMIEAAEASGQLKPGgtIVEPTSGNTGVGLALVAQRRGYKCVF 92
Cdd:cd06448    2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTI 79

                         90       100
                 ....*....|....*....|...
gi 685917698  93 VCPDKVSEDKRNVLIAYGAEVVV 115
Cdd:cd06448   80 VVPESTKPRVVEKLRDEGATVVV 102
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 329-392 4.92e-03

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: 36.84  E-value: 4.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 685917698 329 TVGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSERELL 392
Cdd:cd02205   60 PVAEVMTPD------VITVSPDTDLEEALELMLEHGIRRLPVVDDD-----GKLVGIVTRRDIL 112
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 355-455 5.28e-03

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: 36.55  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 355 DAIGILREYGVSQMPVVGAEppvmAGEVAGSVSERELLsavfegRAKLADAVSAHMSPPLRMIGAGELVSAAGKALRDWD 434
Cdd:cd04638   16 DVLEILKKKAISGVPVVKKE----TGKLVGIVTRKDLL------RNPDEEQIALLMSRDPITISPDDTLSEAAELMLEHN 85

                         90       100
                 ....*....|....*....|...
gi 685917698 435 A--LMVVEEGKPVGVITRYDLLG 455
Cdd:cd04638   86 IrrVPVVDDDKLVGIVTVADLVR 108
PRK06110 PRK06110
threonine dehydratase;
29-114 5.40e-03

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 38.82  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698  29 TVAAKVEYLNPGGSSKDRIAVKMIEAAEASGQLKPGgtIVEPTSGNTGVGLALVAQRRGYKCVFVCPDKVSEDKRNVLIA 108
Cdd:PRK06110  37 EVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRA 114


                 ....*.
gi 685917698 109 YGAEVV 114
Cdd:PRK06110 115 LGAELI 120
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 329-394 6.13e-03

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: 37.02  E-value: 6.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685917698 329 TVGDVLRRKsgalpaLVHTHPSETVRDAIGILREYGVSQMPVVGaeppvmAGEVAGSVSERELLSA 394
Cdd:cd04584   75 PVKDIMTKD------VITVSPDDTVEEAALLMLENKIGCLPVVD------GGKLVGIITETDILRA 128
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 329-455 8.21e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 36.21  E-value: 8.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685917698 329 TVGDVLRRKSgALPaLVHthPSETVRDAIGILREYGVSQMPVVGAEppvmaGEVAGSVSE---RELLSAVFEGRAKLADA 405
Cdd:cd04604    4 RVSDLMHTGD-ELP-LVS--PDTSLKEALLEMTRKGLGCTAVVDED-----GRLVGIITDgdlRRALEKGLDILNLPAKD 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685917698 406 VsahMSPPLRMIGAGELVSAAGKALRDW--DALMVVEE-GKPVGVITRYDLLG 455
Cdd:cd04604   75 V---MTRNPKTISPDALAAEALELMEEHkiTVLPVVDEdGKPVGILHLHDLLR 124
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 410-449 9.67e-03

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: 35.86  E-value: 9.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 685917698 410 MSPPLRMIGAGELVSAAGKALRDWD--ALMVVEEGKPVGVIT 449
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDigALPVCEGDRLVGMVT 42
 
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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