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Conserved domains on  [gi|405778333|ref|NP_001258282|]
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cystathionine beta-synthase isoform 2 [Mus musculus]

Protein Classification

cystathionine beta-synthase( domain architecture ID 11490202)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
73-540 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: 783.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLA 152
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  153 LAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDD 232
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  233 TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  313 DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSDKWMLQK 391
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAeDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  392 GFMKEE-LSVKRPWWWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVR 470
Cdd:TIGR01137 319 GFLDDEdLTVKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  471 PSDEVCKVLYKQFKPIHLTDTLGTLSHILEMDHFALVVHEQIQycsngmsskqqmvFGVVTAIDLLNFVA 540
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKP-------------IGVVTKIDLLSFLA 455
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
73-540 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: 783.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLA 152
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  153 LAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDD 232
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  233 TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  313 DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSDKWMLQK 391
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAeDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  392 GFMKEE-LSVKRPWWWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVR 470
Cdd:TIGR01137 319 GFLDDEdLTVKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  471 PSDEVCKVLYKQFKPIHLTDTLGTLSHILEMDHFALVVHEQIQycsngmsskqqmvFGVVTAIDLLNFVA 540
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKP-------------IGVVTKIDLLSFLA 455
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
82-380 3.34e-165

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: 470.46  E-value: 3.34e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  82 GNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01561    1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQC 241
Cdd:cd01561   79 FIIVMPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 242 DGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWF 321
Cdd:cd01561  158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333 322 KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:cd01561  233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
72-381 1.45e-161

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: 461.44  E-value: 1.45e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  72 KILPDILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGL 151
Cdd:COG0031    2 RIYDSILELIGNTPLVRLNRLSPGPG--AEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYD 231
Cdd:COG0031   80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 232 DTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTV 311
Cdd:COG0031  157 TTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 312 LDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSK 381
Cdd:COG0031  232 LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
71-393 6.46e-117

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 348.77  E-value: 6.46e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  71 PKILPDILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIG 150
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 151 LALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASN 225
Cdd:PRK10717  79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPAN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 226 PLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEV----- 300
Cdd:PRK10717 158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAL-----YSYYKTGELKAegssi 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 301 -EGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYM 379
Cdd:PRK10717 233 tEGIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQ 312
                        330
                 ....*....|....
gi 405778333 380 SKFLSDKWMLQKGF 393
Cdd:PRK10717 313 SKLFNPDFLREKGL 326
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
77-373 2.87e-81

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: 256.08  E-value: 2.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   77 ILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAgnlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdDTAEE 236
Cdd:pfam00291  76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  237 ILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS-ILAEPEELNQTEQTA---YEVEGIGYDFIPTVL 312
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGAL 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405778333  313 DRAVVDKWFKS----NDEDSFAFARMLIAQEGLLCGGSSGSAMAVA-VKAARELQEGQRCVVILPD 373
Cdd:pfam00291 230 ALDLLDEYVGEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
418-465 7.37e-09

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: 51.74  E-value: 7.37e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 405778333   418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
73-540 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: 783.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLA 152
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  153 LAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDD 232
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  233 TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  313 DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSDKWMLQK 391
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAeDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  392 GFMKEE-LSVKRPWWWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVR 470
Cdd:TIGR01137 319 GFLDDEdLTVKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  471 PSDEVCKVLYKQFKPIHLTDTLGTLSHILEMDHFALVVHEQIQycsngmsskqqmvFGVVTAIDLLNFVA 540
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGKP-------------IGVVTKIDLLSFLA 455
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
82-380 3.34e-165

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: 470.46  E-value: 3.34e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  82 GNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01561    1 GNTPLVRLNRLSP--GTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDDTAEEILQQC 241
Cdd:cd01561   79 FIIVMPETMSEEKRKLLRALGAEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 242 DGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWF 321
Cdd:cd01561  158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333 322 KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:cd01561  233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
72-381 1.45e-161

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: 461.44  E-value: 1.45e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  72 KILPDILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGL 151
Cdd:COG0031    2 RIYDSILELIGNTPLVRLNRLSPGPG--AEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYD 231
Cdd:COG0031   80 AMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 232 DTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTV 311
Cdd:COG0031  157 TTGPEIWEQTDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKI 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 312 LDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSK 381
Cdd:COG0031  232 LDPSLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
71-393 6.46e-117

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 348.77  E-value: 6.46e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  71 PKILPDILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIG 150
Cdd:PRK10717   1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 151 LALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASN 225
Cdd:PRK10717  79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPAN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 226 PLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEV----- 300
Cdd:PRK10717 158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAL-----YSYYKTGELKAegssi 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 301 -EGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYM 379
Cdd:PRK10717 233 tEGIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQ 312
                        330
                 ....*....|....
gi 405778333 380 SKFLSDKWMLQKGF 393
Cdd:PRK10717 313 SKLFNPDFLREKGL 326
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
77-380 2.27e-113

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: 338.57  E-value: 2.27e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   77 ILRKIGNTPMVRINKISKNAGlkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIEGCNA---NVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDDTAE 235
Cdd:TIGR01139  78 ARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  236 EILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILaepeeLNQTEQTAYEVEGIGYDFIPTVLDRA 315
Cdd:TIGR01139 155 EIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRS 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 405778333  316 VVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:TIGR01139 230 VIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
77-380 5.21e-110

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: 330.01  E-value: 5.21e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   77 ILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDD 232
Cdd:TIGR01136  79 ARGYKLILTMPETMSLERRKLLRAYGAELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  233 TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPTVL 312
Cdd:TIGR01136 152 TGPEIWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKIL 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333  313 DRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQ-EGQRCVVILPDSVRNYMS 380
Cdd:TIGR01136 227 DLSLIDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
84-374 1.51e-82

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: 257.44  E-value: 1.51e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGnLKPGDTIIEPTSGNTGIGLALAAAVKGYRCI 163
Cdd:cd00640    1 TPLVRLKRLSK--LGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEG-KLPKGVIIESTGGNTGIALAAAAARLGLKCT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 164 IVMPEKMSMEKVDVLRALGAEIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdDTAEEILQQCDG 243
Cdd:cd00640   78 IVMPEGASPEKVAQMRALGAEVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 244 -KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaepeelnqteqtAYEVegigydfiptvldravvdkwfk 322
Cdd:cd00640  152 qKPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE----------------VVTV---------------------- 193
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 405778333 323 sNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDS 374
Cdd:cd00640  194 -SDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
cysM PRK11761
cysteine synthase CysM;
75-380 9.17e-82

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 257.11  E-value: 9.17e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  75 PDILRKIGNTPMVRINKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALA 154
Cdd:PRK11761   4 PTLEDTIGNTPLVKLQRLPPDRGN--TILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 155 AAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDDTA 234
Cdd:PRK11761  82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 235 EEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP-EGS----ILAEPEElnqteqtayevegigydFIP 309
Cdd:PRK11761 158 PEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLP 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405778333 310 TVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELqEGQRCVVILPDSVRNYMS 380
Cdd:PRK11761 221 KIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLS 290
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
77-373 2.87e-81

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: 256.08  E-value: 2.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   77 ILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAgnlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdDTAEE 236
Cdd:pfam00291  76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  237 ILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS-ILAEPEELNQTEQTA---YEVEGIGYDFIPTVL 312
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGAL 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405778333  313 DRAVVDKWFKS----NDEDSFAFARMLIAQEGLLCGGSSGSAMAVA-VKAARELQEGQRCVVILPD 373
Cdd:pfam00291 230 ALDLLDEYVGEvvtvSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
77-387 2.21e-79

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: 251.35  E-value: 2.21e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   77 ILRKIGNTPMVRINKIskNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR03945   1 ILSLIGNTPLVKLERL--FPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLA 228
Cdd:TIGR03945  79 YKGLRFICVVDPNISPQNLKLLRAYGAEVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  229 HYDDTAEEILQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSIL--AEPeelnqteqTAYEVEGIGYD 306
Cdd:TIGR03945 152 HYHGTGREIARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGAS 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  307 FIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDK 386
Cdd:TIGR03945 223 VVPELLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDE 302

                  .
gi 405778333  387 W 387
Cdd:TIGR03945 303 W 303
PLN02565 PLN02565
cysteine synthase
73-385 1.18e-78

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 250.23  E-value: 1.18e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTI-IEPTSGNTGIGL 151
Cdd:PLN02565   5 IAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHY 230
Cdd:PLN02565  83 AFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 231 DDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFIPT 310
Cdd:PLN02565 159 ETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPG 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 405778333 311 VLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVK-AARELQEGQRCVVILPDSVRNYMSKFLSD 385
Cdd:PLN02565 234 VLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKiAKRPENAGKLIVVIFPSFGERYLSSVLFE 309
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
77-380 9.18e-73

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: 233.65  E-value: 9.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   77 ILRKIGNTPMVRINKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:TIGR01138   2 IEQTVGNTPLVRLQRMGPENGS--EVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDDTAEE 236
Cdd:TIGR01138  80 LKGYRMKLLMPDNMSQERKAAMRAYGAELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  237 ILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEgsilaEPeelnqteqtaYEVEGIGY---DFIPTVLD 313
Cdd:TIGR01138 156 IWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFD 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 405778333  314 RAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQrCVVILPDSVRNYMS 380
Cdd:TIGR01138 221 ASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
PLN00011 PLN00011
cysteine synthase
76-385 2.26e-70

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 228.73  E-value: 2.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  76 DILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPG-DTIIEPTSGNTGIGLALA 154
Cdd:PLN00011  10 DVTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 155 AAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLA 228
Cdd:PLN00011  88 GAARGYKVILVMPSTMSLERRIILRALGAEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 229 HYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDFI 308
Cdd:PLN00011 159 HYRTTGPEIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGII 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405778333 309 PTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAA-RELQEGQRCVVILPDSVRNYMSKFLSD 385
Cdd:PLN00011 234 PFNLDLTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAkRPENAGKLIVVIFPSGGERYLSTKLFE 311
PLN03013 PLN03013
cysteine synthase
73-380 2.28e-67

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 224.27  E-value: 2.28e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  73 ILPDILRKIGNTPMVRINKISKnaGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTI-IEPTSGNTGIGL 151
Cdd:PLN03013 113 IADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 152 ALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPL 227
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPK 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 228 AHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEPEELNQTEQTAYEVEGIGYDF 307
Cdd:PLN03013 264 IHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGF 338
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 405778333 308 IPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMS 380
Cdd:PLN03013 339 IPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
56-386 1.83e-66

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 219.83  E-value: 1.83e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  56 AMADSPHYHTVLTKSPKILP------DILRKIGNTPMVRINKISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAER 129
Cdd:PLN02556  26 STVGSPSFAQRLRDLPKDLPgtkiktDASQLIGKTPLVYLNKVTEGCGAY--IAAKQEMFQPTSSIKDRPALAMIEDAEK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 130 AGNLKPGDT-IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNARFDSpeshVGVAWRL 207
Cdd:PLN02556 104 KNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdPTKGMGGT----VKKAYEL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 208 KNEIPNSHILDQYRNASNPLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPegsilAEP 287
Cdd:PLN02556 180 LESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AES 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 288 EELNQTEQTAYEVEGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQ-EGQR 366
Cdd:PLN02556 255 NVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKL 334
                        330       340
                 ....*....|....*....|
gi 405778333 367 CVVILPDSVRNYMSKFLSDK 386
Cdd:PLN02556 335 IVTVHPSFGERYLSSVLFQE 354
PLN02356 PLN02356
phosphateglycerate kinase
77-393 1.28e-59

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 203.30  E-value: 1.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  77 ILRKIGNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:PLN02356  47 LIDAIGNTPLIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNarFDSPESHVGVAWRL---KNEIP-----------------NSH 215
Cdd:PLN02356 125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVrPVS--ITHKDHYVNIARRRaleANELAskrrkgsetdgihlektNGC 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 216 IL-------------------DQYRNASNPLAHYDDTAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIG 276
Cdd:PLN02356 203 ISeeekenslfsssctggffaDQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFL 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 277 VDPEGSIL--------------AEPEELNQTEQTAyeVEGIGYDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLL 342
Cdd:PLN02356 283 IDPPGSGLfnkvtrgvmytreeAEGRRLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLF 360
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 405778333 343 CGGSSGSAMAVAVKAARELQEGQRCVVILPDSVRNYMSKFLSDKWMLQKGF 393
Cdd:PLN02356 361 VGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGL 411
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
408-538 4.38e-52

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: 173.49  E-value: 4.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIH 487
Cdd:cd04608    2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 405778333 488 LTDTLGTLSHILEMDHFALVVHEqiqycsngmsskQQMVFGVVTAIDLLNF 538
Cdd:cd04608   82 LDTPLGALSRILERDHFALVVDG------------QGKVLGIVTRIDLLNY 120
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
84-371 2.03e-28

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: 114.89  E-value: 2.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMI----EDAERAGnlkpgdtIIEPTSGNTGIGLALAAAVKG 159
Cdd:cd01562   18 TPLLTSPTLSELLG--AEVYLKCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 160 YRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHVgvawrlkneipnsHILDQYRNAsnPLAH-YDD------ 232
Cdd:cd01562   89 IPATIVMPETAPAAKVDATRAYGAEVVL--YGEDFDEAEAKA-------------RELAEEEGL--TFIHpFDDpdviag 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 233 ---TAEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTEQTAyevEG 302
Cdd:cd01562  152 qgtIGLEILEQV-PDLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTIA---DG 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 405778333 303 IGydfIPTVLD------RAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVIL 371
Cdd:cd01562  228 LA---VKRPGEltfeiiRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
84-371 5.78e-27

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: 111.28  E-value: 5.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDR------ISLRmieDAERAGnlkpgdTIIEPTSGNTGIGLALAAAV 157
Cdd:COG1171   25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRgaynalASLS---EEERAR------GVVAASAGNHAQGVAYAARL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 158 KGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNEipnshildqyRNASnpLAH-YDDT--- 233
Cdd:COG1171   94 LGIPATIVMPETAPAVKVAATRAYGAEVVLHGDT--YDDAEAA---AAELAEE----------EGAT--FVHpFDDPdvi 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 234 ------AEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA-EPEELNQTeQTAyeV 300
Cdd:COG1171  157 agqgtiALEILEQL-PDLDAVFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTI--A 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 301 EGIG--------YDFIPTVLDRAV-VdkwfksnDEDSFAFA-RMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVI 370
Cdd:COG1171  233 DGLAvgrpgeltFEILRDLVDDIVtV-------SEDEIAAAmRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVV 304

                 .
gi 405778333 371 L 371
Cdd:COG1171  305 L 305
PRK06815 PRK06815
threonine/serine dehydratase;
84-371 2.32e-25

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 106.70  E-value: 2.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERagnlKPGdtIIEPTSGNTGIGLALAAAVKGY 160
Cdd:PRK06815  21 TPLEHSPLLSQHTG--CEVYLKCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 161 RCIIVMPEKMSMEKVDVLRALGAEIVRTPTNArfdspeshvgvawrLKNEI-PNSHILDQYRNASNPlahYDD------- 232
Cdd:PRK06815  93 PVTVYAPEQASAIKLDAIRALGAEVRLYGGDA--------------LNAELaARRAAEQQGKVYISP---YNDpqviagq 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 233 --TAEEILQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG------SILA----EPEELNQ-TEQTAYE 299
Cdd:PRK06815 156 gtIGMELVEQQP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTlSDGTAGG 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 405778333 300 VEGigyDFIPTVLDRAVVDKWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQeGQRCVVIL 371
Cdd:PRK06815 235 VEP---GAITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
82-371 1.71e-20

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: 92.66  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  82 GNTPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd01563   21 GNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDDTAEEILQ 239
Cdd:cd01563   96 CVVFLPAGKALGKLAQALAYGATVLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 240 QCDGKL-DMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS-----------ILAEPEELNQTEQTAYE 299
Cdd:cd01563  166 QLGWEVpDYVVVPVGNGGNITAIWKGFKElkelglidRLP--RMVGVQAEGAapivrafkegkDDIEPVENPETIATAIR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 300 vegIGYdfiPtVLDRAVVDKWFKSN------DEDSFAFARMLIAQ-EGLLCGGSSGSAMAVAVKAARE--LQEGQRCVVI 370
Cdd:cd01563  244 ---IGN---P-ASGPKALRAVRESGgtavavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVV 316

                 .
gi 405778333 371 L 371
Cdd:cd01563  317 L 317
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
43-378 1.75e-15

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: 78.32  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  43 PDTPSRCTWQLGRAMADSPHYHTVLtkspkiLPDILRKI-----GNTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKD 117
Cdd:COG0498   27 PDSYPALSREDLASRRGLWRYRELL------PFDDEEKAvslgeGGTPLVKAPRLADELG--KNLYVKEEGHNPTGSFKD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 118 R-----ISLrmiedAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPE-KMSMEKVDVLRALGAEIVRTPTN 191
Cdd:COG0498   99 RamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQLAQMLTYGAHVIAVDGN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 192 arFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPL-------AHYddtaeEILQQCDGKLDMLVASAGTGGTITGI-- 261
Cdd:COG0498  170 --FD-------DAQRLVKELAADEGL--YaVNSINPArlegqktYAF-----EIAEQLGRVPDWVVVPTGNGGNILAGyk 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 262 ARK------LKEKCPgcKIIGVDPEGS--ILAEPEelnqTEQTAYEVEG---------IGydfIPTVLDRAVVD-----K 319
Cdd:COG0498  234 AFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPERpetiapsmdIG---NPSNGERALFAlresgG 304
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333 320 WF-KSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARE--LQEGQRCVVIL-------PDSVRNY 378
Cdd:COG0498  305 TAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVVLStghglkfPDAVREA 373
PRK06381 PRK06381
threonine synthase; Validated
82-371 2.70e-15

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 77.05  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  82 GNTPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:PRK06381  14 GGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 162 CIIVMPEKMSMEKVDVLRALGAEIVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDDTAEEIL 238
Cdd:PRK06381  89 AVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 239 QQCDGKLDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEGS--------------ILAEPEELNQTEQT 296
Cdd:PRK06381 161 EALGDVPDAVAVPVGNGTTLAGIYHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVN 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 405778333 297 AYEVEGIGYDFIPTVldRAVVD---KWFKSNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARELQEGQRCVVIL 371
Cdd:PRK06381 239 EPLVSYRSFDGDNAL--EAIYDshgYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
PLN02970 PLN02970
serine racemase
84-282 1.55e-14

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 74.71  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGLKCELlaKCEFFNAGGSVKDRISLRMI-----EDAERAgnlkpgdtIIEPTSGNTGIGLALAAAVK 158
Cdd:PLN02970  28 TPVLTSSSLDALAGRSLFF--KCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLR 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 159 GYRCIIVMPEKMSMEKVDVLRALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDDTAEEI 237
Cdd:PLN02970  98 GIPAYIVVPKNAPACKVDAVIRYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEF 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 405778333 238 LQQCDGkLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PLN02970 170 LEQVPE-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
95-280 2.66e-13

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 70.82  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  95 NAGLKCELLAKCEFFNAGGSVKDRIS----LRMIEDAERAGnlkpgdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKM 170
Cdd:PRK07048  34 DARTGAQVFFKCENFQRMGAFKFRGAynalSQFSPEQRRAG-------VVTFSSGNHAQAIALSARLLGIPATIVMPQDA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 171 SMEKVDVLRALGAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------DTAEEIL 238
Cdd:PRK07048 107 PAAKVAATRGYGGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELF 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 405778333 239 QQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 280
Cdd:PRK07048 168 EEV-GPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
145-282 4.08e-12

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 68.63  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 145 GNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 219
Cdd:PRK09224  77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 405778333 220 yrnasnPlahYDDT---------AEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PRK09224 145 ------P---FDDPdviagqgtiAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
PRK08246 PRK08246
serine/threonine dehydratase;
101-282 6.71e-12

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 66.52  E-value: 6.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 101 ELLAKCEFFNAGGSVKDRISL-RMIedaeraGNLKPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLR 179
Cdd:PRK08246  38 PVWLKLEHLQHTGSFKARGAFnRLL------AAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 180 ALGAEIVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDDTAEEILQQCdGKLDMLVASAGT 254
Cdd:PRK08246 112 ALGAEVVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGG 178
                        170       180
                 ....*....|....*....|....*...
gi 405778333 255 GGTITGIARKLKekcPGCKIIGVDPEGS 282
Cdd:PRK08246 179 GGLIAGIAAWFE---GRARVVAVEPEGA 203
PRK06608 PRK06608
serine/threonine dehydratase;
77-279 1.64e-11

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 65.56  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  77 ILRKIGNTPMVriNKISKNAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGnlKPGDTIIEPTSGNTGIGLALAAA 156
Cdd:PRK06608  17 IKQYLHLTPIV--HSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 157 VKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDDT 233
Cdd:PRK06608  93 LFGIKTRIYLPLNTSKVKQQAALYYGGEVILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 405778333 234 AEEILQQCDGKLDMLVASAGTGGTITG--IARKLKEkcPGCKIIGVDP 279
Cdd:PRK06608 161 CYEALQQLGFSPDAIFASCGGGGLISGtyLAKELIS--PTSLLIGSEP 206
PRK12483 PRK12483
threonine dehydratase; Reviewed
139-282 1.80e-11

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 66.36  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 139 IIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNEIPNSHIld 218
Cdd:PRK12483  88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVL--HGESFPDALAH---ALKLAEEEGLTFV-- 160
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 405778333 219 qyrnasNPlahYDD---------TAEEILQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGS 282
Cdd:PRK12483 161 ------PP---FDDpdviagqgtVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
82-278 3.19e-11

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: 64.71  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333   82 GNTPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:TIGR00260  21 GVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  162 CIIVMPE-KMSMEKVDVLRALGAEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnshildqYRNASNPLAHYdd 232
Cdd:TIGR00260  96 VVVLYPAgKISLGKLAQALGYNAEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-------YRLEGQKTYAF-- 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 405778333  233 taeEILQQCDGKL-DMLVASAGTGGTITGIARKLKEKcpgcKIIGVD 278
Cdd:TIGR00260 165 ---EAVEQLGWEApDKVVVPVPNSGNFGAIWKGFKEK----KMLGLD 204
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
77-280 9.03e-11

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 63.22  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  77 ILRKIGNTPMVRINKISKNAglKCELLAKCEFFNAGGSVKDRIS---LRMIEDAERAGNlkpgdtIIEPTSGNTGIGLAL 153
Cdd:PRK08638  21 LAGRIRKTPLPRSNYLSERC--KGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKG------VVACSAGNHAQGVAL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 154 AAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILDQYrNASNPLAHYDDT 233
Cdd:PRK08638  93 SCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIPPY-DDPKVIAGQGTI 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 405778333 234 AEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE 280
Cdd:PRK08638 166 GLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
PRK06450 PRK06450
threonine synthase; Validated
72-280 6.72e-09

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 57.82  E-value: 6.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  72 KILPDILRKI----GNTPMVRINKISknaglkcellAKCEFFNAGGSVKDRISLRMIED-AERAGNlkpgdTIIEPTSGN 146
Cdd:PRK06450  43 KNFPYIKHFIslgeGRTPLIKKGNIW----------FKLDFLNPTGSYKDRGSVTLISYlAEKGIK-----QISEDSSGN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 147 TGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYR 221
Cdd:PRK06450 108 AGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFR 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 222 NASNPLAHyddtaeEILQQCDGKLD---MLVASAGTggTITGIARKLK--------EKCPgcKIIGVDPE 280
Cdd:PRK06450 178 DGIRTLAY------EIAKDLDWKIPnyvFIPVSAGT--LLLGVYSGFKhlldsgviSEMP--KIVAVQTE 237
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
418-465 7.37e-09

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: 51.74  E-value: 7.37e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 405778333   418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
83-282 1.02e-08

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: 56.92  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  83 NTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDR-ISLRMIEDAERAGNLKPGdtIIEPTSGNTGIGLALAAAVKGYR 161
Cdd:cd06448    1 KTPLIESTALSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 162 CIIVMPEKMSMEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDDTAEEILQ 239
Cdd:cd06448   77 CTIVVPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQ 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 405778333 240 QC--DGKLDMLVASAGTGGTITGIARKLkEKCPGCK--IIGVDPEGS 282
Cdd:cd06448  150 QLqsQEKVDAIVCSVGGGGLLNGIVQGL-ERNGWGDipVVAVETEGA 195
PRK07334 PRK07334
threonine dehydratase; Provisional
83-303 5.93e-08

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 54.90  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  83 NTPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRIS---LRMIEDAERAGNlkpgdtIIEPTSGNTGIGLALAAAVKG 159
Cdd:PRK07334  23 RTPCVHSRTLSQITG--AEVWLKFENLQFTASFKERGAlnkLLLLTEEERARG------VIAMSAGNHAQGVAYHAQRLG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 160 YRCIIVMPEKMSMEKVDVLRALGAEIVRtpTNARFDSPESHvgvAWRLKNEipnshildQYRNASNPlahYDD------- 232
Cdd:PRK07334  95 IPATIVMPRFTPTVKVERTRGFGAEVVL--HGETLDEARAH---ARELAEE--------EGLTFVHP---YDDpaviagq 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 405778333 233 --TAEEILQQCdGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG--SILAEPEELNQTEQTAYEVEGI 303
Cdd:PRK07334 159 gtVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELypSMYAAIKGVALPCGGSTIAEGI 232
PRK06110 PRK06110
threonine dehydratase;
95-186 9.31e-08

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 53.84  E-value: 9.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  95 NAGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERAGNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEK 174
Cdd:PRK06110  31 AERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEK 108
                         90
                 ....*....|..
gi 405778333 175 VDVLRALGAEIV 186
Cdd:PRK06110 109 NAAMRALGAELI 120
PRK05638 PRK05638
threonine synthase; Validated
72-374 1.69e-07

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 53.66  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  72 KILPDILRKI----GNTPMVRiNKISKNAGLkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNT 147
Cdd:PRK05638  51 ELLPQVKKIIslgeGGTPLIR-ARISEKLGE--NVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 148 GIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnas 224
Cdd:PRK05638 124 AASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG------ 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 225 npLAHYDDTAEEILQQCDGklDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPE------GSILAEPEEL 290
Cdd:PRK05638 196 --LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSIYKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKC 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 291 NQTEQTA-YEVEGIGYDFIPTVLDR----AVVdkwfksNDEDSFAFARMLIAQEGLLCGGSSGSAMAVAVKAARE--LQE 363
Cdd:PRK05638 270 NETKALGlYVKNPVMKEYVSEAIKEsggtAVV------VNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEK 343
                        330
                 ....*....|.
gi 405778333 364 GQRCVVILPDS 374
Cdd:PRK05638 344 GDKVVLVVTGS 354
CBS COG0517
CBS domain [Signal transduction mechanisms];
408-544 2.28e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 49.86  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLA-GKVRPSDEVCKVLYKQFKPI 486
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAeGKDLLDTPVSEVMTRPPVTV 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 487 HLTDTLGTLSHILEMDHF--ALVVHEQIQYCsngmsskqqmvfGVVTAIDLLNFVAAREQ 544
Cdd:COG0517   81 SPDTSLEEAAELMEEHKIrrLPVVDDDGRLV------------GIITIKDLLKALLEPLA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
418-511 2.84e-07

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: 49.17  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPIHLTDTLGT-LS 496
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEaLE 83
                         90
                 ....*....|....*.
gi 405778333 497 HILEMD-HFALVVHEQ 511
Cdd:cd02205   84 LMLEHGiRRLPVVDDD 99
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
84-191 4.11e-07

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 52.19  E-value: 4.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGLKcELLAKCE---F----FNA-GGS------VKDRISLRMIE---DAERAGNLKP--GD-TIIEPT 143
Cdd:PRK08206  45 TPLVALPDLAAELGVG-SILVKDEsyrFglnaFKAlGGAyavarlLAEKLGLDISElsfEELTSGEVREklGDiTFATAT 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 405778333 144 SGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVRTPTN 191
Cdd:PRK08206 124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN 171
PLN02550 PLN02550
threonine dehydratase
84-279 8.89e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 51.85  E-value: 8.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGLKceLLAKCEFFNAGGSVKDRISLRMIEDAERAgNLKPGdtIIEPTSGNTGIGLALAAAVKGYRCI 163
Cdd:PLN02550 110 SPLQLAKKLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAV 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 164 IVMPEKMSMEKVDVLRALGAEIVRTPTNarFDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYDDTA------EEI 237
Cdd:PLN02550 185 IAMPVTTPEIKWQSVERLGATVVLVGDS--YDEAQAYA-----------KQRALEEGRTFIPPFDHPDVIAgqgtvgMEI 251
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 405778333 238 LQQCDGKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDP 279
Cdd:PLN02550 252 VRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
410-465 9.70e-07

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: 46.05  E-value: 9.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 405778333  410 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
PRK08639 PRK08639
threonine dehydratase; Validated
234-281 9.97e-07

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 51.35  E-value: 9.97e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 405778333 234 AEEILQQCD--GKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEG 281
Cdd:PRK08639 167 AVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
407-539 1.13e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 49.50  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 407 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLLAGKVRPSDEVCKVLYKQFKPI 486
Cdd:COG2524   85 KMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTV 163
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 405778333 487 HLTDTLGT-LSHILEMDHFALVVheqiqycsngMSSKQQMVfGVVTAIDLLNFV 539
Cdd:COG2524  164 SEDDSLEEaLRLMLEHGIGRLPV----------VDDDGKLV-GIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
418-546 1.27e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.94  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDE------VCKVLYKQFKPIHLTDT 491
Cdd:COG3448   12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEErlldlpVEDVMTRPVVTVTPDTP 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 405778333 492 LGTLSHIL-EMDHFALVVheqiqycsngMSSKQQMVfGVVTAIDLLNFVAAREQTQ 546
Cdd:COG3448   92 LEEAAELMlEHGIHRLPV----------VDDDGRLV-GIVTRTDLLRALARLLEEE 136
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
126-342 1.78e-06

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 50.22  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 126 DAERAGnlkpGDTIIepTSGntGIG-----LALAAAVK-GYRCIIVMPEKMSMEKVDVL--------RALGAEIVRTPTN 191
Cdd:PRK03910  58 DALAQG----ADTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 192 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDDTAEEILQQCDG---KLDMLVASAGTGGTITG 260
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 261 IARKLKEKCPGCKIIGVdpegSILAEPEElnQTEQTAYEVEGI-GYDFIPTVLDRAVV---DKWF-----KSNDEDsFAF 331
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV----TVSRSAAE--QEPKVAKLAQATaELLGLPTEIPRADIrlwDDYVgpgygVPTDEM-LEA 272
                        250
                 ....*....|.
gi 405778333 332 ARMLIAQEGLL 342
Cdd:PRK03910 273 VKLLARTEGIL 283
ACCD cd06449
Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme ...
84-342 1.05e-05

Aminocyclopropane-1-carboxylate deaminase (ACCD): Pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of 1-aminocyclopropane-L-carboxylate (ACC), a precursor of the plant hormone ethylene, to alpha-ketobutyrate and ammonia.


Pssm-ID: 107210  Cd Length: 307  Bit Score: 47.42  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGLKCELLAKCEFFN---AGGSVKDRISLRMIEDAERAGnlkpGDTIIepTSG----NTGIGLALAAA 156
Cdd:cd06449    1 TPIQYLPRLSEHLGGKVEIYAKRDDCNsglAFGGNKIRKLEYLLPDALAKG----ADTLV--TVGgiqsNHTRQVAAVAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 157 VKGYRCIIVM--PEKMSMEKVD------VLRALGAEIvrtptnaRFDSPESHVGV-------AWRLKNE------IPNSh 215
Cdd:cd06449   75 KLGLKCVLVQenWVPYSDAVYDrvgnilLSRIMGADV-------RLVSAGFDIGIrksfeeaAEEVEAKggkpyvIPAG- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 216 ildqyrNASNPLAH--YDDTAEEILQQCDG---KLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPEGSILAEPEEL 290
Cdd:cd06449  147 ------GSEHPLGGlgYVGFVLEIAQQEEElgfKFDSIVVCSVTGSTHAGLSVGLAALGRQRRVIGIDASAKPEKTKAQV 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 405778333 291 NQTEQTAYEVEGIGYdfipTVLDRAVVDKWF-----KSNDEDSFAFaRMLIAQEGLL 342
Cdd:cd06449  221 LRIAQAKLAEEGLEV----KEEDVVLDDDYAapeygIPNDETIEAI-KLCARLEGII 272
eutB PRK07476
threonine dehydratase; Provisional
84-371 1.43e-05

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 47.27  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  84 TPMVRINKISKNAGlkCELLAKCEFFNAGGSVKDRISLRMI---EDAERAGNlkpgdtIIEPTSGNTGIGLALAAAVKGY 160
Cdd:PRK07476  20 TPLVASASLSARAG--VPVWLKLETLQPTGSFKLRGATNALlslSAQERARG------VVTASTGNHGRALAYAARALGI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 161 RCIIVMPEKMSMEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYDDTAE 235
Cdd:PRK07476  92 RATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP-------------PFDDPRIIAG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 236 ------EILQQCDgKLDMLVASAGTGGTITGIARKLKEKCPGCKIIGVDPE-GSILAEPEELNQTEQTAyEVE------- 301
Cdd:PRK07476 154 qgtiglEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGVSMErGAAMHASLAAGRPVQVE-EVPtladslg 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 405778333 302 -GIGYDFIPTV-LDRAVVDKWFKSnDEDSFAFA-RMLIAQEGLLCGGSSGSAMAvAVKAARELQEGQRCVVIL 371
Cdd:PRK07476 232 gGIGLDNRYTFaMCRALLDDVVLL-DEAEIAAGiRHAYREERLVVEGAGAVGIA-ALLAGKIAARDGPIVVVV 302
CBS COG0517
CBS domain [Signal transduction mechanisms];
405-465 1.43e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 44.47  E-value: 1.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405778333 405 WWRLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG0517   64 LLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
410-540 2.49e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 43.66  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 410 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLLAGKVRPSDE-VCKVLYKQFKPIHL 488
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 405778333 489 TDTLGTLSHILEMDHF-ALVVheqiqyCSNGmsskqQMVfGVVTAIDLLNFVA 540
Cdd:COG2905   81 DDSLAEALELMEEHRIrHLPV------VDDG-----KLV-GIVSITDLLRALS 121
PRK08197 PRK08197
threonine synthase; Validated
41-187 5.42e-05

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 45.76  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  41 IRPDTPSRCTWQLGRamadsphYHTVLtksPKILPDILRKIGN--TPMVRINKISKNAGLKcELLAKCEFFNAGGSVKDR 118
Cdd:PRK08197  45 VTREALAGRPANLWR-------YHELL---PVRDPEHIVSLGEgmTPLLPLPRLGKALGIG-RLWVKDEGLNPTGSFKAR 113
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333 119 ISLRMIEDAERAGnLKpgdTIIEPTSGNTGIGLALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIVR 187
Cdd:PRK08197 114 GLAVGVSRAKELG-VK---HLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITRLECALAGAELYL 178
PRK08329 PRK08329
threonine synthase; Validated
71-281 8.58e-05

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 44.82  E-value: 8.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  71 PKILPDIlrkignTPMVRINKisknaglkcELLAKCEFFNAGGSVKDRISLRMIEDAERAGNlkpgDTIIEPTSGNTGIG 150
Cdd:PRK08329  58 PHLTPPI------TPTVKRSI---------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALS 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 151 LALAAAVKGYRCIIVMPEKMSMEKVDVLRALGAEIvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRNASNPLA 228
Cdd:PRK08329 119 LALYSLSEGIKVHVFVSYNASKEKISLLSRLGAEL----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYFLEGTKTI 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 405778333 229 HYddtaeEILQQCdGKLDMLVASAGTGGTITGIARKLKE--------KCPgcKIIGVDPEG 281
Cdd:PRK08329 195 AY-----EIYEQI-GVPDYAFVPVGSGTLFLGIWKGFKElhemgeisKMP--KLVAVQAEG 247
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
122-188 1.13e-04

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 44.52  E-value: 1.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 122 RMIEDAeraGNLKPGDTIIEpTSGNTGIGLALA--AAVKGYRCIIVMPEKMSMEK-VDVLRALGAEIVRT 188
Cdd:cd08290  136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
418-523 2.32e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.44  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLssllagKVRPSDEVCKVLYKQFKPIHLTDTLGTLSH 497
Cdd:COG4109   27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
                         90       100
                 ....*....|....*....|....*...
gi 405778333 498 ILEMDHFAL--VVHEQIQYCsnGMSSKQ 523
Cdd:COG4109  101 KMIWEGIELlpVVDDDGRLL--GIISRQ 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
407-465 3.25e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 41.00  E-value: 3.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333 407 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG3448   72 DLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
PLN02569 PLN02569
threonine synthase
55-276 4.35e-04

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 42.88  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333  55 RAMADS-------PHYHTVLTKSPKILP-----DILRKI-GNTPMVRINKISKNAGLKCELLAKCEFFNAGGSVKDRISL 121
Cdd:PLN02569  92 RALFDSrvgkttwPYGSGVWSKKEWVLPeidddDIVSLFeGNSNLFWAERLGKEFLGMNDLWVKHCGISHTGSFKDLGMT 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 122 RMIEDAERAGNL-KPGDTIIEPTSGNTGIGLALAAAVKGYRCIIVMPE-KMSMEKVDVLRALGAEIVRTPTNarFDSPES 199
Cdd:PLN02569 172 VLVSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPAdKISIAQLVQPIANGALVLSIDTD--FDGCMR 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 200 HVGvawRLKNEIP----NShiLDQYRnasnpLAHYDDTAEEILQQCDGKL-DMLVASAGTGGTITGIARKLKEkcpgCKI 274
Cdd:PLN02569 250 LIR---EVTAELPiylaNS--LNSLR-----LEGQKTAAIEILQQFDWEVpDWVIVPGGNLGNIYAFYKGFKM----CKE 315

                 ..
gi 405778333 275 IG 276
Cdd:PLN02569 316 LG 317
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
407-465 5.57e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 42.51  E-value: 5.57e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 405778333 407 RLRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:PRK14869  67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
408-465 6.50e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.81  E-value: 6.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 405778333 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNEsGAILGMVTLGNMLSSLL 465
Cdd:COG2905   65 TPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
408-461 7.04e-04

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: 39.54  E-value: 7.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 405778333 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNML 461
Cdd:cd02205   59 TPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
410-537 7.05e-04

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: 38.85  E-value: 7.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 410 VQELSLSAPLTVLPTVTCEDTIAILREK-GFDQAPVVNESGailgmVTLgNMLSSLLAGKVRPSdevckvlykqfkpihl 488
Cdd:COG3620    1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 405778333 489 TDTLGTLSHILEMDHFALVVHEQIQYcsngmsskqqmvFGVVTAIDLLN 537
Cdd:COG3620   59 VSTLEKIAEALGKELSAVLVVDDGKL------------VGIITRRDLLK 95
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
408-465 1.82e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 38.74  E-value: 1.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 405778333 408 LRVQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNMLSSLL 465
Cdd:COG4109   76 TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
418-456 2.05e-03

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: 38.16  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 405778333 418 PLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVT 456
Cdd:cd04601    4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
410-461 2.68e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 38.22  E-value: 2.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 405778333 410 VQELSLSAPLTVLPTVTCEDTIAILREKGFDQAPVVNESGAILGMVTLGNML 461
Cdd:cd17789   88 VGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
419-536 2.86e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 37.70  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 405778333 419 LTVLPTVTCEDTIAILREKG-----FDQAPVVNESGAILGMVTLGNMLSSllagkvRPSDEVCKVLYKQFKPIHLTDTLG 493
Cdd:cd04606   12 VAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLA------DPDTKVSDIMDTDVISVSADDDQE 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 405778333 494 TLSHILEM-DHFAL-VVHEQiqycsngmsskQQMVfGVVT---AIDLL 536
Cdd:cd04606   86 EVARLFAKyDLLALpVVDEE-----------GRLV-GIITvddVLDVI 121
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
420-461 7.74e-03

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 36.14  E-value: 7.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 405778333 420 TVLPTVTCEDTIAILREKGFDQAPVVnESGAILGMVTLGNML 461
Cdd:cd04610    7 TVSPDDTVKDVIKLIKETGHDGFPVV-DDGKVVGYVTAKDLL 47
 
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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