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Conserved domains on  [gi|1899762177|ref|XP_035913060|]
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cystathionine beta-synthase-like protein [Anopheles stephensi]

Protein Classification

cystathionine beta-synthase( domain architecture ID 1002792)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cysta_beta super family cl36831
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 66-526 0e+00

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


The actual alignment was detected with superfamily member TIGR01137:

Pssm-ID: 273464 [Multi-domain]  Cd Length: 455  Bit Score: 546.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  66 VLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLA 145
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 146 MAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAFDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDG 225
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 226 TGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSILAEPEELNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 306 DRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAK-ELKEGQNCVVVLPDNIRNYLTKFVSDNWMEAR 384
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 385 NFKESDNC--HNQKWWNEKVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAK 462
Cdd:TIGR01137 319 GFLDDEDLtvKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899762177 463 PSDLVHRVIFKQFVKIDHEENVGRASRILEKDSFVLVTRQEIgatpterLVGVLTQREMLNFVA 526
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGK-------PIGVVTKIDLLSFLA 455
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 66-526 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: 546.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  66 VLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLA 145
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 146 MAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAFDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDG 225
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 226 TGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSILAEPEELNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 306 DRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAK-ELKEGQNCVVVLPDNIRNYLTKFVSDNWMEAR 384
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 385 NFKESDNC--HNQKWWNEKVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAK 462
Cdd:TIGR01137 319 GFLDDEDLtvKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899762177 463 PSDLVHRVIFKQFVKIDHEENVGRASRILEKDSFVLVTRQEIgatpterLVGVLTQREMLNFVA 526
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGK-------PIGVVTKIDLLSFLA 455
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 75-373 1.14e-126

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: 371.85  E-value: 1.14e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  75 GGTPLVKLNKIpqSLGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMAAAARGYR 154
Cdd:cd01561     1 GNTPLVRLNRL--SPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 155 CLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAfDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDGTGAEIVEQL 234
Cdd:cd01561    79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEA-DGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 235 GGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSILaepeeLNQTNVSFYEVEGVGYDFLPTVLDRSVVDRWY 314
Cdd:cd01561   158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1899762177 315 KFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLT 373
Cdd:cd01561   233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 66-374 1.24e-125

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: 369.76  E-value: 1.24e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  66 VLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLA 145
Cdd:COG0031     3 IYDSILELIGNTPLVRLNRLSP--GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 146 MAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEaafDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDG 225
Cdd:COG0031    81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYET 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 226 TGAEIVEQLGGRVDMIVigtgtggtmtgigRRIKESCPNCQVIAADPEGSILaepeeLNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:COG0031   158 TGPEIWEQTDGKVDAFVagvgtggtitgvgRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKIL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899762177 306 DRSVVDRWYKFNDRVALPLARRLIRDEgllcggssggNLYVALEAAKELKEGQNCVVVLPDNIRNYLTK 374
Cdd:COG0031   233 DPSLIDEVITVSDEEAFAMARRLAREEgilvgissgaAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
 64-386 3.02e-89

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 277.51  E-value: 3.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  64 PSVLPSILEAVGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIG 143
Cdd:PRK10717    1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 144 LAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPtEAAFDSPEGLIAVSQRL----QRSIPDSVI-LDQYRNAGN 218
Cdd:PRK10717   79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVP-AAPYANPNNYVKGAGRLaeelVASEPNGAIwANQFDNPAN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 219 PLAHYDGTGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSIL---AEPEELNQTNVSFyeVEG 295
Cdd:PRK10717  158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyYKTGELKAEGSSI--TEG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 296 VGYDFLPTVLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLTKF 375
Cdd:PRK10717  236 IGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKL 315

                         330
                  ....*....|.
gi 1899762177 376 VSDNWMEARNF 386
Cdd:PRK10717  316 FNPDFLREKGL 326
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 70-366 1.07e-58

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 196.76  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  70 ILEAVGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKgllKPGCTIIEPTSGNTGIGLAMAAA 149
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 150 ARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPteaafDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYdGTGAE 229
Cdd:pfam00291  76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVG-----GDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 230 IVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSIL----AEPEELNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPAlarsLAAGRPVPVPVADTIADGLGVGDEPGAL 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899762177 306 DRSVVDRW----YKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVA-LEAAKELKEGQNCVVVLPD 366
Cdd:pfam00291 230 ALDLLDEYvgevVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 66-526 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: 546.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  66 VLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLA 145
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRLNKVSK--GLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 146 MAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAFDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDG 225
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 226 TGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSILAEPEELNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:TIGR01137 159 TGPEILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 306 DRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAK-ELKEGQNCVVVLPDNIRNYLTKFVSDNWMEAR 384
Cdd:TIGR01137 239 DRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 385 NFKESDNC--HNQKWWNEKVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAK 462
Cdd:TIGR01137 319 GFLDDEDLtvKDVLWWHARVKDLHLPAPVTVHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQ 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1899762177 463 PSDLVHRVIFKQFVKIDHEENVGRASRILEKDSFVLVTRQEIgatpterLVGVLTQREMLNFVA 526
Cdd:TIGR01137 399 PSDAVSKVMSKKFIQIGLGETLSDLSKFLEMDSSAIVVEEGK-------PIGVVTKIDLLSFLA 455
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 75-373 1.14e-126

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: 371.85  E-value: 1.14e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  75 GGTPLVKLNKIpqSLGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMAAAARGYR 154
Cdd:cd01561     1 GNTPLVRLNRL--SPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 155 CLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAfDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDGTGAEIVEQL 234
Cdd:cd01561    79 FIIVMPETMSEEKRKLLRALGAEVILTPEAEA-DGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 235 GGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSILaepeeLNQTNVSFYEVEGVGYDFLPTVLDRSVVDRWY 314
Cdd:cd01561   158 DGKVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVV 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1899762177 315 KFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLT 373
Cdd:cd01561   233 RVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 66-374 1.24e-125

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: 369.76  E-value: 1.24e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  66 VLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLA 145
Cdd:COG0031     3 IYDSILELIGNTPLVRLNRLSP--GPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 146 MAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEaafDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDG 225
Cdd:COG0031    81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYET 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 226 TGAEIVEQLGGRVDMIVigtgtggtmtgigRRIKESCPNCQVIAADPEGSILaepeeLNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:COG0031   158 TGPEIWEQTDGKVDAFVagvgtggtitgvgRYLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKIL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1899762177 306 DRSVVDRWYKFNDRVALPLARRLIRDEgllcggssggNLYVALEAAKELKEGQNCVVVLPDNIRNYLTK 374
Cdd:COG0031   233 DPSLIDEVITVSDEEAFAMARRLAREEgilvgissgaAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 70-373 1.09e-90

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: 280.32  E-value: 1.09e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  70 ILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMAAA 149
Cdd:TIGR01136   1 IEELIGNTPLVRLNRLAP--GCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 150 ARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEaafDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDGTGAE 229
Cdd:TIGR01136  79 ARGYKLILTMPETMSLERRKLLRAYGAELILTPGE---EGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 230 IVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPegsilAEPEELNQTNVSFYEVEGVGYDFLPTVLDRSV 309
Cdd:TIGR01136 156 IWRDTDGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKILDLSL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899762177 310 VDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELK-EGQNCVVVLPDNIRNYLT 373
Cdd:TIGR01136 231 IDEVITVSDEDAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 70-373 1.61e-89

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: 276.94  E-value: 1.61e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  70 ILEAVGGTPLVKLNKIPqslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMAAA 149
Cdd:TIGR01139   1 ISELIGNTPLVRLNRIE---GCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 150 ARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAFdspEGLIAVSQRLQRSIPDS-VILDQYRNAGNPLAHYDGTGA 228
Cdd:TIGR01139  78 ARGYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGM---KGAIAKAEEIAASTPNSyFMLQQFENPANPEIHRKTTGP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 229 EIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSILaepeeLNQTNVSFYEVEGVGYDFLPTVLDRS 308
Cdd:TIGR01139 155 EIWRDTDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRS 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1899762177 309 VVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLT 373
Cdd:TIGR01139 230 VIDEVITVSDEEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
PRK10717 PRK10717
cysteine synthase A; Provisional
 64-386 3.02e-89

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 277.51  E-value: 3.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  64 PSVLPSILEAVGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIG 143
Cdd:PRK10717    1 MKIFEDVSDTIGNTPLIRLNRASEATG--CEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 144 LAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPtEAAFDSPEGLIAVSQRL----QRSIPDSVI-LDQYRNAGN 218
Cdd:PRK10717   79 LALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVP-AAPYANPNNYVKGAGRLaeelVASEPNGAIwANQFDNPAN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 219 PLAHYDGTGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSIL---AEPEELNQTNVSFyeVEG 295
Cdd:PRK10717  158 REAHYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyYKTGELKAEGSSI--TEG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 296 VGYDFLPTVLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLTKF 375
Cdd:PRK10717  236 IGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKL 315

                         330
                  ....*....|.
gi 1899762177 376 VSDNWMEARNF 386
Cdd:PRK10717  316 FNPDFLREKGL 326
cysM PRK11761
cysteine synthase CysM;
68-363 8.21e-65

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 212.81  E-value: 8.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  68 PSILEAVGGTPLVKLNKIPQSLGLKcnVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMA 147
Cdd:PRK11761    4 PTLEDTIGNTPLVKLQRLPPDRGNT--ILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 148 AAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEaafDSPEGLIAVSQRLQRSiPDSVILDQYRNAGNPLAHYDGTG 227
Cdd:PRK11761   82 AAIKGYRMKLIMPENMSQERRAAMRAYGAELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 228 AEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADP-EGS----ILAEPEElnqtnvsfyevegvgydFLP 302
Cdd:PRK11761  158 PEIWRQTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLP 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1899762177 303 TVLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKegqNCVVV 363
Cdd:PRK11761  221 KIFDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENP---NAVIV 278
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 69-373 9.43e-59

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: 197.06  E-value: 9.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  69 SILEAVGGTPLVKLNKIPQSLGLKcnVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMAA 148
Cdd:TIGR01138   1 TIEQTVGNTPLVRLQRMGPENGSE--VWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 149 AARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEaafDSPEGLIAVSQRLQRSIPDSViLDQYRNAGNPLAHYDGTGA 228
Cdd:TIGR01138  79 ALKGYRMKLLMPDNMSQERKAAMRAYGAELILVTKE---EGMEGARDLALELANRGEGKL-LDQFNNPDNPYAHYTSTGP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 229 EIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEgsilaEPeelnqtnvsfYEVEGVGY---DFLPTVL 305
Cdd:TIGR01138 155 EIWQQTGGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIF 219

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899762177 306 DRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQnCVVVLPDNIRNYLT 373
Cdd:TIGR01138 220 DASLVDRVLDIHQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 70-366 1.07e-58

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 196.76  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  70 ILEAVGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKgllKPGCTIIEPTSGNTGIGLAMAAA 149
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELG--VDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 150 ARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPteaafDSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYdGTGAE 229
Cdd:pfam00291  76 RLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVG-----GDYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 230 IVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSIL----AEPEELNQTNVSFYEVEGVGYDFLPTVL 305
Cdd:pfam00291 150 ILEQLGGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPAlarsLAAGRPVPVPVADTIADGLGVGDEPGAL 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1899762177 306 DRSVVDRW----YKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVA-LEAAKELKEGQNCVVVLPD 366
Cdd:pfam00291 230 ALDLLDEYvgevVTVSDEEALEAMRLLARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 77-366 1.49e-57

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: 191.96  E-value: 1.49e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIpqSLGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGcTIIEPTSGNTGIGLAMAAAARGYRCL 156
Cdd:cd00640     1 TPLVRLKRL--SKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKG-VIIESTGGNTGIALAAAAARLGLKCT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 157 IVMPEKMSNEKVDTLKALGAEVIRTPTeaafdSPEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYdGTGAEIVEQLGG 236
Cdd:cd00640    78 IVMPEGASPEKVAQMRALGAEVVLVPG-----DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 237 -RVDMIVigtgtggtmtgigRRIKESCPNCQVIAADPEgsilaepeelnqtnvsfyevegvgydflptvldrsvvdrWYK 315
Cdd:cd00640   152 qKPDAVVvpvggggniagiaRALKELLPNVKVIGVEPE---------------------------------------VVT 192

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1899762177 316 FNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPD 366
Cdd:cd00640   193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTG 243
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
 70-380 3.46e-55

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: 187.79  E-value: 3.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  70 ILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPTSGNTGIGLAMAAA 149
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFP--DAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 150 ARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTpTEAafDSPEGL----IAVSQRLQRSIPDSVILDQYRNAGNPLAHYDG 225
Cdd:TIGR03945  79 YKGLRFICVVDPNISPQNLKLLRAYGAEVEKV-TEP--DETGGYlgtrIARVRELLASIPDAYWPNQYANPDNPRAHYHG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 226 TGAEIVEQLgGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGSIL--AEPeelnqtnvSFYEVEGVGYDFLPT 303
Cdd:TIGR03945 156 TGREIARAF-PTLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGASVVPE 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899762177 304 VLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLTKFVSDNW 380
Cdd:TIGR03945 227 LLDESLIDDVVHVPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
PLN02565 PLN02565
cysteine synthase
 63-373 3.43e-54

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 185.90  E-value: 3.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  63 KPSVLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTI-IEPTSGNTG 141
Cdd:PLN02565    2 KSSIAKDVTELIGKTPLVYLNNVVD--GCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 142 IGLAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRT-PTEAAfdspEGLIAVSQRLQRSIPDSVILDQYRNAGNPL 220
Cdd:PLN02565   80 IGLAFMAAAKGYKLIITMPASMSLERRIILLAFGAELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 221 AHYDGTGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADP-EGSILA--EPEElnqtnvsfYEVEGVG 297
Cdd:PLN02565  156 IHYETTGPEIWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPvESAVLSggKPGP--------HKIQGIG 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1899762177 298 YDFLPTVLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELK-EGQNCVVVLPDNIRNYLT 373
Cdd:PLN02565  228 AGFIPGVLDVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLS 304
PLN03013 PLN03013
cysteine synthase
 65-373 1.52e-50

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 179.20  E-value: 1.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  65 SVLPSILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTI-IEPTSGNTGIG 143
Cdd:PLN03013  112 NIADNVSQLIGKTPMVYLNSIAK--GCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 144 LAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTpteaafDSPEGLIAVSQRLQ---RSIPDSVILDQYRNAGNPL 220
Cdd:PLN03013  190 LAFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLT------DPAKGMTGAVQKAEeilKNTPDAYMLQQFDNPANPK 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 221 AHYDGTGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPegsilAEPEELNQTNVSFYEVEGVGYDF 300
Cdd:PLN03013  264 IHYETTGPEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGF 338

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1899762177 301 LPTVLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLT 373
Cdd:PLN03013  339 IPKNLDQKIMDEVIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIY 411
PLN00011 PLN00011
cysteine synthase
 70-386 6.23e-47

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 166.72  E-value: 6.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  70 ILEAVGGTPLVKLNKIPQslGLKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPG-CTIIEPTSGNTGIGLAMAA 148
Cdd:PLN00011   11 VTELIGNTPMVYLNNIVD--GCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 149 AARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEAAFdspEGLIAVSQRLQRSIPDSVILDQYRNAGNPLAHYDGTGA 228
Cdd:PLN00011   89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGL---KGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 229 EIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPegsilAEPEELNQTNVSFYEVEGVGYDFLPTVLDRS 308
Cdd:PLN00011  166 EIWRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDLT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 309 VVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELKE-GQNCVVVLPDNIRNYL-TKFVSDNWMEARNF 386
Cdd:PLN00011  241 IVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLsTKLFESVRYEAENL 320
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 50-387 5.21e-46

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 165.13  E-value: 5.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  50 TETSPHHHEPLAPKPSVLP------SILEAVGGTPLVKLNKIPQSLGLKcnVYVKCEFLNPGGSVKDRIGVRMVLEAERK 123
Cdd:PLN02556   27 TVGSPSFAQRLRDLPKDLPgtkiktDASQLIGKTPLVYLNKVTEGCGAY--IAAKQEMFQPTSSIKDRPALAMIEDAEKK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 124 GLLKPG-CTIIEPTSGNTGIGLAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRT-PTEAAfdspEGLIAVSQRLQ 201
Cdd:PLN02556  105 NLITPGkTTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTdPTKGM----GGTVKKAYELL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 202 RSIPDSVILDQYRNAGNPLAHYDGTGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPegsilAEPE 281
Cdd:PLN02556  181 ESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEP-----AESN 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 282 ELNQTNVSFYEVEGVGYDFLPTVLDRSVVDRWYKFNDRVALPLARRLIRDEGLLCGGSSGGNLYVALEAAKELK-EGQNC 360
Cdd:PLN02556  256 VLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPEnKGKLI 335

                         330       340
                  ....*....|....*....|....*...
gi 1899762177 361 VVVLPDNIRNYLTKFVSDNW-MEARNFK 387
Cdd:PLN02556  336 VTVHPSFGERYLSSVLFQELrKEAENMQ 363
PLN02356 PLN02356
phosphateglycerate kinase
 57-375 3.31e-40

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 150.91  E-value: 3.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  57 HEPLApKPSVLPSILEAVGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGCTIIEPT 136
Cdd:PLN02356   35 KKPLS-KKKPRNGLIDAIGNTPLIRINSLSEATG--CEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 137 SGNTGIGLAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRT--------------PTEAAFDSPE----------- 191
Cdd:PLN02356  112 AGSTAISLATVAPAYGCKCHVVIPDDVAIEKSQILEALGATVERVrpvsithkdhyvniARRRALEANElaskrrkgset 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 192 ---------GLIAVSQRLQRSIPDSV----ILDQYRNAGNPLAHYDGTGAEIVEQLGGRVDMIVIGTGTGGTMTGIGRRI 258
Cdd:PLN02356  192 dgihlektnGCISEEEKENSLFSSSCtggfFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 259 KESCPNCQVIAADPEGSIL------------AEPEELNQTNVSFYEVEGVGYDFLPTVLDRSVVDRWYKFNDRVALPLAR 326
Cdd:PLN02356  272 QEKNPNIKCFLIDPPGSGLfnkvtrgvmytrEEAEGRRLKNPFDTITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSR 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1899762177 327 RLIRDEGLLCGGSSGGNLYVALEAAKELKEGQNCVVVLPDNIRNYLTKF 375
Cdd:PLN02356  352 YLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGHTIVTILCDSGMRHLSKF 400
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 401-524 2.19e-28

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: 109.16  E-value: 2.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 401 KVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAKPSDLVHRVIFKQFVKIDH 480
Cdd:cd04608     3 IVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVDL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1899762177 481 EENVGRASRILEKDSFVLVTRQEigatptERLVGVLTQREMLNF 524
Cdd:cd04608    83 DTPLGALSRILERDHFALVVDGQ------GKVLGIVTRIDLLNY 120
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 59-242 2.89e-19

Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.


Pssm-ID: 107206 [Multi-domain]  Cd Length: 324  Bit Score: 88.80  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  59 PLAPKPSVlpSILEavGGTPLVKLNKIPQSLGLKcNVYVKCEFLNPGGSVKDR---IGVRMVLEAERKgllkpgcTIIEP 135
Cdd:cd01563     9 PVTEDDIV--SLGE--GNTPLVRAPRLGERLGGK-NLYVKDEGLNPTGSFKDRgmtVAVSKAKELGVK-------AVACA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 136 TSGNTGIGLAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIrtPTEAAFDspEGLIAVSQRLQRSIPDSVildqyrN 215
Cdd:cd01563    77 STGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVL--AVEGNFD--DALRLVRELAEENWIYLS------N 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1899762177 216 AGNPLaHYDGT---GAEIVEQLGGRV-DMIV 242
Cdd:cd01563   147 SLNPY-RLEGQktiAFEIAEQLGWEVpDYVV 176
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 74-180 1.07e-18

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: 87.95  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  74 VGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDR---IGVRMVLEAERKgllkpgcTIIEPTSGNTGIGLAMAAAA 150
Cdd:COG0498    64 EGGTPLVKAPRLADELG--KNLYVKEEGHNPTGSFKDRamqVAVSLALERGAK-------TIVCASSGNGSAALAAYAAR 134

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1899762177 151 RGYRCLIVMPE-KMSNEKVDTLKALGAEVIR 180
Cdd:COG0498   135 AGIEVFVFVPEgKVSPGQLAQMLTYGAHVIA 165
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 77-275 4.69e-18

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: 85.09  E-value: 4.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVL---EAERKgllkpgCTIIEPTSGNTGIGLAMAAAARGY 153
Cdd:COG1171    25 TPLLRSPTLSERLG--AEVYLKLENLQPTGSFKLRGAYNALAslsEEERA------RGVVAASAGNHAQGVAYAARLLGI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 154 RCLIVMPEKMSNEKVDTLKALGAEVIRtpTEAAFDSPEgliAVSQRLQRS-----IPDS----VIldqyrnAGNplahyd 224
Cdd:COG1171    97 PATIVMPETAPAVKVAATRAYGAEVVL--HGDTYDDAE---AAAAELAEEegatfVHPFddpdVI------AGQ------ 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1899762177 225 GT-GAEIVEQLGGrVDMIVigtgtggtmtgigrrIKESCPNCQVIAADPEGS 275
Cdd:COG1171   160 GTiALEILEQLPD-LDAVFvpvggggliagvaaaLKALSPDIRVIGVEPEGA 210
PRK06381 PRK06381
threonine synthase; Validated
 75-235 2.94e-17

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 82.83  E-value: 2.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  75 GGTPLVKLNKIPQSLGLKcNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLlkpgCTIIEPTSGNTGIGLAMAAAARGYR 154
Cdd:PRK06381   14 GGTPLLRARKLEEELGLR-KIYLKFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 155 CLIVMPEKMSNEKVDTLKALGAEVIRTP---TEAAFDSPEglIAVSQRLQRSIPDSVildqyrnagNPLAHYDGTGA--- 228
Cdd:PRK06381   89 AVIFIPRSYSNSRVKEMEKYGAEIIYVDgkyEEAVERSRK--FAKENGIYDANPGSV---------NSVVDIEAYSAiay 157


                  ....*..
gi 1899762177 229 EIVEQLG 235
Cdd:PRK06381  158 EIYEALG 164
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 77-242 2.39e-16

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: 79.84  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVK---LNKIpqslgLKCNVYVKCEFLNPGGSVKDRIGVRMVL----EAERKGllkpgctIIEPTSGNTGIGLAMAAA 149
Cdd:cd01562    18 TPLLTsptLSEL-----LGAEVYLKCENLQKTGSFKIRGAYNKLLslseEERAKG-------VVAASAGNHAQGVAYAAK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 150 ARGYRCLIVMPEKMSNEKVDTLKALGAEVIRtpTEAAFDSPEgliAVSQRLQRS-----IP----DSVILDQyrnagnpl 220
Cdd:cd01562    86 LLGIPATIVMPETAPAAKVDATRAYGAEVVL--YGEDFDEAE---AKARELAEEegltfIHpfddPDVIAGQ-------- 152

                         170       180
                  ....*....|....*....|...
gi 1899762177 221 ahydGT-GAEIVEQLGGrVDMIV 242
Cdd:cd01562   153 ----GTiGLEILEQVPD-LDAVF 170
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 75-242 3.29e-14

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 73.57  E-value: 3.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  75 GGTPLVKLNKIPQSLGLKcNVYVKCEFLNPGGSVKDRiGVRMVLEAERKGLLKpgcTIIEPTSGNTGIGLAMAAAARGYR 154
Cdd:TIGR00260  21 GVTPLFRAPALAANVGIK-NLYVKELGHNPTLSFKDR-GMAVALTKALELGND---TVLCASTGNTGAAAAAYAGKAGLK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 155 CLIVMPE-KMSNEKVDTLKALGAEVIRtpTEAAFDSpegliavSQRLQRSIPD--------SVILDQYRNAGNPLAHYdg 225
Cdd:TIGR00260  96 VVVLYPAgKISLGKLAQALGYNAEVVA--IDGNFDD-------AQRLVKQLFEdkpalglnSANSIPYRLEGQKTYAF-- 164

                         170
                  ....*....|....*...
gi 1899762177 226 tgaEIVEQLGGRV-DMIV 242
Cdd:TIGR00260 165 ---EAVEQLGWEApDKVV 179
PRK08197 PRK08197
threonine synthase; Validated
 1-242 6.84e-14

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 73.50  E-value: 6.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177   1 MASNNSHRNCPMNG-HLAVNGKQQTIPEDDPManFIRPD-QPSRCTWALGTTETSP----HHHEPLAPK-PSVLPSILEa 73
Cdd:PRK08197    1 PFSYVSHLECSKCGeTYDADQVHNLCKCGKPL--LVRYDlEAVKQAVTREALAGRPanlwRYHELLPVRdPEHIVSLGE- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  74 vGGTPLVKLNKIPQSLGLKcNVYVKCEFLNPGGSVKDR---IGVRMVLEAERKGLLKPgctiiepTSGNTGIGLAMAAAA 150
Cdd:PRK08197   78 -GMTPLLPLPRLGKALGIG-RLWVKDEGLNPTGSFKARglaVGVSRAKELGVKHLAMP-------TNGNAGAAWAAYAAR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 151 RGYRCLIVMPEKMSNEKVDTLKALGAEVIRTpteaafdspEGLIA-----VSQRLQRS--IPDSVILDQYRNAGNPLahy 223
Cdd:PRK08197  149 AGIRATIFMPADAPEITRLECALAGAELYLV---------DGLISdagkiVAEAVAEYgwFDVSTLKEPYRIEGKKT--- 216

                         250       260
                  ....*....|....*....|
gi 1899762177 224 dgTGAEIVEQLGGRV-DMIV 242
Cdd:PRK08197  217 --MGLELAEQLGWRLpDVIL 234
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 77-181 1.78e-12

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 69.14  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGLKcNVYVKCE---F-LNP----GGS------VKDRIGVRM------VLEAERKGLLKPGCTIIEPT 136
Cdd:PRK08206   45 TPLVALPDLAAELGVG-SILVKDEsyrFgLNAfkalGGAyavarlLAEKLGLDIselsfeELTSGEVREKLGDITFATAT 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1899762177 137 SGNTGIGLAMAAAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRT 181
Cdd:PRK08206  124 DGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT 168
PRK08246 PRK08246
serine/threonine dehydratase;
95-242 9.05e-12

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 66.13  E-value: 9.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  95 VYVKCEFLNPGGSVKDRIGVRMVLEAErkgllKPGCTIIEPTSGNTGIGLAMAAAARGYRCLIVMPEKMSNEKVDTLKAL 174
Cdd:PRK08246   39 VWLKLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRAL 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1899762177 175 GAEVIRTPTEAAfdspEGLIAVSQRLQRSipdsvildqyrnaGNPLAH-YD--------GT-GAEIVEQLGGrVDMIV 242
Cdd:PRK08246  114 GAEVVVVGAEYA----DALEAAQAFAAET-------------GALLCHaYDqpevlagaGTlGLEIEEQAPG-VDTVL 173
PRK06450 PRK06450
threonine synthase; Validated
 75-237 2.26e-11

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 65.14  E-value: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  75 GGTPLVKLNkipqslglkcNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLlkpgCTIIEPTSGNTGIGLAMAAAARGYR 154
Cdd:PRK06450   57 GRTPLIKKG----------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 155 CLIVMPEKMSNEKVDTLKALGAEVIRTP------TEAAFDSpeGLIAVSQRLQrsiPdsvildQYRNAGNPLAHydgtga 228
Cdd:PRK06450  123 VKIFVPETASGGKLKQIESYGAEVVRVRgsredvAKAAENS--GYYYASHVLQ---P------QFRDGIRTLAY------ 185


                  ....*....
gi 1899762177 229 EIVEQLGGR 237
Cdd:PRK06450  186 EIAKDLDWK 194
PRK06815 PRK06815
threonine/serine dehydratase;
73-313 6.08e-11

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 63.56  E-value: 6.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  73 AVGGTPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRiGVRMVL-----EAERKGllkpgctIIEPTSGNTGIGLAMA 147
Cdd:PRK06815   17 QVRVTPLEHSPLLSQHTG--CEVYLKCEHLQHTGSFKFR-GASNKLrllneAQRQQG-------VITASSGNHGQGVALA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 148 AAARGYRCLIVMPEKMSNEKVDTLKALGAEVIRTPTEA--------AFDSPEGLIAVS--QRLQrsipdsVILDQyrnag 217
Cdd:PRK06815   87 AKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYGGDAlnaelaarRAAEQQGKVYISpyNDPQ------VIAGQ----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 218 nplahydGT-GAEIVEQLGgRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEG------SILA----EPEElnQT 286
Cdd:PRK06815  156 -------GTiGMELVEQQP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAE--QP 225

                         250       260
                  ....*....|....*....|....*..
gi 1899762177 287 NVSFYEVEGVGYDFLPTVLDRSVVDRW 313
Cdd:PRK06815  226 TLSDGTAGGVEPGAITFPLCQQLIDQK 252
PRK05638 PRK05638
threonine synthase; Validated
 75-180 2.48e-10

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 62.52  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  75 GGTPLVKlNKIPQSLGLkcNVYVKCEFLNPGGSVKDR---IGVRMVLEAERKGLlkpgctiIEPTSGNTGIGLAMAAAAR 151
Cdd:PRK05638   65 GGTPLIR-ARISEKLGE--NVYIKDETRNPTGSFRDRlatVAVSYGLPYAANGF-------IVASDGNAAASVAAYSARA 134

                          90       100
                  ....*....|....*....|....*....
gi 1899762177 152 GYRCLIVMPEKMSNEKVDTLKALGAEVIR 180
Cdd:PRK05638  135 GKEAFVVVPRKVDKGKLIQMIAFGAKIIR 163
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
410-529 4.14e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 57.95  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAK------PSDLVHRVIFKQFVKIDHEEN 483
Cdd:COG3448    12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRPVVTVTPDTP 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1899762177 484 VGRASRIL--EKDSFVLVTRQEigatptERLVGVLTQREMLNFVADRA 529
Cdd:COG3448    92 LEEAAELMleHGIHRLPVVDDD------GRLVGIVTRTDLLRALARLL 133
PRK06608 PRK06608
serine/threonine dehydratase;
77-241 1.14e-09

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 60.17  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGLKcnVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPgcTIIEPTSGNTGIGLAMAAAARGYRCL 156
Cdd:PRK06608   24 TPIVHSESLNEMLGHE--IFFKVESLQKTGAFKVRGVLNHLLELKEQGKLPD--KIVAYSTGNHGQAVAYASKLFGIKTR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 157 IVMPEKMSNEKVDTLKALGAEVIRTPTEAAFDSpegliAVSQRLQRS---IP----DSVIldqyrnAGNPLAHYdgtgaE 229
Cdd:PRK06608  100 IYLPLNTSKVKQQAALYYGGEVILTNTRQEAEE-----KAKEDEEQGfyyIHpsdsDSTI------AGAGTLCY-----E 163

                         170
                  ....*....|..
gi 1899762177 230 IVEQLGGRVDMI 241
Cdd:PRK06608  164 ALQQLGFSPDAI 175
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
410-525 1.37e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 57.97  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVaDTGAIKGVVHLPNLLSKLLNRLAKPSDLVHRVIFKQFVKIDHEENVGRASR 489
Cdd:COG2524    96 VITVSPDTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALR 174

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1899762177 490 ILEKD--SFVLVTRQEigatptERLVGVLTQREMLNFV 525
Cdd:COG2524   175 LMLEHgiGRLPVVDDD------GKLVGIITRTDILRAL 206
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 77-179 2.85e-09

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: 58.46  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDR-IGVRMVLEAERKGLLKPGctIIEPTSGNTGigLAMAAAAR--GY 153
Cdd:cd06448     2 TPLIESTALSKTAG--CNVFLKLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAG--LAAAYAARklGV 75

                          90       100
                  ....*....|....*....|....*.
gi 1899762177 154 RCLIVMPEKMSNEKVDTLKALGAEVI 179
Cdd:cd06448    76 PCTIVVPESTKPRVVEKLRDEGATVV 101
PRK06110 PRK06110
threonine dehydratase;
87-179 7.07e-09

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 57.31  E-value: 7.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  87 QSLGlkCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKPGctIIEPTSGNTGIGLAMAAAARGYRCLIVMPEKMSNE 166
Cdd:PRK06110   32 ERLG--CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVE 107

                          90
                  ....*....|...
gi 1899762177 167 KVDTLKALGAEVI 179
Cdd:PRK06110  108 KNAAMRALGAELI 120
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 410-523 2.83e-08

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 51.86  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAKPSDLVHRVIFKQFVKIDHEENVGRASR 489
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEALE 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1899762177 490 ILEKD--SFVLVTRQEigatptERLVGVLTQREMLN 523
Cdd:cd02205    84 LMLEHgiRRLPVVDDD------GKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
410-528 5.27e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 51.79  E-value: 5.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAKPSDL-VHRVIFKQFVKIDHEENVGRAS 488
Cdd:COG0517    11 VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTVSPDTSLEEAA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1899762177 489 RILEK---DSFVLVTRQeigatptERLVGVLTQREMLNFVADR 528
Cdd:COG0517    91 ELMEEhkiRRLPVVDDD-------GRLVGIITIKDLLKALLEP 126
PLN02970 PLN02970
serine racemase
 77-275 8.05e-08

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 54.30  E-value: 8.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGLKCnvYVKCEFLNPGGSVKDRIGVRMVL----EAERKGllkpgctIIEPTSGNTGIGLAMAAAARG 152
Cdd:PLN02970   28 TPVLTSSSLDALAGRSL--FFKCECFQKGGAFKFRGACNAIFslsdDQAEKG-------VVTHSSGNHAAALALAAKLRG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 153 YRCLIVMPEKMSNEKVDTLKALGAEVIRtpTEAAFDSPEgliAVSQRLQRSiPDSVILDQYrNAGNPLAHYDGTGAEIVE 232
Cdd:PLN02970   99 IPAYIVVPKNAPACKVDAVIRYGGIITW--CEPTVESRE---AVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLE 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1899762177 233 QLGGrVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGS 275
Cdd:PLN02970  172 QVPE-LDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
PRK08329 PRK08329
threonine synthase; Validated
 67-178 1.35e-07

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 53.68  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  67 LPSILEAVggTPLVKLNKipqslglkcNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKpgctIIEPTSGNTGIGLAM 146
Cdd:PRK08329   57 LPHLTPPI--TPTVKRSI---------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINE----VVIDSSGNAALSLAL 121

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1899762177 147 AAAARGYRCLIVMPEKMSNEKVDTLKALGAEV 178
Cdd:PRK08329  122 YSLSEGIKVHVFVSYNASKEKISLLSRLGAEL 153
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 408-527 1.37e-07

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 50.21  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 408 ETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAKPSDL-VHRVIFKQFVKIDHEENVGR 486
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSPDDSLAE 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1899762177 487 ASRILEKDSF--VLVTRQeigatptERLVGVLTQREMLNFVAD 527
Cdd:COG2905    87 ALELMEEHRIrhLPVVDD-------GKLVGIVSITDLLRALSE 122
CBS COG0517
CBS domain [Signal transduction mechanisms];
410-461 7.44e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 48.32  E-value: 7.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLA 461
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 410-458 7.49e-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: 7.49e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLN 458
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
eutB PRK07476
threonine dehydratase; Provisional
 74-244 9.25e-07

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 50.73  E-value: 9.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  74 VGGTPLVklnkIPQSLG--LKCNVYVKCEFLNPGGSVKDRIGVRMVL---EAERKgllkpgCTIIEPTSGNTGIGLAMAA 148
Cdd:PRK07476   17 VRRTPLV----ASASLSarAGVPVWLKLETLQPTGSFKLRGATNALLslsAQERA------RGVVTASTGNHGRALAYAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 149 AARGYRCLIVMPEKMSNEKVDTLKALGAEVI---RTPTEAAFdspEGLIAVSQRLQRSIP----DSVILDQyrnagnpla 221
Cdd:PRK07476   87 RALGIRATICMSRLVPANKVDAIRALGAEVRivgRSQDDAQA---EVERLVREEGLTMVPpfddPRIIAGQ--------- 154

                         170       180
                  ....*....|....*....|....
gi 1899762177 222 hydGT-GAEIVEQLGgRVDMIVIG 244
Cdd:PRK07476  155 ---GTiGLEILEALP-DVATVLVP 174
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
77-179 9.50e-07

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 51.29  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRiGV--RMV-LEAERKGllkpgCTIIEPTSGNTGIGLAMAAAARGY 153
Cdd:PRK09224   21 TPLEKAPKLSARLG--NQVLLKREDLQPVFSFKLR-GAynKMAqLTEEQLA-----RGVITASAGNHAQGVALSAARLGI 92

                          90       100
                  ....*....|....*....|....*.
gi 1899762177 154 RCLIVMPEKMSNEKVDTLKALGAEVI 179
Cdd:PRK09224   93 KAVIVMPVTTPDIKVDAVRAFGGEVV 118
PRK12483 PRK12483
threonine dehydratase; Reviewed
 77-275 2.11e-06

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 50.18  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGlkCNVYVKCEFLNPGGSVKDRIG----VRMVLEAERKGllkpgctIIEPTSGNTGIGLAMAAAARG 152
Cdd:PRK12483   38 TPLQRAPNLSARLG--NQVLLKREDLQPVFSFKIRGAynkmARLPAEQLARG-------VITASAGNHAQGVALAAARLG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 153 YRCLIVMPEKMSNEKVDTLKALGAEVIRtpteaAFDSPEGLIAVSQRLQRSIPDSVIL---DQYRNAGNplahydGT-GA 228
Cdd:PRK12483  109 VKAVIVMPRTTPQLKVDGVRAHGGEVVL-----HGESFPDALAHALKLAEEEGLTFVPpfdDPDVIAGQ------GTvAM 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1899762177 229 EIVEQLGGRVDMIVIGTGTGGTMTGIGRRIKESCPNCQVIAADPEGS 275
Cdd:PRK12483  178 EILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
404-523 5.99e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 46.06  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 404 ILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLlnrlakPSDLVHRVIFKQFVKIDHEEN 483
Cdd:COG4109    21 IMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKD------DDTPIEDVMTKNPITVTPDTS 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1899762177 484 VGRASRIL--EKDSFVLVTRQEigatptERLVGVLTQREMLN 523
Cdd:COG4109    95 LASAAHKMiwEGIELLPVVDDD------GRLLGIISRQDVLK 130
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 408-447 1.80e-05

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 44.05  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1899762177 408 ETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVV 447
Cdd:cd09836    67 KNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVI 106
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
393-448 4.78e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 44.49  E-value: 4.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1899762177 393 HNQKWWNEKVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVH 448
Cdd:COG2524   143 EGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIIT 198
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 410-456 8.63e-05

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 42.14  E-value: 8.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKL 456
Cdd:cd17775    71 LITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
411-462 1.03e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 42.16  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1899762177 411 LTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAK 462
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEE 135
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 408-522 1.10e-04

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 41.93  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 408 ETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLLSKLLNRLAKPS------------DLVHRVIFKQF 475
Cdd:cd04632     2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRggdrggekermlDLPVYDIMSSP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1899762177 476 VK-IDHEENVGRA-SRILEKD-SFVLVTRQEigatptERLVGVLTQREML 522
Cdd:cd04632    82 VVtVTRDATVADAvERMLENDiSGLVVTPDD------NMVIGILTKTDVL 125
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 77-179 3.14e-04

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 43.65  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGLKcnVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKpgcTIIEPTSGNTGIGLAMAAAARGYRCL 156
Cdd:PRK13803  272 TPLTEAKRLSDIYGAR--IYLKREDLNHTGSHKINNALGQALLAKRMGKTR---IIAETGAGQHGVATATACALFGLKCT 346

                          90       100
                  ....*....|....*....|....*.
gi 1899762177 157 IVMPE---KMSNEKVDTLKALGAEVI 179
Cdd:PRK13803  347 IFMGEediKRQALNVERMKLLGANVI 372
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
77-179 3.57e-04

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 42.80  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLglKCNVYVKCEFLNPGGSVKDRIG---VRMVLEAER-KGllkpgctIIEPTSGNTGIGLAMAAAARG 152
Cdd:PRK08638   28 TPLPRSNYLSERC--KGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKrKG-------VVACSAGNHAQGVALSCALLG 98

                          90       100
                  ....*....|....*....|....*..
gi 1899762177 153 YRCLIVMPEKMSNEKVDTLKALGAEVI 179
Cdd:PRK08638   99 IDGKVVMPKGAPKSKVAATCGYGAEVV 125
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 410-524 3.98e-04

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 40.48  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 410 LLTVRDDAHISDAIETMKQNNRTHLPVVaDTGAIKGVV-------HLPNLLSKL--LNRLAKPSDL-VHRVIFKQFVKID 479
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVV-DDGKLVGIVtdrdllrASPSKATSLsiYELNYLLSKIpVKDIMTKDVITVS 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1899762177 480 HEENVGRASRILEKdsfvlvtrQEIGATP---TERLVGVLTQREMLNF 524
Cdd:cd04584    89 PDDTVEEAALLMLE--------NKIGCLPvvdGGKLVGIITETDILRA 128
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 412-517 4.34e-04

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 39.91  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 412 TVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNlLSKllnRLAKPSDLVHRVIFKQFVKIDHEENVGRASRIL 491
Cdd:cd04605    12 TIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWD-ISK---AVALKKDSLEEIMTRNVITARPDEPIELAARKM 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 1899762177 492 EKDSfvlvtrqeIGATPT----ERLVGVLT 517
Cdd:cd04605    88 EKHN--------ISALPVvdddRRVIGIIT 109
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 412-453 8.81e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 39.29  E-value: 8.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1899762177 412 TVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVHLPNLL 453
Cdd:cd04604    82 TISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHDLL 123
PLN02550 PLN02550
threonine dehydratase
 77-179 1.07e-03

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 41.83  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGLKcnVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKpgcTIIEPTSGNTGIGLAMAAAARGYRCL 156
Cdd:PLN02550  110 SPLQLAKKLSERLGVK--VLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDK---GVICSSAGNHAQGVALSAQRLGCDAV 184

                          90       100
                  ....*....|....*....|...
gi 1899762177 157 IVMPEKMSNEKVDTLKALGAEVI 179
Cdd:PLN02550  185 IAMPVTTPEIKWQSVERLGATVV 207
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 411-517 1.51e-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: 38.47  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 411 LTVRDDAHISDAIETMKQNNRT-----HLPVVADTGAIKGVVHLPNLLskllnrLAKPSDLVHRVIFKQFVKIDHEENVG 485
Cdd:cd04606    12 VAVRPDWTVEEALEYLRRLAPDpetiyYIYVVDEDRRLLGVVSLRDLL------LADPDTKVSDIMDTDVISVSADDDQE 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1899762177 486 RASRILEKDSFVlvtrqeigATP----TERLVGVLT 517
Cdd:cd04606    86 EVARLFAKYDLL--------ALPvvdeEGRLVGIIT 113
PLN02569 PLN02569
threonine synthase
 48-238 1.98e-03

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 40.95  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  48 GTTeTSPHHHEPLAPKPSVLP--------SILEavGGTPLV---KLNKipQSLGLKcNVYVKCEFLNPGGSVKDRIGVRM 116
Cdd:PLN02569  100 GKT-TWPYGSGVWSKKEWVLPeiddddivSLFE--GNSNLFwaeRLGK--EFLGMN-DLWVKHCGISHTGSFKDLGMTVL 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177 117 VLEAERKGLL-KPGCTIIEPTSGNTGIGLAMAAAARGYRCLIVMPE-KMSNEKVDTLKALGAEVIRTPTEaaFDSPEGLI 194
Cdd:PLN02569  174 VSQVNRLRKMaKPVVGVGCASTGDTSAALSAYCAAAGIPSIVFLPAdKISIAQLVQPIANGALVLSIDTD--FDGCMRLI 251

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1899762177 195 -AVSQRLqrSIPDSVILDQYRNAGNPLAhydgtGAEIVEQLGGRV 238
Cdd:PLN02569  252 rEVTAEL--PIYLANSLNSLRLEGQKTA-----AIEILQQFDWEV 289
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 77-184 2.20e-03

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


Pssm-ID: 107207  Cd Length: 365  Bit Score: 40.60  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGlKCNVYVKCEFLNPGGSVKDRIGVRMVLEAERKGLLKpgcTIIEPTSGNTGIGLAMAAAARGYRCL 156
Cdd:cd06446    35 TPLYRAKRLSEYLG-GAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKR---VIAETGAGQHGVATATACALFGLECE 110

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1899762177 157 IVMPEKMSNEK---VDTLKALGAEVIRTPTE 184
Cdd:cd06446   111 IYMGAVDVERQplnVFRMELLGAEVVPVPSG 141
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 400-447 2.50e-03

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 38.08  E-value: 2.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1899762177 400 EKVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVV 447
Cdd:cd17778    75 TPVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGII 122
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 411-448 3.39e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 37.57  E-value: 3.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1899762177 411 LTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVVH 448
Cdd:cd17781    71 LCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVLD 108
PRK13028 PRK13028
tryptophan synthase subunit beta; Provisional
 77-179 3.80e-03

tryptophan synthase subunit beta; Provisional


Pssm-ID: 183851  Cd Length: 402  Bit Score: 39.85  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1899762177  77 TPLVKLNKIPQSLGlKCNVYVKCEFLNPGGSVK--DRIGvrMVLEAERKGLLKpgcTIIEPTSGNTGIGLAMAAAARGYR 154
Cdd:PRK13028   63 TPLYHAKRLSEELG-GAQIYLKREDLNHTGAHKinNCLG--QALLAKRMGKKR---LIAETGAGQHGVATATAAALFGLE 136

                          90       100
                  ....*....|....*....|....*...
gi 1899762177 155 CLIVMPEK-MSNEK--VDTLKALGAEVI 179
Cdd:PRK13028  137 CEIYMGEVdIERQHpnVFRMKLLGAEVV 164
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 399-447 9.16e-03

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 36.83  E-value: 9.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1899762177 399 NEKVQILPLETLLTVRDDAHISDAIETMKQNNRTHLPVVADTGAIKGVV 447
Cdd:cd17779    79 NEPVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIV 127
 
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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