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Conserved domains on  [gi|768021879|ref|XP_011528085|]
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cystathionine beta-synthase isoform X6 [Homo sapiens]

Protein Classification

cystathionine beta-synthase( domain architecture ID 11490202)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
1-453 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: 769.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:TIGR01137  29 LAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIVLPEKMSSEKVDVLRALG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   81 AEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:TIGR01137 109 AEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  161 RKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:TIGR01137 189 RYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  241 CGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLT 319
Cdd:TIGR01137 269 VGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHARVKDLHLPAPVT 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  320 VLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILE 399
Cdd:TIGR01137 349 VHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLE 428
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021879  400 MDHFALVVHEQIQsqdqawagvvggpadhstgkssqrqmvFGVVTAIDLLNFVA 453
Cdd:TIGR01137 429 MDSSAIVVEEGKP---------------------------IGVVTKIDLLSFLA 455
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
1-453 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: 769.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:TIGR01137  29 LAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIVLPEKMSSEKVDVLRALG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   81 AEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:TIGR01137 109 AEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  161 RKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:TIGR01137 189 RYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  241 CGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLT 319
Cdd:TIGR01137 269 VGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHARVKDLHLPAPVT 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  320 VLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILE 399
Cdd:TIGR01137 349 VHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLE 428
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021879  400 MDHFALVVHEQIQsqdqawagvvggpadhstgkssqrqmvFGVVTAIDLLNFVA 453
Cdd:TIGR01137 429 MDSSAIVVEEGKP---------------------------IGVVTKIDLLSFLA 455
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
1-278 1.13e-156

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: 445.42  E-value: 1.13e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:cd01561   20 YAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:cd01561  100 AEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGKVDAFVAGVGTGGTITGVA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 161 RKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:cd01561  179 RYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAFAMARRLAREEGLL 253
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768021879 241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 278
Cdd:cd01561  254 VGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
2-279 7.19e-144

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: 413.29  E-value: 7.19e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:COG0031   32 AKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:COG0031  112 EVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDGKVDAFVAGVGTGGTITGVGR 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 162 KLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLC 241
Cdd:COG0031  189 YLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILV 263
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768021879 242 GGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 279
Cdd:COG0031  264 GISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
PRK10717 PRK10717
cysteine synthase A; Provisional
2-291 6.99e-106

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 317.57  E-value: 6.99e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:PRK10717  32 GKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTI 156
Cdd:PRK10717 112 ELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPANREAHYETTGPEIWEQTDGKVDGFVCAVGTGGTL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 157 TGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARM 232
Cdd:PRK10717 191 AGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---EGIGQGRITANLEGAPIDDAIRIPDEEALSTAYR 267
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021879 233 LIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 291
Cdd:PRK10717 268 LLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGL 326
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
2-271 2.39e-73

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: 232.97  E-value: 2.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:pfam00291  26 LKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   82 EIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:pfam00291 103 EVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQLGGDPDAVVVPVGGGGLIAGIAR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  162 KLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTVVDKWFKS----NDEEAFTFARML 233
Cdd:pfam00291 177 GLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDLLDEYVGEvvtvSDEEALEAMRLL 256
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 768021879  234 IAQEGLLCGGSAGSTVAVA-VKAAQELQEGQRCVVILPD 271
Cdd:pfam00291 257 ARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
317-364 2.77e-09

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 52.52  E-value: 2.77e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 768021879   317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
 
Name Accession Description Interval E-value
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
1-453 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: 769.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:TIGR01137  29 LAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAAIKGYKCIIVLPEKMSSEKVDVLRALG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   81 AEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:TIGR01137 109 AEIVRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPEILEQCEGKLDMFVAGVGTGGTITGIA 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  161 RKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:TIGR01137 189 RYLKESCPGCRIVGADPEGSILAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKVVDEWIKTDDKESFTMARRLIKEEGLL 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  241 CGGSAGSTVAVAVKAAQ-ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLT 319
Cdd:TIGR01137 269 VGGSSGSAVVAALKAAEdELQEGQRCVVLLPDSIRNYMTKFLNDEWMLDNGFLDDEDLTVKDVLWWHARVKDLHLPAPVT 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  320 VLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILE 399
Cdd:TIGR01137 349 VHPTETVGDAIEILREYGFDQLPVVDEAGKVLGSVTLRELLSALFAGKAQPSDAVSKVMSKKFIQIGLGETLSDLSKFLE 428
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021879  400 MDHFALVVHEQIQsqdqawagvvggpadhstgkssqrqmvFGVVTAIDLLNFVA 453
Cdd:TIGR01137 429 MDSSAIVVEEGKP---------------------------IGVVTKIDLLSFLA 455
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
1-278 1.13e-156

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: 445.42  E-value: 1.13e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:cd01561   20 YAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRTPTnARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:cd01561  100 AEVILTPE-AEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGKVDAFVAGVGTGGTITGVA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 161 RKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:cd01561  179 RYLKEKNPNVRIVGVDPVGSVL-----FSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAFAMARRLAREEGLL 253
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768021879 241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 278
Cdd:cd01561  254 VGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
2-279 7.19e-144

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: 413.29  E-value: 7.19e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:COG0031   32 AKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTNarfDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:COG0031  112 EVVLTPGA---EGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDGKVDAFVAGVGTGGTITGVGR 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 162 KLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLC 241
Cdd:COG0031  189 YLKERNPDIKIVAVEPEGSPL-----LSGGEPGPHKIEGIGAGFVPKILDPSLIDEVITVSDEEAFAMARRLAREEGILV 263
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768021879 242 GGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK 279
Cdd:COG0031  264 GISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLST 301
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
2-278 1.86e-106

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: 317.77  E-value: 1.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR01139  25 VKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAARGYKLILTMPETMSIERRKLLKAYGA 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   82 EIVRTPTNARFdspESHVGVAWRLKNEIPNSH-ILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIA 160
Cdd:TIGR01139 105 ELVLTPGAEGM---KGAIAKAEEIAASTPNSYfMLQQFENPANPEIHRKTTGPEIWRDTDGKLDAFVAGVGTGGTITGVG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  161 RKLKEKCPGCRIIGVDPEGSILaepeeLNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:TIGR01139 182 EVLKEQKPNIKIVAVEPAESPV-----LSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSDEEAIETARRLAAEEGIL 256
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 768021879  241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMT 278
Cdd:TIGR01139 257 VGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLS 294
PRK10717 PRK10717
cysteine synthase A; Provisional
2-291 6.99e-106

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 317.57  E-value: 6.99e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:PRK10717  32 GKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLALVAAARGYKTVIVMPETQSQEKKDLLRALGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTnARFDSPESHVGVAWRLKNEI----PNSHI-LDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTI 156
Cdd:PRK10717 112 ELVLVPA-APYANPNNYVKGAGRLAEELvasePNGAIwANQFDNPANREAHYETTGPEIWEQTDGKVDGFVCAVGTGGTL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 157 TGIARKLKEKCPGCRIIGVDPEGSIL----AEPEELNQTEQTTyevEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARM 232
Cdd:PRK10717 191 AGVSRYLKETNPKVKIVLADPTGSALysyyKTGELKAEGSSIT---EGIGQGRITANLEGAPIDDAIRIPDEEALSTAYR 267
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021879 233 LIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGF 291
Cdd:PRK10717 268 LLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQSKLFNPDFLREKGL 326
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
2-278 1.16e-101

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


Pssm-ID: 273463  Cd Length: 299  Bit Score: 305.74  E-value: 1.16e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR01136  26 AKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAARGYKLILTMPETMSLERRKLLRAYGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   82 EIVRTPtnarfdsPESHVGVAWRLKNEIPNSH----ILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTIT 157
Cdd:TIGR01136 106 ELILTP-------GEEGMKGAIDKAEELAAETnkyvMLDQFENPANPEAHYKTTGPEIWRDTDGRIDHFVAGVGTGGTIT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  158 GIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQE 237
Cdd:TIGR01136 179 GVGRYLKEQNPNIQIVAVEP-----AESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDEDAIETARRLAREE 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 768021879  238 GLLCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMT 278
Cdd:TIGR01136 254 GILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLS 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
2-272 1.14e-77

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: 242.04  E-value: 1.14e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLkPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:cd00640   19 LKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIVMPEGASPEKVAQMRALGA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTNarfdsPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDG-KLDMLVASVGTGGTITGIA 160
Cdd:cd00640   98 EVVLVPGD-----FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPDAVVVPVGGGGNIAGIA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 161 RKLKEKCPGCRIIGVDPEgsilaepeelnqteqttyevegigydfiptvldrtvvdkWFKSNDEEAFTFARMLIAQEGLL 240
Cdd:cd00640  172 RALKELLPNVKVIGVEPE---------------------------------------VVTVSDEEALEAIRLLAREEGIL 212
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768021879 241 CGGSAGSTVAVAVKAAQELQEGQRCVVILPDS 272
Cdd:cd00640  213 VEPSSAAALAAALKLAKKLGKGKTVVVILTGG 244
cysM PRK11761
cysteine synthase CysM;
2-271 1.89e-73

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 233.23  E-value: 1.89e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:PRK11761  31 AKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGYRMKLIMPENMSQERRAAMRAYGA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTNarfDSPESHVGVAWRLKNEiPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:PRK11761 111 ELILVPKE---QGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTGPEIWRQTEGRITHFVSSMGTTGTIMGVSR 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 162 KLKEKCPGCRIIGVDP-EGS----ILAEPEElnqteqttyevegigydFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQ 236
Cdd:PRK11761 187 YLKEQNPAVQIVGLQPeEGSsipgIRRWPEE-----------------YLPKIFDASRVDRVLDVSQQEAENTMRRLARE 249
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768021879 237 EGLLCGGSAGSTVAVAVKAAQELqEGQRCVVILPD 271
Cdd:PRK11761 250 EGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICD 283
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
2-271 2.39e-73

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: 232.97  E-value: 2.39e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERdgtLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:pfam00291  26 LKLESLNPTGSFKDRGALNLLLRLKE---GEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   82 EIVRTPTNarFDSPESHVGvawRLKNEIPNSHILDQYRNASNPLAHYdTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:pfam00291 103 EVVLVGGD--YDEAVAAAR---ELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQLGGDPDAVVVPVGGGGLIAGIAR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  162 KLKEKCPGCRIIGVDPEGS-ILAEPEELNQTEQTT---YEVEGIGYDFIPTVLDRTVVDKWFKS----NDEEAFTFARML 233
Cdd:pfam00291 177 GLKELGPDVRVIGVEPEGApALARSLAAGRPVPVPvadTIADGLGVGDEPGALALDLLDEYVGEvvtvSDEEALEAMRLL 256
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 768021879  234 IAQEGLLCGGSAGSTVAVA-VKAAQELQEGQRCVVILPD 271
Cdd:pfam00291 257 ARREGIVVEPSSAAALAALkLALAGELKGGDRVVVVLTG 295
PLN02565 PLN02565
cysteine synthase
2-283 9.03e-73

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 232.12  E-value: 9.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN02565  34 AKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAFMAAAKGYKLIITMPASMSLERRIILLAFG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRT-PTNARfdspESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 159
Cdd:PLN02565 114 AELVLTdPAKGM----KGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIWKGTGGKVDAFVSGIGTGGTITGA 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 160 ARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGL 239
Cdd:PLN02565 190 GKYLKEQNPDIKLYGVEP-----VESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQVSSDEAIETAKLLALKEGL 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768021879 240 LCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 283
Cdd:PLN02565 265 LVGISSGAAAAAAIKIAKRPEnAGKLIVVIFPSFGERYLSSVLFE 309
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
2-285 9.62e-73

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: 231.32  E-value: 9.62e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR03945  26 AKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYKGLRFICVVDPNISPQNLKLLRAYGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   82 EIVRTptnarfDSPESHVG--------VAwRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDgKLDMLVASVGTG 153
Cdd:TIGR03945 106 EVEKV------TEPDETGGylgtriarVR-ELLASIPDAYWPNQYANPDNPRAHYHGTGREIARAFP-TLDYLFVGVSTT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  154 GTITGIARKLKEKCPGCRIIGVDPEGSIL--AEPeelnqteqTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFAR 231
Cdd:TIGR03945 178 GTLMGCSRRLRERGPNTKVIAVDAVGSVIfgGPP--------GRRHIPGLGASVVPELLDESLIDDVVHVPEYDTVAGCR 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768021879  232 MLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRW 285
Cdd:TIGR03945 250 RLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYLDTVYNDEW 303
PLN00011 PLN00011
cysteine synthase
2-283 1.27e-65

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 213.71  E-value: 1.27e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPG-DTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN00011  36 AKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIGAARGYKVILVMPSTMSLERRIILRALG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRTptnarfdspESHVGVAWRLK------NEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGG 154
Cdd:PLN00011 116 AEVHLT---------DQSIGLKGMLEkaeeilSKTPGGYIPQQFENPANPEIHYRTTGPEIWRDSAGKVDILVAGVGTGG 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 155 TITGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLI 234
Cdd:PLN00011 187 TATGVGKFLKEKNKDIKVCVVEP-----VESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQVTGEEAIETAKLLA 261
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768021879 235 AQEGLLCGGSAGSTVAVAVKAAQELQE-GQRCVVILPDSVRNYMTKFLSD 283
Cdd:PLN00011 262 LKEGLLVGISSGAAAAAALKVAKRPENaGKLIVVIFPSGGERYLSTKLFE 311
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
2-278 2.20e-65

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: 212.08  E-value: 2.20e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:TIGR01138  27 LKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALKGYRMKLLMPDNMSQERKAAMRAYGA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   82 EIVRTptnARFDSPESHVGVAWRLKNEIPNShILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIAR 161
Cdd:TIGR01138 107 ELILV---TKEEGMEGARDLALELANRGEGK-LLDQFNNPDNPYAHYTSTGPEIWQQTGGRITHFVSSMGTTGTIMGVSR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  162 KLKEKCPGCRIIGVDPEgsilaEPeelnqteqttYEVEGIGY---DFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEG 238
Cdd:TIGR01138 183 FLKEQNPPVQIVGLQPE-----EG----------SSIPGIRRwptEYLPGIFDASLVDRVLDIHQRDAENTMRELAVREG 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 768021879  239 LLCGGSAGSTVAVAVKAAQELQEGQrCVVILPDSVRNYMT 278
Cdd:TIGR01138 248 IFCGVSSGGAVAAALRLARELPDAV-VVAIICDRGDRYLS 286
PLN03013 PLN03013
cysteine synthase
2-289 1.93e-63

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 211.56  E-value: 1.93e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTI-IEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN03013 142 AKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGLAFIAASRGYRLILTMPASMSMERRVLLKAFG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRTptnarfDSPESHVGVAWR----LKNeIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTI 156
Cdd:PLN03013 222 AELVLT------DPAKGMTGAVQKaeeiLKN-TPDAYMLQQFDNPANPKIHYETTGPEIWDDTKGKVDIFVAGIGTGGTI 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 157 TGIARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQ 236
Cdd:PLN03013 295 TGVGRFIKEKNPKTQVIGVEP-----TESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEVIAISSEEAIETAKQLALK 369
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768021879 237 EGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTK--FLSDRWMLQK 289
Cdd:PLN03013 370 EGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASGRDIYTprCSSLSGKRWR 424
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
2-283 1.80e-59

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 199.03  E-value: 1.80e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   2 AKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDT-IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN02556  78 AKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRT-PTNARFDSpeshVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 159
Cdd:PLN02556 158 AELVLTdPTKGMGGT----VKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGV 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 160 ARKLKEKCPGCRIIGVDPegsilAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGL 239
Cdd:PLN02556 234 GKYLKSKNPNVKIYGVEP-----AESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGL 308
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768021879 240 LCGGSAGSTVAVAVKAAQELQ-EGQRCVVILPDSVRNYMTKFLSD 283
Cdd:PLN02556 309 MVGISSGANTVAALRLAKMPEnKGKLIVTVHPSFGERYLSSVLFQ 353
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
307-451 1.17e-53

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: 175.41  E-value: 1.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 307 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 386
Cdd:cd04608    2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVD 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021879 387 LTDTLGRLSHILEMDHFALVVHEQiqsqdqawagvvggpadhstgkssqrQMVFGVVTAIDLLNF 451
Cdd:cd04608   82 LDTPLGALSRILERDHFALVVDGQ--------------------------GKVLGIVTRIDLLNY 120
PLN02356 PLN02356
phosphateglycerate kinase
1-291 4.76e-48

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 170.56  E-value: 4.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   1 MAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALG 80
Cdd:PLN02356  71 LGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGCKCHVVIPDDVAIEKSQILEALG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  81 AEIVRT-PTNarFDSPESHVGVAWRLK---NEIP-----------------NSHIL-------------------DQYRN 120
Cdd:PLN02356 151 ATVERVrPVS--ITHKDHYVNIARRRAleaNELAskrrkgsetdgihlektNGCISeeekenslfsssctggffaDQFEN 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 121 ASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSIL--------------AEPE 186
Cdd:PLN02356 229 LANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGLfnkvtrgvmytreeAEGR 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 187 ELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCV 266
Cdd:PLN02356 309 RLKNPFDTI--TEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNCVGAVRVAQSLGPGHTIV 386
                        330       340
                 ....*....|....*....|....*
gi 768021879 267 VILPDSVRNYMTKFLSDRWMLQKGF 291
Cdd:PLN02356 387 TILCDSGMRHLSKFHDPQYLSQHGL 411
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
3-269 4.36e-26

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: 107.57  E-value: 4.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMI----EDAERDGtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRA 78
Cdd:cd01562   37 KCENLQKTGSFKIRGAYNKLlslsEEERAKG-------VVAASAGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  79 LGAEIVRTptNARFDSPESHvgvAWRLKNEIPNSHIldqyrnasNPLAHYD------TTADEILQQCdGKLDMLVASVGT 152
Cdd:cd01562  110 YGAEVVLY--GEDFDEAEAK---ARELAEEEGLTFI--------HPFDDPDviagqgTIGLEILEQV-PDLDAVFVPVGG 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 153 GGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTEQTtyeVEGIGydfIPTVLDRT------VVDKWF 219
Cdd:cd01562  176 GGLIAGIATAVKALSPNTKVIGVEPEGapamaqSLAAgKPVTLPEVDTI---ADGLA---VKRPGELTfeiirkLVDDVV 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768021879 220 KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 269
Cdd:cd01562  250 TVSEDEIAAAMLLLFEREKLVAEPAGALALA-ALLSGKLDLKGKKVVVVL 298
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
3-269 6.55e-26

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: 107.43  E-value: 6.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDR------ISLRmieDAERDGTlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVL 76
Cdd:COG1171   44 KLENLQPTGSFKLRgaynalASLS---EEERARG------VVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAAT 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  77 RALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDM 145
Cdd:COG1171  115 RAYGAEVVLHGDT--YDDAEAA---AAELAEEegatfVH-------------PFDDPDviagqgTIALEILEQL-PDLDA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 146 LVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG------SILA-EPEELNQTeQT------TYEVEGIGYDFIPTVLDR 212
Cdd:COG1171  176 VFVPVGGGGLIAGVAAALKALSPDIRVIGVEPEGaaamyrSLAAgEPVTLPGV-DTiadglaVGRPGELTFEILRDLVDD 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768021879 213 TV-VDkwfksnDEEAFTFARMLIAQEGLLCGGSAGSTVAvAVKAAQELQEGQRCVVIL 269
Cdd:COG1171  255 IVtVS------EDEIAAAMRLLLERTKIVVEPAGAAALA-ALLAGKERLKGKRVVVVL 305
PRK06815 PRK06815
threonine/serine dehydratase;
3-269 3.09e-25

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 105.54  E-value: 3.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRIS---LRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRAL 79
Cdd:PRK06815  40 KCEHLQHTGSFKFRGAsnkLRLLNEAQR----QQG--VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRAL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  80 GAEIVRTPTNArfDSPESHvgvAWRLKNEIPNSHIlDQYrNASNPLAHYDTTADEILQQCDgKLDMLVASVGTGGTITGI 159
Cdd:PRK06815 114 GAEVRLYGGDA--LNAELA---ARRAAEQQGKVYI-SPY-NDPQVIAGQGTIGMELVEQQP-DLDAVFVAVGGGGLISGI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 160 ARKLKEKCPGCRIIGVDPEG------SILA----EPEELNQTEQTTyeVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTF 229
Cdd:PRK06815 186 ATYLKTLSPKTEIIGCWPANspslytSLEAgeivEVAEQPTLSDGT--AGGVEPGAITFPLCQQLIDQKVLVSEEEIKEA 263
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768021879 230 ARMLIAQEGLLCGGSAGSTVAVAVKAAQELQeGQRCVVIL 269
Cdd:PRK06815 264 MRLIAETDRWLIEGAAGVALAAALKLAPRYQ-GKKVAVVL 302
PLN02970 PLN02970
serine racemase
3-180 5.37e-16

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 78.57  E-value: 5.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMI-----EDAERDgtlkpgdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLR 77
Cdd:PLN02970  47 KCECFQKGGAFKFRGACNAIfslsdDQAEKG--------VVTHSSGNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVI 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  78 ALGAEIVRT-PTNarfdspESHVGVAWRLKNEiPNSHILDQYrNASNPLAHYDTTADEILQQCDGkLDMLVASVGTGGTI 156
Cdd:PLN02970 119 RYGGIITWCePTV------ESREAVAARVQQE-TGAVLIHPY-NDGRVISGQGTIALEFLEQVPE-LDVIIVPISGGGLI 189
                        170       180
                 ....*....|....*....|....
gi 768021879 157 TGIARKLKEKCPGCRIIGVDPEGS 180
Cdd:PLN02970 190 SGIALAAKAIKPSIKIIAAEPKGA 213
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
3-269 5.18e-15

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: 75.71  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:cd01563   43 KDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGAT 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IVRTPTNarFDSpeshvgvAWRLKNEIPNSHILDqYRNASNPLAH--YDTTADEILQQCDGKL-DMLVASVGTGGTITGI 159
Cdd:cd01563  119 VLAVEGN--FDD-------ALRLVRELAEENWIY-LSNSLNPYRLegQKTIAFEIAEQLGWEVpDYVVVPVGNGGNITAI 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 160 ARKLKE--------KCPgcRIIGVDPEGS------ILAEPEELNQTEQTTYEVEGIGydfIPT-VLDRTVVDKWFKSN-- 222
Cdd:cd01563  189 WKGFKElkelglidRLP--RMVGVQAEGAapivraFKEGKDDIEPVENPETIATAIR---IGNpASGPKALRAVRESGgt 263
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768021879 223 ----DEEAFTFARMLIAQ-EGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL 269
Cdd:cd01563  264 avavSDEEILEAQKLLARtEGIFVEPASAASLAGLKKLREEgiIDKGERVVVVL 317
PRK06381 PRK06381
threonine synthase; Validated
3-269 1.35e-14

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 74.36  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK06381  36 KFEGANPTGTQKDRIAEAHVRRAMRLGY----SGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAE 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IVRTP---TNARFDSPESHVGVAWRLKNeiPNShildqyRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGI 159
Cdd:PRK06381 112 IIYVDgkyEEAVERSRKFAKENGIYDAN--PGS------VNSVVDIEAYSAIAYEIYEALGDVPDAVAVPVGNGTTLAGI 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 160 ARKLKE--------KCPgcRIIGVDPEGS--------------ILAEPEELNQTEQTTYEVEGIGYDFiPTVLD--RTVV 215
Cdd:PRK06381 184 YHGFRRlydrgktsRMP--RMIGVSTSGGnqivesfkrgssevVDLEVDEIRETAVNEPLVSYRSFDG-DNALEaiYDSH 260
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768021879 216 DKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVIL 269
Cdd:PRK06381 261 GYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLKKNGVNDNVVAVI 314
PRK08246 PRK08246
serine/threonine dehydratase;
3-180 4.34e-14

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 72.68  E-value: 4.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAErdgtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK08246  42 KLEHLQHTGSFKARGAFNRLLAAP-----VPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IVRTPT---NARFDSpeshvgVAWRLKNEIPNSHILDQyrnasnP--LAHYDTTADEILQQCdGKLDMLVASVGTGGTIT 157
Cdd:PRK08246 117 VVVVGAeyaDALEAA------QAFAAETGALLCHAYDQ------PevLAGAGTLGLEIEEQA-PGVDTVLVAVGGGGLIA 183
                        170       180
                 ....*....|....*....|...
gi 768021879 158 GIARKLKekcPGCRIIGVDPEGS 180
Cdd:PRK08246 184 GIAAWFE---GRARVVAVEPEGA 203
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
43-180 6.94e-14

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 73.63  E-value: 6.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  43 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHvgvAWRLKNE-----IPnshildq 117
Cdd:PRK09224  77 GNHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDS--FDEAYAH---AIELAEEegltfIH------- 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021879 118 yrnasnPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 180
Cdd:PRK09224 145 ------PFDDPDviagqgTIAMEILQQHPHPLDAVFVPVGGGGLIAGVAAYIKQLRPEIKVIGVEPEDS 207
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
3-178 1.25e-13

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 71.59  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDR---ISLRMIEDAERdgtlKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRAL 79
Cdd:PRK07048  44 KCENFQRMGAFKFRgayNALSQFSPEQR----RAG--VVTFSSGNHAQAIALSARLLGIPATIVMPQDAPAAKVAATRGY 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  80 GAEIVRtptnarFD-SPESHVGVAWRLKNE-----IPnshildqyrnasnPLAHYD------TTADEILQQCdGKLDMLV 147
Cdd:PRK07048 118 GGEVVT------YDrYTEDREEIGRRLAEErgltlIP-------------PYDHPHviagqgTAAKELFEEV-GPLDALF 177
                        170       180       190
                 ....*....|....*....|....*....|.
gi 768021879 148 ASVGTGGTITGIARKLKEKCPGCRIIGVDPE 178
Cdd:PRK07048 178 VCLGGGGLLSGCALAARALSPGCKVYGVEPE 208
PRK12483 PRK12483
threonine dehydratase; Reviewed
37-180 5.72e-13

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 70.60  E-value: 5.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  37 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEIPNS--HI 114
Cdd:PRK12483  88 VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLH--GESFPDALAH---ALKLAEEEGLTfvPP 162
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768021879 115 LDQyrnaSNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGS 180
Cdd:PRK12483 163 FDD----PDVIAGQGTVAMEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDS 224
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
3-276 2.42e-12

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: 68.30  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDR-----ISLrmiedAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVL 76
Cdd:COG0498   86 KEEGHNPTGSFKDRamqvaVSL-----ALERGA----KTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQLAQM 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  77 RALGAEIVRTPTNarFDspeshvgVAWRLKNEIPNSHILdqY-RNASNPLAH--YDTTADEILQQCDGKLDMLVASVGTG 153
Cdd:COG0498  157 LTYGAHVIAVDGN--FD-------DAQRLVKELAADEGL--YaVNSINPARLegQKTYAFEIAEQLGRVPDWVVVPTGNG 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 154 GTITGI--ARK------LKEKCPgcRIIGVDPEGS--ILAEPEelnqTEQTTYEVEG---------IGydfIPT------ 208
Cdd:COG0498  226 GNILAGykAFKelkelgLIDRLP--RLIAVQATGCnpILTAFE----TGRDEYEPERpetiapsmdIG---NPSngeral 296
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021879 209 -VLDRTvvDKWF-KSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVIL-------PDSVRNY 276
Cdd:COG0498  297 fALRES--GGTAvAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPDEPVVVLStghglkfPDAVREA 373
PRK06608 PRK06608
serine/threonine dehydratase;
3-177 6.79e-11

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 63.25  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAERDGtlKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK06608  43 KVESLQKTGAFKVRGVLNHLLELKEQG--KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IVRTPTNARFDSP---ESHVGVAWrlkneIPNShildqyrNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITG- 158
Cdd:PRK06608 121 VILTNTRQEAEEKakeDEEQGFYY-----IHPS-------DSDSTIAGAGTLCYEALQQLGFSPDAIFASCGGGGLISGt 188
                        170       180
                 ....*....|....*....|
gi 768021879 159 -IARKLKEkcPGCRIIGVDP 177
Cdd:PRK06608 189 yLAKELIS--PTSLLIGSEP 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
317-364 2.77e-09

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 52.52  E-value: 2.77e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 768021879   317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
317-400 6.30e-09

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: 53.79  E-value: 6.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTlgrLSH 396
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTD---LEE 80

                 ....
gi 768021879 397 ILEM 400
Cdd:cd02205   81 ALEL 84
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
37-178 1.10e-08

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 56.67  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  37 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDSPESHVGVAWRLKNEIpnshILD 116
Cdd:PRK08638  78 VVACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDN--FNDTIAKVEEIVEEEGRT----FIP 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021879 117 QYrNASNPLAHYDTTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 178
Cdd:PRK08638 152 PY-DDPKVIAGQGTIGLEILEDL-WDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQSE 211
PRK08639 PRK08639
threonine dehydratase; Validated
130-179 2.15e-08

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 55.97  E-value: 2.15e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768021879 130 TTADEILQQCD--GKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEG 179
Cdd:PRK08639 165 TVAVEILEQLEkeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAG 216
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
36-178 6.22e-08

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 54.50  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  36 TIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNarFDspEShVGVAWRLKNEipNSHIL 115
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITDGN--YD--DS-VRLAAQEAQE--NGWVV 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768021879 116 DQyrNASNP---------LAHYDTTADEILQQCDGKLD-----MLVASVGT--GGTITGIARKLKEKCPgcRIIGVDPE 178
Cdd:PRK08206 191 VQ--DTAWEgyeeiptwiMQGYGTMADEAVEQLKEMGVppthvFLQAGVGSlaGAVLGYFAEVYGEQRP--HFVVVEPD 265
PLN02550 PLN02550
threonine dehydratase
12-177 1.05e-07

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 54.16  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  12 SVKDRISLRMIEDAERDgTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNar 91
Cdd:PLN02550 138 SFKLRGAYNMMAKLPKE-QLDKG--VICSSAGNHAQGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDS-- 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  92 FDSPESHVgvawrlkneipNSHILDQYRNASNPLAHYD------TTADEILQQCDGKLDMLVASVGTGGTITGIARKLKE 165
Cdd:PLN02550 213 YDEAQAYA-----------KQRALEEGRTFIPPFDHPDviagqgTVGMEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKR 281
                        170
                 ....*....|..
gi 768021879 166 KCPGCRIIGVDP 177
Cdd:PLN02550 282 VRPEVKIIGVEP 293
CBS COG0517
CBS domain [Signal transduction mechanisms];
307-399 3.96e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 48.71  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 307 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQI 385
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTV 80
                         90
                 ....*....|....
gi 768021879 386 RLTDTLGRLSHILE 399
Cdd:COG0517   81 SPDTSLEEAAELME 94
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
2-166 5.40e-07

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: 51.23  E-value: 5.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879    2 AKCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPE-KMSSEKVDVLRALG 80
Cdd:TIGR00260  42 VKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYN 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   81 AEIVRtpTNARFDSPESHV------GVAWRLK--NEIPnSHILDQYrnasnplahydTTADEILQQCDGKL-DMLVASVG 151
Cdd:TIGR00260 118 AEVVA--IDGNFDDAQRLVkqlfedKPALGLNsaNSIP-YRLEGQK-----------TYAFEAVEQLGWEApDKVVVPVP 183
                         170
                  ....*....|....*
gi 768021879  152 TGGTITGIARKLKEK 166
Cdd:TIGR00260 184 NSGNFGAIWKGFKEK 198
PRK06450 PRK06450
threonine synthase; Validated
3-178 5.71e-07

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 51.27  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK06450  70 KLDFLNPTGSYKDRGSVTLISYLAEKGI----KQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IVRTPTNaRFD----SPESHVGVAwrlkneipnSHILD-QYRNASNPLAHydttadEILQQCDGKL-DMLVASVGTGGTI 156
Cdd:PRK06450 146 VVRVRGS-REDvakaAENSGYYYA---------SHVLQpQFRDGIRTLAY------EIAKDLDWKIpNYVFIPVSAGTLL 209
                        170       180       190
                 ....*....|....*....|....*....|
gi 768021879 157 TGIARKLK--------EKCPgcRIIGVDPE 178
Cdd:PRK06450 210 LGVYSGFKhlldsgviSEMP--KIVAVQTE 237
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
309-364 9.50e-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: 45.67  E-value: 9.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 768021879  309 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
3-180 1.11e-06

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


Pssm-ID: 107209  Cd Length: 316  Bit Score: 50.38  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDR-ISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGA 81
Cdd:cd06448   21 KLENLQPSGSFKIRgIGHLCQKSAKQGLNECVH--VVCSSGGNAGLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  82 EIVRTPTNARFDSPESHVGVAWRLKNEIpNSHILDqyrnasNPL--AHYDTTADEILQQC--DGKLDMLVASVGTGGTIT 157
Cdd:cd06448   99 TVVVHGKVWWEADNYLREELAENDPGPV-YVHPFD------DPLiwEGHSSMVDEIAQQLqsQEKVDAIVCSVGGGGLLN 171
                        170       180
                 ....*....|....*....|....*
gi 768021879 158 GIARKLkEKCPGCR--IIGVDPEGS 180
Cdd:cd06448  172 GIVQGL-ERNGWGDipVVAVETEGA 195
PRK06110 PRK06110
threonine dehydratase;
11-84 1.17e-06

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 50.38  E-value: 1.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021879  11 GSVKDRISLRMIEDAERDGTLKPGdtIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIV 84
Cdd:PRK06110  49 GAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELI 120
PRK07334 PRK07334
threonine dehydratase; Provisional
37-178 2.06e-06

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 49.89  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  37 IIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTptNARFDSPESHvgvAWRLKNEipnshild 116
Cdd:PRK07334  74 VIAMSAGNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLH--GETLDEARAH---ARELAEE-------- 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021879 117 QYRNASNPLAHYD------TTADEILQQCdGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPE 178
Cdd:PRK07334 141 EGLTFVHPYDDPAviagqgTVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTE 207
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
307-399 6.00e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 47.19  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 307 LRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEaGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIR 386
Cdd:COG2524   86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVS 164
                         90
                 ....*....|...
gi 768021879 387 LTDTLGRLSHILE 399
Cdd:COG2524  165 EDDSLEEALRLML 177
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
317-398 1.10e-05

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 44.86  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQ------PSDQVGKVIYKQFKQIRLTDT 390
Cdd:COG3448   12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRPVVTVTPDTP 91

                 ....*...
gi 768021879 391 LGRLSHIL 398
Cdd:COG3448   92 LEEAAELM 99
PRK08329 PRK08329
threonine synthase; Validated
3-179 2.99e-05

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 45.97  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK08329  77 KLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGAE 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IvrtpTNARFDSPESHV-GVAWRLKNEIPN-SHILDQYRnasnpLAHYDTTADEILQQCdGKLDMLVASVGTGGTITGIA 160
Cdd:PRK08329 153 L----HFVEGDRMEVHEeAVKFSKRNNIPYvSHWLNPYF-----LEGTKTIAYEIYEQI-GVPDYAFVPVGSGTLFLGIW 222
                        170       180
                 ....*....|....*....|....*..
gi 768021879 161 RKLKE--------KCPgcRIIGVDPEG 179
Cdd:PRK08329 223 KGFKElhemgeisKMP--KLVAVQAEG 247
PRK03910 PRK03910
D-cysteine desulfhydrase; Validated
24-175 6.16e-05

D-cysteine desulfhydrase; Validated


Pssm-ID: 179673  Cd Length: 331  Bit Score: 44.82  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  24 DAERDGTlkpgDTIIepTSGntGIG-----LALAAAVR-GYRCIIVMPEKMSSEKVDVL--------RALGAEIVRTPTN 89
Cdd:PRK03910  58 DALAQGA----DTLI--TAG--AIQsnharQTAAAAAKlGLKCVLLLENPVPTEAENYLangnvlldDLFGAEIHVVPAG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  90 ARFDSPESHVgvAWRLKNE------IPNShildqyrnASNPL-AH-YDTTADEILQQCDG---KLDMLVASVGTGGTITG 158
Cdd:PRK03910 130 TDMDAQLEEL--AEELRAQgrrpyvIPVG--------GSNALgALgYVACALEIAQQLAEggvDFDAVVVASGSGGTHAG 199
                        170
                 ....*....|....*..
gi 768021879 159 IARKLKEKCPGCRIIGV 175
Cdd:PRK03910 200 LAAGLAALGPDIPVIGV 216
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
20-86 6.91e-05

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 44.90  E-value: 6.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  20 RMIEDAerdGTLKPGDTIIEpTSGNTGIGLALA--AAVRGYRCIIVMPEKMSSEK-VDVLRALGAEIVRT 86
Cdd:cd08290  136 RLLEDF---VKLQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEElKERLKALGADHVLT 201
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
290-364 7.39e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 42.59  E-value: 7.39e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768021879 290 GFLKEEDLTEKKPwwwHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:COG4109   62 GIVTSKDILGKDD---DTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
CBS COG0517
CBS domain [Signal transduction mechanisms];
297-364 7.54e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 42.16  E-value: 7.54e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768021879 297 LTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:COG0517   57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
eutB PRK07476
threonine dehydratase; Provisional
43-175 9.99e-05

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 44.19  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  43 GNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPtnarfDSPESHVGVAWRLKNE-----IPnshildq 117
Cdd:PRK07476  76 GNHGRALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVG-----RSQDDAQAEVERLVREegltmVP------- 143
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021879 118 yrnasnPLAHYD------TTADEILQQCDgKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGV 175
Cdd:PRK07476 144 ------PFDDPRiiagqgTIGLEILEALP-DVATVLVPLSGGGLASGVAAAVKAIRPAIRVIGV 200
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
317-410 1.34e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.82  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLssllagKVQPSDQVGKVIYKQFKQIRLTDTLGRLSH 396
Cdd:COG4109   27 VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPITVTPDTSLASAAH 100
                         90
                 ....*....|....*.
gi 768021879 397 ILEMDHFAL--VVHEQ 410
Cdd:COG4109  101 KMIWEGIELlpVVDDD 116
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
309-391 1.49e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 41.35  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 309 VQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQ-VGKVIYKQFKQIRL 387
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80

                 ....
gi 768021879 388 TDTL 391
Cdd:COG2905   81 DDSL 84
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
290-360 1.64e-04

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 41.08  E-value: 1.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021879 290 GFLKEEDLTEK---KPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNML 360
Cdd:cd02205   39 GIVTERDILRAlveGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
226-363 2.71e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 42.18  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 226 AFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRcVVILPDSVRNYMTKF---------LSD--RWMLQK----- 289
Cdd:COG2524   42 LLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL-GLVLKMKVKDIMTKDvitvspdttLEEalELMLEKgisgl 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 290 ---------GFLKEEDL---TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLG 357
Cdd:COG2524  121 pvvddgklvGIITERDLlkaLAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRT 200

                 ....*.
gi 768021879 358 NMLSSL 363
Cdd:COG2524  201 DILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
255-364 4.61e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.81  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 255 AAQELQE-GQRCVVILPDSvrNYMTKFLSDRWMLQKGFLKEEDLTEKKpwwwhlrVQELGLSAPLTVLPTITCGHTIEIL 333
Cdd:COG2905   21 AARLMTEkGVGSLVVVDDD--GRLVGIITDRDLRRRVLAEGLDPLDTP-------VSEVMTRPPITVSPDDSLAEALELM 91
                         90       100       110
                 ....*....|....*....|....*....|.
gi 768021879 334 REKGFDQAPVVDEaGVILGMVTLGNMLSSLL 364
Cdd:COG2905   92 EEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
PRK05638 PRK05638
threonine synthase; Validated
3-272 6.81e-04

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 41.72  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879   3 KCEFFNAGGSVKDRISLRMIEDAERDGTlkpgDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAE 82
Cdd:PRK05638  85 KDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAK 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879  83 IVRTPTNarFDSPESHVGVAWRLK---NEIPNSHILDqyrnasnpLAHYDTTADEILQQCDGklDMLVASVGTGGTITGI 159
Cdd:PRK05638 161 IIRYGES--VDEAIEYAEELARLNglyNVTPEYNIIG--------LEGQKTIAFELWEEINP--THVIVPTGSGSYLYSI 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 160 ARKLKE--------KCPgcRIIGVDPE------GSILAEPEELNQTeqttyevEGIGYDFIPTVLDRTVVDKWFKS---- 221
Cdd:PRK05638 229 YKGFKElleigvieEIP--KLIAVQTErcnpiaSEILGNKTKCNET-------KALGLYVKNPVMKEYVSEAIKESggta 299
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768021879 222 --NDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQE--LQEGQRCVVILPDS 272
Cdd:PRK05638 300 vvVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLGEEgyIEKGDKVVLVVTGS 354
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
306-364 8.02e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.74  E-value: 8.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768021879 306 HLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:PRK14869  67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
317-355 8.40e-04

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 38.93  E-value: 8.40e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 768021879 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 355
Cdd:cd04601    4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT 42
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
291-364 1.07e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.08  E-value: 1.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768021879 291 FLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLL 364
Cdd:COG3448   57 ALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
309-450 1.84e-03

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


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 37.69  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768021879 309 VQELGLSAPLTVLPTITCGHTIEILREK-GFDQAPVVDEAGvilgmVTLgNMLSSLLAGKVQPSdqvgkviykqfkqirl 387
Cdd:COG3620    1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAELVG-----VSQ-SDILRIESGKRDPT---------------- 58
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768021879 388 TDTLGRLSHILEMDHFALVVHEQiqsqdqawagvvggpadhstGKssqrqmVFGVVTAIDLLN 450
Cdd:COG3620   59 VSTLEKIAEALGKELSAVLVVDD--------------------GK------LVGIITRRDLLK 95
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
318-389 1.92e-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: 38.08  E-value: 1.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768021879 318 LTVLPTITCGHTIEILREKG-----FDQAPVVDEAGVILGMVTLGNMLSSllagkvQPSDQVGKVIYKQFKQIRLTD 389
Cdd:cd04606   12 VAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLA------DPDTKVSDIMDTDVISVSADD 82
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
290-361 8.74e-03

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 35.88  E-value: 8.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768021879 290 GFLKEEDLTEKkpwwwhlrVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLS 361
Cdd:cd04607   49 GLLKGLSLDAP--------VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
317-355 9.66e-03

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 36.25  E-value: 9.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 768021879 317 PLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVT 355
Cdd:cd04586    5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVS 43
 
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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