NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15233111|ref|NP_191703|]
View 

cysteine synthase C1 [Arabidopsis thaliana]

Protein Classification

PALP domain-containing protein; threonine synthase( domain architecture ID 10791409)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions| threonine synthase catalyzes the final step of threonine biosynthesis, the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 1-368 0e+00

cysteine synthase/L-3-cyanoalanine synthase


:

Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 690.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    1 MASVSRRLLRRETIPCFSHTVRKLFSTVGSPSFAQRLRDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQ 80
Cdd:PLN02556   1 MAALLSRLKRRSSIPPSSHTLRKLFSTVGSPSFAQRLRDLPKDLPGTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   81 EHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAEL 160
Cdd:PLN02556  81 EMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  161 VLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSK 240
Cdd:PLN02556 161 VLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  241 NPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVA 320
Cdd:PLN02556 241 NPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15233111  321 AIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEMKPVSVD 368
Cdd:PLN02556 321 ALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENMQPVSVD 368
 
Name Accession Description Interval E-value
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 1-368 0e+00

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 690.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    1 MASVSRRLLRRETIPCFSHTVRKLFSTVGSPSFAQRLRDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQ 80
Cdd:PLN02556   1 MAALLSRLKRRSSIPPSSHTLRKLFSTVGSPSFAQRLRDLPKDLPGTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   81 EHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAEL 160
Cdd:PLN02556  81 EMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  161 VLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSK 240
Cdd:PLN02556 161 VLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  241 NPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVA 320
Cdd:PLN02556 241 NPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15233111  321 AIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEMKPVSVD 368
Cdd:PLN02556 321 ALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENMQPVSVD 368
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 54-352 1.95e-143

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: 408.29  E-value: 1.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    54 SLLIGKTPLVFLNKVtEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMK 133
Cdd:TIGR01139   2 SELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPG-KTIVEPTSGNTGIALAMVAAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDA-FMCQQFANPANTQIHFDTTGPEIWED 212
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyFMLQQFENPANPEIHRKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   213 TLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSS 292
Cdd:TIGR01139 160 TDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   293 EDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLSSVLF 352
Cdd:TIGR01139 240 EEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 56-349 5.16e-140

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: 399.81  E-value: 5.16e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  56 LIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMKGY 135
Cdd:COG0031  10 LIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLAMVAAAKGY 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 136 RIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLG 215
Cdd:COG0031  89 RLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDG 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 216 NVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMES 286
Cdd:COG0031 169 KVDAFVagvgtggtiTGV---------GRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDE 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233111 287 VLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMpENKGKLIVTIHASFGERYLSS 349
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 58-348 5.03e-137

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 391.88  E-value: 5.03e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  58 GKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMKGYRI 137
Cdd:cd01561   1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 138 IMTMPSYTSLERRVTMRSFGAELVLTDPAK--GMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLG 215
Cdd:cd01561  80 IIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 216 NVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMES 286
Cdd:cd01561 160 KVDAFVagvgtggtiTGV---------ARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDE 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233111 287 VLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLS 348
Cdd:cd01561 231 VVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 54-339 1.96e-68

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: 217.18  E-value: 1.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    54 SLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKliipGKTTLIEPTSGNMGISLAFMAAMK 133
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGE----GGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDPakGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFdTTGPEIWEDT 213
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   214 LGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGG---------KPGPHAITGNGVGFKPEILDMDVM 284
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDLL 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   285 E----SVLEVSSEDAIKMARELALKEGLMVGISSGANtVAAIRLAKMPE-NKGKLIVTIH 339
Cdd:pfam00291 235 DeyvgEVVTVSDEEALEAMRLLARREGIVVEPSSAAA-LAALKLALAGElKGGDRVVVVL 293
 
Name Accession Description Interval E-value
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 1-368 0e+00

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 690.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    1 MASVSRRLLRRETIPCFSHTVRKLFSTVGSPSFAQRLRDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQ 80
Cdd:PLN02556   1 MAALLSRLKRRSSIPPSSHTLRKLFSTVGSPSFAQRLRDLPKDLPGTKIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   81 EHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAEL 160
Cdd:PLN02556  81 EMFQPTSSIKDRPALAMIEDAEKKNLITPGKTTLIEPTSGNMGISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  161 VLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSK 240
Cdd:PLN02556 161 VLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGPEIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  241 NPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVA 320
Cdd:PLN02556 241 NPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVA 320

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15233111  321 AIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEMKPVSVD 368
Cdd:PLN02556 321 ALRLAKMPENKGKLIVTVHPSFGERYLSSVLFQELRKEAENMQPVSVD 368
PLN02565 PLN02565
cysteine synthase
 51-363 6.41e-156

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 440.90  E-value: 6.41e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   51 RDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMA 130
Cdd:PLN02565   7 KDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVLIEPTSGNTGIGLAFMA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  131 AMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIW 210
Cdd:PLN02565  87 AAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPEIW 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  211 EDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEV 290
Cdd:PLN02565 167 KGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVVQV 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233111  291 SSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEMK 363
Cdd:PLN02565 247 SSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRPENAGKLIVVIFPSFGERYLSSVLFESVKKEAENMV 319
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 54-352 1.95e-143

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: 408.29  E-value: 1.95e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    54 SLLIGKTPLVFLNKVtEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMK 133
Cdd:TIGR01139   2 SELIGNTPLVRLNRI-EGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPG-KTIVEPTSGNTGIALAMVAAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDA-FMCQQFANPANTQIHFDTTGPEIWED 212
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyFMLQQFENPANPEIHRKTTGPEIWRD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   213 TLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSS 292
Cdd:TIGR01139 160 TDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSD 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   293 EDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLSSVLF 352
Cdd:TIGR01139 240 EEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPE-PDKLIVVILPSTGERYLSTPLF 298
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 54-352 4.25e-142

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: 405.13  E-value: 4.25e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    54 SLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMK 133
Cdd:TIGR01136   2 EELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPG-DTIIEATSGNTGIALAMVAAAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDT 213
Cdd:TIGR01136  81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   214 LGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSE 293
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15233111   294 DAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLF 352
Cdd:TIGR01136 241 DAIETARRLAREEGILVGISSGAAVAAALKLAKRLENADKVIVAILPDTGERYLSTGLF 299
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 56-349 5.16e-140

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: 399.81  E-value: 5.16e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  56 LIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMKGY 135
Cdd:COG0031  10 LIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPG-GTIVEATSGNTGIGLAMVAAAKGY 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 136 RIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLG 215
Cdd:COG0031  89 RLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGPEIWEQTDG 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 216 NVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMES 286
Cdd:COG0031 169 KVDAFVagvgtggtiTGV---------GRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDE 239

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233111 287 VLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMpENKGKLIVTIHASFGERYLSS 349
Cdd:COG0031 240 VITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKR-LGPGKTIVTILPDSGERYLST 301
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 58-348 5.03e-137

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 391.88  E-value: 5.03e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  58 GKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMKGYRI 137
Cdd:cd01561   1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPG-TTIIEPTSGNTGIGLAMVAAAKGYRF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 138 IMTMPSYTSLERRVTMRSFGAELVLTDPAK--GMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLG 215
Cdd:cd01561  80 IIVMPETMSEEKRKLLRALGAEVILTPEAEadGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 216 NVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMES 286
Cdd:cd01561 160 KVDAFVagvgtggtiTGV---------ARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDE 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233111 287 VLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPEnKGKLIVTIHASFGERYLS 348
Cdd:cd01561 231 VVRVSDEEAFAMARRLAREEGLLVGGSSGAAVAAALKLAKRLG-PGKTIVTILPDSGERYLS 291
PLN03013 PLN03013
cysteine synthase
 48-364 3.26e-135

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 392.60  E-value: 3.26e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   48 NAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLA 127
Cdd:PLN03013 112 NIADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVLVEPTSGNTGIGLA 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  128 FMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGP 207
Cdd:PLN03013 192 FIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTGP 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  208 EIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESV 287
Cdd:PLN03013 272 EIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDEV 351

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233111  288 LEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGeRYLSSVLFDELRKEAEEMKP 364
Cdd:PLN03013 352 IAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRPENAGKLIAVSLFASG-RDIYTPRCSSLSGKRWRKCS 427
PLN00011 PLN00011
cysteine synthase
 50-362 8.67e-134

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 384.74  E-value: 8.67e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   50 KRDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFM 129
Cdd:PLN00011   8 KNDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGKSTLIEATAGNTGIGLACI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  130 AAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEI 209
Cdd:PLN00011  88 GAARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPEI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  210 WEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLE 289
Cdd:PLN00011 168 WRDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQ 247

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233111  290 VSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEM 362
Cdd:PLN00011 248 VTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKLIVVIFPSGGERYLSTKLFESVRYEAENL 320
cysM PRK11761
cysteine synthase CysM;
56-354 3.67e-90

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 272.90  E-value: 3.67e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   56 LIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMKGY 135
Cdd:PRK11761   9 TIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPG-DTLIEATSGNTGIALAMIAAIKGY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  136 RIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGtvkkAYDLLDSTPDA---FMCQQFANPANTQIHFDTTGPEIWED 212
Cdd:PRK11761  88 RMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEG----ARDLALQMQAEgegKVLDQFANPDNPLAHYETTGPEIWRQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  213 TLGNVDIFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAE-SNIlnggkPG----PHAitgngvgFKPEI 278
Cdd:PRK11761 164 TEGRITHFVssmgttgtiMGV---------SRYLKEQNPAVQIVGLQPEEgSSI-----PGirrwPEE-------YLPKI 222

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233111  279 LDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmpENKGKLIVTIHASFGERYLSSVLFDE 354
Cdd:PRK11761 223 FDASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIAR--ENPNAVIVAIICDRGDRYLSTGVFPA 296
PRK10717 PRK10717
cysteine synthase A; Provisional
 50-358 1.51e-87

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 267.50  E-value: 1.51e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   50 KRDASLLIGKTPLVFLNKVTE--GCEAYvaAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTtLIEPTSGNMGISLA 127
Cdd:PRK10717   4 FEDVSDTIGNTPLIRLNRASEatGCEIL--GKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGT-IVEGTAGNTGIGLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  128 FMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLT------DPAKGMGGTVKKAYDLLDSTPD-AFMCQQFANPANTQI 200
Cdd:PRK10717  81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVpaapyaNPNNYVKGAGRLAEELVASEPNgAIWANQFDNPANREA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  201 HFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNI----LNG--GKPGPHAITGNGVGF 274
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALysyyKTGelKAEGSSITEGIGQGR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  275 KPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmPENKGKLIVTIHASFGERYLSSVLFDE 354
Cdd:PRK10717 241 ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLAR-ELGPGHTIVTILCDSGERYQSKLFNPD 319


                 ....
gi 15233111  355 LRKE 358
Cdd:PRK10717 320 FLRE 323
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 56-354 2.44e-75

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: 240.09  E-value: 2.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    56 LIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGkTTLIEPTSGNMGISLAFMAAMKGY 135
Cdd:TIGR01137   8 LIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPG-DTIIEPTSGNTGIGLALVAAIKGY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   136 RIIMTMPSYTSLERRVTMRSFGAELVLT-------DPAKGMGgtvkKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPE 208
Cdd:TIGR01137  87 KCIIVLPEKMSSEKVDVLRALGAEIVRTptaaafdSPESHIG----VAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   209 IWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEP-----AESNILNGGKPGPHAITGNGVGFKPEILDMDV 283
Cdd:TIGR01137 163 ILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPegsilAQPEELNQTGRTPYKVEGIGYDFIPTVLDRKV 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233111   284 MESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDE 354
Cdd:TIGR01137 243 VDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQEGQRCVVLLPDSIRNYMTKFLNDE 313
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 54-339 1.96e-68

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: 217.18  E-value: 1.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111    54 SLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKliipGKTTLIEPTSGNMGISLAFMAAMK 133
Cdd:pfam00291   2 SLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGE----GGKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDPakGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFdTTGPEIWEDT 213
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGG--DYDEAVAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   214 LGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGG---------KPGPHAITGNGVGFKPEILDMDVM 284
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDLL 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   285 E----SVLEVSSEDAIKMARELALKEGLMVGISSGANtVAAIRLAKMPE-NKGKLIVTIH 339
Cdd:pfam00291 235 DeyvgEVVTVSDEEALEAMRLLARREGIVVEPSSAAA-LAALKLALAGElKGGDRVVVVL 293
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 60-339 7.20e-64

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: 203.52  E-value: 7.20e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  60 TPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIipGKTTLIEPTSGNMGISLAFMAAMKGYRIIM 139
Cdd:cd00640   1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL--PKGVIIESTGGNTGIALAAAAARLGLKCTI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 140 TMPSYTSLERRVTMRSFGAELVLTDPakGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFdTTGPEIWEDTLG-NVD 218
Cdd:cd00640  79 VMPEGASPEKVAQMRALGAEVVLVPG--DFDDAIALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILEQLGGqKPD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 219 IFV---------MGIgsggtvsgvGRYLKSKNPNVKIYGVEPAesnilnggkpgphaitgngvgfkpeildmdvmesVLE 289
Cdd:cd00640 156 AVVvpvggggniAGI---------ARALKELLPNVKVIGVEPE----------------------------------VVT 192

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15233111 290 VSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmPENKGKLIVTIH 339
Cdd:cd00640 193 VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAK-KLGKGKTVVVIL 241
PLN02356 PLN02356
phosphateglycerate kinase
 26-348 3.23e-32

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 125.10  E-value: 3.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   26 STVGSPSFAQRL---RDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTE--GCEayVAAKQEHFQPTCSIKDRPAIAMIAD 100
Cdd:PLN02356  17 LMLLSYSFLLCNsrkRKTKKPLSKKKPRNGLIDAIGNTPLIRINSLSEatGCE--ILGKCEFLNPGGSVKDRVAVKIIEE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  101 AEKKKLIIPGKTtLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAK------------- 167
Cdd:PLN02356  95 ALESGQLFPGGV-VTEGSAGSTAISLATVAPAYGCKCHVVIPDDVAIEKSQILEALGATVERVRPVSithkdhyvniarr 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  168 ----------------GMGGT------------VKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDI 219
Cdd:PLN02356 174 raleanelaskrrkgsETDGIhlektngciseeEKENSLFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDA 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  220 FVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPG---------------PHAITGNGVGFK--PEILDMD 282
Cdd:PLN02356 254 FVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGSGLFNKVTRGvmytreeaegrrlknPFDTITEGIGINrlTQNFLMA 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233111  283 VMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKmPENKGKLIVTIHASFGERYLS 348
Cdd:PLN02356 334 KLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMNCVGAVRVAQ-SLGPGHTIVTILCDSGMRHLS 398
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 59-338 1.49e-15

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: 76.61  E-value: 1.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  59 KTPLVFLNKVTE--GCEAYVaaKQEHFQPTCSIKDRPAIAMIA---DAEKKKliipgktTLIEPTSGNMGISLAFMAAMK 133
Cdd:COG1171  24 RTPLLRSPTLSErlGAEVYL--KLENLQPTGSFKLRGAYNALAslsEEERAR-------GVVAASAGNHAQGVAYAARLL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDpakgmggtvkkaydllDSTPDAF-MCQQFANPAN-TQIH-FD------- 203
Cdd:COG1171  95 GIPATIVMPETAPAVKVAATRAYGAEVVLHG----------------DTYDDAEaAAAELAEEEGaTFVHpFDdpdviag 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 204 --TTGPEIWEDtLGNVD-IFV--------MGIGSggtvsgvgrYLKSKNPNVKIYGVEPAESN----------------- 255
Cdd:COG1171 159 qgTIALEILEQ-LPDLDaVFVpvggggliAGVAA---------ALKALSPDIRVIGVEPEGAAamyrslaagepvtlpgv 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 256 --I---LNGGKPGPHAitgngvgFkpEILDMDVMESVLeVsSEDAIKMA-RELALKEGLMVGiSSGANTVAAIrLAKMPE 329
Cdd:COG1171 229 dtIadgLAVGRPGELT-------F--EILRDLVDDIVT-V-SEDEIAAAmRLLLERTKIVVE-PAGAAALAAL-LAGKER 295


                ....*....
gi 15233111 330 NKGKLIVTI 338
Cdd:COG1171 296 LKGKRVVVV 304
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 59-338 2.15e-15

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: 75.99  E-value: 2.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  59 KTPLVF---LNKVTeGCEAYVaaKQEHFQPTCSIKDRPAIAMIA---DAEKKKLIIPGkttliepTSGNMGISLAFMAAM 132
Cdd:cd01562  17 RTPLLTsptLSELL-GAEVYL--KCENLQKTGSFKIRGAYNKLLslsEEERAKGVVAA-------SAGNHAQGVAYAAKL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 133 KGYRIIMTMPSYTSLERRVTMRSFGAELVLTDpakgmggtvkkaydllDSTPDAF-MCQQFANPAN-TQIH-FD------ 203
Cdd:cd01562  87 LGIPATIVMPETAPAAKVDATRAYGAEVVLYG----------------EDFDEAEaKARELAEEEGlTFIHpFDdpdvia 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 204 ---TTGPEIWEDtLGNVD-IFV--------MGIGSggtvsgvgrYLKSKNPNVKIYGVEPAESNI----LNGGKPGPHAI 267
Cdd:cd01562 151 gqgTIGLEILEQ-VPDLDaVFVpvggggliAGIAT---------AVKALSPNTKVIGVEPEGAPAmaqsLAAGKPVTLPE 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 268 TGN---GVGFK------PEILdMDVMESVLEVsSEDAIKMA-RELALKEGLMV-GisSGANTVAAIrLAKMPENKGKLIV 336
Cdd:cd01562 221 VDTiadGLAVKrpgeltFEII-RKLVDDVVTV-SEDEIAAAmLLLFEREKLVAeP--AGALALAAL-LSGKLDLKGKKVV 295


                ..
gi 15233111 337 TI 338
Cdd:cd01562 296 VV 297
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 54-338 2.03e-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: 67.92  E-value: 2.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  54 SLLIGKTPLVFLNKVTE--GCEAYVaaKQEHFQPTCSIKDRPAIAMIADAekKKLiipGKTTLIEPTSGNMGISLAFMAA 131
Cdd:COG0498  61 SLGEGGTPLVKAPRLADelGKNLYV--KEEGHNPTGSFKDRAMQVAVSLA--LER---GAKTIVCASSGNGSAALAAYAA 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 132 MKGYRIIMTMPS-YTSLERRVTMRSFGAELVLTDpakgmgGTvkkaYDlldstpDAF-MCQQFAN-----PANT------ 198
Cdd:COG0498 134 RAGIEVFVFVPEgKVSPGQLAQMLTYGAHVIAVD------GN----FD------DAQrLVKELAAdeglyAVNSinparl 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 199 --QIhfdTTGPEIWEDtLGNV-DIFV---------------------MGIGsggtvsgvgrylkSKNPnvKIYGVEPA-E 253
Cdd:COG0498 198 egQK---TYAFEIAEQ-LGRVpDWVVvptgnggnilagykafkelkeLGLI-------------DRLP--RLIAVQATgC 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 254 SNIL---NGGKPGP---HAIT-------GNGVGFkPEILDmDVMES---VLEVSSEDAIKMARELALKEGLMVGISSGAn 317
Cdd:COG0498 259 NPILtafETGRDEYepeRPETiapsmdiGNPSNG-ERALF-ALRESggtAVAVSDEEILEAIRLLARREGIFVEPATAV- 335

                       330       340
                ....*....|....*....|...
gi 15233111 318 TVAAIR--LAKMPENKGKLIVTI 338
Cdd:COG0498 336 AVAGLRklREEGEIDPDEPVVVL 358
PRK06815 PRK06815
threonine/serine dehydratase;
60-338 5.92e-11

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 62.79  E-value: 5.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   60 TPL---VFLNKVTeGCEAYVaaKQEHFQPTCSIKDRPA---IAMIADAEKKKLIIPGkttliepTSGNMGISLAFMAAMK 133
Cdd:PRK06815  21 TPLehsPLLSQHT-GCEVYL--KCEHLQHTGSFKFRGAsnkLRLLNEAQRQQGVITA-------SSGNHGQGVALAAKLA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTDPakgmggtvkkayDLLDSTPDA--FMCQQ---FANPANtqihfD----- 203
Cdd:PRK06815  91 GIPVTVYAPEQASAIKLDAIRALGAEVRLYGG------------DALNAELAArrAAEQQgkvYISPYN-----Dpqvia 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  204 ---TTGPEIwEDTLGNVD-IFVM--------GIGSggtvsgvgrYLKSKNPNVKIYG------------------VEPAE 253
Cdd:PRK06815 154 gqgTIGMEL-VEQQPDLDaVFVAvgggglisGIAT---------YLKTLSPKTEIIGcwpanspslytsleageiVEVAE 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  254 SNILNGGKPG---PHAITgngvgFkpEILDMDVMESVLevSSEDAIKMA-RELALKEGLMVGISSGANTVAAIRLAkmPE 329
Cdd:PRK06815 224 QPTLSDGTAGgvePGAIT-----F--PLCQQLIDQKVL--VSEEEIKEAmRLIAETDRWLIEGAAGVALAAALKLA--PR 292


                 ....*....
gi 15233111  330 NKGKLIVTI 338
Cdd:PRK06815 293 YQGKKVAVV 301
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 48-161 1.52e-08

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: 55.68  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  48 NAKRDASLLIGKTPLVFLNKVTE---GCEAYVaaKQEHFQPTCSIKDRPAIAMIADAekKKLiipGKTTLIEPTSGNMGI 124
Cdd:cd01563  11 TEDDIVSLGEGNTPLVRAPRLGErlgGKNLYV--KDEGLNPTGSFKDRGMTVAVSKA--KEL---GVKAVACASTGNTSA 83

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15233111 125 SLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELV 161
Cdd:cd01563  84 SLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVL 120
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
57-250 7.52e-07

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


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 50.50  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   57 IGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPA---IAMIADAEKKKLIIPGkttliepTSGNMGISLAFMAAMK 133
Cdd:PRK08638  25 IRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAfnkLSSLTDAEKRKGVVAC-------SAGNHAQGVALSCALL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  134 GYRIIMTMPSYTSLERRVTMRSFGAELVLTdpakgmGGTVKKAYdlldstpdAFMCQQFANPANTQIH-FD--------- 203
Cdd:PRK08638  98 GIDGKVVMPKGAPKSKVAATCGYGAEVVLH------GDNFNDTI--------AKVEEIVEEEGRTFIPpYDdpkviagqg 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15233111  204 TTGPEIWEDtLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVE 250
Cdd:PRK08638 164 TIGLEILED-LWDVDTVIVPIGGGGLIAGIAVALKSINPTIHIIGVQ 209
PRK06110 PRK06110
threonine dehydratase;
71-161 1.84e-06

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 49.22  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   71 GCEAYVaaKQEHFQPTCSIKDRPAIAMIADAEKKKliiPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERR 150
Cdd:PRK06110  35 GCEVWV--KHENHTPTGAFKVRGGLVYFDRLARRG---PRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109

                         90
                 ....*....|.
gi 15233111  151 VTMRSFGAELV 161
Cdd:PRK06110 110 AAMRALGAELI 120
PRK06381 PRK06381
threonine synthase; Validated
 79-164 1.96e-06

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 48.93  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   79 KQEHFQPTCSIKDRpaiamIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGA 158
Cdd:PRK06381  36 KFEGANPTGTQKDR-----IAEAHVRRAMRLGYSGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGA 110


                 ....*.
gi 15233111  159 ELVLTD 164
Cdd:PRK06381 111 EIIYVD 116
PRK12483 PRK12483
threonine dehydratase; Reviewed
 76-317 8.12e-06

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 47.48  E-value: 8.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   76 VAAKQEHFQPTCSIKDRPA---IAMIADAEKKKLIIPGkttliepTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVT 152
Cdd:PRK12483  54 VLLKREDLQPVFSFKIRGAynkMARLPAEQLARGVITA-------SAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDG 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  153 MRSFGAELVLTDpakgmggtvkkaydllDSTPDAFM-CQQFANPAN-TQIH-FD---------TTGPEIWEDTLGNVD-I 219
Cdd:PRK12483 127 VRAHGGEVVLHG----------------ESFPDALAhALKLAEEEGlTFVPpFDdpdviagqgTVAMEILRQHPGPLDaI 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  220 FVmGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVG---------------------FKPEI 278
Cdd:PRK12483 191 FV-PVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGlfadgvavaqigehtfelcrhYVDEV 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15233111  279 LDMDVME-------------SVLEVSSEDAIKMARELALKEGL----MVGISSGAN 317
Cdd:PRK12483 270 VTVSTDElcaaikdiyddtrSITEPAGALAVAGIKKYAEREGIegqtLVAIDSGAN 325
PLN02550 PLN02550
threonine dehydratase
 59-257 1.60e-05

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 46.84  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   59 KTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLiipgKTTLIEPTSGNMGISLAFMAAMKGYRII 138
Cdd:PLN02550 109 ESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQL----DKGVICSSAGNHAQGVALSAQRLGCDAV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  139 MTMPSYTSLERRVTMRSFGAELVLT----DPAKGM--------GGTVKKAYDlldsTPDAFMCQqfanpantqihfDTTG 206
Cdd:PLN02550 185 IAMPVTTPEIKWQSVERLGATVVLVgdsyDEAQAYakqraleeGRTFIPPFD----HPDVIAGQ------------GTVG 248

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15233111  207 PEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNIL 257
Cdd:PLN02550 249 MEIVRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAM 299
PRK06608 PRK06608
serine/threonine dehydratase;
57-164 1.66e-05

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 46.30  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   57 IGKTPLV---FLNKVTeGCEAYVaaKQEHFQPTCSIKDRPAIAMIADA-EKKKLIipgkTTLIEPTSGNMGISLAFMAAM 132
Cdd:PRK06608  21 LHLTPIVhseSLNEML-GHEIFF--KVESLQKTGAFKVRGVLNHLLELkEQGKLP----DKIVAYSTGNHGQAVAYASKL 93

                         90       100       110
                 ....*....|....*....|....*....|..
gi 15233111  133 KGYRIIMTMPSYTSLERRVTMRSFGAELVLTD 164
Cdd:PRK06608  94 FGIKTRIYLPLNTSKVKQQAALYYGGEVILTN 125
PRK06450 PRK06450
threonine synthase; Validated
 42-161 3.32e-05

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 45.11  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   42 KDFPSTnaKRDASLLIGKTPLVFLNKVTegceayvaAKQEHFQPTCSIKDRPAIAMIADAEKKkliipGKTTLIEPTSGN 121
Cdd:PRK06450  43 KNFPYI--KHFISLGEGRTPLIKKGNIW--------FKLDFLNPTGSYKDRGSVTLISYLAEK-----GIKQISEDSSGN 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15233111  122 MGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELV 161
Cdd:PRK06450 108 AGASIAAYGAAAGIEVKIFVPETASGGKLKQIESYGAEVV 147
PRK05638 PRK05638
threonine synthase; Validated
 50-161 4.53e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 45.19  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   50 KRDASLLIGKTPLVfLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAekkklIIPGKTTLIEPTSGNMGISLAFM 129
Cdd:PRK05638  57 KKIISLGEGGTPLI-RARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYG-----LPYAANGFIVASDGNAAASVAAY 130

                         90       100       110
                 ....*....|....*....|....*....|..
gi 15233111  130 AAMKGYRIIMTMPSYTSLERRVTMRSFGAELV 161
Cdd:PRK05638 131 SARAGKEAFVVVPRKVDKGKLIQMIAFGAKII 162
PRK08329 PRK08329
threonine synthase; Validated
 79-160 6.67e-05

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 44.43  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   79 KQEHFQPTCSIKDRPAIAMIAdaekkKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGA 158
Cdd:PRK08329  77 KLDYLQPTGSFKDRGTYVTVA-----KLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151


                 ..
gi 15233111  159 EL 160
Cdd:PRK08329 152 EL 153
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
 291-341 2.33e-04

periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa.


Pssm-ID: 380553 [Multi-domain]  Cd Length: 342  Bit Score: 42.55  E-value: 2.33e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15233111 291 SSEDAIKMARELALKEG--LMVGISSGANTVAAIRLAKmpENKGKLIVTIHAS 341
Cdd:cd06330  51 KPDEAVRAARELVLQEGvdFLIGTISSGVALAVAPVAE--ELKVLFIATDAAT 101
PRK08197 PRK08197
threonine synthase; Validated
 54-164 2.76e-04

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 42.68  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   54 SLLIGKTPLVFLNKVTE---GCEAYVaaKQEHFQPTCSIKDRPAIAMIADAekKKLiipGKTTLIEPTSGNMGISLAFMA 130
Cdd:PRK08197  74 SLGEGMTPLLPLPRLGKalgIGRLWV--KDEGLNPTGSFKARGLAVGVSRA--KEL---GVKHLAMPTNGNAGAAWAAYA 146

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15233111  131 AMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTD 164
Cdd:PRK08197 147 ARAGIRATIFMPADAPEITRLECALAGAELYLVD 180
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
59-255 1.51e-03

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


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 40.00  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   59 KTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDR---PAIAMIADAEKKKliipGKTTLiepTSGNMGISLAFMAAMKGY 135
Cdd:PRK07048  24 RTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRgayNALSQFSPEQRRA----GVVTF---SSGNHAQAIALSARLLGI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  136 RIIMTMPSYTSLERRVTMRSFGAELVLTDP------------AKGMGGTVKKAYDlldsTPDAFMCQqfanpantqihfD 203
Cdd:PRK07048  97 PATIVMPQDAPAAKVAATRGYGGEVVTYDRytedreeigrrlAEERGLTLIPPYD----HPHVIAGQ------------G 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15233111  204 TTGPEIWEDTlGNVDIFVM---GIGSGGTVSGVGRYLkskNPNVKIYGVEPAESN 255
Cdd:PRK07048 161 TAAKELFEEV-GPLDALFVclgGGGLLSGCALAARAL---SPGCKVYGVEPEAGN 211
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
59-257 1.98e-03

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 40.12  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   59 KTPLVFLNKVTE--GCEAYVaaKQEHFQPTCSIKDRPAIAMIA---DAEKKKLIIpgkttliepTS--GNMGISLAFMAA 131
Cdd:PRK09224  20 ETPLEKAPKLSArlGNQVLL--KREDLQPVFSFKLRGAYNKMAqltEEQLARGVI---------TAsaGNHAQGVALSAA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  132 MKGYRIIMTMPSYTSLERRVTMRSFGAELVLT----DPAKgmggtvKKAYDLLDSTPDAFmcqqfanpantqIH-FD--- 203
Cdd:PRK09224  89 RLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHgdsfDEAY------AHAIELAEEEGLTF------------IHpFDdpd 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15233111  204 ------TTGPEIWEDTLGNVD-IFV--------MGIGSggtvsgvgrYLKSKNPNVKIYGVEPAESNIL 257
Cdd:PRK09224 151 viagqgTIAMEILQQHPHPLDaVFVpvggggliAGVAA---------YIKQLRPEIKVIGVEPEDSACL 210
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 95-164 2.34e-03

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 39.48  E-value: 2.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   95 IAMIADAEKKKLIipGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTD 164
Cdd:PRK08206 102 FEELTSGEVREKL--GDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIITD 169
PRK08639 PRK08639
threonine dehydratase; Validated
 56-252 5.52e-03

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 38.63  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   56 LIGKTPLVF---LNKVTeGCEAYVaaKQEHFQPTCSIKDRPA---IAMIADAEKKKLIIPgkttliePTSGNMGISLAFM 129
Cdd:PRK08639  22 VVPETPLQRndyLSEKY-GANVYL--KREDLQPVRSYKLRGAynaISQLSDEELAAGVVC-------ASAGNHAQGVAYA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111  130 AAMKGYRIIMTMPSYTSLERRVTMRSFGA---ELVLTdpakgmGGTvkkaYDllDSTPDAfmcQQFANPAN-TQIH-FD- 203
Cdd:PRK08639  92 CRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLV------GDT----FD--DSAAAA---QEYAEETGaTFIPpFDd 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15233111  204 --------TTGPEIWED--TLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPA 252
Cdd:PRK08639 157 pdviagqgTVAVEILEQleKEGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPA 215
eutB PRK07476
threonine dehydratase; Provisional
 49-163 7.06e-03

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 38.02  E-value: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111   49 AKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPA---IAMIADAEKKKLIIPGKTtlieptsGNMGIS 125
Cdd:PRK07476   9 ARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGAtnaLLSLSAQERARGVVTAST-------GNHGRA 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 15233111  126 LAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLT 163
Cdd:PRK07476  82 LAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIV 119
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 240-336 9.71e-03

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


Pssm-ID: 107207  Cd Length: 365  Bit Score: 37.52  E-value: 9.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233111 240 KNPNVKIYGVEPAESNI--------LNGGKPG-------------------PHAITGN----GVGfkPEI---LDMDVME 285
Cdd:cd06446 225 NDKDVKLIGVEAGGCGLetgghaayLFGGTAGvlhglkmytlqdedgqivpPHSISAGldypGVG--PEHaylKDSGRVE 302

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15233111 286 SVlEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLA-KMPenKGKLIV 336
Cdd:cd06446 303 YV-AVTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAkKLG--KEKVIV 351
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH