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Conserved domains on  [gi|1049755379|gb|ANY68633|]
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cysteine synthase [Paenibacillus sp. BIHB4019]

Protein Classification

cysteine synthase family protein( domain architecture ID 10107527)

cysteine synthase family protein is a pyridoxal 5'-phosphate (PLP)-dependent enzyme; similar to Bacillus subtilis O-acetylserine dependent cystathionine beta-synthase, which catalyzes the conversion of O-acetylserine and homocysteine to cystathionine, and to Helicobacter pylori cysteine synthase, which catalyzes the last step of cysteine biosynthesis

CATH:  3.40.50.1100
EC:  2.5.1.-
Gene Ontology:  GO:0006535|GO:0016765
SCOP:  4000798

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 11-298 2.34e-99

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: 294.81  E-value: 2.34e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVYGFRVI 90
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  91 IVVDPKVSESLLRWYQAYGAEISMVtsPAADGGFQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQTTALEIV-DLP 169
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILT--PEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWeQLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 170 --VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNTDISVLDQVCIASDQE 246
Cdd:cd01561   159 gkVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGgPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1049755379 247 AISMCRLLARHHGILIGGSGGLTVVAALAWLN-NSDSQAAVAIIPDTGINYLD 298
Cdd:cd01561   239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKrLGPGKTIVTILPDSGERYLS 291
 
Name Accession Description Interval E-value
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 11-298 2.34e-99

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: 294.81  E-value: 2.34e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVYGFRVI 90
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  91 IVVDPKVSESLLRWYQAYGAEISMVtsPAADGGFQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQTTALEIV-DLP 169
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILT--PEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWeQLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 170 --VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNTDISVLDQVCIASDQE 246
Cdd:cd01561   159 gkVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGgPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1049755379 247 AISMCRLLARHHGILIGGSGGLTVVAALAWLN-NSDSQAAVAIIPDTGINYLD 298
Cdd:cd01561   239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKrLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 1-298 5.97e-98

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: 291.57  E-value: 5.97e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   1 MIYNNITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAM 80
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  81 LGAVYGFRVIIVVDPKVSE---SLLRwyqAYGAEIsmVTSPAADGgfQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYH 157
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKerrALLR---AYGAEV--VLTPGAEG--MKGAIDKAEELAAETPGAFWPNQFENPANPEAH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 158 SQTTALEIV---DLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVF-REKFSPYLINGVGLSWRSDNTDI 233
Cdd:COG0031   155 YETTGPEIWeqtDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDP 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049755379 234 SVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQA-AVAIIPDTGINYLD 298
Cdd:COG0031   235 SLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKtIVTILPDSGERYLS 300
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
 6-306 2.27e-96

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: 287.95  E-value: 2.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVY 85
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  86 GFRVIIVVDPKVSESLLRWYQAYGAEISMVTSPAADGGFQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQTTALEI 165
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 166 V-DLP-VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFREKFSPYLINGVGLSWRSDNTDISVLDQVCIAS 243
Cdd:TIGR03945 161 ArAFPtLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHVP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049755379 244 DQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQA-AVAIIPDTGINYLDQFYDDEWL 306
Cdd:TIGR03945 241 EYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGStVVAILPDRGERYLDTVYNDEWV 304
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 6-258 2.29e-57

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: 187.52  E-value: 2.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKlnhDSILVESTSGNLGKSLAMLGAVY 85
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEG---GKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  86 GFRVIIVVDPKVSESLLRWYQAYGAEISMVtspaaDGGFQRARlNRVQELLQQFPNAYWTNQYDNPQNPQYHSqTTALEI 165
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV-----GGDYDEAV-AAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 166 VD---LPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFREKF----------SPYLINGVGLSWRSDNTD 232
Cdd:pfam00291 151 LEqlgGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLaagrpvpvpvADTIADGLGVGDEPGALA 230

                         250       260       270
                  ....*....|....*....|....*....|
gi 1049755379 233 ISVLDQVCIA----SDQEAISMCRLLARHH 258
Cdd:pfam00291 231 LDLLDEYVGEvvtvSDEEALEAMRLLARRE 260
PRK10717 PRK10717
cysteine synthase A; Provisional
 1-311 1.40e-52

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 176.21  E-value: 1.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   1 MIYNNITECIGNTPVLAL--ADDLVpkGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSL 78
Cdd:PRK10717    2 KIFEDVSDTIGNTPLIRLnrASEAT--GCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  79 AMLGAVYGFRVIIVVDPKVS---ESLLRwyqAYGAEIsmVTSPAA----DGGFQRARLNRVQELLQQFPN-AYWTNQYDN 150
Cdd:PRK10717   80 ALVAAARGYKTVIVMPETQSqekKDLLR---ALGAEL--VLVPAApyanPNNYVKGAGRLAEELVASEPNgAIWANQFDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 151 PQNPQYHSQTTALEI---VDLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFR-------EKFSPYLIN 220
Cdd:PRK10717  155 PANREAHYETTGPEIweqTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 221 GVGLSWRSDNTDISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAALAwlnnsdsqAA---------VAIIPD 291
Cdd:PRK10717  235 GIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALR--------LArelgpghtiVTILCD 306

                         330       340
                  ....*....|....*....|
gi 1049755379 292 TGINYLDQFYDDEWLVEKNI 311
Cdd:PRK10717  307 SGERYQSKLFNPDFLREKGL 326
 
Name Accession Description Interval E-value
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 11-298 2.34e-99

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: 294.81  E-value: 2.34e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVYGFRVI 90
Cdd:cd01561     1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  91 IVVDPKVSESLLRWYQAYGAEISMVtsPAADGGFQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQTTALEIV-DLP 169
Cdd:cd01561    81 IVMPETMSEEKRKLLRALGAEVILT--PEAEADGMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWeQLD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 170 --VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNTDISVLDQVCIASDQE 246
Cdd:cd01561   159 gkVDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGgPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1049755379 247 AISMCRLLARHHGILIGGSGGLTVVAALAWLN-NSDSQAAVAIIPDTGINYLD 298
Cdd:cd01561   239 AFAMARRLAREEGLLVGGSSGAAVAAALKLAKrLGPGKTIVTILPDSGERYLS 291
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 1-298 5.97e-98

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: 291.57  E-value: 5.97e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   1 MIYNNITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAM 80
Cdd:COG0031     2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLAM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  81 LGAVYGFRVIIVVDPKVSE---SLLRwyqAYGAEIsmVTSPAADGgfQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYH 157
Cdd:COG0031    82 VAAAKGYRLILVMPETMSKerrALLR---AYGAEV--VLTPGAEG--MKGAIDKAEELAAETPGAFWPNQFENPANPEAH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 158 SQTTALEIV---DLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVF-REKFSPYLINGVGLSWRSDNTDI 233
Cdd:COG0031   155 YETTGPEIWeqtDGKVDAFVAGVGTGGTITGVGRYLKERNPDIKIVAVEPEGSPLLsGGEPGPHKIEGIGAGFVPKILDP 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049755379 234 SVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQA-AVAIIPDTGINYLD 298
Cdd:COG0031   235 SLIDEVITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKtIVTILPDSGERYLS 300
PLP_SbnA_fam TIGR03945
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ...
 6-306 2.27e-96

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: 287.95  E-value: 2.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVY 85
Cdd:TIGR03945   1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  86 GFRVIIVVDPKVSESLLRWYQAYGAEISMVTSPAADGGFQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQTTALEI 165
Cdd:TIGR03945  81 GLRFICVVDPNISPQNLKLLRAYGAEVEKVTEPDETGGYLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 166 V-DLP-VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFREKFSPYLINGVGLSWRSDNTDISVLDQVCIAS 243
Cdd:TIGR03945 161 ArAFPtLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGSVIFGGPPGRRHIPGLGASVVPELLDESLIDDVVHVP 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049755379 244 DQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQA-AVAIIPDTGINYLDQFYDDEWL 306
Cdd:TIGR03945 241 EYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGStVVAILPDRGERYLDTVYNDEWV 304
cysK TIGR01139
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ...
 6-297 3.16e-67

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: 213.00  E-value: 3.16e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALaDDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVY 85
Cdd:TIGR01139   1 ISELIGNTPLVRL-NRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  86 GFRVIIVVDPKVSESLLRWYQAYGAEisMVTSPAADGGfqRARLNRVQELLQQFPNAYWT-NQYDNPQNPQYHSQTTALE 164
Cdd:TIGR01139  80 GYKLILTMPETMSIERRKLLKAYGAE--LVLTPGAEGM--KGAIAKAEEIAASTPNSYFMlQQFENPANPEIHRKTTGPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 165 IV---DLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNTDISVLDQVC 240
Cdd:TIGR01139 156 IWrdtDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGgKPGPHKIQGIGAGFIPKNLNRSVIDEVI 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1049755379 241 IASDQEAISMCRLLARHHGILIGGSGGLTVVAAL--AWLNNSDsQAAVAIIPDTGINYL 297
Cdd:TIGR01139 236 TVSDEEAIETARRLAAEEGILVGISSGAAVAAALklAKRPEPD-KLIVVILPSTGERYL 293
cysta_beta TIGR01137
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ...
 2-337 4.75e-63

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: 206.96  E-value: 4.75e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   2 IYNNITECIGNTPVLALadDLVPKG--KSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLA 79
Cdd:TIGR01137   1 ILDNILDLIGNTPLVRL--NKVSKGlkCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  80 MLGAVYGFRVIIVVDPKVSESLLRWYQAYGAEIsMVTSPAADGGFQRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQ 159
Cdd:TIGR01137  79 LVAAIKGYKCIIVLPEKMSSEKVDVLRALGAEI-VRTPTAAAFDSPESHIGVAKRLVREIPGAHILDQYRNPSNPLAHYD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 160 TTALEI---VDLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGS------AVFREKFSPYLINGVGLSWRSDN 230
Cdd:TIGR01137 158 TTGPEIleqCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGSilaqpeELNQTGRTPYKVEGIGYDFIPTV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 231 TDISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAAL--AWLNNSDSQAAVAIIPDTGINYLDQFYDDEWLVE 308
Cdd:TIGR01137 238 LDRKVVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALkaAEDELQEGQRCVVLLPDSIRNYMTKFLNDEWMLD 317

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1049755379 309 KNitLLDRSEL---QQMIQNKTFDSLQMKSNV 337
Cdd:TIGR01137 318 NG--FLDDEDLtvkDVLWWHARVKDLHLPAPV 347
cysKM TIGR01136
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ...
 6-297 4.40e-62

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: 199.81  E-value: 4.40e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALaDDLVPK-GKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAV 84
Cdd:TIGR01136   1 IEELIGNTPLVRL-NRLAPGcDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  85 YGFRVIIVVDPKVSESLLRWYQAYGAEIsmVTSPAADGGfqRARLNRVQELLQQFPNAYWTNQYDNPQNPQYHSQTTALE 164
Cdd:TIGR01136  80 RGYKLILTMPETMSLERRKLLRAYGAEL--ILTPGEEGM--KGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 165 IV-DLP--VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNTDISVLDQVC 240
Cdd:TIGR01136 156 IWrDTDgrIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGgEPGPHKIQGIGAGFIPKILDLSLIDEVI 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 241 IASDQEAISMCRLLARHHGILIGGSGGLTVVAAL---AWLNNSDSQaAVAIIPDTGINYL 297
Cdd:TIGR01136 236 TVSDEDAIETARRLAREEGILVGISSGAAVAAALklaKRLENADKV-IVAILPDTGERYL 294
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 6-258 2.29e-57

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: 187.52  E-value: 2.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKlnhDSILVESTSGNLGKSLAMLGAVY 85
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEG---GKTVVEASSGNHGRALAAAAARL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  86 GFRVIIVVDPKVSESLLRWYQAYGAEISMVtspaaDGGFQRARlNRVQELLQQFPNAYWTNQYDNPQNPQYHSqTTALEI 165
Cdd:pfam00291  78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLV-----GGDYDEAV-AAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 166 VD---LPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFREKF----------SPYLINGVGLSWRSDNTD 232
Cdd:pfam00291 151 LEqlgGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLaagrpvpvpvADTIADGLGVGDEPGALA 230

                         250       260       270
                  ....*....|....*....|....*....|
gi 1049755379 233 ISVLDQVCIA----SDQEAISMCRLLARHH 258
Cdd:pfam00291 231 LDLLDEYVGEvvtvSDEEALEAMRLLARRE 260
PRK10717 PRK10717
cysteine synthase A; Provisional
 1-311 1.40e-52

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 176.21  E-value: 1.40e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   1 MIYNNITECIGNTPVLAL--ADDLVpkGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSL 78
Cdd:PRK10717    2 KIFEDVSDTIGNTPLIRLnrASEAT--GCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  79 AMLGAVYGFRVIIVVDPKVS---ESLLRwyqAYGAEIsmVTSPAA----DGGFQRARLNRVQELLQQFPN-AYWTNQYDN 150
Cdd:PRK10717   80 ALVAAARGYKTVIVMPETQSqekKDLLR---ALGAEL--VLVPAApyanPNNYVKGAGRLAEELVASEPNgAIWANQFDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 151 PQNPQYHSQTTALEI---VDLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFR-------EKFSPYLIN 220
Cdd:PRK10717  155 PANREAHYETTGPEIweqTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSALYSyyktgelKAEGSSITE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 221 GVGLSWRSDNTDISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAALAwlnnsdsqAA---------VAIIPD 291
Cdd:PRK10717  235 GIGQGRITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALR--------LArelgpghtiVTILCD 306

                         330       340
                  ....*....|....*....|
gi 1049755379 292 TGINYLDQFYDDEWLVEKNI 311
Cdd:PRK10717  307 SGERYQSKLFNPDFLREKGL 326
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 13-258 3.38e-50

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: 167.31  E-value: 3.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  13 TPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSIlVESTSGNLGKSLAMLGAVYGFRVIIV 92
Cdd:cd00640     1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKGVI-IESTGGNTGIALAAAAARLGLKCTIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  93 VDPKVSESLLRWYQAYGAEISMVtspaaDGGFQRARlNRVQELLQQFPNAYWTNQYDNPQNPQYHSqTTALEIV----DL 168
Cdd:cd00640    80 MPEGASPEKVAQMRALGAEVVLV-----PGDFDDAI-ALAKELAEEDPGAYYVNQFDNPANIAGQG-TIGLEILeqlgGQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 169 PVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACdvagsavfrekfspylingvglswrsDNTDISVldqvciaSDQEAI 248
Cdd:cd00640   153 KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGV--------------------------EPEVVTV-------SDEEAL 199

                         250
                  ....*....|
gi 1049755379 249 SMCRLLARHH 258
Cdd:cd00640   200 EAIRLLAREE 209
PLN02565 PLN02565
cysteine synthase
 2-297 1.39e-44

cysteine synthase


Pssm-ID: 166206  Cd Length: 322  Bit Score: 155.08  E-value: 1.39e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   2 IYNNITECIGNTPVLAL---ADDLVPKgksLYLKLDYFNPNFSIKDRTALGLVKSALASGKLN-HDSILVESTSGNLGKS 77
Cdd:PLN02565    5 IAKDVTELIGKTPLVYLnnvVDGCVAR---IAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKpGESVLIEPTSGNTGIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  78 LAMLGAVYGFRVIIVVDPKVSESLLRWYQAYGAEIsMVTSPA--ADGGFQRArlnrvQELLQQFPNAYWTNQYDNPQNPQ 155
Cdd:PLN02565   82 LAFMAAAKGYKLIITMPASMSLERRIILLAFGAEL-VLTDPAkgMKGAVQKA-----EEILAKTPNSYILQQFENPANPK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 156 YHSQTTALEI---VDLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNT 231
Cdd:PLN02565  156 IHYETTGPEIwkgTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGgKPGPHKIQGIGAGFIPGVL 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1049755379 232 DISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAA--LAWLNNSDSQAAVAIIPDTGINYL 297
Cdd:PLN02565  236 DVDLLDEVVQVSSDEAIETAKLLALKEGLLVGISSGAAAAAAikIAKRPENAGKLIVVIFPSFGERYL 303
PLN00011 PLN00011
cysteine synthase
 1-297 9.52e-44

cysteine synthase


Pssm-ID: 177651  Cd Length: 323  Bit Score: 153.24  E-value: 9.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   1 MIYNNITECIGNTPVLAL---ADDLVPKgksLYLKLDYFNPNFSIKDRTALGLVKSALASGKLN-HDSILVESTSGNLGK 76
Cdd:PLN00011    6 LIKNDVTELIGNTPMVYLnniVDGCVAR---IAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITpGKSTLIEATAGNTGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  77 SLAMLGAVYGFRVIIVVDPKVSESLLRWYQAYGAEISMvTSPAAdgGFQrARLNRVQELLQQFPNAYWTNQYDNPQNPQY 156
Cdd:PLN00011   83 GLACIGAARGYKVILVMPSTMSLERRIILRALGAEVHL-TDQSI--GLK-GMLEKAEEILSKTPGGYIPQQFENPANPEI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 157 HSQTTALEI---VDLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDNTD 232
Cdd:PLN00011  159 HYRTTGPEIwrdSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGgQPGPHLIQGIGSGIIPFNLD 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1049755379 233 ISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQAA--VAIIPDTGINYL 297
Cdd:PLN00011  239 LTIVDEIIQVTGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRPENAGKliVVIFPSGGERYL 305
PLN02556 PLN02556
cysteine synthase/L-3-cyanoalanine synthase
 2-304 3.29e-41

cysteine synthase/L-3-cyanoalanine synthase


Pssm-ID: 178171 [Multi-domain]  Cd Length: 368  Bit Score: 147.41  E-value: 3.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   2 IYNNITECIGNTPVLALadDLVPKGKSLYL--KLDYFNPNFSIKDRTALGLVKSA-----LASGKlnhdSILVESTSGNL 74
Cdd:PLN02556   49 IKTDASQLIGKTPLVYL--NKVTEGCGAYIaaKQEMFQPTSSIKDRPALAMIEDAekknlITPGK----TTLIEPTSGNM 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  75 GKSLAMLGAVYGFRVIIVVDPKVSESLLRWYQAYGAEIsMVTSPAADGGfqrARLNRVQELLQQFPNAYWTNQYDNPQNP 154
Cdd:PLN02556  123 GISLAFMAAMKGYKMILTMPSYTSLERRVTMRAFGAEL-VLTDPTKGMG---GTVKKAYELLESTPDAFMLQQFSNPANT 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 155 QYHSQTTALEIVDLP---VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFRE-KFSPYLINGVGLSWRSDN 230
Cdd:PLN02556  199 QVHFETTGPEIWEDTlgqVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGgKPGPHHITGNGVGFKPDI 278

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049755379 231 TDISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAA--LAWLNNSDSQAAVAIIPDTGINYLDQFYDDE 304
Cdd:PLN02556  279 LDMDVMEKVLEVSSEDAVNMARELALKEGLMVGISSGANTVAAlrLAKMPENKGKLIVTVHPSFGERYLSSVLFQE 354
cysM TIGR01138
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ...
 6-297 5.71e-41

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: 145.06  E-value: 5.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   6 ITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGAVY 85
Cdd:TIGR01138   2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  86 GFRVIIVVDPKVSESLLRWYQAYGAEISMVTSpaaDGGFQRARLnRVQELLQQFPNAYwTNQYDNPQNPQYHSQTTALEI 165
Cdd:TIGR01138  82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTK---EEGMEGARD-LALELANRGEGKL-LDQFNNPDNPYAHYTSTGPEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 166 VDLPVDSI---IGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAgsavfrEKFSPYLINGVGLSWRSDNTDISVLDQVCIA 242
Cdd:TIGR01138 157 WQQTGGRIthfVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPE------EGSSIPGIRRWPTEYLPGIFDASLVDRVLDI 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1049755379 243 SDQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQAAVAIIPDTGINYL 297
Cdd:TIGR01138 231 HQRDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDAVVVAIICDRGDRYL 285
PLN03013 PLN03013
cysteine synthase
 2-255 8.52e-40

cysteine synthase


Pssm-ID: 178587 [Multi-domain]  Cd Length: 429  Bit Score: 145.30  E-value: 8.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   2 IYNNITECIGNTPVLALadDLVPKG--KSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLN-HDSILVESTSGNLGKSL 78
Cdd:PLN03013  113 IADNVSQLIGKTPMVYL--NSIAKGcvANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISpGKSVLVEPTSGNTGIGL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  79 AMLGAVYGFRVIIVVDPKVSESLLRWYQAYGAEIsMVTSPAA--DGGFQRArlnrvQELLQQFPNAYWTNQYDNPQNPQY 156
Cdd:PLN03013  191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAEL-VLTDPAKgmTGAVQKA-----EEILKNTPDAYMLQQFDNPANPKI 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 157 HSQTTALEIVDL---PVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSAVFR-EKFSPYLINGVGLSWRSDNTD 232
Cdd:PLN03013  265 HYETTGPEIWDDtkgKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSgGKPGPHKIQGIGAGFIPKNLD 344

                         250       260
                  ....*....|....*....|...
gi 1049755379 233 ISVLDQVCIASDQEAISMCRLLA 255
Cdd:PLN03013  345 QKIMDEVIAISSEEAIETAKQLA 367
cysM PRK11761
cysteine synthase CysM;
1-297 8.54e-37

cysteine synthase CysM;


Pssm-ID: 236972  Cd Length: 296  Bit Score: 133.85  E-value: 8.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   1 MIYNNITECIGNTPVLALaDDLVPKGKS-LYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLA 79
Cdd:PRK11761    1 MAYPTLEDTIGNTPLVKL-QRLPPDRGNtILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  80 MLGAVYGFRVIIVVDPKVSESLLRWYQAYGAEISMVTspaADGGFQRARlnRVQELLQQFPNAYWTNQYDNPQNPQYHSQ 159
Cdd:PRK11761   80 MIAAIKGYRMKLIMPENMSQERRAAMRAYGAELILVP---KEQGMEGAR--DLALQMQAEGEGKVLDQFANPDNPLAHYE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 160 TTALEI---VDLPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVA-GSAV--FREKFSPYL--IngvglswrsdnT 231
Cdd:PRK11761  155 TTGPEIwrqTEGRITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEeGSSIpgIRRWPEEYLpkI-----------F 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049755379 232 DISVLDQVCIASDQEAISMCRLLARHHGILIGGSGGLTVVAALAWLNNSDSQAAVAIIPDTGINYL 297
Cdd:PRK11761  224 DASRVDRVLDVSQQEAENTMRRLAREEGIFCGVSSGGAVAAALRIARENPNAVIVAIICDRGDRYL 289
PLN02356 PLN02356
phosphateglycerate kinase
 4-312 2.36e-23

phosphateglycerate kinase


Pssm-ID: 215204  Cd Length: 423  Bit Score: 99.68  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   4 NNITECIGNTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKLNHDSILVESTSGNLGKSLAMLGA 83
Cdd:PLN02356   45 NGLIDAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAP 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  84 VYGFRVIIVVDPKVSESLLRWYQAYGAEISMV-----TSPAADGGFQRARLNRVQELLQQF------------------- 139
Cdd:PLN02356  125 AYGCKCHVVIPDDVAIEKSQILEALGATVERVrpvsiTHKDHYVNIARRRALEANELASKRrkgsetdgihlektngcis 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 140 -------------PNAYWTNQYDNPQNPQYHSQTTALEIVDLP---VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACD 203
Cdd:PLN02356  205 eeekenslfssscTGGFFADQFENLANFRAHYEGTGPEIWEQTqgnLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLID 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 204 VAGSAVF----------REKF------SPY--LINGVGLSWRSDNTDISVLDQVCIASDQEAISMCRLLARHHGILIGGS 265
Cdd:PLN02356  285 PPGSGLFnkvtrgvmytREEAegrrlkNPFdtITEGIGINRLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSS 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1049755379 266 GGLTVVAALAWLNN-SDSQAAVAIIPDTGINYLDQFYDDEWLVEKNIT 312
Cdd:PLN02356  365 SAMNCVGAVRVAQSlGPGHTIVTILCDSGMRHLSKFHDPQYLSQHGLT 412
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 11-192 1.44e-14

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: 73.40  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVLAlADDL--VPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKlnhdSILVESTSGNLGKSLAMLGAVYGFR 88
Cdd:cd01563    21 GNTPLVR-APRLgeRLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIK 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  89 VIIVVdP------KVSESLlrwyqAYGAEISMVtspaaDGGFQRArLNRVQELLQQFPnAYWTNQYdnpqNPQYH--SQT 160
Cdd:cd01563    96 CVVFL-PagkalgKLAQAL-----AYGATVLAV-----EGNFDDA-LRLVRELAEENW-IYLSNSL----NPYRLegQKT 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1049755379 161 TALEIVD-----LPvDSIIGAVSTGGHLCGIGKYVKE 192
Cdd:cd01563   159 IAFEIAEqlgweVP-DYVVVPVGNGGNITAIWKGFKE 194
PRK06450 PRK06450
threonine synthase; Validated
 11-112 3.30e-14

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 72.46  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVLaladdlvpKGKSLYLKLDYFNPNFSIKDRTALGLVkSALASGKLNHDSilvESTSGNLGKSLAMLGAVYGFRVI 90
Cdd:PRK06450   57 GRTPLI--------KKGNIWFKLDFLNPTGSYKDRGSVTLI-SYLAEKGIKQIS---EDSSGNAGASIAAYGAAAGIEVK 124

                          90       100
                  ....*....|....*....|..
gi 1049755379  91 IVVDPKVSESLLRWYQAYGAEI 112
Cdd:PRK06450  125 IFVPETASGGKLKQIESYGAEV 146
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 11-188 4.98e-13

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: 69.07  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVL---ALADDLvpkGKSLYLKLDYFNPNFSIKDR-TALGLVKsALASGKLNhdsiLVESTSGNLGKSLAMLGAVYG 86
Cdd:COG0498    65 GGTPLVkapRLADEL---GKNLYVKEEGHNPTGSFKDRaMQVAVSL-ALERGAKT----IVCASSGNGSAALAAYAARAG 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  87 FRVIIVVdP--KVSESLLRWYQAYGAEISMVtspaaDGGFQRArLNRVQELLQQFPnayWTNqyDNPQNPQYH--SQTTA 162
Cdd:COG0498   137 IEVFVFV-PegKVSPGQLAQMLTYGAHVIAV-----DGNFDDA-QRLVKELAADEG---LYA--VNSINPARLegQKTYA 204

                         170       180       190
                  ....*....|....*....|....*....|
gi 1049755379 163 LEIV----DLPvDSIIGAVSTGGHLCGIGK 188
Cdd:COG0498   205 FEIAeqlgRVP-DWVVVPTGNGGNILAGYK 233
PRK06815 PRK06815
threonine/serine dehydratase;
26-209 7.27e-11

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 62.40  E-value: 7.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  26 GKSLYLKLDYFNPNFSIKDRTALGLVKSalasgkLNHDSI---LVESTSGNLGKSLAMLGAVYGFRVIIVVDPKVSESLL 102
Cdd:PRK06815   34 GCEVYLKCEHLQHTGSFKFRGASNKLRL------LNEAQRqqgVITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 103 RWYQAYGAEISMVTSPAADGGFQRARLNRVQELLQQFPnaywtnqYDNPQnpQYHSQ-TTALEIVD-LP-VDSIIGAVST 179
Cdd:PRK06815  108 DAIRALGAEVRLYGGDALNAELAARRAAEQQGKVYISP-------YNDPQ--VIAGQgTIGMELVEqQPdLDAVFVAVGG 178

                         170       180       190
                  ....*....|....*....|....*....|
gi 1049755379 180 GGHLCGIGKYVKEQRPDVNIVACDVAGSAV 209
Cdd:PRK06815  179 GGLISGIATYLKTLSPKTEIIGCWPANSPS 208
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 13-208 1.47e-09

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: 58.27  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  13 TPVL--ALADDLVpkGKSLYLKLDYFNPNFSIKDRTA----LGLVKSALASGklnhdsiLVESTSGNLGKSLAMLGAVYG 86
Cdd:cd01562    18 TPLLtsPTLSELL--GAEVYLKCENLQKTGSFKIRGAynklLSLSEEERAKG-------VVAASAGNHAQGVAYAAKLLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  87 FRVIIVV-----DPKVSEsllrwYQAYGAEISMVtspaadGGFQRARLNRVQElLQQFPNAYWTNQYDNP-----QNpqy 156
Cdd:cd01562    89 IPATIVMpetapAAKVDA-----TRAYGAEVVLY------GEDFDEAEAKARE-LAEEEGLTFIHPFDDPdviagQG--- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1049755379 157 hsqTTALEIV-DLP-VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSA 208
Cdd:cd01562   154 ---TIGLEILeQVPdLDAVFVPVGGGGLIAGIATAVKALSPNTKVIGVEPEGAP 204
PRK06381 PRK06381
threonine synthase; Validated
 29-186 1.34e-07

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 52.40  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  29 LYLKLDYFNPNFSIKDRTALGLVKSALasgKLNHDSILVeSTSGNLGKSLAMLGAVYGFRVIIVVDPKVSESLLRWYQAY 108
Cdd:PRK06381   33 IYLKFEGANPTGTQKDRIAEAHVRRAM---RLGYSGITV-GTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 109 GAEISMVtspaaDGGFQRArlnrvQELLQQFPNAYwtNQYD-NPQNPQYHSQ-----TTALEIV----DLPvDSIIGAVS 178
Cdd:PRK06381  109 GAEIIYV-----DGKYEEA-----VERSRKFAKEN--GIYDaNPGSVNSVVDieaysAIAYEIYealgDVP-DAVAVPVG 175


                  ....*...
gi 1049755379 179 TGGHLCGI 186
Cdd:PRK06381  176 NGTTLAGI 183
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 12-210 5.93e-07

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: 5.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  12 NTPVLALADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGkLNHDSILVESTSGNLGKSLAMLGAVYGFRVII 91
Cdd:cd06448     1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQG-LNECVHVVCSSGGNAGLAAAYAARKLGVPCTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  92 VV----DPKVSESLlrwyQAYGAEISMVTSPAADGGFQRArlnrvQELLQQFPNAYWTNQYDNPQNPQYHSqTTALEIVD 167
Cdd:cd06448    80 VVpestKPRVVEKL----RDEGATVVVHGKVWWEADNYLR-----EELAENDPGPVYVHPFDDPLIWEGHS-SMVDEIAQ 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1049755379 168 -----LPVDSIIGAVSTGGHLCGIGKYVKE-QRPDVNIVACDVAGSAVF 210
Cdd:cd06448   150 qlqsqEKVDAIVCSVGGGGLLNGIVQGLERnGWGDIPVVAVETEGAHSL 198
PRK08329 PRK08329
threonine synthase; Validated
 23-115 1.21e-05

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 46.36  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  23 VPKGKSLYLKLDYFNPNFSIKDRTALGLVksalasGKLNHDSI--LVESTSGNLGKSLAMLGAVYGFRVIIVVDPKVSES 100
Cdd:PRK08329   68 VKRSIKVYFKLDYLQPTGSFKDRGTYVTV------AKLKEEGIneVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKE 141

                          90
                  ....*....|....*
gi 1049755379 101 LLRWYQAYGAEISMV 115
Cdd:PRK08329  142 KISLLSRLGAELHFV 156
PRK12483 PRK12483
threonine dehydratase; Reviewed
 26-200 1.90e-05

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 46.33  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  26 GKSLYLKLDYFNPNFSIKDRTALG----LVKSALASGklnhdsiLVESTSGNLGKSLAMLGAVYGFRVIIVVDPKVSESL 101
Cdd:PRK12483   51 GNQVLLKREDLQPVFSFKIRGAYNkmarLPAEQLARG-------VITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 102 LRWYQAYGAEISMvtspaADGGFQRARLNRVQelLQQFPNAYWTNQYDNP-----QNpqyhsqTTALEIVDL---PVDSI 173
Cdd:PRK12483  124 VDGVRAHGGEVVL-----HGESFPDALAHALK--LAEEEGLTFVPPFDDPdviagQG------TVAMEILRQhpgPLDAI 190

                         170       180
                  ....*....|....*....|....*..
gi 1049755379 174 IGAVSTGGHLCGIGKYVKEQRPDVNIV 200
Cdd:PRK12483  191 FVPVGGGGLIAGIAAYVKYVRPEIKVI 217
PRK05638 PRK05638
threonine synthase; Validated
 11-130 9.03e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 44.03  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  11 GNTPVLAlADDLVPKGKSLYLKLDYFNPNFSIKDRTALGLVKSALASGKlnhdSILVESTSGNLGKSLAMLGAVYGFRVI 90
Cdd:PRK05638   65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYGLPYAA----NGFIVASDGNAAASVAAYSARAGKEAF 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1049755379  91 IVVDPKVSESLLRWYQAYGAEIsMVTSPAADGGFQ----RARLN 130
Cdd:PRK05638  140 VVVPRKVDKGKLIQMIAFGAKI-IRYGESVDEAIEyaeeLARLN 182
PLN02970 PLN02970
serine racemase
 3-253 1.62e-04

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 42.74  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379   3 YNNITECIGNTPVL--ALADDLVpkGKSLYLKLDYFNPNFSIKDRTALGLVKSA----LASGKLNHdsilvesTSGNLGK 76
Cdd:PLN02970   18 RKRIAPFIHRTPVLtsSSLDALA--GRSLFFKCECFQKGGAFKFRGACNAIFSLsddqAEKGVVTH-------SSGNHAA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  77 SLAMLGAVYGFRVIIVVdPKVSESL-LRWYQAYGAEI--SMVTSPAADGGFQRarlnrvqelLQQFPNAYWTNQYDNPqn 153
Cdd:PLN02970   89 ALALAAKLRGIPAYIVV-PKNAPACkVDAVIRYGGIItwCEPTVESREAVAAR---------VQQETGAVLIHPYNDG-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379 154 PQYHSQ-TTALEIV-DLP-VDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSA-VFREKFSPYLI-----NGV-- 222
Cdd:PLN02970  157 RVISGQgTIALEFLeQVPeLDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADdAAQSKAAGEIItlpvtNTIad 236

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1049755379 223 GLSWR-SDNTDISV---LDQVCIASDQEAISMCRL 253
Cdd:PLN02970  237 GLRASlGDLTWPVVrdlVDDVITVDDKEIIEAMKL 271
PLN02550 PLN02550
threonine dehydratase
 16-200 1.79e-03

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 39.90  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  16 LALADDLVPK-GKSLYLKLDYFNPNFSIKDRTALG----LVKSALASGklnhdsiLVESTSGNLGKSLAMLGAVYGFRVI 90
Cdd:PLN02550  112 LQLAKKLSERlGVKVLLKREDLQPVFSFKLRGAYNmmakLPKEQLDKG-------VICSSAGNHAQGVALSAQRLGCDAV 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049755379  91 IVVDPKVSESLLRWYQAYGAEISMVtSPAADGGFQRARLNRVQELLQQFPnaywtnQYDNPQNPQYHSqTTALEIVDL-- 168
Cdd:PLN02550  185 IAMPVTTPEIKWQSVERLGATVVLV-GDSYDEAQAYAKQRALEEGRTFIP------PFDHPDVIAGQG-TVGMEIVRQhq 256

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1049755379 169 -PVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIV 200
Cdd:PLN02550  257 gPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKII 289
PRK08639 PRK08639
threonine dehydratase; Validated
 160-208 5.42e-03

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 38.25  E-value: 5.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1049755379 160 TTALEIVD-----LPVDSIIGAVSTGGHLCGIGKYVKEQRPDVNIVACDVAGSA 208
Cdd:PRK08639  165 TVAVEILEqlekeGSPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAA 218
 
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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