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Conserved domains on  [gi|2250742642|ref|WP_250871876|]
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threonine synthase [Halomarina rubra]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 9-391 5.18e-128

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: 373.77  E-value: 5.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642   9 GLRCVDCGETFDAETPHRCPDCGGILDPTYDydrvDLTRADLEARRfdTMWRYEELLPF-AREHAVTMDEGATALVEAPA 87
Cdd:COG0498     1 KLRCTRCGATFSDALLYLCPDCGGLLPDSYP----ALSREDLASRR--GLWRYRELLPFdDEEKAVSLGEGGTPLVKAPR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  88 LAERMGvERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPE-RAGFTQK 166
Cdd:COG0498    75 LADELG-KNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 167 SMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYSTKTFvTPYRHEGKKTMLYETVEQLDwQVPDAVVYPTGGGVGLVGM 246
Cdd:COG0498   154 AQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLG-RVPDWVVVPTGNGGNILAG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 247 HKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEiDTVFGGIAIPDPGASPLILDALEESGGGAVAAS 326
Cdd:COG0498   232 YKAFKELKELGLIDRLPRLIAVQATGCNPILTAFETGRDEYEPERP-ETIAPSMDIGNPSNGERALFALRESGGTAVAVS 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250742642 327 DDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNKDDDVLRGHLG 391
Cdd:COG0498   311 DEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALG 375
 
Name Accession Description Interval E-value
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 9-391 5.18e-128

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: 373.77  E-value: 5.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642   9 GLRCVDCGETFDAETPHRCPDCGGILDPTYDydrvDLTRADLEARRfdTMWRYEELLPF-AREHAVTMDEGATALVEAPA 87
Cdd:COG0498     1 KLRCTRCGATFSDALLYLCPDCGGLLPDSYP----ALSREDLASRR--GLWRYRELLPFdDEEKAVSLGEGGTPLVKAPR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  88 LAERMGvERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPE-RAGFTQK 166
Cdd:COG0498    75 LADELG-KNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 167 SMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYSTKTFvTPYRHEGKKTMLYETVEQLDwQVPDAVVYPTGGGVGLVGM 246
Cdd:COG0498   154 AQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLG-RVPDWVVVPTGNGGNILAG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 247 HKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEiDTVFGGIAIPDPGASPLILDALEESGGGAVAAS 326
Cdd:COG0498   232 YKAFKELKELGLIDRLPRLIAVQATGCNPILTAFETGRDEYEPERP-ETIAPSMDIGNPSNGERALFALRESGGTAVAVS 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250742642 327 DDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNKDDDVLRGHLG 391
Cdd:COG0498   311 DEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALG 375
PRK08197 PRK08197
threonine synthase; Validated
 10-381 4.41e-121

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 356.23  E-value: 4.41e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  10 LRCVDCGETFDAETPHRCPDCGGILDPTYDYDRVD--LTRADLeARRFDTMWRYEELLPFAR-EHAVTMDEGATALVEAP 86
Cdd:PRK08197    8 LECSKCGETYDADQVHNLCKCGKPLLVRYDLEAVKqaVTREAL-AGRPANLWRYHELLPVRDpEHIVSLGEGMTPLLPLP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  87 ALAERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTQK 166
Cdd:PRK08197   87 RLGKALGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 167 SMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYSTKTFVTPYRHEGKKTMLYETVEQLDWQVPDAVVYPTGGGVGLVGM 246
Cdd:PRK08197  167 LECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGWRLPDVILYPTGGGVGLIGI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 247 HKAAREFRDLGLVD-DLPPMYAAQASGCAPIVDAWESGADRHEAWGEIDTVFGGIAIPDPGASPLILDALEESGGGAVAA 325
Cdd:PRK08197  247 WKAFDELEALGWIGgKRPRLVAVQAEGCAPIVKAWEEGKEESEFWEDAHTVAFGIRVPKALGDFLVLDAVRETGGCAIAV 326

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2250742642 326 SDDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNK 381
Cdd:PRK08197  327 SDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWLKGDERVVLFNTGSGLK 382
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 58-382 1.39e-119

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: 349.58  E-value: 1.39e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  58 MWRYEELLPFAREHAVTMDEGATALVEAPALAERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGN 137
Cdd:cd01563     1 LWRYRELLPVTEDDIVSLGEGNTPLVRAPRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 138 AGQSAAAYAAEAGLDAHVFLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHdWYSTKTFVTPYRHEGKKTM 217
Cdd:cd01563    81 TSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN-WIYLSNSLNPYRLEGQKTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 218 LYETVEQLDWQVPDAVVYPTGGGVGLVGMHKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEIDTVF 297
Cdd:cd01563   160 AFEIAEQLGWEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAFKEGKDDIEPVENPETIA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 298 GGIAIPDPGASPLILDALEESGGGAVAASDDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTG 377
Cdd:cd01563   240 TAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVLTG 319


                  ....*
gi 2250742642 378 AGNKD 382
Cdd:cd01563   320 HGLKD 324
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 58-384 2.39e-53

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 179.89  E-value: 2.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  58 MWRYEELLPFAREHAVTMDEGATALVEAPALAERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGN 137
Cdd:TIGR00260   1 VWRYREFLPVTEKDLVDLGEGVTPLFRAPALAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 138 AGQSAAAYAAEAGLDAHVFLPE-RAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAmADHD--WYSTKTFVTPYRHEGK 214
Cdd:TIGR00260  81 TGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQL-FEDKpaLGLNSANSIPYRLEGQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 215 KTMLYETVEQLDWQVPDAVVYPTGGGVGLVGMHKAAREFRDLGLvDDLPPMYAAQASGCAPIVDAWESGADrheaWGEI- 293
Cdd:TIGR00260 160 KTYAFEAVEQLGWEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGL-DSLPVKRGIQAEGAADIVRAFLEGGQ----WEPIe 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 294 --DTVFGGIAIPDPGASPLILDALEESGGGAVAASDDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTV 371
Cdd:TIGR00260 235 tpETLSTAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADPAERV 314

                         330
                  ....*....|...
gi 2250742642 372 VLLNTGAGNKDDD 384
Cdd:TIGR00260 315 VCALTGNGLKDPE 327
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 73-377 5.11e-49

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: 167.49  E-value: 5.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  73 VTMDEGATALVEAPALAERMGVeRVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATD-VALNSAGNAGQSAAAYAAEAGL 151
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKtVVEASSGNHGRALAAAAARLGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 152 DAHVFLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMAD-HDWYSTKTFVTPYRHEGKKTMLYETVEQLDwQVP 230
Cdd:pfam00291  80 KVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLG-GDP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 231 DAVVYPTGGGVGLVGMHKAAREFRdlglvdDLPPMYAAQASGCAPIVDAWESGadRHEAWGEIDTVFGGIAIPDPgASPL 310
Cdd:pfam00291 159 DAVVVPVGGGGLIAGIARGLKELG------PDVRVIGVEPEGAPALARSLAAG--RPVPVPVADTIADGLGVGDE-PGAL 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250742642 311 ILDALEESGGGAVAASDDAILDAAVAVARETGIEMGaTCAAAAAGAFELAERGEFDADDTVVLLNTG 377
Cdd:pfam00291 230 ALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVE-PSSAAALAALKLALAGELKGGDRVVVVLTG 295
CxxC_CXXC_SSSS smart00834
Putative regulatory protein; CxxC_CXXC_SSSS represents a region of about 41 amino acids found ...
 11-32 5.21e-03

Putative regulatory protein; CxxC_CXXC_SSSS represents a region of about 41 amino acids found in a number of small proteins in a wide range of bacteria. The region usually begins with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One protein in this entry has been noted as a putative regulatory protein, designated FmdB. Most proteins in this entry have a C-terminal region containing highly degenerate sequence.


Pssm-ID: 197903  Cd Length: 41  Bit Score: 34.45  E-value: 5.21e-03
                           10        20
                   ....*....|....*....|....*...
gi 2250742642   11 RCVDCGETFDA------ETPHRCPDCGG 32
Cdd:smart00834   7 RCEDCGHTFEVlqkisdDPLTTCPECGG 34
 
Name Accession Description Interval E-value
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 9-391 5.18e-128

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: 373.77  E-value: 5.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642   9 GLRCVDCGETFDAETPHRCPDCGGILDPTYDydrvDLTRADLEARRfdTMWRYEELLPF-AREHAVTMDEGATALVEAPA 87
Cdd:COG0498     1 KLRCTRCGATFSDALLYLCPDCGGLLPDSYP----ALSREDLASRR--GLWRYRELLPFdDEEKAVSLGEGGTPLVKAPR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  88 LAERMGvERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPE-RAGFTQK 166
Cdd:COG0498    75 LADELG-KNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPEgKVSPGQL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 167 SMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYSTKTFvTPYRHEGKKTMLYETVEQLDwQVPDAVVYPTGGGVGLVGM 246
Cdd:COG0498   154 AQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSI-NPARLEGQKTYAFEIAEQLG-RVPDWVVVPTGNGGNILAG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 247 HKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEiDTVFGGIAIPDPGASPLILDALEESGGGAVAAS 326
Cdd:COG0498   232 YKAFKELKELGLIDRLPRLIAVQATGCNPILTAFETGRDEYEPERP-ETIAPSMDIGNPSNGERALFALRESGGTAVAVS 310

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250742642 327 DDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNKDDDVLRGHLG 391
Cdd:COG0498   311 DEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALG 375
PRK08197 PRK08197
threonine synthase; Validated
 10-381 4.41e-121

threonine synthase; Validated


Pssm-ID: 181283 [Multi-domain]  Cd Length: 394  Bit Score: 356.23  E-value: 4.41e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  10 LRCVDCGETFDAETPHRCPDCGGILDPTYDYDRVD--LTRADLeARRFDTMWRYEELLPFAR-EHAVTMDEGATALVEAP 86
Cdd:PRK08197    8 LECSKCGETYDADQVHNLCKCGKPLLVRYDLEAVKqaVTREAL-AGRPANLWRYHELLPVRDpEHIVSLGEGMTPLLPLP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  87 ALAERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTQK 166
Cdd:PRK08197   87 RLGKALGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMPADAPEITR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 167 SMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYSTKTFVTPYRHEGKKTMLYETVEQLDWQVPDAVVYPTGGGVGLVGM 246
Cdd:PRK08197  167 LECALAGAELYLVDGLISDAGKIVAEAVAEYGWFDVSTLKEPYRIEGKKTMGLELAEQLGWRLPDVILYPTGGGVGLIGI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 247 HKAAREFRDLGLVD-DLPPMYAAQASGCAPIVDAWESGADRHEAWGEIDTVFGGIAIPDPGASPLILDALEESGGGAVAA 325
Cdd:PRK08197  247 WKAFDELEALGWIGgKRPRLVAVQAEGCAPIVKAWEEGKEESEFWEDAHTVAFGIRVPKALGDFLVLDAVRETGGCAIAV 326

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2250742642 326 SDDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNK 381
Cdd:PRK08197  327 SDDAILAAQRELAREEGLFACPEGAATFAAARQLRESGWLKGDERVVLFNTGSGLK 382
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 58-382 1.39e-119

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: 349.58  E-value: 1.39e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  58 MWRYEELLPFAREHAVTMDEGATALVEAPALAERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGN 137
Cdd:cd01563     1 LWRYRELLPVTEDDIVSLGEGNTPLVRAPRLGERLGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGVKAVACASTGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 138 AGQSAAAYAAEAGLDAHVFLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHdWYSTKTFVTPYRHEGKKTM 217
Cdd:cd01563    81 TSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEEN-WIYLSNSLNPYRLEGQKTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 218 LYETVEQLDWQVPDAVVYPTGGGVGLVGMHKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEIDTVF 297
Cdd:cd01563   160 AFEIAEQLGWEVPDYVVVPVGNGGNITAIWKGFKELKELGLIDRLPRMVGVQAEGAAPIVRAFKEGKDDIEPVENPETIA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 298 GGIAIPDPGASPLILDALEESGGGAVAASDDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTG 377
Cdd:cd01563   240 TAIRIGNPASGPKALRAVRESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEGIIDKGERVVVVLTG 319


                  ....*
gi 2250742642 378 AGNKD 382
Cdd:cd01563   320 HGLKD 324
PLN02569 PLN02569
threonine synthase
 12-381 8.23e-62

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 206.59  E-value: 8.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  12 CVDCGETFDAETPHRCPDCGGILDPTYDYDRV-----DLTRADLEARRFDTMWRY--------EELLP-FAREHAVTMDE 77
Cdd:PLN02569   52 CPLTGEKYSLDEVVYRSKSGGLLDVRHDMEALkrydgKYWRALFDSRVGKTTWPYgsgvwskkEWVLPeIDDDDIVSLFE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  78 GATALVEAPALA-ERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAA----RMHG-ATDVALNSAGNAGQSAAAYAAEAGL 151
Cdd:PLN02569  132 GNSNLFWAERLGkEFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVnrlrKMAKpVVGVGCASTGDTSAALSAYCAAAGI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 152 DAHVFLPE-RAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYSTKTfVTPYRHEGKKTMLYETVEQLDWQVP 230
Cdd:PLN02569  212 PSIVFLPAdKISIAQLVQPIANGALVLSIDTDFDGCMRLIREVTAELPIYLANS-LNSLRLEGQKTAAIEILQQFDWEVP 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 231 DAVVYPTGGGVGLVGMHKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEIDTVFGGIAIPDPGASPL 310
Cdd:PLN02569  291 DWVIVPGGNLGNIYAFYKGFKMCKELGLVDRLPRLVCAQAANANPLYRAYKSGWEEFKPVKANPTFASAIQIGDPVSIDR 370

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2250742642 311 ILDALEESGGGAVAASDDAILDAAvAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNK 381
Cdd:PLN02569  371 AVYALKESNGIVEEATEEELMDAQ-AEADKTGMFLCPHTGVALAALKKLRASGVIGPTDRTVVVSTAHGLK 440
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 58-384 2.39e-53

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


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 179.89  E-value: 2.39e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  58 MWRYEELLPFAREHAVTMDEGATALVEAPALAERMGVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGN 137
Cdd:TIGR00260   1 VWRYREFLPVTEKDLVDLGEGVTPLFRAPALAANVGIKNLYVKELGHNPTLSFKDRGMAVALTKALELGNDTVLCASTGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 138 AGQSAAAYAAEAGLDAHVFLPE-RAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAmADHD--WYSTKTFVTPYRHEGK 214
Cdd:TIGR00260  81 TGAAAAAYAGKAGLKVVVLYPAgKISLGKLAQALGYNAEVVAIDGNFDDAQRLVKQL-FEDKpaLGLNSANSIPYRLEGQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 215 KTMLYETVEQLDWQVPDAVVYPTGGGVGLVGMHKAAREFRDLGLvDDLPPMYAAQASGCAPIVDAWESGADrheaWGEI- 293
Cdd:TIGR00260 160 KTYAFEAVEQLGWEAPDKVVVPVPNSGNFGAIWKGFKEKKMLGL-DSLPVKRGIQAEGAADIVRAFLEGGQ----WEPIe 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 294 --DTVFGGIAIPDPGASPLILDALEESGGGAVAASDDAILDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTV 371
Cdd:TIGR00260 235 tpETLSTAMDIGNPANWPRALEAFRRSNGYAEDLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKGTADPAERV 314

                         330
                  ....*....|...
gi 2250742642 372 VLLNTGAGNKDDD 384
Cdd:TIGR00260 315 VCALTGNGLKDPE 327
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 73-377 5.11e-49

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: 167.49  E-value: 5.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  73 VTMDEGATALVEAPALAERMGVeRVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATD-VALNSAGNAGQSAAAYAAEAGL 151
Cdd:pfam00291   1 ISLGIGPTPLVRLPRLSKELGV-DVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKtVVEASSGNHGRALAAAAARLGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 152 DAHVFLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMAD-HDWYSTKTFVTPYRHEGKKTMLYETVEQLDwQVP 230
Cdd:pfam00291  80 KVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAEgPGAYYINQYDNPLNIEGYGTIGLEILEQLG-GDP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 231 DAVVYPTGGGVGLVGMHKAAREFRdlglvdDLPPMYAAQASGCAPIVDAWESGadRHEAWGEIDTVFGGIAIPDPgASPL 310
Cdd:pfam00291 159 DAVVVPVGGGGLIAGIARGLKELG------PDVRVIGVEPEGAPALARSLAAG--RPVPVPVADTIADGLGVGDE-PGAL 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250742642 311 ILDALEESGGGAVAASDDAILDAAVAVARETGIEMGaTCAAAAAGAFELAERGEFDADDTVVLLNTG 377
Cdd:pfam00291 230 ALDLLDEYVGEVVTVSDEEALEAMRLLARREGIVVE-PSSAAALAALKLALAGELKGGDRVVVVLTG 295
PRK05638 PRK05638
threonine synthase; Validated
 10-381 3.16e-47

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 166.91  E-value: 3.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  10 LRCVDCGETFDAETPHRCpDCGGILDPTYDYDRVDLTRADleaRRFDTMWRYEELLPFAReHAVTMDEGATALVEApALA 89
Cdd:PRK05638    2 MKCPKCGREYNSYIPPFC-ICGELLEIIYDYSSVDVRKWK---NRDPGVWRYKELLPQVK-KIISLGEGGTPLIRA-RIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  90 ERMGVErVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTQKSMT 169
Cdd:PRK05638   76 EKLGEN-VYIKDETRNPTGSFRDRLATVAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 170 LVHGADLtVVPGEIGDAGAAYTDAMADHD-WYStktfVTPYRH----EGKKTMLYETVEQLDwqvPDAVVYPTGGGVGLV 244
Cdd:PRK05638  155 IAFGAKI-IRYGESVDEAIEYAEELARLNgLYN----VTPEYNiiglEGQKTIAFELWEEIN---PTHVIVPTGSGSYLY 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 245 GMHKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEawgeiDTVFGGIAIPDPGASPLILDALEESGGGAVA 324
Cdd:PRK05638  227 SIYKGFKELLEIGVIEEIPKLIAVQTERCNPIASEILGNKTKCN-----ETKALGLYVKNPVMKEYVSEAIKESGGTAVV 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2250742642 325 ASDDAIlDAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNK 381
Cdd:PRK05638  302 VNEEEI-MAGEKLLAKEGIFAELSSAVVMPALLKLGEEGYIEKGDKVVLVVTGSGLK 357
PRK08329 PRK08329
threonine synthase; Validated
 10-381 3.66e-42

threonine synthase; Validated


Pssm-ID: 236244 [Multi-domain]  Cd Length: 347  Bit Score: 151.13  E-value: 3.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  10 LRCVDCGETFDAETPHRCpDCGGILDPTYDYDrvdltrADLEARRFDTMWRYEELLPFAREHAVTMDEGATALVEAPala 89
Cdd:PRK08329    2 LRCTKCGRTYEEKFKLRC-DCGGTLLVEREYG------SFDSPREYLDMRRYIDYLPVDEEFLPHLTPPITPTVKRS--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  90 ermgvERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTQKSMT 169
Cdd:PRK08329   72 -----IKVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGINEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 170 LVHGADLTVVPGeigdagaaytDAMADHD---WYSTKTFVT-------PYRHEGKKTMLYETVEQLdwQVPDAVVYPTGG 239
Cdd:PRK08329  147 SRLGAELHFVEG----------DRMEVHEeavKFSKRNNIPyvshwlnPYFLEGTKTIAYEIYEQI--GVPDYAFVPVGS 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 240 GVGLVGMHKAAREFRDLGLVDDLPPMYAAQASGcapivdaWESGADRHEawgEIDTVFGGIAIPDPGASPLILDALEESG 319
Cdd:PRK08329  215 GTLFLGIWKGFKELHEMGEISKMPKLVAVQAEG-------YESLCKRSK---SENKLADGIAIPEPPRKEEMLRALEESN 284

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2250742642 320 GGAVAASDDAILdAAVAVARETGIEMGATCAAAAAGAFELAERGEFDADDTVVLLNTGAGNK 381
Cdd:PRK08329  285 GFCISVGEEETR-AALHWLRRMGFLVEPTSAVALAAYWKLLEEGLIEGGSKVLLPLSGSGLK 345
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 80-346 1.06e-29

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: 114.92  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVeRVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATD---VALNSAGNAGQSAAAYAAEAGLDAHVF 156
Cdd:cd00640     1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPkgvIIESTGGNTGIALAAAAARLGLKCTIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 157 LPERAGFTQKSMTLVHGADLTVVPGEIGDAGA-AYTDAMADHDWYSTKTFVTPYRHEGKKTMLYETVEQLDWQVPDAVVY 235
Cdd:cd00640    80 MPEGASPEKVAQMRALGAEVVLVPGDFDDAIAlAKELAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLGGQKPDAVVV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 236 PTGGGVGLVGMHKAAREFRdlglvdDLPPMYAAQAsgcapivdawesgadrheawgeidtvfggiaipdpgasplildal 315
Cdd:cd00640   160 PVGGGGNIAGIARALKELL------PNVKVIGVEP--------------------------------------------- 188

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2250742642 316 eesggGAVAASDDAILDAAVAVARETGIEMG 346
Cdd:cd00640   189 -----EVVTVSDEEALEAIRLLAREEGILVE 214
PRK06381 PRK06381
threonine synthase; Validated
 78-377 1.96e-28

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 113.26  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  78 GATALVEAPALAERMGVERVFVKDEGRNPTGTFKDRgqtvamtAARMH-------GATDVALNSAGNAGQSAAAYAAEAG 150
Cdd:PRK06381   14 GGTPLLRARKLEEELGLRKIYLKFEGANPTGTQKDR-------IAEAHvrramrlGYSGITVGTCGNYGASIAYFARLYG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 151 LDAHVFLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWY-----STKTFVTpyrHEGKKTMLYETVEQL 225
Cdd:PRK06381   87 LKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFAKENGIYdanpgSVNSVVD---IEAYSAIAYEIYEAL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 226 DwQVPDAVVYPTGGGVGLVGMHKAAREFRDLGLVDDLPPMYAAQASGCAPIVDAWESGADRHEAWGEIDTVFGGIaipdp 305
Cdd:PRK06381  164 G-DVPDAVAVPVGNGTTLAGIYHGFRRLYDRGKTSRMPRMIGVSTSGGNQIVESFKRGSSEVVDLEVDEIRETAV----- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 306 gASPLI----------LDALEESGGGAVAASDDAILDAAVAVARETGIEMGATCAAAAAGAFELAErgEFDADDTVVLLN 375
Cdd:PRK06381  238 -NEPLVsyrsfdgdnaLEAIYDSHGYAFGFSDDEMVKYAELLRRMEGLNALPASASALAALVKYLK--KNGVNDNVVAVI 314


                  ..
gi 2250742642 376 TG 377
Cdd:PRK06381  315 TG 316
PRK06450 PRK06450
threonine synthase; Validated
 11-276 5.06e-26

threonine synthase; Validated


Pssm-ID: 180565 [Multi-domain]  Cd Length: 338  Bit Score: 107.13  E-value: 5.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  11 RCVDCGETFDAETPHRCPDCGGILD--PTYDYDRvdltraDLEARRFdtmwryeellPFAREHaVTMDEGATALVEapal 88
Cdd:PRK06450    5 VCMKCGKERESIYEIRCKKCGGPFEilIDFEFDK------NLERKNF----------PYIKHF-ISLGEGRTPLIK---- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  89 aermgVERVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTQKSM 168
Cdd:PRK06450   64 -----KGNIWFKLDFLNPTGSYKDRGSVTLISYLAEKGIKQISEDSSGNAGASIAAYGAAAGIEVKIFVPETASGGKLKQ 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 169 TLVHGADLTVVPGEIGDAGAAytdAMADHDWYSTKTFVTPYRhEGKKTMLYETVEQLDWQVPDAVVYPTGGGVGLVGMHK 248
Cdd:PRK06450  139 IESYGAEVVRVRGSREDVAKA---AENSGYYYASHVLQPQFR-DGIRTLAYEIAKDLDWKIPNYVFIPVSAGTLLLGVYS 214

                         250       260
                  ....*....|....*....|....*...
gi 2250742642 249 AAREFRDLGLVDDLPPMYAAQASGCAPI 276
Cdd:PRK06450  215 GFKHLLDSGVISEMPKIVAVQTEQVSPL 242
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 80-343 1.45e-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: 77.00  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAMT----AARMHGatdVALNSAGNAGQSAAAYAAEAGLDAHV 155
Cdd:COG1171    25 TPLLRSPTLSERLGAE-VYLKLENLQPTGSFKLRGAYNALAslseEERARG---VVAASAGNHAQGVAYAARLLGIPATI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 156 FLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWystkTFVTPYRH----EGKKTMLYETVEQLDwqVPD 231
Cdd:COG1171   101 VMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELAEEEGA----TFVHPFDDpdviAGQGTIALEILEQLP--DLD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 232 AVVYPTGGGvGLV-GMHKAAREFRdlglvddlPPM--YAAQASGCAPIVDAWESGAdRHEAwGEIDTVFGGIAIPDPGas 308
Cdd:COG1171   175 AVFVPVGGG-GLIaGVAAALKALS--------PDIrvIGVEPEGAAAMYRSLAAGE-PVTL-PGVDTIADGLAVGRPG-- 241

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2250742642 309 PLILDALEESGGGAVAASDDAILDAAVAVARETGI 343
Cdd:COG1171   242 ELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKI 276
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 80-343 1.26e-12

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: 67.90  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAMT----AARMHGatdVALNSAGNAGQSAAAYAAEAGLDAHV 155
Cdd:cd01562    18 TPLLTSPTLSELLGAE-VYLKCENLQKTGSFKIRGAYNKLLslseEERAKG---VVAASAGNHAQGVAYAAKLLGIPATI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 156 FLPERAGFTQKSMTLVHGADLTVVpGEIGDAGAAYTDAMAD-HDWystkTFVTPYRHE----GKKTMLYETVEQLDwqVP 230
Cdd:cd01562    94 VMPETAPAAKVDATRAYGAEVVLY-GEDFDEAEAKARELAEeEGL----TFIHPFDDPdviaGQGTIGLEILEQVP--DL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 231 DAVVYPTGGGVGLVGMHKAAREFRDLGLVddlppmYAAQASGCAPIVDAWESGAdRHEAwGEIDTVFGGIAIPDPGASPL 310
Cdd:cd01562   167 DAVFVPVGGGGLIAGIATAVKALSPNTKV------IGVEPEGAPAMAQSLAAGK-PVTL-PEVDTIADGLAVKRPGELTF 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2250742642 311 ILdaLEESGGGAVAASDDAILDAAVAVARETGI 343
Cdd:cd01562   239 EI--IRKLVDDVVTVSEDEIAAAMLLLFEREKL 269
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 80-244 3.90e-11

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: 63.47  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVeRVFVKDEGRNPTGTFKDRG-QTVAMTAARMHGATDVAL--NSAGNAGQSAAAYAAEAGLDAHVF 156
Cdd:cd06448     2 TPLIESTALSKTAGC-NVFLKLENLQPSGSFKIRGiGHLCQKSAKQGLNECVHVvcSSGGNAGLAAAYAARKLGVPCTIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 157 LPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWYStkTFVTPYRH----EGKKTMLYETVEQLDWQV-PD 231
Cdd:cd06448    81 VPESTKPRVVEKLRDEGATVVVHGKVWWEADNYLREELAENDPGP--VYVHPFDDpliwEGHSSMVDEIAQQLQSQEkVD 158

                         170
                  ....*....|...
gi 2250742642 232 AVVYPTGGGvGLV 244
Cdd:cd06448   159 AIVCSVGGG-GLL 170
PRK06815 PRK06815
threonine/serine dehydratase;
80-245 1.28e-10

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 62.02  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAM----TAARMHGatdVALNSAGNAGQSAAAYAAEAGLDAHV 155
Cdd:PRK06815   21 TPLEHSPLLSQHTGCE-VYLKCEHLQHTGSFKFRGASNKLrllnEAQRQQG---VITASSGNHGQGVALAAKLAGIPVTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 156 FLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDwystKTFVTPYRHE----GKKTMLYETVEQLDwqVPD 231
Cdd:PRK06815   97 YAPEQASAIKLDAIRALGAEVRLYGGDALNAELAARRAAEQQG----KVYISPYNDPqviaGQGTIGMELVEQQP--DLD 170

                         170
                  ....*....|....
gi 2250742642 232 AVVYPTGGGvGLVG 245
Cdd:PRK06815  171 AVFVAVGGG-GLIS 183
PRK06608 PRK06608
serine/threonine dehydratase;
80-271 6.19e-10

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 60.17  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAMTAARMHG--ATDVALNSAGNAGQSAAAYAAEAGLDAHVFL 157
Cdd:PRK06608   24 TPIVHSESLNEMLGHE-IFFKVESLQKTGAFKVRGVLNHLLELKEQGklPDKIVAYSTGNHGQAVAYASKLFGIKTRIYL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 158 PERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWystktfVTPYRHE----GKKTMLYETVEQLDWQvPDAV 233
Cdd:PRK06608  103 PLNTSKVKQQAALYYGGEVILTNTRQEAEEKAKEDEEQGFYY------IHPSDSDstiaGAGTLCYEALQQLGFS-PDAI 175

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2250742642 234 VYPTGGGVGLVGMHKAAREFRDLGLVDDLPPMYAAQAS 271
Cdd:PRK06608  176 FASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAY 213
eutB PRK07476
threonine dehydratase; Provisional
 80-245 5.33e-07

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 51.12  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAM----TAARMHGatdVALNSAGNAGQSAAAYAAEAGLDAHV 155
Cdd:PRK07476   20 TPLVASASLSARAGVP-VWLKLETLQPTGSFKLRGATNALlslsAQERARG---VVTASTGNHGRALAYAARALGIRATI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 156 FLPERAGFTQKSMTLVHGADLTVVPGEIGDAGAAYTDAMADHDWystkTFVTPYRHE----GKKTMLYETVEQLdwqvPD 231
Cdd:PRK07476   96 CMSRLVPANKVDAIRALGAEVRIVGRSQDDAQAEVERLVREEGL----TMVPPFDDPriiaGQGTIGLEILEAL----PD 167

                         170
                  ....*....|....*.
gi 2250742642 232 A--VVYPTGGGvGLVG 245
Cdd:PRK07476  168 VatVLVPLSGG-GLAS 182
PRK08246 PRK08246
serine/threonine dehydratase;
107-343 7.91e-06

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 47.26  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 107 TGTFKDRGQTVAMTAARMHGATDVALnSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTQKSMTLVHGADLTVVPGEIGDA 186
Cdd:PRK08246   49 TGSFKARGAFNRLLAAPVPAAGVVAA-SGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 187 GAAYTDAMADHDWYSTKTFVTPYRHEGKKTMLYETVEQLdwQVPDAVVYPTGGGvGLVGMHKAAREFRDLglvddlppMY 266
Cdd:PRK08246  128 LEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQA--PGVDTVLVAVGGG-GLIAGIAAWFEGRAR--------VV 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 267 AAQASGCAPIVDAWESGADrheawgeIDTVFGGIAIPDPGAS---PLILDALEESGGGAVAASDDAILDAAVAVARETGI 343
Cdd:PRK08246  197 AVEPEGAPTLHAALAAGEP-------VDVPVSGIAADSLGARrvgEIAFALARAHVVTSVLVSDEAIIAARRALWEELRL 269
PRK06110 PRK06110
threonine dehydratase;
86-333 8.87e-06

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 47.30  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  86 PALAERMGVErVFVKDEGRNPTGTFKDRGQTVAMTAARMHGATDVALNSA--GNAGQSAAAYAAEAGLDAHVFLPERAGF 163
Cdd:PRK06110   28 PLLAERLGCE-VWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRGVISAtrGNHGQSVAFAARRHGLAATIVVPHGNSV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 164 TQKSMTLVHGADLtVVPGEIGDAGAAYTDAMADHDWYstktFVTPYRHE----GKKTM---LYETVEQLDwqvpdaVVY- 235
Cdd:PRK06110  107 EKNAAMRALGAEL-IEHGEDFQAAREEAARLAAERGL----HMVPSFHPdlvrGVATYaleLFRAVPDLD------VVYv 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 236 PTGGGVGLVGMhKAAREFrdLGLVDDLPPMYAAQASGCApivDAWESGADRHEAWGeiDTVFGGIA--IPDPGASPLILD 313
Cdd:PRK06110  176 PIGMGSGICGA-IAARDA--LGLKTRIVGVVSAHAPAYA---LSFEAGRVVTTPVA--TTLADGMAcrTPDPEALEVIRA 247

                         250       260
                  ....*....|....*....|
gi 2250742642 314 ALEEsgggAVAASDDAILDA 333
Cdd:PRK06110  248 GADR----IVRVTDDEVAAA 263
PRK07334 PRK07334
threonine dehydratase; Provisional
 80-310 9.89e-06

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 47.20  E-value: 9.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  80 TALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAMT----AARMHGatdVALNSAGNAGQSAAAYAAEAGLDAHV 155
Cdd:PRK07334   24 TPCVHSRTLSQITGAE-VWLKFENLQFTASFKERGALNKLLllteEERARG---VIAMSAGNHAQGVAYHAQRLGIPATI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 156 FLPERAGFTQKSMTLVHGADLtVVPGEIGDAGAAYTDAMADHDwysTKTFVTPYRHE----GKKTMLYETVEqldwQVP- 230
Cdd:PRK07334  100 VMPRFTPTVKVERTRGFGAEV-VLHGETLDEARAHARELAEEE---GLTFVHPYDDPaviaGQGTVALEMLE----DAPd 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 231 -DAVVYPTGGGVGLVGMHKAAREFR-DLGLV----DDLPPMYAAQASGCAPivdaweSGAdrheawgeiDTVFGGIAIPD 304
Cdd:PRK07334  172 lDTLVVPIGGGGLISGMATAAKALKpDIEIIgvqtELYPSMYAAIKGVALP------CGG---------STIAEGIAVKQ 236


                  ....*.
gi 2250742642 305 PGASPL 310
Cdd:PRK07334  237 PGQLTL 242
PRK08813 PRK08813
threonine dehydratase; Provisional
 89-240 1.68e-04

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 43.46  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  89 AERMGVervFVKDEGRNPTGTFKDRGQTVAMTAARMHGAT-DVALNSAGNAGQSAAAYAAEAGLDAHVFLPERAGFTqKS 167
Cdd:PRK08813   45 AERFGV---WLKLENLQRTGSYKVRGALNALLAGLERGDErPVICASAGNHAQGVAWSAYRLGVQAITVMPHGAPQT-KI 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2250742642 168 MTLVHGADLTVVPGEIGDAGAAYTDAMAD-HDWYSTKTFVTPYRHEGKKTMLYEtveqLDWQVPDAVVYPTGGG 240
Cdd:PRK08813  121 AGVAHWGATVRQHGNSYDEAYAFARELADqNGYRFLSAFDDPDVIAGQGTVGIE----LAAHAPDVVIVPIGGG 190
PRK08639 PRK08639
threonine dehydratase; Validated
 79-243 1.28e-03

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 40.56  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642  79 ATALVEAPALAERMGVErVFVKDEGRNPTGTFKDRGQTVAM----TAARMHGatdVALNSAGNAGQSAAAYAAEAGLDAH 154
Cdd:PRK08639   25 ETPLQRNDYLSEKYGAN-VYLKREDLQPVRSYKLRGAYNAIsqlsDEELAAG---VVCASAGNHAQGVAYACRHLGIPGV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250742642 155 VFLPEragfT---QK-SMTLVHGADLT--VVPGEIGDAgaAYTDAMAD---HDwystKTFVTPYRH----EGKKTMLYET 221
Cdd:PRK08639  101 IFMPV----TtpqQKiDQVRFFGGEFVeiVLVGDTFDD--SAAAAQEYaeeTG----ATFIPPFDDpdviAGQGTVAVEI 170

                         170       180
                  ....*....|....*....|...
gi 2250742642 222 VEQLDWQ-VPDAVVYPTGGGvGL 243
Cdd:PRK08639  171 LEQLEKEgSPDYVFVPVGGG-GL 192
PRK00481 PRK00481
NAD-dependent deacetylase; Provisional
 10-36 1.99e-03

NAD-dependent deacetylase; Provisional


Pssm-ID: 234777  Cd Length: 242  Bit Score: 39.39  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2250742642  10 LRCVDCGETFDAE-----TPHRCPDCGGILDP 36
Cdd:PRK00481  123 ARCTKCGQTYDLDeylkpEPPRCPKCGGILRP 154
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 78-113 3.97e-03

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: 38.88  E-value: 3.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2250742642  78 GATALVEAPALAERMGVeRVFVKDEGRNPTGTFKDR 113
Cdd:COG0031    12 GNTPLVRLNRLSPGPGA-EIYAKLESFNPGGSVKDR 46
SIR2 pfam02146
Sir2 family; This region is characteriztic of Silent information regulator 2 (Sir2) proteins, ...
 7-38 4.92e-03

Sir2 family; This region is characteriztic of Silent information regulator 2 (Sir2) proteins, or sirtuins. These are protein deacetylases that depend on nicotine adenine dinucleotide (NAD). They are found in many subcellular locations, including the nucleus, cytoplasm and mitochondria. Eukaryotic forms play in important role in the regulation of transcriptional repression. Moreover, they are involved in microtubule organization and DNA damage repair processes.i


Pssm-ID: 426621  Cd Length: 179  Bit Score: 37.62  E-value: 4.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2250742642   7 FAGLRCVDCGETFDAET---------PHRCPDCGGILDPTY 38
Cdd:pfam02146 104 FAKARCVSCHQKYTGETlyerirpekVPHCPQCGGLLKPDI 144
CxxC_CXXC_SSSS smart00834
Putative regulatory protein; CxxC_CXXC_SSSS represents a region of about 41 amino acids found ...
 11-32 5.21e-03

Putative regulatory protein; CxxC_CXXC_SSSS represents a region of about 41 amino acids found in a number of small proteins in a wide range of bacteria. The region usually begins with the initiator Met and contains two CxxC motifs separated by 17 amino acids. One protein in this entry has been noted as a putative regulatory protein, designated FmdB. Most proteins in this entry have a C-terminal region containing highly degenerate sequence.


Pssm-ID: 197903  Cd Length: 41  Bit Score: 34.45  E-value: 5.21e-03
                           10        20
                   ....*....|....*....|....*...
gi 2250742642   11 RCVDCGETFDA------ETPHRCPDCGG 32
Cdd:smart00834   7 RCEDCGHTFEVlqkisdDPLTTCPECGG 34
SIR2_Af2 cd01413
SIR2_Af2: Archaeal and prokaryotic group which includes Archaeoglobus fulgidus Sir2-Af2, ...
 12-36 5.58e-03

SIR2_Af2: Archaeal and prokaryotic group which includes Archaeoglobus fulgidus Sir2-Af2, Sulfolobus solfataricus ssSir2, and several bacterial homologs; and are members of the SIR2 family of proteins, silent information regulator 2 (Sir2) enzymes which catalyze NAD+-dependent protein/histone deacetylation. Sir2 proteins have been shown to regulate gene silencing, DNA repair, metabolic enzymes, and life span. The Sir2 homolog from the archaea Sulfolobus solftaricus deacetylates the non-specific DNA protein Alba to mediate transcription repression.


Pssm-ID: 238704  Cd Length: 222  Bit Score: 38.12  E-value: 5.58e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2250742642  12 CVDCGETFDAET--------PHRCPDCGGILDP 36
Cdd:cd01413   116 CVNCGSKYDLEEvkyakkheVPRCPKCGGIIRP 148
 
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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