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Conserved domains on  [gi|1760014705|gb|KAB2970033|]
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MAG: cysteine synthase [Thermoanaerobaculia bacterium]

Protein Classification

pyridoxal phosphate-dependent decarboxylase family protein( domain architecture ID 10000562)

pyridoxal phosphate-dependent decarboxylase family protein is primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but it is also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters

CATH:  3.40.640.10
EC:  4.1.1.-
Gene Ontology:  GO:0016830|GO:0030170|GO:0019752
PubMed:  8690703|7748903
SCOP:  4003328

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 116-497 4.76e-122

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 365.31  E-value: 4.76e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 116 RFVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMASHAGL-AGAEGCFTPGGSIANLVALLLARNV 194
Cdd:COG0076    69 RFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 195 AAPE-SRDRGLGDA-RLAVYSSAEGHYSIPKNAGILGLGRESVRRIPTDGAGRMDVGALARRLEDDRARGIRPTLINATA 272
Cdd:COG0076   149 ALARrVRAEGLPGApRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATA 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 273 GTTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVARRGELT 352
Cdd:COG0076   229 GTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLR 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 353 RSLDETADYLFQSHADDFNPGHRSIQCGRRNDALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAADPALELIEPPPS 432
Cdd:COG0076   309 EAFSFHASYLGPADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPEL 388

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1760014705 433 INVCFAVRG-------RDSAAICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTAARA 497
Cdd:COG0076   389 NIVCFRYKPagldeedALNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 116-497 4.76e-122

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 365.31  E-value: 4.76e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 116 RFVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMASHAGL-AGAEGCFTPGGSIANLVALLLARNV 194
Cdd:COG0076    69 RFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 195 AAPE-SRDRGLGDA-RLAVYSSAEGHYSIPKNAGILGLGRESVRRIPTDGAGRMDVGALARRLEDDRARGIRPTLINATA 272
Cdd:COG0076   149 ALARrVRAEGLPGApRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATA 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 273 GTTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVARRGELT 352
Cdd:COG0076   229 GTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLR 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 353 RSLDETADYLFQSHADDFNPGHRSIQCGRRNDALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAADPALELIEPPPS 432
Cdd:COG0076   309 EAFSFHASYLGPADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPEL 388

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1760014705 433 INVCFAVRG-------RDSAAICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTAARA 497
Cdd:COG0076   389 NIVCFRYKPagldeedALNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 117-494 5.11e-88

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 273.70  E-value: 5.11e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 117 FVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMAS--HAGLAGAEGCFTPGGSIANLVALLLARNV 194
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKlfGLPSEDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 195 AAPESRDRGLGDA-RLAVYSSAEGHYSIPKNAGILGlgrESVRRIPTDGAGRMDVGALARRLEDDRARGIRPTLINATAG 273
Cdd:cd06450    81 ARKRLKAGGGRGIdKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 274 TTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVArrgeltr 353
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 354 sldetadylfqshaddfnpghrsiqcgrrndALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAADPALELIEPPPSI 433
Cdd:cd06450   231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014705 434 NVCFAVRGRDSA-----AICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTA 494
Cdd:cd06450   280 LVCFRLKPSVKLdelnyDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIERA 345
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
116-437 2.84e-71

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 231.15  E-value: 2.84e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 116 RFVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVE-------RELLrHMASHAGLAGAEGCFTPGGSIANLVAL 188
Cdd:pfam00282  41 HFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELEnvvmnwlGEML-GLPAEFLGQEGGGVLQPGSSESNLLAL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 189 LLARNVAAPESRDRGLGD------ARLAVYSSAEGHYSIPKNAGILGLGresVRRIPTDGAGRMDVGALARRLEDDRARG 262
Cdd:pfam00282 120 LAARTKWIKRMKAAGKPAdssgilAKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 263 IRPTLINATAGTTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSV 342
Cdd:pfam00282 197 LIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 343 LLVARRGELTRSLDETADYLFQSH-ADDFnpGHRSIQCGRRNDALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAAD 421
Cdd:pfam00282 277 VWVKDKEALQQAFQFNPLYLGHTDsAYDT--GHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKD 354

                         330
                  ....*....|....*.
gi 1760014705 422 PALELIEPPPSINVCF 437
Cdd:pfam00282 355 GRFEICAEVGLGLVCF 370
PLN02880 PLN02880
tyrosine decarboxylase
 128-498 2.10e-35

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 138.12  E-value: 2.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 128 AAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMAS---------HAGLAGaeGCFTPGGSIANLVALLLARNVAAPE 198
Cdd:PLN02880   96 AGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKllnlpeqflSTGNGG--GVIQGTASEAVLVVLLAARDRVLRK 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 199 SRDRGLgdARLAVYSSAEGHYSIPKNAGILGLGRESVRRIPTDGAGRMDVG--ALARRLEDDRARGIRPTLINATAGTTV 276
Cdd:PLN02880  174 VGKNAL--EKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALApeLLSEAISTDLSSGLIPFFLCATVGTTS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 277 RGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVARRGELTRSLD 356
Cdd:PLN02880  252 STAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLS 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 357 ETADYLfQSHADDFNP----GHRSIQCGRRNDALKLWAAwLRL-GDRGWDERIRHQFSLARLAAAKIAADPALELIEPPP 431
Cdd:PLN02880  332 TNPEFL-KNKASQANSvvdyKDWQIPLGRRFRSLKLWMV-LRLyGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRI 409

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014705 432 SINVCFAV--------RGRD-SAAICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTAARAL 498
Cdd:PLN02880  410 FSLVCFRLvppknnedNGNKlNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASKL 485
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 116-497 4.76e-122

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 365.31  E-value: 4.76e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 116 RFVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMASHAGL-AGAEGCFTPGGSIANLVALLLARNV 194
Cdd:COG0076    69 RFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLpEGAGGVFTSGGTEANLLALLAARDR 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 195 AAPE-SRDRGLGDA-RLAVYSSAEGHYSIPKNAGILGLGRESVRRIPTDGAGRMDVGALARRLEDDRARGIRPTLINATA 272
Cdd:COG0076   149 ALARrVRAEGLPGApRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATA 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 273 GTTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVARRGELT 352
Cdd:COG0076   229 GTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLR 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 353 RSLDETADYLFQSHADDFNPGHRSIQCGRRNDALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAADPALELIEPPPS 432
Cdd:COG0076   309 EAFSFHASYLGPADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPEL 388

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1760014705 433 INVCFAVRG-------RDSAAICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTAARA 497
Cdd:COG0076   389 NIVCFRYKPagldeedALNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 117-494 5.11e-88

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 273.70  E-value: 5.11e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 117 FVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMAS--HAGLAGAEGCFTPGGSIANLVALLLARNV 194
Cdd:cd06450     1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKlfGLPSEDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 195 AAPESRDRGLGDA-RLAVYSSAEGHYSIPKNAGILGlgrESVRRIPTDGAGRMDVGALARRLEDDRARGIRPTLINATAG 273
Cdd:cd06450    81 ARKRLKAGGGRGIdKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 274 TTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVArrgeltr 353
Cdd:cd06450   158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 354 sldetadylfqshaddfnpghrsiqcgrrndALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAADPALELIEPPPSI 433
Cdd:cd06450   231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014705 434 NVCFAVRGRDSA-----AICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTA 494
Cdd:cd06450   280 LVCFRLKPSVKLdelnyDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIERA 345
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
116-437 2.84e-71

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 231.15  E-value: 2.84e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 116 RFVNQLFGGREPAAMAAEMLVAVPNVSMYTFKAAGAQILVE-------RELLrHMASHAGLAGAEGCFTPGGSIANLVAL 188
Cdd:pfam00282  41 HFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELEnvvmnwlGEML-GLPAEFLGQEGGGVLQPGSSESNLLAL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 189 LLARNVAAPESRDRGLGD------ARLAVYSSAEGHYSIPKNAGILGLGresVRRIPTDGAGRMDVGALARRLEDDRARG 262
Cdd:pfam00282 120 LAARTKWIKRMKAAGKPAdssgilAKLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENG 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 263 IRPTLINATAGTTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSV 342
Cdd:pfam00282 197 LIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 343 LLVARRGELTRSLDETADYLFQSH-ADDFnpGHRSIQCGRRNDALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAAD 421
Cdd:pfam00282 277 VWVKDKEALQQAFQFNPLYLGHTDsAYDT--GHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKD 354

                         330
                  ....*....|....*.
gi 1760014705 422 PALELIEPPPSINVCF 437
Cdd:pfam00282 355 GRFEICAEVGLGLVCF 370
PLN02880 PLN02880
tyrosine decarboxylase
 128-498 2.10e-35

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 138.12  E-value: 2.10e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 128 AAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMAS---------HAGLAGaeGCFTPGGSIANLVALLLARNVAAPE 198
Cdd:PLN02880   96 AGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKllnlpeqflSTGNGG--GVIQGTASEAVLVVLLAARDRVLRK 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 199 SRDRGLgdARLAVYSSAEGHYSIPKNAGILGLGRESVRRIPTDGAGRMDVG--ALARRLEDDRARGIRPTLINATAGTTV 276
Cdd:PLN02880  174 VGKNAL--EKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALApeLLSEAISTDLSSGLIPFFLCATVGTTS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 277 RGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVARRGELTRSLD 356
Cdd:PLN02880  252 STAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLS 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 357 ETADYLfQSHADDFNP----GHRSIQCGRRNDALKLWAAwLRL-GDRGWDERIRHQFSLARLAAAKIAADPALELIEPPP 431
Cdd:PLN02880  332 TNPEFL-KNKASQANSvvdyKDWQIPLGRRFRSLKLWMV-LRLyGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPRI 409

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014705 432 SINVCFAV--------RGRD-SAAICDWLDREGRLKIGYGTVAGRRVLRLVCVNPDLEESDLDAILAEIRTAARAL 498
Cdd:PLN02880  410 FSLVCFRLvppknnedNGNKlNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASKL 485
PLN02590 PLN02590
probable tyrosine decarboxylase
 128-481 8.98e-28

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 116.73  E-value: 8.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 128 AAMAAEMLVAVPNVSMYTFKAAGAQILVERELLRHMAS------HAGLAGAEGCFTPG-GSIANLVALLLARNVAAPESR 200
Cdd:PLN02590  144 AGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKllqlpdHFLSTGNGGGVIQGtGCEAVLVVVLAARDRILKKVG 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 201 DRGLgdARLAVYSSAEGHYSIPKNAGILGLGRESVRRIPTDGAGR--MDVGALARRLEDDRARGIRPTLINATAGTTVRG 278
Cdd:PLN02590  224 KTLL--PQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSA 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 279 AFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAWNPHKMMGVALQCSVLLVARRGELTRSLDET 358
Cdd:PLN02590  302 AVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTN 381

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 359 ADYL-FQSHADD--FNPGHRSIQCGRRNDALKLWAAWLRLGDRGWDERIRHQFSLARLAAAKIAADPALELIEPPPSINV 435
Cdd:PLN02590  382 PEYLeFKVSKKDtvVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLV 461

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1760014705 436 CFAVRGRD-SAAICDWLDRE--------GRLKIGYGTVAGRRVLRLVCVNPDLEE 481
Cdd:PLN02590  462 CFRLAPVDgDEDQCNERNREllaavnstGKIFISHTALSGKFVLRFAVGAPLTEE 516
PRK02769 PRK02769
histidine decarboxylase; Provisional
 156-406 4.95e-24

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 103.58  E-value: 4.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 156 ERELLRHMASHAGLAGAE--GCFTPGGSIANLVALLLARNvAAPESrdrglgdarlAVYSSAEGHYSIPKNAGILGLGRE 233
Cdd:PRK02769   67 ERDVMNFFAELFKIPFNEswGYITNGGTEGNLYGCYLARE-LFPDG----------TLYYSKDTHYSVSKIARLLRIKSR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 234 SVRRIPTdgaGRMDVGALARRLEDDRArgiRPTLINATAGTTVRGAFDPL-RAIAALARE--HDAWLHVDGALGGsVVLC 310
Cdd:PRK02769  136 VITSLPN---GEIDYDDLISKIKENKN---QPPIIFANIGTTMTGAIDNIkEIQEILKKIgiDDYYIHADAALSG-MILP 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 311 ----PSRRELVDGVelaDSFAWNPHKMMGVALQCSVLLvARRGELTRSLDETaDYLfqsHADDFNPGhrsiqcGRRN--D 384
Cdd:PRK02769  209 fvnnPPPFSFADGI---DSIAISGHKFIGSPMPCGIVL-AKKKYVERISVDV-DYI---GSRDQTIS------GSRNghT 274

                         250       260
                  ....*....|....*....|..
gi 1760014705 385 ALKLWAAWLRLGDRGWDERIRH 406
Cdd:PRK02769  275 ALLLWAAIRSLGSKGLRQRVQH 296
PLN03032 PLN03032
serine decarboxylase; Provisional
 174-406 9.00e-15

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 75.63  E-value: 9.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 174 GCFTPGGSIANLVALLLARNVaapesrdrgLGDARLavYSSAEGHYSIPKNAGILglgRESVRRIPTDGAGRMDVGALAR 253
Cdd:PLN03032   88 GYITTCGTEGNLHGILVGREV---------FPDGIL--YASRESHYSVFKAARMY---RMEAVKVPTLPSGEIDYDDLER 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 254 RLEDDRARgirPTLINATAGTTVRGAFDPL-RAIAALAR----EHDAWLHVDGALGGSVVLCPSRRELVDGVELADSFAW 328
Cdd:PLN03032  154 ALAKNRDK---PAILNVNIGTTVKGAVDDLdRILRILKElgytEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSV 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 329 NPHKMMGVALQCSVLLVarRGELTRSLDETADYLfqshaddfNPGHRSIQcGRRND--ALKLWAAWLRLGDRGWDERIRH 406
Cdd:PLN03032  231 SGHKFLGCPMPCGVALT--RKKHVKALSQNVEYL--------NSRDATIM-GSRNGhaPLYLWYTLRRKGYRGIKRDVQH 299
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 176-345 7.74e-14

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 69.33  E-value: 7.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 176 FTPGGSIANLVALLLARNvaapesrdrglgdARLAVYSSAEGHYSIPKNAGILGLGResVRRIPTDGAGRMDVGALARRl 255
Cdd:cd01494    22 FVPSGTGANEAALLALLG-------------PGDEVIVDANGHGSRYWVAAELAGAK--PVPVPVDDAGYGGLDVAILE- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 256 edDRARGIRPTLINATAGTTVRGAFDPLRAIAALAREHDAWLHVDGALGGSVVLCPSRRELVDGvelADSFAWNPHKMMG 335
Cdd:cd01494    86 --ELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGG---ADVVTFSLHKNLG 160

                         170
                  ....*....|
gi 1760014705 336 VAlQCSVLLV 345
Cdd:cd01494   161 GE-GGGVVIV 169
PLN02263 PLN02263
serine decarboxylase
 174-399 6.21e-09

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 58.29  E-value: 6.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 174 GCFTPGGSIANLVALLLARNVaapesrdrgLGDARLavYSSAEGHYSIPKNAGILglgRESVRRIPTDGAGRMDVGALAR 253
Cdd:PLN02263  155 GYITNCGTEGNLHGILVGREV---------FPDGIL--YASRESHYSVFKAARMY---RMECVKVDTLVSGEIDCADFKA 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 254 RLEDDRARgirPTLINATAGTTVRGAFDPLRAIAALARE----HDA-WLHVDGALGGSVVLCPSRRELVDGVELADSFAW 328
Cdd:PLN02263  221 KLLANKDK---PAIINVNIGTTVKGAVDDLDLVIKTLEEcgfsQDRfYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSV 297

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1760014705 329 NPHKMMGVALQCSVLLVarRGELTRSLDETADYLFQSHAddfnpghrSIQCGRRNDA-LKLWAAWLRLGDRG 399
Cdd:PLN02263  298 SGHKFVGCPMPCGVQIT--RMEHINVLSSNVEYLASRDA--------TIMGSRNGHApIFLWYTLNRKGYRG 359
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
235-335 6.36e-09

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 57.84  E-value: 6.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 235 VRRIPTDGAGRMDVGALARRLeDDRARgirptLINATAGTTVRGAFDPLRAIAALAREHDAWLHVDGAlgGSVVLCPsrr 314
Cdd:COG0520   131 VRVIPLDEDGELDLEALEALL-TPRTK-----LVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGA--QSVPHLP--- 199

                          90       100
                  ....*....|....*....|..
gi 1760014705 315 elVDGVEL-ADSFAWNPHKMMG 335
Cdd:COG0520   200 --VDVQALgCDFYAFSGHKLYG 219
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
172-302 2.61e-06

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 441611 [Multi-domain]  Cd Length: 333  Bit Score: 49.29  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 172 AEGCFTPGGSIANLVALLLarnVAAPesrdrglGDArlaVYSSAEGHY------SIPKNAGIlglgreSVRRIPTDGaGR 245
Cdd:COG2008    51 EAALFVPSGTMANQLALRA---HTRP-------GDE---VICHETAHIyvdeggAPEALSGV------KLLPVPGED-GK 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1760014705 246 MDVGALARRLEDDRARGIRPTLI---NAT-AGTTVRgaFDPLRAIAALAREHDAWLHVDGA 302
Cdd:COG2008   111 LTPEDLEAAIRPGDVHFPQPGLVsleNTTeGGTVYP--LEELRAIAAVAREHGLPLHLDGA 169
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
167-302 1.99e-05

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 46.44  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 167 AGLAGAE-GCFTPGGSIANLVAL--LLARnvaapesrdrglGDARLAvysSAEGHYSIPKNAGILGLGRESVRRIPTDGA 243
Cdd:pfam01212  42 AELFGKEaALFVPSGTAANQLALmaHCQR------------GDEVIC---GEPAHIHFDETGGHAELGGVQPRPLDGDEA 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1760014705 244 GRMDVGALARRL-EDDRARGIRPTLI------NATAGTTVRgaFDPLRAIAALAREHDAWLHVDGA 302
Cdd:pfam01212 107 GNMDLEDLEAAIrEVGADIFPPTGLIslenthNSAGGQVVS--LENLREIAALAREHGIPVHLDGA 170
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 157-302 2.83e-05

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 46.17  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 157 RELLRHMASHAGlaGAEGCFTPGGSIANLVALLLarNVAAPESrdrglgdarlaVYSSAEGHYSIPKNAGILGLGreSVR 236
Cdd:cd06502    35 AKLEARAAELFG--KEAALFVPSGTAANQLALAA--HTQPGGS-----------VICHETAHIYTDEAGAPEFLS--GVK 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1760014705 237 RIPTDGA-GRMDVGALARRLE-DDRARGIRPTLI---NATAGTTVRgAFDPLRAIAALAREHDAWLHVDGA 302
Cdd:cd06502    98 LLPVPGEnGKLTPEDLEAAIRpRDDIHFPPPSLVsleNTTEGGTVY-PLDELKAISALAKENGLPLHLDGA 167
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 176-335 3.06e-05

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 46.09  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 176 FTPGGSIA-NLVALLLARNvaapesrdrgLGDARLAVYSSAEGHysipknAGILG---LGRES---VRRIPTDGAGRMDV 248
Cdd:pfam00266  66 FTSGTTEAiNLVALSLGRS----------LKPGDEIVITEMEHH------ANLVPwqeLAKRTgarVRVLPLDEDGLLDL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 249 GALaRRLEDDRARgirptLINATAGTTVRGAFDPLRAIAALAREHDAWLHVDGALGgsvvlCPSRRelVDGVEL-ADSFA 327
Cdd:pfam00266 130 DEL-EKLITPKTK-----LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA-----IGHRP--IDVQKLgVDFLA 196


                  ....*...
gi 1760014705 328 WNPHKMMG 335
Cdd:pfam00266 197 FSGHKLYG 204
PLN02721 PLN02721
threonine aldolase
 157-302 1.54e-04

threonine aldolase


Pssm-ID: 178323 [Multi-domain]  Cd Length: 353  Bit Score: 43.91  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1760014705 157 RELLRHMAShagLAGAE-GCFTPGGSIANLVALLLARNVAAPESRdrgLGDarlavyssaEGHYSIPKNAGILGLGRESV 235
Cdd:PLN02721   43 LRLEEEMAK---IFGKEaALFVPSGTMGNLISVLVHCDVRGSEVI---LGD---------NSHIHLYENGGISTLGGVHP 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1760014705 236 RRIPTDGAGRMDVGALA---RRLEDDRARGIRPTLINATAGTTvRGAFDPL---RAIAALAREHDAWLHVDGA 302
Cdd:PLN02721  108 RTVKNNEDGTMDLDAIEaaiRPKGDDHFPTTRLICLENTHANC-GGRCLSVeytDKVGELAKRHGLKLHIDGA 179
PRK09295 PRK09295
cysteine desulfurase SufS;
235-302 4.04e-03

cysteine desulfurase SufS;


Pssm-ID: 181766 [Multi-domain]  Cd Length: 406  Bit Score: 39.73  E-value: 4.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1760014705 235 VRRIPTDGAGRMDVGALARrLEDDRARgirptLINATAGTTVRGAFDPLRAIAALAREHDAWLHVDGA 302
Cdd:PRK09295  141 LRVIPLNPDGTLQLETLPA-LFDERTR-----LLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGA 202
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 247-304 4.37e-03

KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.


Pssm-ID: 99747 [Multi-domain]  Cd Length: 349  Bit Score: 39.47  E-value: 4.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1760014705 247 DVGALARRLEDDRaRGIRPTLInATAGT-TVRGAFDPLRAIAALAREHDAWLHVD-----GALG 304
Cdd:cd06454   116 DMEDLEKLLREAR-RPYGKKLI-VTEGVySMDGDIAPLPELVDLAKKYGAILFVDeahsvGVYG 177
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 247-302 9.23e-03

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 38.22  E-value: 9.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1760014705 247 DVGALARRLEDDRARgirPTLInATAGT-TVRGAFDPLRAIAALAREHDAWLHVDGA 302
Cdd:PRK05958  154 DVDALEALLAKWRAG---RALI-VTESVfSMDGDLAPLAELVALARRHGAWLLVDEA 206
 
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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