NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|643375266|ref|WP_025203662|]
View 

MULTISPECIES: aspartate aminotransferase family protein [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 17-484 0e+00

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: 524.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  17 AYQQAIEQSTQAVMQWLKQ-PEMYQGKTVAELRDRIKLDFNPKGLGNEAAIERAVEFFLKDSLSVHHPQCVAHLHCPSLV 95
Cdd:COG0076    1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  96 VSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGDAGVFTSGGTQSNLMGLMLARDAFFARQghsVQQD 175
Cdd:COG0076   81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 176 GLVGdLRKIRVLCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSRMDLNDLAAKIEQCNANGEQILAIVATAGTTDAGAI 255
Cdd:COG0076  158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 256 DPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKEAR-HYELMRYQAA 334
Cdd:COG0076  237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPElLREAFSFHAS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 335 YLNsefDEEAGVPNLVSKSLQTTRRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALELVMQPQLASVLF 414
Cdd:COG0076  317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 415 RFRGQVQMDDagiALLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVERTAQE 484
Cdd:COG0076  394 RYKPAGLDEE---DALNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 17-484 0e+00

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: 524.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  17 AYQQAIEQSTQAVMQWLKQ-PEMYQGKTVAELRDRIKLDFNPKGLGNEAAIERAVEFFLKDSLSVHHPQCVAHLHCPSLV 95
Cdd:COG0076    1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  96 VSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGDAGVFTSGGTQSNLMGLMLARDAFFARQghsVQQD 175
Cdd:COG0076   81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 176 GLVGdLRKIRVLCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSRMDLNDLAAKIEQCNANGEQILAIVATAGTTDAGAI 255
Cdd:COG0076  158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 256 DPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKEAR-HYELMRYQAA 334
Cdd:COG0076  237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPElLREAFSFHAS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 335 YLNsefDEEAGVPNLVSKSLQTTRRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALELVMQPQLASVLF 414
Cdd:COG0076  317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 415 RFRGQVQMDDagiALLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVERTAQE 484
Cdd:COG0076  394 RYKPAGLDEE---DALNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 85-480 5.51e-121

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: 357.67  E-value: 5.51e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  85 CVAHLHCPSLVVSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGDA-GVFTSGGTQSNLMGLMLARDA 163
Cdd:cd06450    1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDAdGVFTSGGSESNLLALLAARDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 164 FFARQghsvqQDGLVGDLRKIRVLCSENAHFSVQKNMALMGlgyQSVVQVKTDEFSRMDLNDLAAKIEQCNANGEQILAI 243
Cdd:cd06450   81 ARKRL-----KAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 244 VATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKea 323
Cdd:cd06450  153 VATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 324 rhyelmryqaaylnsefdeeagvpnlvskslqttrrfdALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALEL 403
Cdd:cd06450  231 --------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFEL 272

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643375266 404 VMQPQLASVLFRFRGQVQMDdagiaLLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVER 480
Cdd:cd06450  273 LGEPNLSLVCFRLKPSVKLD-----ELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIER 344
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
81-417 9.02e-63

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 208.81  E-value: 9.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266   81 HHPQCVAHLHCPSLVVSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGD-----AGVFTSGGTQSNLM 155
Cdd:pfam00282  38 HSPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFlgqegGGVLQPGSSESNLL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  156 GLMLARDAFFAR---QGHSVQQDGLVGdlrKIRVLCSENAHFSVQKNMALMGLGyqsVVQVKTDEFSRMDLNDLAAKIEQ 232
Cdd:pfam00282 118 ALLAARTKWIKRmkaAGKPADSSGILA---KLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  233 CNANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQT 312
Cdd:pfam00282 192 DKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  313 ISCGAFLLKE--ARHYELmRYQAAYLNsefdEEAGVPNLVSKSLQTTRRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQ 390
Cdd:pfam00282 272 LDCSAVWVKDkeALQQAF-QFNPLYLG----HTDSAYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQY 346

                         330       340
                  ....*....|....*....|....*..
gi 643375266  391 VAAYVKEQPALELVMQPQLASVLFRFR 417
Cdd:pfam00282 347 LEALIRKDGRFEICAEVGLGLVCFRLK 373
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
 143-471 8.75e-61

putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 274791  Cd Length: 522  Bit Score: 207.67  E-value: 8.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  143 GVFTSGGTQSNLMGLMLARDAFFARQG--HSVQQDGLVGDLR-----KIRVLCSENAHFSVQKNMALMGLGYQSVVQVKT 215
Cdd:TIGR03799 162 GAFCSGGTVANITALWVARNRLLKADGdfRGIAREGLFAALRhygydGLAILVSERGHYSLGKAADVLGIGRDNLVPVKT 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  216 DEFSRMDLNDLAAKIEQCNANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGI 295
Cdd:TIGR03799 242 DENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGI 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  296 ELVDSVTLDFHKQFFQTISCGAFLLKEARHYELMRYQAAYLNSEfdeeaGVPNLVSKSLQTTRRFDALKLWMSLEALGQE 375
Cdd:TIGR03799 322 ERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEHHAEYILRK-----GSKDLGSHTLEGSRPGMAMLVYACLHIIGRK 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  376 QYAAIIDHGVTLAQQVAAYVKEQPALELVMQPQLASVLFRF---RGQVQMDDAgIALLNQKIGDAL-----------LES 441
Cdd:TIGR03799 397 GYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYvpeNVKAALAIA-DEEQREKINDALnaltkfiqkrqRET 475

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 643375266  442 GRANVGVTE-------HNGVTCLKLTLLNPTVT---LEDI 471
Cdd:TIGR03799 476 GKSFVSRTRltpaqydHQPTIVFRVVLANPLTTheiLQDI 515
PLN02880 PLN02880
tyrosine decarboxylase
 101-488 1.01e-36

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 141.58  E-value: 1.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 101 EVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGY------QAGDAGVFTSGGTQSNLMGLMLARDAFFARQGHSVqq 174
Cdd:PLN02880 101 EMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLpeqflsTGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKNA-- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 175 dglvgdLRKIRVLCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSRMDL--NDLAAKIEQCNANGEQILAIVATAGTTDA 252
Cdd:PLN02880 179 ------LEKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALapELLSEAISTDLSSGLIPFFLCATVGTTSS 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 253 GAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKEaRHYELmryQ 332
Cdd:PLN02880 253 TAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKD-RNALI---Q 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 333 AAYLNSEF-DEEAGVPNLVS--KSLQTT--RRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALELVMQP 407
Cdd:PLN02880 329 SLSTNPEFlKNKASQANSVVdyKDWQIPlgRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPR 408

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 408 QLASVLFRFRGQVQMDDAGIAlLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVERTAQEVLA 487
Cdd:PLN02880 409 IFSLVCFRLVPPKNNEDNGNK-LNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASKLLG 487


                 .
gi 643375266 488 K 488
Cdd:PLN02880 488 K 488
 
Name Accession Description Interval E-value
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 17-484 0e+00

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: 524.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  17 AYQQAIEQSTQAVMQWLKQ-PEMYQGKTVAELRDRIKLDFNPKGLGNEAAIERAVEFFLKDSLSVHHPQCVAHLHCPSLV 95
Cdd:COG0076    1 EFRALLHQALDLAADYLAGlDRPVFGPSPEELRAALDEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGGTTP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  96 VSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGDAGVFTSGGTQSNLMGLMLARDAFFARQghsVQQD 175
Cdd:COG0076   81 AALAADLLASALNQNMGDWDTSPAATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARR---VRAE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 176 GLVGdLRKIRVLCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSRMDLNDLAAKIEQCNANGEQILAIVATAGTTDAGAI 255
Cdd:COG0076  158 GLPG-APRPRIVVSEEAHSSVDKAARLLGLGRDALRKVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 256 DPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKEAR-HYELMRYQAA 334
Cdd:COG0076  237 DPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHLLDGIERADSITVDPHKWLYVPYGCGAVLVRDPElLREAFSFHAS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 335 YLNsefDEEAGVPNLVSKSLQTTRRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALELVMQPQLASVLF 414
Cdd:COG0076  317 YLG---PADDGVPNLGDYTLELSRRFRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCF 393

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 415 RFRGQVQMDDagiALLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVERTAQE 484
Cdd:COG0076  394 RYKPAGLDEE---DALNYALRDRLRARGRAFLSPTKLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 85-480 5.51e-121

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: 357.67  E-value: 5.51e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  85 CVAHLHCPSLVVSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGDA-GVFTSGGTQSNLMGLMLARDA 163
Cdd:cd06450    1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDAdGVFTSGGSESNLLALLAARDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 164 FFARQghsvqQDGLVGDLRKIRVLCSENAHFSVQKNMALMGlgyQSVVQVKTDEFSRMDLNDLAAKIEQCNANGEQILAI 243
Cdd:cd06450   81 ARKRL-----KAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 244 VATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKea 323
Cdd:cd06450  153 VATAGTTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 324 rhyelmryqaaylnsefdeeagvpnlvskslqttrrfdALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALEL 403
Cdd:cd06450  231 --------------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFEL 272

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643375266 404 VMQPQLASVLFRFRGQVQMDdagiaLLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVER 480
Cdd:cd06450  273 LGEPNLSLVCFRLKPSVKLD-----ELNYDLSDRLNERGGWHVPATTLGGPNVLRFVVTNPLTTRDDADALLEDIER 344
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
81-417 9.02e-63

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 208.81  E-value: 9.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266   81 HHPQCVAHLHCPSLVVSQAAEVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGYQAGD-----AGVFTSGGTQSNLM 155
Cdd:pfam00282  38 HSPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWLGEMLGLPAEFlgqegGGVLQPGSSESNLL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  156 GLMLARDAFFAR---QGHSVQQDGLVGdlrKIRVLCSENAHFSVQKNMALMGLGyqsVVQVKTDEFSRMDLNDLAAKIEQ 232
Cdd:pfam00282 118 ALLAARTKWIKRmkaAGKPADSSGILA---KLVAYTSDQAHSSIEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  233 CNANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQT 312
Cdd:pfam00282 192 DKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVL 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  313 ISCGAFLLKE--ARHYELmRYQAAYLNsefdEEAGVPNLVSKSLQTTRRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQ 390
Cdd:pfam00282 272 LDCSAVWVKDkeALQQAF-QFNPLYLG----HTDSAYDTGHKQIPLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQY 346

                         330       340
                  ....*....|....*....|....*..
gi 643375266  391 VAAYVKEQPALELVMQPQLASVLFRFR 417
Cdd:pfam00282 347 LEALIRKDGRFEICAEVGLGLVCFRLK 373
NOD_PanD_pyr TIGR03799
putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a ...
 143-471 8.75e-61

putative pyridoxal-dependent aspartate 1-decarboxylase; This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see pfam00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, G. metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent). [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 274791  Cd Length: 522  Bit Score: 207.67  E-value: 8.75e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  143 GVFTSGGTQSNLMGLMLARDAFFARQG--HSVQQDGLVGDLR-----KIRVLCSENAHFSVQKNMALMGLGYQSVVQVKT 215
Cdd:TIGR03799 162 GAFCSGGTVANITALWVARNRLLKADGdfRGIAREGLFAALRhygydGLAILVSERGHYSLGKAADVLGIGRDNLVPVKT 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  216 DEFSRMDLNDLAAKIEQCNANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGI 295
Cdd:TIGR03799 242 DENNRIRVDALRDKCLELAAQNIKPMAIVGVAGTTETGNIDPLDEMADIAQEAGCHFHVDAAWGGATLLSNTYRHLLKGI 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  296 ELVDSVTLDFHKQFFQTISCGAFLLKEARHYELMRYQAAYLNSEfdeeaGVPNLVSKSLQTTRRFDALKLWMSLEALGQE 375
Cdd:TIGR03799 322 ERADSVTIDAHKQMYVPMGAGMVLFKDPALTSAIEHHAEYILRK-----GSKDLGSHTLEGSRPGMAMLVYACLHIIGRK 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  376 QYAAIIDHGVTLAQQVAAYVKEQPALELVMQPQLASVLFRF---RGQVQMDDAgIALLNQKIGDAL-----------LES 441
Cdd:TIGR03799 397 GYEMLINQSIDKAHYFANLIDQQPDFELVTEPELCLLTYRYvpeNVKAALAIA-DEEQREKINDALnaltkfiqkrqRET 475

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 643375266  442 GRANVGVTE-------HNGVTCLKLTLLNPTVT---LEDI 471
Cdd:TIGR03799 476 GKSFVSRTRltpaqydHQPTIVFRVVLANPLTTheiLQDI 515
PLN02880 PLN02880
tyrosine decarboxylase
 101-488 1.01e-36

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 141.58  E-value: 1.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 101 EVLINATNQSMDSWDQSPSATIIEIKLIEWLRTRVGY------QAGDAGVFTSGGTQSNLMGLMLARDAFFARQGHSVqq 174
Cdd:PLN02880 101 EMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLNLpeqflsTGNGGGVIQGTASEAVLVVLLAARDRVLRKVGKNA-- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 175 dglvgdLRKIRVLCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSRMDL--NDLAAKIEQCNANGEQILAIVATAGTTDA 252
Cdd:PLN02880 179 ------LEKLVVYASDQTHSALQKACQIAGIHPENCRLLKTDSSTNYALapELLSEAISTDLSSGLIPFFLCATVGTTSS 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 253 GAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKEaRHYELmryQ 332
Cdd:PLN02880 253 TAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYIDGVEEADSFNMNAHKWFLTNFDCSLLWVKD-RNALI---Q 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 333 AAYLNSEF-DEEAGVPNLVS--KSLQTT--RRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALELVMQP 407
Cdd:PLN02880 329 SLSTNPEFlKNKASQANSVVdyKDWQIPlgRRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQLVAQDSRFEVVTPR 408

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 408 QLASVLFRFRGQVQMDDAGIAlLNQKIGDALLESGRANVGVTEHNGVTCLKLTLLNPTVTLEDIKVLLSLVERTAQEVLA 487
Cdd:PLN02880 409 IFSLVCFRLVPPKNNEDNGNK-LNHDLLDAVNSSGKIFISHTVLSGKYVLRFAVGAPLTEERHVTAAWKVLQDEASKLLG 487


                 .
gi 643375266 488 K 488
Cdd:PLN02880 488 K 488
PLN02590 PLN02590
probable tyrosine decarboxylase
 113-416 3.39e-36

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 140.62  E-value: 3.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 113 SWDQSPSATIIEIKLIEWLRTRVGY------QAGDAGVFTSGGTQSNLMGLMLARDAFFARQGHSVqqdglvgdLRKIRV 186
Cdd:PLN02590 161 TWLTSPAATELEIIVLDWLAKLLQLpdhflsTGNGGGVIQGTGCEAVLVVVLAARDRILKKVGKTL--------LPQLVV 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 187 LCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSR--MDLNDLAAKIEQCNANGEQILAIVATAGTTDAGAIDPLRAIAEL 264
Cdd:PLN02590 233 YGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNI 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 265 AAKQNIWVHVDAAWGGALLMSEQYRHYLDGIELVDSVTLDFHKQFFQTISCGAFLLKEarHYEL---MRYQAAYLNSEFD 341
Cdd:PLN02590 313 AKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKD--RYSLidaLKTNPEYLEFKVS 390

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643375266 342 EEAGVPNLVSKSLQTTRRFDALKLWMSLEALGQEQYAAIIDHGVTLAQQVAAYVKEQPALELVMQPQLASVLFRF 416
Cdd:PLN02590 391 KKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRL 465
PRK02769 PRK02769
histidine decarboxylase; Provisional
 143-389 8.06e-18

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 85.09  E-value: 8.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 143 GVFTSGGTQSNLMGLMLARDAFfarqghsvqQDGLVgdlrkirvLCSENAHFSVQKNMALMGLGYQSVVQVKTDEfsrMD 222
Cdd:PRK02769  87 GYITNGGTEGNLYGCYLARELF---------PDGTL--------YYSKDTHYSVSKIARLLRIKSRVITSLPNGE---ID 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 223 LNDLAAKIEqcnANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNI---WVHVDAAWGGA---LLMSEQYRHYLDGIe 296
Cdd:PRK02769 147 YDDLISKIK---ENKNQPPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMilpFVNNPPPFSFADGI- 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 297 lvDSVTLDFHKQFFQTISCGAFLLKeaRHYelmrYQAAYLNSEFdeeagvpnlVSKSLQT---TRR-FDALKLWMSLEAL 372
Cdd:PRK02769 223 --DSIAISGHKFIGSPMPCGIVLAK--KKY----VERISVDVDY---------IGSRDQTisgSRNgHTALLLWAAIRSL 285

                        250
                 ....*....|....*..
gi 643375266 373 GQEQYAAIIDHGVTLAQ 389
Cdd:PRK02769 286 GSKGLRQRVQHCLDMAQ 302
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 126-309 2.95e-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: 70.49  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 126 KLIEWLRtRVgYQAG-DAGVFTSGGTQSNLMGLMlardafFARQGHSVqqdglvgdlrkirVLCSENAHFSVQKNMALMG 204
Cdd:cd01494    4 ELEEKLA-RL-LQPGnDKAVFVPSGTGANEAALL------ALLGPGDE-------------VIVDANGHGSRYWVAAELA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 205 lGYQSVVQVKTDEFsrMDLNDLAAKIEqcNANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNIWVHVDAAWGGaLLM 284
Cdd:cd01494   63 -GAKPVPVPVDDAG--YGGLDVAILEE--LKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAG-GAS 136

                        170       180
                 ....*....|....*....|....*
gi 643375266 285 SEQYrhYLDGIELVDSVTLDFHKQF 309
Cdd:cd01494  137 PAPG--VLIPEGGADVVTFSLHKNL 159
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
126-347 6.89e-09

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 56.84  E-value: 6.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  126 KLIEWLRTRVGYqagDAGVFTSGGTQSNLMGLMLardafFARQGHSVqqdglvgdlrkirvLCSENAH--FSVQKNMALM 203
Cdd:pfam01212  36 RLEDRVAELFGK---EAALFVPSGTAANQLALMA-----HCQRGDEV--------------ICGEPAHihFDETGGHAEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  204 GlGYQsVVQVKTDEFSRMDLNDLAAKIEQCNANGEQILAIVATAGTTDAGA-----IDPLRAIAELAAKQNIWVHVD--- 275
Cdd:pfam01212  94 G-GVQ-PRPLDGDEAGNMDLEDLEAAIREVGADIFPPTGLISLENTHNSAGgqvvsLENLREIAALAREHGIPVHLDgar 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  276 ---AAWGGALLMSEQYRHyldgielVDSVTLDFHKQFFQTIscGAFL------LKEARHyelmryQAAYLNSEFDeEAGV 346
Cdd:pfam01212 172 fanAAVALGVIVKEITSY-------ADSVTMCLSKGLGAPV--GSVLagsddfIAKAIR------QRKYLGGGLR-QAGV 235


                  .
gi 643375266  347 P 347
Cdd:pfam01212 236 L 236
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 144-277 4.08e-07

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 51.97  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 144 VFTSGGTQSN---LMGLMLARDAffarqghsvqqdglvgdlRKIRVLCSENAHFSVQKNM-ALMGLGYQsVVQVKTDEFS 219
Cdd:COG1104   66 IFTSGGTEANnlaIKGAARAYRK------------------KGKHIITSAIEHPAVLETArFLEKEGFE-VTYLPVDEDG 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643375266 220 RMDLNDLAAKIeqcnaNGEQILAIVATA----GTtdagaIDPLRAIAELAAKQNIWVHVDAA 277
Cdd:COG1104  127 RVDLEALEAAL-----RPDTALVSVMHAnnetGT-----IQPIAEIAEIAKEHGVLFHTDAV 178
PLN02651 PLN02651
cysteine desulfurase
 144-277 2.02e-05

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 46.57  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 144 VFTSGGTQSNLMGLMLARDAFFARQGHsvqqdglvgdlrkirVLCSENAHFSVQKNMALMGLGYQSVVQVKTDEFSRMDL 223
Cdd:PLN02651  64 IFTSGATESNNLAIKGVMHFYKDKKKH---------------VITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDL 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 643375266 224 NDLAAKIEQcnangEQILAIVATAgTTDAGAIDPLRAIAELAAKQNIWVHVDAA 277
Cdd:PLN02651 129 DELAAAIRP-----DTALVSVMAV-NNEIGVIQPVEEIGELCREKKVLFHTDAA 176
PLN03032 PLN03032
serine decarboxylase; Provisional
 143-338 2.43e-05

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 46.36  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 143 GVFTSGGTQSNLMGLMLARDAFfarqghsvqQDGLvgdlrkirVLCSENAHFSVQK--NMALMglgyqSVVQVKTDEFSR 220
Cdd:PLN03032  88 GYITTCGTEGNLHGILVGREVF---------PDGI--------LYASRESHYSVFKaaRMYRM-----EAVKVPTLPSGE 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 221 MDLNDLAAKIEQcNANGEQILAIvaTAGTTDAGAIDPLRAIAELAAKQNI-----WVHVDAAWGGALLMSEQYRHYLDGI 295
Cdd:PLN03032 146 IDYDDLERALAK-NRDKPAILNV--NIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGALFGLMMPFVSRAPEVTFR 222

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 643375266 296 ELVDSVTLDFHKQFFQTISCGAFLLKEaRHYELMRYQAAYLNS 338
Cdd:PLN03032 223 KPIGSVSVSGHKFLGCPMPCGVALTRK-KHVKALSQNVEYLNS 264
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 142-307 2.98e-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: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 142 AGVFTSGGTQSNLMGLMLardafFARQGHSVqqdglvgdlrkirvLCSENAHFSVQKNMALMGLGYQSVVQVKTDEfSRM 221
Cdd:cd06502   49 AALFVPSGTAANQLALAA-----HTQPGGSV--------------ICHETAHIYTDEAGAPEFLSGVKLLPVPGEN-GKL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 222 DLNDLAAKIEQCNANGEQILAIVATAGTTDAGAIDP---LRAIAELAAKQNIWVHVD--------AAWGGALlmsEQYRH 290
Cdd:cd06502  109 TPEDLEAAIRPRDDIHFPPPSLVSLENTTEGGTVYPldeLKAISALAKENGLPLHLDgarlanaaAALGVAL---KTYKS 185

                        170
                 ....*....|....*..
gi 643375266 291 YldgielVDSVTLDFHK 307
Cdd:cd06502  186 G------VDSVSFCLSK 196
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
145-276 2.87e-04

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 43.18  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 145 FTSGGTQSNLmglmLARDAFFARQGHsvqqdglvgdlRKIRVLCSENAHFSVQKNMA-LMGLGYqSVVQVKTDEFSRMDL 223
Cdd:PRK02948  65 FTSGGTESNY----LAIQSLLNALPQ-----------NKKHIITTPMEHASIHSYFQsLESQGY-TVTEIPVDKSGLIRL 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 643375266 224 NDLAAKIEQcnangEQILAIVATAgTTDAGAIDPLRAIAELAAKQNIWVHVDA 276
Cdd:PRK02948 129 VDLERAITP-----DTVLASIQHA-NSEIGTIQPIAEIGALLKKYNVLFHSDC 175
SepSecS pfam05889
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ...
 192-310 2.33e-03

O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes.


Pssm-ID: 399111  Cd Length: 389  Bit Score: 40.27  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266  192 AHFSVQKNMALMGLGYQSVVQVKTDEFSRMDLNDLAAKIEQcnANGEQILAIVATAGTTDAGAIDPLRAIAELAAKQNIW 271
Cdd:pfam05889 110 DQKSSIKAAERAGFEPRLVETVLDGDYLITDVNDVETIIEE--KGEEVILAVLSTTSCFAPRSPDNVKEIAKICAEYDVP 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 643375266  272 VHVDAAWGgalLMSEQYRHYLD-GIEL--VDSVTLDFHKQFF 310
Cdd:pfam05889 188 HLVNGAYG---IQSEEYIRKIAaAHKCgrVDAVVQSLDKNFI 226
PLN02263 PLN02263
serine decarboxylase
 143-284 3.22e-03

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 39.80  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643375266 143 GVFTSGGTQSNLMGLMLARDAFfarqghsvqQDGLvgdlrkirVLCSENAHFSVQK--NMALMGlgyqsVVQVKTDEFSR 220
Cdd:PLN02263 155 GYITNCGTEGNLHGILVGREVF---------PDGI--------LYASRESHYSVFKaaRMYRME-----CVKVDTLVSGE 212

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 643375266 221 MDLNDLAAKIEQcNANGEQILAIvaTAGTTDAGAIDPL-RAIAELA----AKQNIWVHVDAAWGGaLLM 284
Cdd:PLN02263 213 IDCADFKAKLLA-NKDKPAIINV--NIGTTVKGAVDDLdLVIKTLEecgfSQDRFYIHCDGALFG-LMM 277
LdcC COG1982
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
242-291 7.33e-03

Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441585 [Multi-domain]  Cd Length: 486  Bit Score: 38.94  E-value: 7.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 643375266 242 AIVATAGTTDaGAIDPLRAIAELAAKQNIWVHVDAAWGGALLMSEQYRHY 291
Cdd:COG1982  164 AVLITNPTYY-GVCYDLKAIAELAHEHGIPVLVDEAHGAHFGFHPDLPRS 212
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH