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Conserved domains on  [gi|1907074168|ref|XP_036011604|]
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sphingosine-1-phosphate lyase 1 isoform X1 [Mus musculus]

Protein Classification

aspartate aminotransferase family protein( domain architecture ID 10157828)

aspartate aminotransferase family protein is a pyridoxal phosphate (PLP)-dependent enzyme similar to cysteine sulfinic acid decarboxylase that catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine, and taurine, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 146-507 9.40e-113

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: 339.56  E-value: 9.40e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 146 SGAVYNGEPKLTELLVQAYGEFTWSNPlhPDIFPGLRKLEAEIVRMTCSLFNGGP-DSCGCVTSGGTESILMACKAYRDL 224
Cdd:cd06450     3 AGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 225 ALE-------KGIKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISR------NTAMLVCSTPQFP 291
Cdd:cd06450    81 ARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 292 HGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYplekpfDFRVKGVTSISADTHKYGYAPKGSSVVMYSneky 371
Cdd:cd06450   161 TGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 372 rtyqffvgadwqggvyaspsiagsrpggiIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVI 451
Cdd:cd06450   231 -----------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLV 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074168 452 ALGSN-----DFDIYRLSNMMSAKG-WNFNYLQFPR--SIHFCITLVHTRKRVAIQFLKDIRES 507
Cdd:cd06450   282 CFRLKpsvklDELNYDLSDRLNERGgWHVPATTLGGpnVLRFVVTNPLTTRDDADALLEDIERA 345
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 146-507 9.40e-113

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: 339.56  E-value: 9.40e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 146 SGAVYNGEPKLTELLVQAYGEFTWSNPlhPDIFPGLRKLEAEIVRMTCSLFNGGP-DSCGCVTSGGTESILMACKAYRDL 224
Cdd:cd06450     3 AGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 225 ALE-------KGIKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISR------NTAMLVCSTPQFP 291
Cdd:cd06450    81 ARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 292 HGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYplekpfDFRVKGVTSISADTHKYGYAPKGSSVVMYSneky 371
Cdd:cd06450   161 TGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 372 rtyqffvgadwqggvyaspsiagsrpggiIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVI 451
Cdd:cd06450   231 -----------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLV 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074168 452 ALGSN-----DFDIYRLSNMMSAKG-WNFNYLQFPR--SIHFCITLVHTRKRVAIQFLKDIRES 507
Cdd:cd06450   282 CFRLKpsvklDELNYDLSDRLNERGgWHVPATTLGGpnVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 115-508 1.61e-92

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: 291.35  E-value: 1.61e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 115 TLPAQGMGTAEVLERLKE-YSSMDGSWQEGKASGAVYNGePKLTELLVQAYGEFTWSNPLHPDIFPGLRKLEAEIVRMTC 193
Cdd:COG0076    39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGG-TTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 194 SLFNGGPDSCGCVTSGGTESILMACKAYRDLALEK--------GIKTPEIVAPESAHAAFDKAAHYFGMK---IVRVALK 262
Cdd:COG0076   118 DLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKVPVD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 263 KNMEVDVQAMKRAISR------NTAMLVCSTPQFPHGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVfmEKAGYPLekp 336
Cdd:COG0076   198 EDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALP--SPELRHL--- 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 337 FDfRVKGVTSISADTHKYGYAPKGSSVVMYSNEKYRTYQFFVGAD-----WQGGV-YASPSIAGSRPGGIIAAcWAALMH 410
Cdd:COG0076   273 LD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASylgpaDDGVPnLGDYTLELSRRFRALKL-WATLRA 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 411 FGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVIA-------LGSNDFDIYRLSNMMSAKG--------WNFN 475
Cdd:COG0076   351 LGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARGraflsptkLDGR 430

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1907074168 476 YlqfprSIHFCITLVHTRKRVAIQFLKDIRESV 508
Cdd:COG0076   431 V-----VLRLVVLNPRTTEDDVDALLDDLREAA 458
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 125-506 1.44e-78

tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274796  Cd Length: 373  Bit Score: 252.27  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 125 EVLERLKEYSSMDGSWQEGKASGAVYNgepKLTELLVQAYGEFTWSNPLHPDIFPGLRKLEAEIVRMTCSLFNGgPDSCG 204
Cdd:TIGR03812   4 EVLEELKEYRSEDLKYSDGRILGSMCT---NPHPIAVKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PDAYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 205 CVTSGGTESILMACKAYRDLALEKGiKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTAMLV 284
Cdd:TIGR03812  80 YIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTIGIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 285 --CSTPQFphGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYPLekPFDFRVKGVTSISADTHKYGYAPKGSS 362
Cdd:TIGR03812 159 giAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPIPAG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 363 VVMYSNEKYRTYqFFVGADW-QGGVYAspSIAGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIF 441
Cdd:TIGR03812 235 GILFRSKSYLKY-LSVDAPYlTVKKQA--TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGFEP 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074168 442 IFgDPQLSVIALGSNDFDiyRLSNMMSAKGWNFNYLQFPRSIHFcITLVHTRKRVAIQFLKDIRE 506
Cdd:TIGR03812 312 VI-EPVLNIVAFEVDDPE--EVRKKLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 207-459 2.53e-13

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: 71.51  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 207 TSGGTESILMACKAYRDlALEKGiktPEIVAPESAHAA----FDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTAm 282
Cdd:pfam00266  67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMEHHAnlvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 283 LVCSTP-QFPHGVMDPVPEVAKLAVRYKIPLHVDAClggflivfmekAGYPlEKPFDFRVKGVTSISADTHKYgYAPKGS 361
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 362 SVVMYSN---EKYRTYQFFVG----ADWQGGVYASPSI---AGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLK 431
Cdd:pfam00266 209 GVLYGRRdllEKMPPLLGGGGmietVSLQESTFADAPWkfeAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLY 288

                         250       260
                  ....*....|....*....|....*....
gi 1907074168 432 SELENIKNIFIFGDPQL-SVIALGSNDFD 459
Cdd:pfam00266 289 ERLLSLPGIRLYGPERRaSIISFNFKGVH 317
PRK02769 PRK02769
histidine decarboxylase; Provisional
 201-437 5.29e-10

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 61.60  E-value: 5.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 201 DSCGCVTSGGTESILMACKAYRDLalekgIKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNT 280
Cdd:PRK02769   84 ESWGYITNGGTEGNLYGCYLAREL-----FPDGTLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 281 ---AMLVCSTPQFPHGVMDPVPEVAKLAVRYKIP---LHVDACLGGFLIVFMEKagyplEKPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769  159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 355 GYAPKGSSVVMySNEKYrTYQFFVGADWQGGvyASPSIAGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSEL 434
Cdd:PRK02769  233 IGSPMPCGIVL-AKKKY-VERISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308


                  ...
gi 1907074168 435 ENI 437
Cdd:PRK02769  309 QAN 311
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 146-507 9.40e-113

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: 339.56  E-value: 9.40e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 146 SGAVYNGEPKLTELLVQAYGEFTWSNPlhPDIFPGLRKLEAEIVRMTCSLFNGGP-DSCGCVTSGGTESILMACKAYRDL 224
Cdd:cd06450     3 AGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 225 ALE-------KGIKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISR------NTAMLVCSTPQFP 291
Cdd:cd06450    81 ARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 292 HGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYplekpfDFRVKGVTSISADTHKYGYAPKGSSVVMYSneky 371
Cdd:cd06450   161 TGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 372 rtyqffvgadwqggvyaspsiagsrpggiIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVI 451
Cdd:cd06450   231 -----------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLV 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074168 452 ALGSN-----DFDIYRLSNMMSAKG-WNFNYLQFPR--SIHFCITLVHTRKRVAIQFLKDIRES 507
Cdd:cd06450   282 CFRLKpsvklDELNYDLSDRLNERGgWHVPATTLGGpnVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 115-508 1.61e-92

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: 291.35  E-value: 1.61e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 115 TLPAQGMGTAEVLERLKE-YSSMDGSWQEGKASGAVYNGePKLTELLVQAYGEFTWSNPLHPDIFPGLRKLEAEIVRMTC 193
Cdd:COG0076    39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGG-TTPAALAADLLASALNQNMGDWDTSPAATELEREVVRWLA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 194 SLFNGGPDSCGCVTSGGTESILMACKAYRDLALEK--------GIKTPEIVAPESAHAAFDKAAHYFGMK---IVRVALK 262
Cdd:COG0076   118 DLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKVPVD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 263 KNMEVDVQAMKRAISR------NTAMLVCSTPQFPHGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVfmEKAGYPLekp 336
Cdd:COG0076   198 EDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALP--SPELRHL--- 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 337 FDfRVKGVTSISADTHKYGYAPKGSSVVMYSNEKYRTYQFFVGAD-----WQGGV-YASPSIAGSRPGGIIAAcWAALMH 410
Cdd:COG0076   273 LD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASylgpaDDGVPnLGDYTLELSRRFRALKL-WATLRA 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 411 FGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVIA-------LGSNDFDIYRLSNMMSAKG--------WNFN 475
Cdd:COG0076   351 LGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARGraflsptkLDGR 430

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1907074168 476 YlqfprSIHFCITLVHTRKRVAIQFLKDIRESV 508
Cdd:COG0076   431 V-----VLRLVVLNPRTTEDDVDALLDDLREAA 458
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 125-506 1.44e-78

tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274796  Cd Length: 373  Bit Score: 252.27  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 125 EVLERLKEYSSMDGSWQEGKASGAVYNgepKLTELLVQAYGEFTWSNPLHPDIFPGLRKLEAEIVRMTCSLFNGgPDSCG 204
Cdd:TIGR03812   4 EVLEELKEYRSEDLKYSDGRILGSMCT---NPHPIAVKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PDAYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 205 CVTSGGTESILMACKAYRDLALEKGiKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTAMLV 284
Cdd:TIGR03812  80 YIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTIGIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 285 --CSTPQFphGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYPLekPFDFRVKGVTSISADTHKYGYAPKGSS 362
Cdd:TIGR03812 159 giAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPIPAG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 363 VVMYSNEKYRTYqFFVGADW-QGGVYAspSIAGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIF 441
Cdd:TIGR03812 235 GILFRSKSYLKY-LSVDAPYlTVKKQA--TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGFEP 311

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907074168 442 IFgDPQLSVIALGSNDFDiyRLSNMMSAKGWNFNYLQFPRSIHFcITLVHTRKRVAIQFLKDIRE 506
Cdd:TIGR03812 312 VI-EPVLNIVAFEVDDPE--EVRKKLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 207-459 2.53e-13

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: 71.51  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 207 TSGGTESILMACKAYRDlALEKGiktPEIVAPESAHAA----FDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTAm 282
Cdd:pfam00266  67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMEHHAnlvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 283 LVCSTP-QFPHGVMDPVPEVAKLAVRYKIPLHVDAClggflivfmekAGYPlEKPFDFRVKGVTSISADTHKYgYAPKGS 361
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 362 SVVMYSN---EKYRTYQFFVG----ADWQGGVYASPSI---AGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLK 431
Cdd:pfam00266 209 GVLYGRRdllEKMPPLLGGGGmietVSLQESTFADAPWkfeAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLY 288

                         250       260
                  ....*....|....*....|....*....
gi 1907074168 432 SELENIKNIFIFGDPQL-SVIALGSNDFD 459
Cdd:pfam00266 289 ERLLSLPGIRLYGPERRaSIISFNFKGVH 317
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
167-452 3.37e-13

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 71.29  E-value: 3.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 167 FTWsnplhpDIFPGLRKLEAEIVRMTCSLFN-----GGPDSCGCVTSGGTESILMACKAYR------------DLALEKG 229
Cdd:pfam00282  69 FTW------ESSPACTELENVVMNWLGEMLGlpaefLGQEGGGVLQPGSSESNLLALLAARtkwikrmkaagkPADSSGI 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 230 IKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRN-----TAMLVCSTPQFP-HGVMDPVPEVAK 303
Cdd:pfam00282 143 LAKLVAYTSDQAHSSIEKAALYGGVKLREIPSDDNGKMRGMDLEKAIEEDkenglIPFFVVATLGTTgSGAFDDLQELGD 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 304 LAVRYKIPLHVDACLGGFLivFMEkagyPLEKPFDFRVKGVTSISADTHKYGYAPKGSSVVMYSNEKYRTYQFFVGADWQ 383
Cdd:pfam00282 223 ICAKHNLWLHVDAAYGGSA--FIC----PEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYL 296

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907074168 384 GGVYASP-----SIAGSRpGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKNIFIFGDPQLSVIA 452
Cdd:pfam00282 297 GHTDSAYdtghkQIPLSR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGLGLVC 369
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 207-450 1.55e-11

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: 66.23  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 207 TSGGTESILMACKAyrdLALEKGIKTPEIVAPESAHAAFDKAAHYF---GMKIVRVALKKNMEVDVQAMKRAISRNTA-- 281
Cdd:COG1104    68 TSGGTEANNLAIKG---AARAYRKKGKHIITSAIEHPAVLETARFLekeGFEVTYLPVDEDGRVDLEALEAALRPDTAlv 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 282 --MLVCS-TpqfphGVMDPVPEVAKLAVRYKIPLHVDAC--LGgflivfmekagypleK-PFDFRVKGVTSISADTHKYg 355
Cdd:COG1104   145 svMHANNeT-----GTIQPIAEIAEIAKEHGVLFHTDAVqaVG---------------KiPVDVKELGVDLLSLSAHKI- 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 356 YAPKGSSvVMYSNEKYRTYQFFVGADWQGGVyaspsiagsRPG-----GIIA---ACWAALMHF-GENGYVEATKQiikt 426
Cdd:COG1104   204 YGPKGVG-ALYVRKGVRLEPLIHGGGQERGL---------RSGtenvpGIVGlgkAAELAAEELeEEAARLRALRD---- 269

                         250       260
                  ....*....|....*....|....
gi 1907074168 427 aRFLKSELENIKNIFIFGDPQLSV 450
Cdd:COG1104   270 -RLEEGLLAAIPGVVINGDPENRL 292
PRK02769 PRK02769
histidine decarboxylase; Provisional
 201-437 5.29e-10

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 61.60  E-value: 5.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 201 DSCGCVTSGGTESILMACKAYRDLalekgIKTPEIVAPESAHAAFDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNT 280
Cdd:PRK02769   84 ESWGYITNGGTEGNLYGCYLAREL-----FPDGTLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 281 ---AMLVCSTPQFPHGVMDPVPEVAKLAVRYKIP---LHVDACLGGFLIVFMEKagyplEKPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769  159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 355 GYAPKGSSVVMySNEKYrTYQFFVGADWQGGvyASPSIAGSRPGGIIAACWAALMHFGENGYVEATKQIIKTARFLKSEL 434
Cdd:PRK02769  233 IGSPMPCGIVL-AKKKY-VERISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308


                  ...
gi 1907074168 435 ENI 437
Cdd:PRK02769  309 QAN 311
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 124-446 1.28e-07

Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.


Pssm-ID: 99737 [Multi-domain]  Cd Length: 398  Bit Score: 54.16  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 124 AEVLERLKEYSSMDGSWQEGK---ASGAvYNGEPKLTELLVQAYGEFTWSNPLH-PDIFPGLRKLEAEIVRMTCSLfNGG 199
Cdd:cd00613     2 TEVLRHLKRLASKNKALDQSMsflGSGT-YKHNPPAVIKRNILENEFYTAYTPYqPEISQGRLQALFELQTMLCEL-TGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 200 PDSCGCVTSGGT---ESILMAC---KAYRDlalekgiktpEIVAPESAH------AAFdkAAHYFGMKIVRVALKKNMEV 267
Cdd:cd00613    80 DVANASLQDEATaaaEAAGLAAiraYHKRN----------KVLVPDSAHptnpavART--RGEPLGIEVVEVPSDEGGTV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 268 DVQAMKRAISRNTAMLVCSTPQFpHGVM-DPVPEVAKLAVRYKIPLHVDA---CLGGflivfmekagypLEKPFDFrvkG 343
Cdd:cd00613   148 DLEALKEEVSEEVAALMVQYPNT-LGVFeDLIKEIADIAHSAGALVYVDGdnlNLTG------------LKPPGEY---G 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 344 VTSISADTHKYG------------------YAPK------GSSVVMYSNEKYR-TYQffvgADWQGGV---------YAS 389
Cdd:cd00613   212 ADIVVGNLQKTGvphggggpgagffavkkeLVRFlpgrlvGVTKDAEGNRAFRlALQ----TREQHIRrekatsnicTGQ 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074168 390 PSIAgsrpggIIAACWAALMhfGENGYVEATKQIIKTARFLKSELENIKNIFIFGDP 446
Cdd:cd00613   288 ALLA------LMAAMYIVYL--GPEGLKEIAERAHLNANYLAKRLKEVGGVLPFNGP 336
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 205-321 1.84e-07

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 53.50  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 205 CVTSGGTESILMACKAYrdlaLEKGiktPEIVAPESAHAAFDKAAHYFGMKIVRVALKKN--MEVDVQAMKRAISRNTAM 282
Cdd:cd00609    63 VVTNGAQEALSLLLRAL----LNPG---DEVLVPDPTYPGYEAAARLAGAEVVPVPLDEEggFLLDLELLEAAKTPKTKL 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907074168 283 LVCSTPQFPHG-VMDP--VPEVAKLAVRYKIPLHVDACLGGF 321
Cdd:cd00609   136 LYLNNPNNPTGaVLSEeeLEELAELAKKHGILIISDEAYAEL 177
PLN02651 PLN02651
cysteine desulfurase
 207-360 3.36e-07

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 52.73  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 207 TSGGTESILMACKAYRDLALEKgikTPEIVAPESAH-AAFDKAAHYF--GMKIVRVALKKNMEVDVQAMKRAISRNTAML 283
Cdd:PLN02651   66 TSGATESNNLAIKGVMHFYKDK---KKHVITTQTEHkCVLDSCRHLQqeGFEVTYLPVKSDGLVDLDELAAAIRPDTALV 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074168 284 VCSTPQFPHGVMDPVPEVAKLAVRYKIPLHVDAClggflivfmEKAGyplEKPFDFRVKGVTSISADTHKYgYAPKG 360
Cdd:PLN02651  143 SVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA---------QAVG---KIPVDVDDLGVDLMSISGHKI-YGPKG 206
PLN02590 PLN02590
probable tyrosine decarboxylase
 197-362 4.19e-07

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 52.79  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 197 NGGpdscGCVTSGGTESILMACKAYRDLALEKGIKT--PEIVA--PESAHAAFDKAA-----HYFGMKIVRVALKKNMEV 267
Cdd:PLN02590  194 NGG----GVIQGTGCEAVLVVVLAARDRILKKVGKTllPQLVVygSDQTHSSFRKACliggiHEENIRLLKTDSSTNYGM 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 268 DVQAMKRAISRNTA-----MLVCST-PQFPHGVMDPVPEVAKLAVRYKIPLHVDACLGGFLIVFmekagyPLEKPFDFRV 341
Cdd:PLN02590  270 PPESLEEAISHDLAkgfipFFICATvGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIC------PEYRKFIDGI 343

                         170       180
                  ....*....|....*....|.
gi 1907074168 342 KGVTSISADTHKYGYAPKGSS 362
Cdd:PLN02590  344 ENADSFNMNAHKWLFANQTCS 364
PLN03032 PLN03032
serine decarboxylase; Provisional
 182-435 8.79e-07

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 51.37  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 182 RKLEAEIVRMTCSLFNGGPDS-CGCVTSGGTES----ILMACKAYRDlalekGIktpeIVAPESAHAAFDKAAHYFGMKI 256
Cdd:PLN03032   65 RQFEVGVLDWFARLWELEKDEyWGYITTCGTEGnlhgILVGREVFPD-----GI----LYASRESHYSVFKAARMYRMEA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 257 VRVALKKNMEVDVQAMKRAISRNT---AMLVCSTPQFPHGVMDPVPEVAKLAVRYKIP-----LHVDACLGGFLIVFMEK 328
Cdd:PLN03032  136 VKVPTLPSGEIDYDDLERALAKNRdkpAILNVNIGTTVKGAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSR 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 329 A-GYPLEKPFDfrvkgvtSISADTHKYGYAPKGSSVVM----YSNEKYRTYQFFVGADwqggvyasPSIAGSRPGGIIAA 403
Cdd:PLN03032  216 ApEVTFRKPIG-------SVSVSGHKFLGCPMPCGVALtrkkHVKALSQNVEYLNSRD--------ATIMGSRNGHAPLY 280

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1907074168 404 CWAALMHFGENGYVEATKQIIKTARFLKSELE 435
Cdd:PLN03032  281 LWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
205-315 1.03e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 51.15  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 205 CVTSGGTESILMACKayrdLALEKGiktPEIVAPESAHAAFDKAAHYFGMKIVRVALK--KNMEVDVQAMKRAISRNTAM 282
Cdd:pfam00155  67 VFGSGAGANIEALIF----LLANPG---DAILVPAPTYASYIRIARLAGGEVVRYPLYdsNDFHLDFDALEAALKEKPKV 139

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907074168 283 LVCSTPQFPHGVMDPVPE---VAKLAVRYKIPLHVD 315
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVD 175
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
207-317 1.40e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 50.91  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 207 TSGGTESILMACKAYRDLalEKGiktPEIVAPESAHAA----FDKAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTAM 282
Cdd:COG0520    83 TRGTTEAINLVAYGLGRL--KPG---DEILITEMEHHSnivpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKL 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907074168 283 LVCStpqfpH-----GVMDPVPEVAKLAVRYKIPLHVDAC 317
Cdd:COG0520   158 VAVT-----HvsnvtGTVNPVKEIAALAHAHGALVLVDGA 192
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 184-316 1.78e-06

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: 48.15  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 184 LEAEIVRMTCSLFNGGpDSCGCVTSGGTESILMACKAYrdlaLEKGiktPEIVAPESAHAA--FDKAA-HYFGMKIVRVA 260
Cdd:cd01494     1 KLEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLAL----LGPG---DEVIVDANGHGSryWVAAElAGAKPVPVPVD 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907074168 261 LKKNMEVDVQAM-KRAISRNTAMLVCSTPQFPHGVMDPVPEVAKLAVRYKIPLHVDA 316
Cdd:cd01494    73 DAGYGGLDVAILeELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDA 129
PLN02880 PLN02880
tyrosine decarboxylase
 197-320 5.01e-04

tyrosine decarboxylase


Pssm-ID: 215475 [Multi-domain]  Cd Length: 490  Bit Score: 42.97  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 197 NGGpdscGCVTSGGTESILMACKAYRDLALEKGIKTP----EIVAPESAHAAFDKAAHYFGM-----KIVRVALKKNMEV 267
Cdd:PLN02880  146 NGG----GVIQGTASEAVLVVLLAARDRVLRKVGKNAleklVVYASDQTHSALQKACQIAGIhpencRLLKTDSSTNYAL 221

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907074168 268 DVQAMKRAISRNTA-----MLVCST-PQFPHGVMDPVPEVAKLAVRYKIPLHVDACLGG 320
Cdd:PLN02880  222 APELLSEAISTDLSsglipFFLCATvGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAG 280
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 206-312 7.16e-04

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 42.03  E-value: 7.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 206 VTSGGTESILMACKAYrdlaLEKGiktPEIVAPESAHAAFDKAAHYFGMKIVRVALK--KNMEVDVQAMKRAISRNTAML 283
Cdd:PRK05764   96 VTTGAKQALYNAFMAL----LDPG---DEVIIPAPYWVSYPEMVKLAGGVPVFVPTGeeNGFKLTVEQLEAAITPKTKAL 168

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907074168 284 VCSTPQFPHG-VMDP--VPEVAKLAVRYKIPL 312
Cdd:PRK05764  169 ILNSPSNPTGaVYSPeeLEAIADVAVEHDIWV 200
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
207-414 7.34e-04

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 42.02  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 207 TSGGTESILMACKAYRDLALEKG---IKTPeiVAPESAHAAFDKAAHYfGMKIVRVALKKNMEVDVQAMKRAISRNTAML 283
Cdd:PRK02948   66 TSGGTESNYLAIQSLLNALPQNKkhiITTP--MEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 284 VCSTPQFPHGVMDPVPEVAKLAVRYKIPLHVDaCLGGFLIVfmekagyplekPFDFRVKGVTSISADTHKYgYAPKGSSV 363
Cdd:PRK02948  143 SIQHANSEIGTIQPIAEIGALLKKYNVLFHSD-CVQTFGKL-----------PIDVFEMGIDSLSVSAHKI-YGPKGVGA 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907074168 364 VmYSNEKYRTYQFFVGADWQGGVyaspsiagsRPGGI----IAACWAALMHFGEN 414
Cdd:PRK02948  210 V-YINPQVRWKPVFPGTTHEKGF---------RPGTVnvpgIAAFLTAAENILKN 254
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
209-305 8.94e-04

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 42.05  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 209 GGT---ESILMACKAYrdlalekgiKTPEIVAPESAHAAFDKA----AHYFGMKIVRVALKKNMeVDVQAMKRAISRNTA 281
Cdd:PRK00451  137 GATalaEAALMAVRIT---------KRKKVLVSGAVHPEYREVlktyLKGQGIEVVEVPYEDGV-TDLEALEAAVDDDTA 206

                          90       100
                  ....*....|....*....|....
gi 1907074168 282 MLVCSTPQFpHGVMDPVPEVAKLA 305
Cdd:PRK00451  207 AVVVQYPNF-FGVIEDLEEIAEIA 229
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 215-304 1.07e-03

Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain is part of the Pathway/BioSystem: Glycine cleavage


Pssm-ID: 440627  Cd Length: 468  Bit Score: 41.56  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 215 LMACKAY--------RDlalekgiktpEIVAPESAH---AAfdkAAHYFGMKIVRVALKKNMEVDVQAMKRAISRNTA-- 281
Cdd:COG1003   126 LLAIRAYhesrgeghRN----------EILIPDSAHgtnPA---SAAMAGFKVVVVKSDEDGNVDLEDLKAKVGDRTAal 192

                          90       100
                  ....*....|....*....|....*
gi 1907074168 282 MLVC-STpqfpHGVMDP-VPEVAKL 304
Cdd:COG1003   193 MLTNpST----HGVFEEdIKEICDI 213
SepSecS pfam05889
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ...
 206-319 4.39e-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: 39.49  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 206 VTSGGTESILMACKayrdLALEKGIKTPEIVAPESAHAAFDKAAHY--FGMKIVRVALKKN-MEVDVQAMKRAISR---N 279
Cdd:pfam05889  79 VVPLATGMSLALCL----SALRKRPKAKYVIWPRIDQKSSIKAAERagFEPRLVETVLDGDyLITDVNDVETIIEEkgeE 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907074168 280 TAMLVCSTPQ-FPHGVMDPVPEVAKLAVRYKIPLHVDACLG 319
Cdd:pfam05889 155 VILAVLSTTScFAPRSPDNVKEIAKICAEYDVPHLVNGAYG 195
PRK08361 PRK08361
aspartate aminotransferase; Provisional
 206-310 8.80e-03

aspartate aminotransferase; Provisional


Pssm-ID: 236248 [Multi-domain]  Cd Length: 391  Bit Score: 38.71  E-value: 8.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907074168 206 VTSGGTESILMACKAYrdlaLEKGiktPEIVAPESAHAAFDKAAHYFGMKIVRVALKK--NMEVDVQAMKRAISRNTAML 283
Cdd:PRK08361   98 VTAGAYEATYLAFESL----LEEG---DEVIIPDPAFVCYVEDAKIAEAKPIRIPLREenEFQPDPDELLELITKRTRMI 170

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907074168 284 VCSTPQFPHGVM---DPVPEVAKLAVRYKI 310
Cdd:PRK08361  171 VINYPNNPTGATldkEVAKAIADIAEDYNI 200
 
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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