NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2080418298|ref|XP_042816796|]
View 

sphingosine-1-phosphate lyase 1 isoform X1 [Panthera tigris]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 3.66e-111

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: 335.33  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 146 SGAVYSGEEELTELLVKAYGNFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYRDL 224
Cdd:cd06450     3 AGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 225 AFAN-------GIRTPEIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISR------NTAMLVCSTPQFP 291
Cdd:cd06450    81 ARKRlkagggrGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 292 HGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYpleqpfDFRVKGVTSISADTHKYGYAPKGSSVVLYSdkky 371
Cdd:cd06450   161 TGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 372 rshqffvatdwqggiyasptiagsrpggiSAACWAALMYFGESGYVEATKQIIKTTRFLKSELENIKGIFVFGNPQLSVI 451
Cdd:cd06450   231 -----------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLV 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080418298 452 ALGSR-----DFDIYRLFNLMTAKG-WNLNHLQF--PPSIHFCITLVHTRKRVAIQFLKDIRES 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 3.66e-111

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: 335.33  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 146 SGAVYSGEEELTELLVKAYGNFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYRDL 224
Cdd:cd06450     3 AGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 225 AFAN-------GIRTPEIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISR------NTAMLVCSTPQFP 291
Cdd:cd06450    81 ARKRlkagggrGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 292 HGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYpleqpfDFRVKGVTSISADTHKYGYAPKGSSVVLYSdkky 371
Cdd:cd06450   161 TGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 372 rshqffvatdwqggiyasptiagsrpggiSAACWAALMYFGESGYVEATKQIIKTTRFLKSELENIKGIFVFGNPQLSVI 451
Cdd:cd06450   231 -----------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLV 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080418298 452 ALGSR-----DFDIYRLFNLMTAKG-WNLNHLQF--PPSIHFCITLVHTRKRVAIQFLKDIRES 507
Cdd:cd06450   282 CFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 115-508 1.82e-89

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: 283.26  E-value: 1.82e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 115 ALPVQGLSSSAVLEKLKE-YSSMDVFWQEGKASGAVYSG---EEELTELLVKAYGnfawSNPLHPDIFPGLRKIEAEIVR 190
Cdd:COG0076    39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFAN--------GIRTPEIVAPQSAHAAFDKAANYFGMK---IIRV 259
Cdd:COG0076   115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 260 PLNKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVfmEKAGYPL 333
Cdd:COG0076   195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALP--SPELRHL 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 334 eqpFDfRVKGVTSISADTHKYGYAPKGSSVVLYSDKKYRSHQF-FVATDWQ-----GGIYASPTIAGSRPGGIsAACWAA 407
Cdd:COG0076   273 ---LD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFsFHASYLGpaddgVPNLGDYTLELSRRFRA-LKLWAT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 408 LMYFGESGYVEATKQIIKTTRFLKSELENIKGIFVFGNPQLSVIA-------LGSRDFDIYRLFNLMTAKG--W-NLNHL 477
Cdd:COG0076   348 LRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARGraFlSPTKL 427

                         410       420       430
                  ....*....|....*....|....*....|.
gi 2080418298 478 QFPPSIHFCITLVHTRKRVAIQFLKDIRESV 508
Cdd:COG0076   428 DGRVVLRLVVLNPRTTEDDVDALLDDLREAA 458
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 122-506 5.45e-81

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: 258.43  E-value: 5.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 122 SSSAVLEKLKEYSSMDVFWQEGKASGAVYSGEEELTellVKAYGNFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 201
Cdd:TIGR03812   1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 202 SCGCVTSGGTESILMACKAYRDLAFAnGIRTPEIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNTA 281
Cdd:TIGR03812  77 AYGYIVSGGTEANIQAVRAAKNLARE-EKRTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 282 MLV--CSTPQFphGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYPleQPFDFRVKGVTSISADTHKYGYAPK 359
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNP--PPFDFSLPGVQSITIDPHKMGLSPI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 360 GSSVVLYSDKKYRSH----QFFVATDWQGgiyaspTIAGSRPGGISAACWAALMYFGESGYVEATKQIIKTTRFLKSELE 435
Cdd:TIGR03812 232 PAGGILFRSKSYLKYlsvdAPYLTVKKQA------TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELK 305

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080418298 436 NIKGIFVFgNPQLSVIALGSRDFDIYRLfnLMTAKGWNLNHLQFPPSIHFcITLVHTRKRVAIQFLKDIRE 506
Cdd:TIGR03812 306 KIGFEPVI-EPVLNIVAFEVDDPEEVRK--KLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
PRK02769 PRK02769
histidine decarboxylase; Provisional
 201-504 6.28e-16

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 79.70  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 201 DSCGCVTSGGTESILMACKAYRDLaFANGIrtpeIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNT 280
Cdd:PRK02769   84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 281 ---AMLVCSTPQFPHGILDPVPEVAKLAVRYKIP---LHVDACLGGFLIVFMEKagyplEQPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769  159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 355 GYAPKGSSVVLySDKKYRShQFFVATDWQGGiyASPTIAGSRPGGISAACWAALMYFGESGYVEATKQIIKTTRFLKSEL 434
Cdd:PRK02769  233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 435 ENIkGIFVFGNPQLSVIALGSRDFDIYRLFNLMTAKgwNLNHLqfppsihfcITLVHTRKRVAIQFLKDI 504
Cdd:PRK02769  309 QAN-GIPAWRNPNSITVVFPCPSERIWKKWHLATSG--NQAHI---------ITMPHHNKQQIDSLIDEL 366
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
191-438 1.07e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.75  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYR------------DLAFANGIRTPEIVAPQSAHAAFDKAANYFGMKIIR 258
Cdd:pfam00282  92 LGLPAEFLGQEGGGVLQPGSSESNLLALLAARtkwikrmkaagkPADSSGILAKLVAYTSDQAHSSIEKAALYGGVKLRE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 259 VPLNKMMEVDVRAMRRAISRNTAMLVcsTPQFPHGIL--------DPVPEVAKLAVRYKIPLHVDACLGGFLivFMEkag 330
Cdd:pfam00282 172 IPSDDNGKMRGMDLEKAIEEDKENGL--IPFFVVATLgttgsgafDDLQELGDICAKHNLWLHVDAAYGGSA--FIC--- 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 331 yPLEQPFDFRVKGVTSISADTHKYGYAPKGSSVVLYSDKKYRSHQFFVATDWQGGIYASP-----TIAGSRPGGIsAACW 405
Cdd:pfam00282 245 -PEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLSRRFRI-LKLW 322

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2080418298 406 AALMYFGESGYveaTKQIIKTTRFLKSELENIK 438
Cdd:pfam00282 323 FVIRSLGVEGL---QNQIRRHVELAQYLEALIR 352
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 146-507 3.66e-111

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: 335.33  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 146 SGAVYSGEEELTELLVKAYGNFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYRDL 224
Cdd:cd06450     3 AGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAARDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 225 AFAN-------GIRTPEIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISR------NTAMLVCSTPQFP 291
Cdd:cd06450    81 ARKRlkagggrGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGTTD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 292 HGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYpleqpfDFRVKGVTSISADTHKYGYAPKGSSVVLYSdkky 371
Cdd:cd06450   161 TGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 372 rshqffvatdwqggiyasptiagsrpggiSAACWAALMYFGESGYVEATKQIIKTTRFLKSELENIKGIFVFGNPQLSVI 451
Cdd:cd06450   231 -----------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLSLV 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2080418298 452 ALGSR-----DFDIYRLFNLMTAKG-WNLNHLQF--PPSIHFCITLVHTRKRVAIQFLKDIRES 507
Cdd:cd06450   282 CFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 115-508 1.82e-89

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: 283.26  E-value: 1.82e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 115 ALPVQGLSSSAVLEKLKE-YSSMDVFWQEGKASGAVYSG---EEELTELLVKAYGnfawSNPLHPDIFPGLRKIEAEIVR 190
Cdd:COG0076    39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFAN--------GIRTPEIVAPQSAHAAFDKAANYFGMK---IIRV 259
Cdd:COG0076   115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 260 PLNKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVfmEKAGYPL 333
Cdd:COG0076   195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALP--SPELRHL 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 334 eqpFDfRVKGVTSISADTHKYGYAPKGSSVVLYSDKKYRSHQF-FVATDWQ-----GGIYASPTIAGSRPGGIsAACWAA 407
Cdd:COG0076   273 ---LD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFsFHASYLGpaddgVPNLGDYTLELSRRFRA-LKLWAT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 408 LMYFGESGYVEATKQIIKTTRFLKSELENIKGIFVFGNPQLSVIA-------LGSRDFDIYRLFNLMTAKG--W-NLNHL 477
Cdd:COG0076   348 LRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARGraFlSPTKL 427

                         410       420       430
                  ....*....|....*....|....*....|.
gi 2080418298 478 QFPPSIHFCITLVHTRKRVAIQFLKDIRESV 508
Cdd:COG0076   428 DGRVVLRLVVLNPRTTEDDVDALLDDLREAA 458
tyr_de_CO2_Arch TIGR03812
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ...
 122-506 5.45e-81

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: 258.43  E-value: 5.45e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 122 SSSAVLEKLKEYSSMDVFWQEGKASGAVYSGEEELTellVKAYGNFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 201
Cdd:TIGR03812   1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 202 SCGCVTSGGTESILMACKAYRDLAFAnGIRTPEIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNTA 281
Cdd:TIGR03812  77 AYGYIVSGGTEANIQAVRAAKNLARE-EKRTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 282 MLV--CSTPQFphGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFMEKAGYPleQPFDFRVKGVTSISADTHKYGYAPK 359
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNP--PPFDFSLPGVQSITIDPHKMGLSPI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 360 GSSVVLYSDKKYRSH----QFFVATDWQGgiyaspTIAGSRPGGISAACWAALMYFGESGYVEATKQIIKTTRFLKSELE 435
Cdd:TIGR03812 232 PAGGILFRSKSYLKYlsvdAPYLTVKKQA------TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELK 305

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2080418298 436 NIKGIFVFgNPQLSVIALGSRDFDIYRLfnLMTAKGWNLNHLQFPPSIHFcITLVHTRKRVAIQFLKDIRE 506
Cdd:TIGR03812 306 KIGFEPVI-EPVLNIVAFEVDDPEEVRK--KLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
PRK02769 PRK02769
histidine decarboxylase; Provisional
 201-504 6.28e-16

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 79.70  E-value: 6.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 201 DSCGCVTSGGTESILMACKAYRDLaFANGIrtpeIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNT 280
Cdd:PRK02769   84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 281 ---AMLVCSTPQFPHGILDPVPEVAKLAVRYKIP---LHVDACLGGFLIVFMEKagyplEQPFDFRvKGVTSISADTHKY 354
Cdd:PRK02769  159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 355 GYAPKGSSVVLySDKKYRShQFFVATDWQGGiyASPTIAGSRPGGISAACWAALMYFGESGYVEATKQIIKTTRFLKSEL 434
Cdd:PRK02769  233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 435 ENIkGIFVFGNPQLSVIALGSRDFDIYRLFNLMTAKgwNLNHLqfppsihfcITLVHTRKRVAIQFLKDI 504
Cdd:PRK02769  309 QAN-GIPAWRNPNSITVVFPCPSERIWKKWHLATSG--NQAHI---------ITMPHHNKQQIDSLIDEL 366
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
191-438 1.07e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.75  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 191 IACSLFNGGPDSCGCVTSGGTESILMACKAYR------------DLAFANGIRTPEIVAPQSAHAAFDKAANYFGMKIIR 258
Cdd:pfam00282  92 LGLPAEFLGQEGGGVLQPGSSESNLLALLAARtkwikrmkaagkPADSSGILAKLVAYTSDQAHSSIEKAALYGGVKLRE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 259 VPLNKMMEVDVRAMRRAISRNTAMLVcsTPQFPHGIL--------DPVPEVAKLAVRYKIPLHVDACLGGFLivFMEkag 330
Cdd:pfam00282 172 IPSDDNGKMRGMDLEKAIEEDKENGL--IPFFVVATLgttgsgafDDLQELGDICAKHNLWLHVDAAYGGSA--FIC--- 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 331 yPLEQPFDFRVKGVTSISADTHKYGYAPKGSSVVLYSDKKYRSHQFFVATDWQGGIYASP-----TIAGSRPGGIsAACW 405
Cdd:pfam00282 245 -PEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLSRRFRI-LKLW 322

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2080418298 406 AALMYFGESGYveaTKQIIKTTRFLKSELENIK 438
Cdd:pfam00282 323 FVIRSLGVEGL---QNQIRRHVELAQYLEALIR 352
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 207-452 6.89e-12

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: 67.27  E-value: 6.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 207 TSGGTESILMAckayrdlafANGIRTP-----EIVAPQSAHAA----FDKAANYFGMKIIRVPLNKMMEVDVRAMRRAIS 277
Cdd:pfam00266  67 TSGTTEAINLV---------ALSLGRSlkpgdEIVITEMEHHAnlvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 278 RNTAmLVCSTP-QFPHGILDPVPEVAKLAVRYKIPLHVDAClggflivfmekAGYPlEQPFDFRVKGVTSISADTHKYgY 356
Cdd:pfam00266 138 PKTK-LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-Y 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 357 APKGSSVVLYSDK--------KYRSHQFFVaTDWQGGIYASPTI---AGSRP-GGIsAACWAALMYFGESGYVEATKQII 424
Cdd:pfam00266 204 GPTGIGVLYGRRDllekmpplLGGGGMIET-VSLQESTFADAPWkfeAGTPNiAGI-IGLGAALEYLSEIGLEAIEKHEH 281

                         250       260
                  ....*....|....*....|....*....
gi 2080418298 425 KTTRFLKSELENIKGIFVFGNPQL-SVIA 452
Cdd:pfam00266 282 ELAQYLYERLLSLPGIRLYGPERRaSIIS 310
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 207-360 1.23e-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: 66.61  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 207 TSGGTESILMACKAyrdLAFANGIRTPEIVAPQSAHAAFDKAANYF---GMKIIRVPLNKMMEVDVRAMRRAISRNTA-- 281
Cdd:COG1104    68 TSGGTEANNLAIKG---AARAYRKKGKHIITSAIEHPAVLETARFLekeGFEVTYLPVDEDGRVDLEALEAALRPDTAlv 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 282 --MLVCS-TpqfphGILDPVPEVAKLAVRYKIPLHVDAClggflivfmekagypleQ-----PFDFRVKGVTSISADTHK 353
Cdd:COG1104   145 svMHANNeT-----GTIQPIAEIAEIAKEHGVLFHTDAV-----------------QavgkiPVDVKELGVDLLSLSAHK 202


                  ....*..
gi 2080418298 354 YgYAPKG 360
Cdd:COG1104   203 I-YGPKG 208
PLN03032 PLN03032
serine decarboxylase; Provisional
 182-435 1.28e-08

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 57.14  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 182 RKIEAEIVRIACSLFNGGPDS-CGCVTSGGTESILMACKAYRDlAFANGIrtpeIVAPQSAHAAFDKAANYFGMKIIRVP 260
Cdd:PLN03032   65 RQFEVGVLDWFARLWELEKDEyWGYITTCGTEGNLHGILVGRE-VFPDGI----LYASRESHYSVFKAARMYRMEAVKVP 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 261 LNKMMEVDVRAMRRAISRNT---AMLVCSTPQFPHGILDPVPEVAKLAVRYKIP-----LHVDACLGGFLIVFMEKAgyp 332
Cdd:PLN03032  140 TLPSGEIDYDDLERALAKNRdkpAILNVNIGTTVKGAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSRA--- 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 333 leQPFDFRvKGVTSISADTHKYGYAPKGSSVVLySDKKY-----RSHQFFVATDwqggiyasPTIAGSRPGGISAACWAA 407
Cdd:PLN03032  217 --PEVTFR-KPIGSVSVSGHKFLGCPMPCGVAL-TRKKHvkalsQNVEYLNSRD--------ATIMGSRNGHAPLYLWYT 284

                         250       260
                  ....*....|....*....|....*...
gi 2080418298 408 LMYFGESGYVEATKQIIKTTRFLKSELE 435
Cdd:PLN03032  285 LRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 185-339 7.96e-08

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: 52.38  E-value: 7.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 185 EAEIVRIACSLFNGGpDSCGCVTSGGTESILMACKAYRdlafanGIRTpEIVAPQSAHAA--FDKAA-NYFGMKIIRVPL 261
Cdd:cd01494     2 LEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLALL------GPGD-EVIVDANGHGSryWVAAElAGAKPVPVPVDD 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2080418298 262 NKMMEVDVRAMR-RAISRNTAMLVCSTPQFPHGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFmeKAGYPLEQPFDF 339
Cdd:cd01494    74 AGYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPA--PGVLIPEGGADV 150
GDC-P cd00613
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ...
 235-446 9.68e-08

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: 54.54  E-value: 9.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 235 IVAPQSAH------AAFdkAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNTAMLVCSTPQFpHGIL-DPVPEVAKLAVR 307
Cdd:cd00613   111 VLVPDSAHptnpavART--RGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNT-LGVFeDLIKEIADIAHS 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 308 YKIPLHVDA---CLGGflivfmekagypLEQPFDFrvkGVTSISADTHKYG------------------YAPK--GSSVV 364
Cdd:cd00613   188 AGALVYVDGdnlNLTG------------LKPPGEY---GADIVVGNLQKTGvphggggpgagffavkkeLVRFlpGRLVG 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 365 lYSDKKYRSHQFFVAtdwqggiYASPTIAGSRPGGISAACWA-------ALMY---FGESGYVEATKQIIKTTRFLKSEL 434
Cdd:cd00613   253 -VTKDAEGNRAFRLA-------LQTREQHIRREKATSNICTGqallalmAAMYivyLGPEGLKEIAERAHLNANYLAKRL 324

                         250
                  ....*....|..
gi 2080418298 435 ENIKGIFVFGNP 446
Cdd:cd00613   325 KEVGGVLPFNGP 336
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 205-321 2.15e-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: 53.11  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 205 CVTSGGTESILMACKAYRDlafangiRTPEIVAPQSAHAAFDKAANYFGMKIIRVPL--NKMMEVDVRAMRRAISRNTAM 282
Cdd:cd00609    63 VVTNGAQEALSLLLRALLN-------PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLdeEGGFLLDLELLEAAKTPKTKL 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2080418298 283 LVCSTPQFPHGILDPVPE---VAKLAVRYKIPLHVDACLGGF 321
Cdd:cd00609   136 LYLNNPNNPTGAVLSEEEleeLAELAKKHGILIISDEAYAEL 177
PLN02651 PLN02651
cysteine desulfurase
 207-360 7.05e-07

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 51.58  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 207 TSGGTES----ILMACKAYRDlafangiRTPEIVAPQSAHAAFDKAANYF---GMKIIRVPLNKMMEVDVRAMRRAISRN 279
Cdd:PLN02651   66 TSGATESnnlaIKGVMHFYKD-------KKKHVITTQTEHKCVLDSCRHLqqeGFEVTYLPVKSDGLVDLDELAAAIRPD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 280 TAMLVCSTPQFPHGILDPVPEVAKLAVRYKIPLHVDAClggflivfmEKAGyplEQPFDFRVKGVTSISADTHKYgYAPK 359
Cdd:PLN02651  139 TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA---------QAVG---KIPVDVDDLGVDLMSISGHKI-YGPK 205


                  .
gi 2080418298 360 G 360
Cdd:PLN02651  206 G 206
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
205-315 3.18e-06

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 49.61  E-value: 3.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 205 CVTSGGTESILMAckayrDLAFANGIRtpEIVAPQSAHAAFDKAANYFGMKIIRVPLNKM--MEVDVRAMRRAISRNTAM 282
Cdd:pfam00155  67 VFGSGAGANIEAL-----IFLLANPGD--AILVPAPTYASYIRIARLAGGEVVRYPLYDSndFHLDFDALEAALKEKPKV 139

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2080418298 283 LVCSTPQFPHGILDPVPE---VAKLAVRYKIPLHVD 315
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVD 175
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
207-407 5.75e-06

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 48.57  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 207 TSGGTESILMACKAYRDLAFANG---IRTPeiVAPQSAHAAFDKAANYfGMKIIRVPLNKMMEVDVRAMRRAISRNTAML 283
Cdd:PRK02948   66 TSGGTESNYLAIQSLLNALPQNKkhiITTP--MEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 284 VCSTPQFPHGILDPVPEVAKLAVRYKIPLHVDaCLGGFLIVfmekagypleqPFDFRVKGVTSISADTHKYgYAPKGSSV 363
Cdd:PRK02948  143 SIQHANSEIGTIQPIAEIGALLKKYNVLFHSD-CVQTFGKL-----------PIDVFEMGIDSLSVSAHKI-YGPKGVGA 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2080418298 364 VlYSDKKYRSHQFFVATDWQGGIyasptiagsRPG-----GISAACWAA 407
Cdd:PRK02948  210 V-YINPQVRWKPVFPGTTHEKGF---------RPGtvnvpGIAAFLTAA 248
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
207-317 3.10e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 46.29  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 207 TSGGTESILMACKAYRDLafangirTP--EIVAPQSAHAA----FDKAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNT 280
Cdd:COG0520    83 TRGTTEAINLVAYGLGRL-------KPgdEILITEMEHHSnivpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRT 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2080418298 281 AMLVCStpqfpH-----GILDPVPEVAKLAVRYKIPLHVDAC 317
Cdd:COG0520   156 KLVAVT-----HvsnvtGTVNPVKEIAALAHAHGALVLVDGA 192
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
209-305 2.72e-04

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 43.59  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 209 GGT---ESILMACKAYRdlafangirTPEIVAPQSAHA-AFDKAANYF---GMKIIRVPLNKMMeVDVRAMRRAISRNTA 281
Cdd:PRK00451  137 GATalaEAALMAVRITK---------RKKVLVSGAVHPeYREVLKTYLkgqGIEVVEVPYEDGV-TDLEALEAAVDDDTA 206

                          90       100
                  ....*....|....*....|....
gi 2080418298 282 MLVCSTPQFpHGILDPVPEVAKLA 305
Cdd:PRK00451  207 AVVVQYPNF-FGVIEDLEEIAEIA 229
PLN02590 PLN02590
probable tyrosine decarboxylase
 197-369 6.53e-04

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 42.39  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 197 NGGpdscGCVTSGGTESILMACKAYRDLAFANGIRT--PEIVAPQS--AHAAFDKAANYFGM-----KIIRVPLNKMMEV 267
Cdd:PLN02590  194 NGG----GVIQGTGCEAVLVVVLAARDRILKKVGKTllPQLVVYGSdqTHSSFRKACLIGGIheeniRLLKTDSSTNYGM 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 268 DVRAMRRAISRNTA-----MLVCST-PQFPHGILDPVPEVAKLAVRYKIPLHVDACLGGFLIVFmekagyPLEQPFDFRV 341
Cdd:PLN02590  270 PPESLEEAISHDLAkgfipFFICATvGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIC------PEYRKFIDGI 343

                         170       180
                  ....*....|....*....|....*...
gi 2080418298 342 KGVTSISADTHKYGYAPKGSSVVLYSDK 369
Cdd:PLN02590  344 ENADSFNMNAHKWLFANQTCSPLWVKDR 371
GcvP2 COG1003
Glycine cleavage system protein P (pyridoxal-binding), C-terminal domain [Amino acid transport ...
 215-304 4.41e-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: 39.63  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 215 LMACKAYRDlafANG--IRTpEIVAPQSAH---AAfdkAANYFGMKIIRVPLNKMMEVDVRAMRRAISRNTA--MLVC-S 286
Cdd:COG1003   126 LLAIRAYHE---SRGegHRN-EILIPDSAHgtnPA---SAAMAGFKVVVVKSDEDGNVDLEDLKAKVGDRTAalMLTNpS 198

                          90
                  ....*....|....*....
gi 2080418298 287 TpqfpHGILDP-VPEVAKL 304
Cdd:COG1003   199 T----HGVFEEdIKEICDI 213
PRK09105 PRK09105
pyridoxal phosphate-dependent aminotransferase;
220-304 8.27e-03

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181651  Cd Length: 370  Bit Score: 38.87  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080418298 220 AYRDLAFANgiRTPEIVAPQSAHAAFDKAANYFGMKIIRVPLNKMMEVDVRAMRRAiSRNTAMLVCSTPQFPHGILDPVP 299
Cdd:PRK09105  109 NYAVLAFTS--PTAGLVTADPTYEAGWRAADAQGAPVAKVPLRADGAHDVKAMLAA-DPNAGLIYICNPNNPTGTVTPRA 185


                  ....*
gi 2080418298 300 EVAKL 304
Cdd:PRK09105  186 DIEWL 190
 
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