|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
138-501 |
1.07e-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: 341.49 E-value: 1.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 138 RVSGAVYTDrHAEHINLLGKIYEKYAFSNPlhPDVFPGARKMEAELIRMVLNLYNGP-EDSSGSVTSGGTESIIMACFSY 216
Cdd:cd06450 1 FLAGFVTTM-DPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPsEDADGVFTSGGSESNLLALLAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 217 RNRAH-------SLGIEHPVILACKTAHAAFDKAAHLCGMRLRHVPVDSDNRVDLKEMERLIDS------NVCMLVGSAP 283
Cdd:cd06450 78 RDRARkrlkaggGRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 284 NFPSGTIDPIPEIAKLGKKYGIPVHVDACLGGFMIPFMNDAGYlipvfDFRNPGVTSISCDTHKYGCTPKGSSIVMYRSk 363
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL-----DFGIERVDSISVDPHKYGLVPLGCSAVLVRA- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 364 elhhfqyfsvadwcggiyatptiagsragantAVAWATLLSFGRDEYVRRCAQIVKHTRMLAEKIEKIKWIKPYGKSDVS 443
Cdd:cd06450 232 --------------------------------LKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17543922 444 LVAF-----SGNGVNIYEVSDKMMKLG-WNLNTLQ--NPAAIHICLTINQANEEVVNAFAVDLEKI 501
Cdd:cd06450 280 LVCFrlkpsVKLDELNYDLSDRLNERGgWHVPATTlgGPNVLRFVVTNPLTTRDDADALLEDIERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
99-504 |
7.89e-78 |
|
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: 252.45 E-value: 7.89e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 99 DDKDKQFISTLPIAPLSQDSIM-ELAKKYEDYNTfNIDGGRVSGAVY--TDRHAehinLLGKIYEKYAFSNPLHPDVFPG 175
Cdd:COG0076 30 EELRAALDEPLPEEGLPPEEALaELEDLVLPGSV-DWNHPRFLAFVTggTTPAA----LAADLLASALNQNMGDWDTSPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 176 ARKMEAELIRMVLNLYNGPEDSSGSVTSGGTESIIMACFSYRNRA--------HSLGIEHPVILACKTAHAAFDKAAHLC 247
Cdd:COG0076 105 ATELEREVVRWLADLLGLPEGAGGVFTSGGTEANLLALLAARDRAlarrvraeGLPGAPRPRIVVSEEAHSSVDKAARLL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 248 GM---RLRHVPVDSDNRVDLKEMERLID------SNVCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDACLGGFMI 318
Cdd:COG0076 185 GLgrdALRKVPVDEDGRMDPDALEAAIDedraagLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFAL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 319 PFMNdagyLIPVFDfRNPGVTSISCDTHKYGCTPKGSSIVMYRSKELHHFQ-YFSVADW----CGGI-YATPTIAGSRaG 392
Cdd:COG0076 265 PSPE----LRHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAfSFHASYLgpadDGVPnLGDYTLELSR-R 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 393 ANTAVAWATLLSFGRDEYVRRCAQIVKHTRMLAEKIEKIKWIKPYGKSDVSLVAF-------SGNGVNIYEVSDKMMKLG 465
Cdd:COG0076 339 FRALKLWATLRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCFrykpaglDEEDALNYALRDRLRARG 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 17543922 466 --WNLNT-LQNPAAIHICLTINQANEEVVNAFAVDLEKICEE 504
Cdd:COG0076 419 raFLSPTkLDGRVVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| tyr_de_CO2_Arch |
TIGR03812 |
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ... |
115-501 |
2.19e-76 |
|
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: 246.11 E-value: 2.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 115 SQDSIMELAKKYEDYNTfNIDGGRVSGAVYTDRHAEHInllgKIYEKYAFSNPLHPDVFPGARKMEAELIRMVLNLYNGP 194
Cdd:TIGR03812 1 SEEEVLEELKEYRSEDL-KYSDGRILGSMCTNPHPIAV----KAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 195 eDSSGSVTSGGTESIIMACFSYRNRAHSlGIEHPVILACKTAHAAFDKAAHLCGMRLRHVPVDSDNRVDLKEMERLIDSN 274
Cdd:TIGR03812 76 -DAYGYIVSGGTEANIQAVRAAKNLARE-EKRTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 275 VCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDACLGGFMIPFMNDaGYLIPVFDFRNPGVTSISCDTHKYGCTPKG 354
Cdd:TIGR03812 154 TIGIVGIAGTTELGQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKK-GYNPPPFDFSLPGVQSITIDPHKMGLSPIP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 355 SSIVMYRSKELhhFQYFSV-ADWCGGIYATpTIAGSRAGANTAVAWATLLSFGRDEYVRRCAQIVKHTRMLAEKIEKIKw 433
Cdd:TIGR03812 233 AGGILFRSKSY--LKYLSVdAPYLTVKKQA-TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIG- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17543922 434 IKPYGKSDVSLVAFsgNGVNIYEVSDKMMKLGWNLNTLQNPAAIHICLtINQANEEVVNAFAVDLEKI 501
Cdd:TIGR03812 309 FEPVIEPVLNIVAF--EVDDPEEVRKKLRDRGWYVSVTRCPKALRIVV-MPHVTREHIEEFLEDLKEI 373
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
150-433 |
1.70e-20 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 93.57 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 150 EHINLLGKIYEK--YAFSnplhpdvfpgARKMEAELIRMVLNLYNGP-EDSSGSVTSGGTESIIMACFSYRNRahslgie 226
Cdd:PRK02769 45 FSINNCGDPYSKsnYPLN----------SFDFERDVMNFFAELFKIPfNESWGYITNGGTEGNLYGCYLAREL------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 227 HP--VILACKTAHAAFDKAAHLCGMRLRHVPVDSDNRVDLKEMERLIDSN------VCMLVGSAPnfpSGTIDPIPEIAK 298
Cdd:PRK02769 108 FPdgTLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENknqppiIFANIGTTM---TGAIDNIKEIQE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 299 LGKKYGIP---VHVDACLGGFMIPFMNDAgyliPVFDFRNPgVTSISCDTHKYGCTPKGSSIVMYRSKELHHF----QYF 371
Cdd:PRK02769 185 ILKKIGIDdyyIHADAALSGMILPFVNNP----PPFSFADG-IDSIAISGHKFIGSPMPCGIVLAKKKYVERIsvdvDYI 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17543922 372 SVADwcggiyatPTIAGSRAGANTAVAWATLLSFGRDEYVRRCAQIVKHTRMLAEKIEKIKW 433
Cdd:PRK02769 260 GSRD--------QTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRLQANGI 313
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
202-354 |
5.00e-18 |
|
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: 85.87 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 202 TSGGTESIIMA----CFSYRNRAHSL---GIEHPVILACktahaafdkAAHL--CGMRLRHVPVDSDNRVDLKEMERLID 272
Cdd:COG1104 68 TSGGTEANNLAikgaARAYRKKGKHIitsAIEHPAVLET---------ARFLekEGFEVTYLPVDEDGRVDLEALEAALR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 273 SNV----CMLVgsapNFPSGTIDPIPEIAKLGKKYGIPVHVDAC--LGgfmipfmndagyLIPVfDFRNPGVTSISCDTH 346
Cdd:COG1104 139 PDTalvsVMHA----NNETGTIQPIAEIAEIAKEHGVLFHTDAVqaVG------------KIPV-DVKELGVDLLSLSAH 201
|
....*....
gi 17543922 347 K-YGctPKG 354
Cdd:COG1104 202 KiYG--PKG 208
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
187-457 |
2.16e-16 |
|
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: 80.75 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 187 VLNLYNGPEDSSGSVTSGGTESIIMACFSYrnrAHSLGIEHPVILACKTAHAAFDKAAHLC---GMRLRHVPVDSDNRVD 263
Cdd:pfam00266 52 VAEFINAPSNDEIIFTSGTTEAINLVALSL---GRSLKPGDEIVITEMEHHANLVPWQELAkrtGARVRVLPLDEDGLLD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 264 LKEMERLIDSNVCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDACLGgfmIPFMndagyliPVfDFRNPGVTSISC 343
Cdd:pfam00266 129 LDELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA---IGHR-------PI-DVQKLGVDFLAF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 344 DTHK-YGctPKGSSIVMYRS---KELHHFQY----FSVADWCGGIYA---------TPTIAGSrAGANTAVAWATLLSFg 406
Cdd:pfam00266 198 SGHKlYG--PTGIGVLYGRRdllEKMPPLLGgggmIETVSLQESTFAdapwkfeagTPNIAGI-IGLGAALEYLSEIGL- 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17543922 407 rdeyvrrcAQIVKH----TRMLAEKIEKIKWIKPYG-KSDVSLVAFSGNGVNIYEV 457
Cdd:pfam00266 274 --------EAIEKHehelAQYLYERLLSLPGIRLYGpERRASIISFNFKGVHPHDV 321
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
108-430 |
5.51e-16 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 79.77 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 108 TLPIAPLSQDSIMELAKK--------YEDYNTFN-IDGGRVSGAVYTDRHAEHINLLGKIYEKYafsnplhpdvfPGARK 178
Cdd:pfam00282 11 AAPIIPEPELQIDGDIRRnlmpgvttWHSPHFHAyMPTGNSYPSLLGDMLTDAINCNGFTWESS-----------PACTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 179 MEAELIRMVLNLYNGPE-----DSSGSVTSGGTESIIMACFSYR----NRAHSLGIEH--------PVILACKTAHAAFD 241
Cdd:pfam00282 80 LENVVMNWLGEMLGLPAeflgqEGGGVLQPGSSESNLLALLAARtkwiKRMKAAGKPAdssgilakLVAYTSDQAHSSIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 242 KAAHLCGMRLRHVPVDSDNRVDLKEMERLI---DSNVCMLVGSAPNFPS---GTIDPIPEIAKLGKKYGIPVHVDACLGG 315
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIeedKENGLIPFFVVATLGTtgsGAFDDLQELGDICAKHNLWLHVDAAYGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 316 --FMIPFmndagylIPVFDFRNPGVTSISCDTHKYGCTPKGSSIVMYRSKE-LHH---------FQYFSVADwcggiYAT 383
Cdd:pfam00282 240 saFICPE-------FRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEaLQQafqfnplylGHTDSAYD-----TGH 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 17543922 384 PTIAGSRaGANTAVAWATLLSFGRDEY---VRRCAQIVKHtrmLAEKIEK 430
Cdd:pfam00282 308 KQIPLSR-RFRILKLWFVIRSLGVEGLqnqIRRHVELAQY---LEALIRK 353
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
202-465 |
6.12e-16 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 79.80 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 202 TSGGTESIimacfsyrNR-AHSLGIEHP--VILACKTAHAA----FDKAAHLCGMRLRHVPVDSDNRVDLKEMERLIDSN 274
Cdd:COG0520 83 TRGTTEAI--------NLvAYGLGRLKPgdEILITEMEHHSnivpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 275 VCML-VGSAPNFpSGTIDPIPEIAKLGKKYGIPVHVDACLGgfmipfmndAGYLiPVfDfrnpgVTSISCD-----THK- 347
Cdd:COG0520 155 TKLVaVTHVSNV-TGTVNPVKEIAALAHAHGALVLVDGAQS---------VPHL-PV-D-----VQALGCDfyafsGHKl 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 348 YGctPKGSSiVMYRSKELHH----FQY---------FSVADWCGGIY----ATPTIAGsRAGANTAVAWatLLSFGRDEY 410
Cdd:COG0520 218 YG--PTGIG-VLYGKRELLEalppFLGgggmiewvsFDGTTYADLPRrfeaGTPNIAG-AIGLGAAIDY--LEAIGMEAI 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 17543922 411 VRRCAQIvkhTRMLAEKIEKIKWIKPYGKSD----VSLVAFSGNGVNIYEVSDKMMKLG 465
Cdd:COG0520 292 EAREREL---TAYALEGLAAIPGVRILGPADpedrSGIVSFNVDGVHPHDVAALLDDEG 347
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
202-398 |
4.76e-13 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 70.84 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 202 TSGGTES----IIMACFSYRNRA-H--SLGIEHPVILACKTAHAAfdkaahlCGMRLRHVPVDSDNRVDLKEMERLIDSN 274
Cdd:PLN02651 66 TSGATESnnlaIKGVMHFYKDKKkHviTTQTEHKCVLDSCRHLQQ-------EGFEVTYLPVKSDGLVDLDELAAAIRPD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 275 VCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDAC--LGGfmipfmndagylIPVfDFRNPGVTSISCDTHKYGcTP 352
Cdd:PLN02651 139 TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAAqaVGK------------IPV-DVDDLGVDLMSISGHKIY-GP 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17543922 353 KGSSIVMYRSKELHHFQ-YFSVADWCGGIYA----TPTIAGsrAGANTAVA 398
Cdd:PLN02651 205 KGVGALYVRRRPRVRLEpLMSGGGQERGRRSgtenTPLVVG--LGAACELA 253
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
171-458 |
9.84e-12 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 66.72 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 171 DVFPGARKMEAELIrmvlnlyNGPEDSSGSVTSGGTESIIMACFSYRnRAHSLGIE--------HPVILACKTAhaafdk 242
Cdd:cd06453 43 DAYEAAREKVARFI-------NAPSPDEIIFTRNTTEAINLVAYGLG-RANKPGDEivtsvmehHSNIVPWQQL------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 243 aAHLCGMRLRHVPVDSDNRVDLKEMERLIDSNVCML-VGSAPNFpSGTIDPIPEIAKLGKKYGIPVHVDACLggfMIPFM 321
Cdd:cd06453 109 -AERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVaVTHVSNV-LGTINPVKEIGEIAHEAGVPVLVDGAQ---SAGHM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 322 ndagyliPVfDfrnpgVTSISCD-----THK-YGCT----------------PKGSSIVMYRSKELHHFQYfsvadwcGG 379
Cdd:cd06453 184 -------PV-D-----VQDLGCDflafsGHKmLGPTgigvlygkeelleempPYGGGGEMIEEVSFEETTY-------AD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 380 IYA-----TPTIAGsRAGANTAVAWatLLSFGRDEyvrrcaqIVKH----TRMLAEKIEKIKWIKPYGKSD--VSLVAFS 448
Cdd:cd06453 244 LPHkfeagTPNIAG-AIGLGAAIDY--LEKIGMEA-------IAAHehelTAYALERLSEIPGVRVYGDAEdrAGVVSFN 313
|
330
....*....|
gi 17543922 449 GNGVNIYEVS 458
Cdd:cd06453 314 LEGIHPHDVA 323
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
177-354 |
3.40e-09 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 58.97 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 177 RKMEAELIrmvlnlynGPEDSSGSVTSGGTESIIMACFSYRNrAHSLGIEHpvILACKTAHAAFDK-AAHLC--GMRLRH 253
Cdd:PRK02948 49 RKTFAEMI--------GGEEQGIYFTSGGTESNYLAIQSLLN-ALPQNKKH--IITTPMEHASIHSyFQSLEsqGYTVTE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 254 VPVDSDNRVDLKEMERLIDSNVCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDaCLGGFMipfmndagyLIPVfDF 333
Cdd:PRK02948 118 IPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSD-CVQTFG---------KLPI-DV 186
|
170 180
....*....|....*....|..
gi 17543922 334 RNPGVTSISCDTHK-YGctPKG 354
Cdd:PRK02948 187 FEMGIDSLSVSAHKiYG--PKG 206
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
173-310 |
1.89e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 56.16 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 173 FPGARKMEAELIRMVLNLYNGPEDSSGSV--TSGGTESIIMACFSYRNRahslgieHPVILACKTAHAAFDKAAHLCGMR 250
Cdd:pfam00155 38 TDGHPELREALAKFLGRSPVLKLDREAAVvfGSGAGANIEALIFLLANP-------GDAILVPAPTYASYIRIARLAGGE 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17543922 251 LRHVPVDSDN--RVDLKEMERLIDSNVCMLVGSAPNFPSGTIDPIPEIAKLG---KKYGIPVHVD 310
Cdd:pfam00155 111 VVRYPLYDSNdfHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLLdlaKEHNILLLVD 175
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
176-429 |
2.04e-08 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 56.37 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 176 ARKMEAELIRMVLNLYNGPEDSS-GSVTSGGTESIIMACFSYRNRahslgieHP--VILACKTAHAAFDKAAHLCGMRLR 252
Cdd:PLN03032 64 SRQFEVGVLDWFARLWELEKDEYwGYITTCGTEGNLHGILVGREV-------FPdgILYASRESHYSVFKAARMYRMEAV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 253 HVPVDSDNRVDLKEMERLIDSNVCMLVGSAPNFPS---GTIDPIPEIAKLGKKYGIP-----VHVDACLGGFMIPFMNDA 324
Cdd:PLN03032 137 KVPTLPSGEIDYDDLERALAKNRDKPAILNVNIGTtvkGAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSRA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 325 gyliPVFDFRNPgVTSISCDTHKYGCTPKGSSIVMYRSKEL----HHFQYFSVADwcggiyatPTIAGSRAGANTAVAWA 400
Cdd:PLN03032 217 ----PEVTFRKP-IGSVSVSGHKFLGCPMPCGVALTRKKHVkalsQNVEYLNSRD--------ATIMGSRNGHAPLYLWY 283
|
250 260
....*....|....*....|....*....
gi 17543922 401 TLLSFGRDEYVRRCAQIVKHTRMLAEKIE 429
Cdd:PLN03032 284 TLRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
201-437 |
1.31e-06 |
|
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: 50.42 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 201 VTSGGTESIIMACFSYRNRAHSLGIEHPvilacktAHAAFDKAAHLCGMRLRHVPVDSDNR--VDLKEMERLIDSNVCML 278
Cdd:cd00609 64 VTNGAQEALSLLLRALLNPGDEVLVPDP-------TYPGYEAAARLAGAEVVPVPLDEEGGflLDLELLEAAKTPKTKLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 279 VGSAPNFPSGTIDPIPE---IAKLGKKYGIPVHVDACLGGFMipfMNDAGYLIPVFDFRNPGVtsISCDTHkygctpkgs 355
Cdd:cd00609 137 YLNNPNNPTGAVLSEEEleeLAELAKKHGILIISDEAYAELV---YDGEPPPALALLDAYERV--IVLRSF--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 356 sivmyrSKElhhfqyFSVADW-CGGIYATPTIAGSRA---------GANTAVAWAT--LLSFGRDEYVRRCAQIVKHTRM 423
Cdd:cd00609 203 ------SKT------FGLPGLrIGYLIAPPEELLERLkkllpyttsGPSTLSQAAAaaALDDGEEHLEELRERYRRRRDA 270
|
250
....*....|....
gi 17543922 424 LAEKIEKIKWIKPY 437
Cdd:cd00609 271 LLEALKELGPLVVV 284
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
171-379 |
1.49e-06 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 50.52 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 171 DVFPGARKMEAELIrmvlnlyNGPEDSSGSVTSGGTESIIMACFSYrNRAHsLGIEHPVILACKTAHAA---FDKAAHLC 247
Cdd:PLN02855 76 DAYELARKKVAAFI-------NASTSREIVFTRNATEAINLVAYTW-GLAN-LKPGDEVILSVAEHHSNivpWQLVAQKT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 248 GMRLRHVPVDSDNRVDLKEMERLIDSNVCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDACLGgfmIPFMndagyl 327
Cdd:PLN02855 147 GAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQS---VPHM------ 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17543922 328 iPVfDFRNPGVTSISCDTHKYgCTPKGSSIVMYRSKELHhfqyfSVADWCGG 379
Cdd:PLN02855 218 -PV-DVQTLGADFLVASSHKM-CGPTGIGFLWGKSDLLE-----SMPPFLGG 261
|
|
| tyr_amTase_E |
TIGR01264 |
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ... |
202-344 |
3.18e-06 |
|
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273529 [Multi-domain] Cd Length: 401 Bit Score: 49.40 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 202 TSGGTESIIMACFSYRNRAHSLGIEHPVILACKTAHAAFDkaahlCGMRLRHVPVDSDNRVDLKEMERLIDSNVCMLVGS 281
Cdd:TIGR01264 101 CSGCSHAIEMCIAALANAGQNILVPRPGFPLYETLAESMG-----IEVKLYNLLPDKSWEIDLKQLESLIDEKTAALIVN 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17543922 282 APNFPSGTI---DPIPEIAKLGKKYGIPVHVDACLGGFMIPfmnDAGYLiPVFDFrNPGVTSISCD 344
Cdd:TIGR01264 176 NPSNPCGSVfsrQHLEEILAVAERQCLPIIADEIYGDMVFS---GATFE-PLASL-SSTVPILSCG 236
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
180-333 |
3.37e-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: 47.38 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 180 EAELIRMVLNLYNgPEDSSGSVTSGGTESIIMAcfsyrnrAHSLGIEHPVILACKTAHAA--FDKAAhLCGMRLRHVPVD 257
Cdd:cd01494 2 LEELEEKLARLLQ-PGNDKAVFVPSGTGANEAA-------LLALLGPGDEVIVDANGHGSryWVAAE-LAGAKPVPVPVD 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17543922 258 --SDNRVDLKEMERLIDS-NVCMLVGSAPNFPSGTIDPIPEIAKLGKKYGIPVHVDAclgGFMIPFMNDAGYLIPVFDF 333
Cdd:cd01494 73 daGYGGLDVAILEELKAKpNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDA---ASAGGASPAPGVLIPEGGA 148
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
201-344 |
4.80e-06 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 48.88 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 201 VTSGGTESIIMACFSYRNRAHSLGIEHPvilacktAHAAFDKAAHLCGMRLRHVPV--DSDNRVDLKEMERLIDSN-VCM 277
Cdd:TIGR01265 101 LTSGCSQAIEICIEALANPGANILVPRP-------GFPLYDTRAAFSGLEVRLYDLlpEKDWEIDLDGLESLADEKtVAI 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 278 LVGSaPNFPSGTI---DPIPEIAKLGKKYGIPVHVDACLGGFMipfMNDAGYlIPVFDFrNPGVTSISCD 344
Cdd:TIGR01265 174 VVIN-PSNPCGSVfsrDHLQKIAEVAEKLGIPIIADEIYGHMV---FGDAPF-IPMASF-ASIVPVLSLG 237
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
174-315 |
3.50e-05 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 46.63 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 174 PGARKMEAELIRMVLNLYNGPE------DSSGSVTSGGTESIIMACFSYRNRA-HSLG---IEHPVILACKTAHAAFDKA 243
Cdd:PLN02590 166 PAATELEIIVLDWLAKLLQLPDhflstgNGGGVIQGTGCEAVLVVVLAARDRIlKKVGktlLPQLVVYGSDQTHSSFRKA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 244 AHLCGMR---LRHVPVDSDNRVDL--KEMERLIDSN---------VCMLVGSAPnfpSGTIDPIPEIAKLGKKYGIPVHV 309
Cdd:PLN02590 246 CLIGGIHeenIRLLKTDSSTNYGMppESLEEAISHDlakgfipffICATVGTTS---SAAVDPLVPLGNIAKKYGIWLHV 322
|
....*.
gi 17543922 310 DACLGG 315
Cdd:PLN02590 323 DAAYAG 328
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
174-315 |
1.12e-04 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 44.90 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 174 PGARKMEAELIRMVLNLYNGPEDSSGSVTSGG------TESIIMACFSYRNRA-HSLG---IEHPVILACKTAHAAFDKA 243
Cdd:PLN02880 118 PAATELEMIVLDWLAKLLNLPEQFLSTGNGGGviqgtaSEAVLVVLLAARDRVlRKVGknaLEKLVVYASDQTHSALQKA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 244 AHLCGM---RLRHVPVDSDNRVDLKEM-----------ERLIDSNVCMLVGSAPnfpSGTIDPIPEIAKLGKKYGIPVHV 309
Cdd:PLN02880 198 CQIAGIhpeNCRLLKTDSSTNYALAPEllseaistdlsSGLIPFFLCATVGTTS---STAVDPLLELGKIAKSNGMWFHV 274
|
....*.
gi 17543922 310 DACLGG 315
Cdd:PLN02880 275 DAAYAG 280
|
|
| PRK06207 |
PRK06207 |
pyridoxal phosphate-dependent aminotransferase; |
249-310 |
1.58e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235742 Cd Length: 405 Bit Score: 44.37 E-value: 1.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17543922 249 MRLRHVPVDSDNRVDLKEMERLIDSNVCMLVGSAPNFPSGTI---DPIPEIAKLGKKYGIPVHVD 310
Cdd:PRK06207 153 VQLDYLSADKRAGLDLDQLEEAFKAGVRVFLFSNPNNPAGVVysaEEIAQIAALARRYGATVIVD 217
|
|
| SepSecS |
pfam05889 |
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ... |
137-314 |
1.62e-04 |
|
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: 44.12 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 137 GRVSGAVYTDRHAEHINLLGKIyekyafSNPLHPD-VFPGARKMEA---ELIRMVLNLYNGPEDSSGSVTSGGTESIIMA 212
Cdd:pfam05889 17 GRVLTELVTRPHFDFIHGIGRS------GNLLDPQpKALGSSVLAKltnELVKDFLKLLGLREVKNCFVVPLATGMSLAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 213 CFS-YRNRAHSLGIEHPVIlacktAHAAFDKAAHLCGMRLRHVP--VDSDN-RVDLKEMERLI-----DSNVCMLV---G 280
Cdd:pfam05889 91 CLSaLRKRPKAKYVIWPRI-----DQKSSIKAAERAGFEPRLVEtvLDGDYlITDVNDVETIIeekgeEVILAVLSttsC 165
|
170 180 190
....*....|....*....|....*....|....
gi 17543922 281 SAPNFPsgtiDPIPEIAKLGKKYGIPVHVDACLG 314
Cdd:pfam05889 166 FAPRSP----DNVKEIAKICAEYDVPHLVNGAYG 195
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
230-312 |
2.36e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 43.36 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 230 ILACKTAHAAFDK---AAHLCGMRLRHVPVDSDNRVDLKEMERLIDSN----------VCMLVgsAPNFPSGTIDPIP-- 294
Cdd:pfam01212 74 VICGEPAHIHFDEtggHAELGGVQPRPLDGDEAGNMDLEDLEAAIREVgadifpptglISLEN--THNSAGGQVVSLEnl 151
|
90
....*....|....*....
gi 17543922 295 -EIAKLGKKYGIPVHVDAC 312
Cdd:pfam01212 152 rEIAALAREHGIPVHLDGA 170
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
307-429 |
6.81e-04 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 42.50 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 307 VHVDACLGGFMIPFMNDAgyliPVFDFRNPgVTSISCDTHKY-GCtPKGSSIVMYRSKELH----HFQYFSVADwcggiy 381
Cdd:PLN02263 266 IHCDGALFGLMMPFVKRA----PKVTFKKP-IGSVSVSGHKFvGC-PMPCGVQITRMEHINvlssNVEYLASRD------ 333
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17543922 382 atPTIAGSRAGANTAVAWATLLSFGRDEYVRRCAQIVKHTRMLAEKIE 429
Cdd:PLN02263 334 --ATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLR 379
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
248-304 |
7.23e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 42.05 E-value: 7.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17543922 248 GMRLRHVPVDsDNRVDLKEMERLIDSNVCMLVGSAPNFpSGTIDPIPEIAKLGKKYG 304
Cdd:PRK00451 179 GIEVVEVPYE-DGVTDLEALEAAVDDDTAAVVVQYPNF-FGVIEDLEEIAEIAHAGG 233
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
141-311 |
1.34e-03 |
|
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: 41.06 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 141 GAVYTDRHA----EHINLLGKIYEKYAfsnPLHPDVFPGARKMEAELIRMVLNLYnGPEDSSGSVTSGGTESIIMACFSY 216
Cdd:cd00613 26 GSGTYKHNPpaviKRNILENEFYTAYT---PYQPEISQGRLQALFELQTMLCELT-GMDVANASLQDEATAAAEAAGLAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 217 RNRAHslgiEHPVILACKTAH------AAFdkAAHLCGMRLRHVPVDSDNRVDLKEMERLIDSNVCMLVGSAPNFpSGTI 290
Cdd:cd00613 102 IRAYH----KRNKVLVPDSAHptnpavART--RGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNT-LGVF 174
|
170 180
....*....|....*....|..
gi 17543922 291 -DPIPEIAKLGKKYGIPVHVDA 311
Cdd:cd00613 175 eDLIKEIADIAHSAGALVYVDG 196
|
|
| PLN02656 |
PLN02656 |
tyrosine transaminase |
201-331 |
1.38e-03 |
|
tyrosine transaminase
Pssm-ID: 178262 [Multi-domain] Cd Length: 409 Bit Score: 41.06 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 201 VTSGGTESIIMA-CFSYRNRAHslgiehpvILACKTAHAAFDKAAHLCGMRLRHVPVDSDN--RVDLKEMERLIDSNVCM 277
Cdd:PLN02656 101 ITSGCTQAIDVAlSMLARPGAN--------ILLPRPGFPIYELCAAFRHLEVRYVDLLPEKgwEVDLDAVEALADQNTVA 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17543922 278 LVGSAPNFPSGTI---DPIPEIAKLGKKYGIPVHVDACLGGFMI---PF--MNDAGYLIPVF 331
Cdd:PLN02656 173 LVIINPGNPCGNVysyQHLKKIAETAEKLKILVIADEVYGHLAFgsnPFvpMGVFGSIVPVL 234
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
204-310 |
3.32e-03 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 40.12 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17543922 204 GGTESIIMACFSYRNRAHSLGieHPVILACKTAHAAFDKAAHLC---GMRLRHVPVDSDNRVDLKEMERLIDSNVCMLVG 280
Cdd:PRK09295 93 GTTEGINLVANSWGNSNVRAG--DNIIISEMEHHANIVPWQMLCarvGAELRVIPLNPDGTLQLETLPALFDERTRLLAI 170
|
90 100 110
....*....|....*....|....*....|
gi 17543922 281 SAPNFPSGTIDPIPEIAKLGKKYGIPVHVD 310
Cdd:PRK09295 171 THVSNVLGTENPLAEMIALAHQHGAKVLVD 200
|
|
| |
