|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
1-366 |
0e+00 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 739.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 1 SDILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWG 80
Cdd:PLN03032 9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 81 YVTTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVN 160
Cdd:PLN03032 89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 161 IGTTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 241 KEHVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 224006580 321 LERPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECK 366
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVEVR 374
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
41-365 |
3.31e-54 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];
Pssm-ID: 223154 [Multi-domain] Cd Length: 460 Bit Score: 184.88 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 41 NNLGDPFITSNygvhSRQFECSVIDFFAKLWKAePDSYWGYVTTCGTEGNLHGILLARE--CHPDG-----------ILY 107
Cdd:COG0076 88 KNLGDPDESPA----AAELEERVVNMLSDLLGA-PEEASGTFTSGGTEANLLALLAARErwRKRALaesgkpggkpnIVC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 108 SSrETHYSVFKAARYYRMDAKAIPTLP-MGEIDYDALQSEIAKNRDRPVIInVNIGTTVKGAVDNLDRILRILKTLGIPr 186
Cdd:COG0076 163 SE-TAHFSFEKAARYLGLGLRRVPTVPtDYRIDVDALEEAIDENTIGGVVV-GTAGTTDTGSIDDIEELADIAEEYGIW- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 187 erfhIHCDGALFAMMMPFVDWAPEVSFQ-KPIDSIAVSGHKMLGCPMPCGIALTR-KEHVKKVEQKIDYLNS----VDTT 260
Cdd:COG0076 240 ----LHVDAAFGGFLLPFLEPDGRWDFGlEGVDSITVDGHKYGLAPIGCGVVLFRdEEALRRILIFADYYLPgggiPNFT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 261 IMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG------------LTCRLNDLSSTVVLERPMDDA 328
Cdd:COG0076 316 ILGSRPGRQALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGdfelvnepelpiVAFRLKDDEDTLADLSERLDR 395
|
330 340 350
....*....|....*....|....*....|....*..
gi 224006580 329 FIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVEC 365
Cdd:COG0076 396 RGWQVPAQLLPKGLAIVFGTHVTGRQGLKFIVANLLI 432
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
20-303 |
1.59e-34 |
|
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: 130.02 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 20 GYPYNLMYNHEELyEFMKYSINNLGDPFitSNYGVhSRQFECSVIDFFAKLWKAEPDSYWGYVTTCGTEGNLHGILLAR- 98
Cdd:cd06450 4 GFVTTMDPPALLL-EMLTSAKNAIDFTW--DESPA-ATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 99 -------ECHPDGI----LYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDR---PVIINVNIGTT 164
Cdd:cd06450 80 rarkrlkAGGGRGIdklvIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVVATAGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 165 VKGAVDNLDRILRILKTLGIPrerfhIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRkehv 244
Cdd:cd06450 160 DTGAIDPLEEIADLAEKYDLW-----LHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 224006580 245 kkveqkidylnsvdttimgsrngqaALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKI 303
Cdd:cd06450 231 -------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELI 264
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
60-307 |
8.59e-23 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 98.26 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 60 ECSVIDFFAKLWKAePDSYW-----GYVTTCGTEGNLHGILLAR--------ECHPDG---------ILYSSRETHYSVF 117
Cdd:pfam00282 81 ENVVMNWLGEMLGL-PAEFLgqeggGVLQPGSSESNLLALLAARtkwikrmkAAGKPAdssgilaklVAYTSDQAHSSIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 118 KAARYYRMDAKAIPTLPMGEIDYDALQSEIA---KNRDRPVIINVNIGTTVKGAVDNLDRILRILKTLGIPrerfhIHCD 194
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIEedkENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLW-----LHVD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 195 GAL--FAMMMPF-------VDWApevsfqkpiDSIAVSGHKMLGCPMPCGIALTRKEHvkKVEQ----KIDYL----NSV 257
Cdd:pfam00282 235 AAYggSAFICPEfrhwlfgIERA---------DSITFNPHKWMLVLLDCSAVWVKDKE--ALQQafqfNPLYLghtdSAY 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 224006580 258 DT---TIMGSRnGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG 307
Cdd:pfam00282 304 DTghkQIPLSR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDG 355
|
|
| SepCysS |
TIGR02539 |
O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine ... |
100-250 |
5.70e-03 |
|
O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine biosynthesis in the process, happens in Methanocaldococcus jannaschii and several other archaea by misacylation of tRNA(Cys) with O-phosphoserine (Sep), followed by modification of the phosphoserine to cysteine. In some species, direct tRNA-cys aminoacylation also occurs but this pathway is required for Cys biosynthesis. Members of this protein catalyze the second step in this two step pathway, using pyridoxal phosphate and a sulfur donor to synthesize Cys from Sep while attached to the tRNA.
Pssm-ID: 274187 Cd Length: 369 Bit Score: 38.27 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 100 CHPDGILYSSRETHYSVFKAARYYRMDAKAIPTL--PMGEIDYDALQSEIAKNRDRPVIINVNIGTTVKGAVDNL---DR 174
Cdd:TIGR02539 87 CKEGDYVVLDGNAHYTSYVAAERAGLNVAEVPETghPEYKVNPEGYKEVIDEVEDEGKPVGLALLTHVDGEYGNLndaKK 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224006580 175 ILRILKTLGIPrerFHIHCdgALFAMMMPFVDWAPEVSFqkpidsIAVSGHKMLGCPMPCGIALTRKEHVKKVEQK 250
Cdd:TIGR02539 167 VAKICREKGVP---LLLNC--AYTVGRMPVNGKEVKADF------IVGSGHKSMAASAPCGVLAMSEEWEDKVLRT 231
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
1-366 |
0e+00 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 739.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 1 SDILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWG 80
Cdd:PLN03032 9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 81 YVTTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVN 160
Cdd:PLN03032 89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 161 IGTTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 241 KEHVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 224006580 321 LERPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECK 366
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVEVR 374
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
3-369 |
0e+00 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 568.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 3 ILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWGYV 82
Cdd:PLN02263 78 VLARYRKTLVERTKHHLGYPYNLDFDYGALGQLQHFSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWEIEKNEYWGYI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 83 TTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVNIG 162
Cdd:PLN02263 158 TNCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMECVKVDTLVSGEIDCADFKAKLLANKDKPAIINVNIG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 163 TTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRKE 242
Cdd:PLN02263 238 TTVKGAVDDLDLVIKTLEECGFSQDRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRME 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 243 HVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVVLE 322
Cdd:PLN02263 318 HINVLSSNVEYLASRDATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLREAGISAMLNELSSTVVFE 397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 224006580 323 RPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECKNVY 369
Cdd:PLN02263 398 RPKDEEFVRRWQLACQGNIAHVVVMPSVTIEKLDYFLKELVEKRSTW 444
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
4-364 |
4.84e-170 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 479.15 E-value: 4.84e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 4 LASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWGYVT 83
Cdd:PRK02769 11 IEDFWLYLRHNQYFNVGYPEAADFDYSALKRFFSFSINNCGDPYSKSNYPLNSFDFERDVMNFFAELFKIPFNESWGYIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 84 TCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVNIGT 163
Cdd:PRK02769 91 NGGTEGNLYGCYLARELFPDGTLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENKNQPPIIFANIGT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 164 TVKGAVDNLDRILRILKTLGIprERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRKEH 243
Cdd:PRK02769 171 TMTGAIDNIKEIQEILKKIGI--DDYYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFIGSPMPCGIVLAKKKY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 244 VKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVVLER 323
Cdd:PRK02769 249 VERISVDVDYIGSRDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRLQANGIPAWRNPNSITVVFPC 328
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 224006580 324 PmDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVE 364
Cdd:PRK02769 329 P-SERIWKKWHLATSGNQAHIITMPHHNKQQIDSLIDELIF 368
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
41-365 |
3.31e-54 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];
Pssm-ID: 223154 [Multi-domain] Cd Length: 460 Bit Score: 184.88 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 41 NNLGDPFITSNygvhSRQFECSVIDFFAKLWKAePDSYWGYVTTCGTEGNLHGILLARE--CHPDG-----------ILY 107
Cdd:COG0076 88 KNLGDPDESPA----AAELEERVVNMLSDLLGA-PEEASGTFTSGGTEANLLALLAARErwRKRALaesgkpggkpnIVC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 108 SSrETHYSVFKAARYYRMDAKAIPTLP-MGEIDYDALQSEIAKNRDRPVIInVNIGTTVKGAVDNLDRILRILKTLGIPr 186
Cdd:COG0076 163 SE-TAHFSFEKAARYLGLGLRRVPTVPtDYRIDVDALEEAIDENTIGGVVV-GTAGTTDTGSIDDIEELADIAEEYGIW- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 187 erfhIHCDGALFAMMMPFVDWAPEVSFQ-KPIDSIAVSGHKMLGCPMPCGIALTR-KEHVKKVEQKIDYLNS----VDTT 260
Cdd:COG0076 240 ----LHVDAAFGGFLLPFLEPDGRWDFGlEGVDSITVDGHKYGLAPIGCGVVLFRdEEALRRILIFADYYLPgggiPNFT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 261 IMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG------------LTCRLNDLSSTVVLERPMDDA 328
Cdd:COG0076 316 ILGSRPGRQALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGdfelvnepelpiVAFRLKDDEDTLADLSERLDR 395
|
330 340 350
....*....|....*....|....*....|....*..
gi 224006580 329 FIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVEC 365
Cdd:COG0076 396 RGWQVPAQLLPKGLAIVFGTHVTGRQGLKFIVANLLI 432
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
20-303 |
1.59e-34 |
|
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: 130.02 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 20 GYPYNLMYNHEELyEFMKYSINNLGDPFitSNYGVhSRQFECSVIDFFAKLWKAEPDSYWGYVTTCGTEGNLHGILLAR- 98
Cdd:cd06450 4 GFVTTMDPPALLL-EMLTSAKNAIDFTW--DESPA-ATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 99 -------ECHPDGI----LYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDR---PVIINVNIGTT 164
Cdd:cd06450 80 rarkrlkAGGGRGIdklvIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVVATAGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 165 VKGAVDNLDRILRILKTLGIPrerfhIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRkehv 244
Cdd:cd06450 160 DTGAIDPLEEIADLAEKYDLW-----LHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 224006580 245 kkveqkidylnsvdttimgsrngqaALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKI 303
Cdd:cd06450 231 -------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELI 264
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
60-307 |
8.59e-23 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 98.26 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 60 ECSVIDFFAKLWKAePDSYW-----GYVTTCGTEGNLHGILLAR--------ECHPDG---------ILYSSRETHYSVF 117
Cdd:pfam00282 81 ENVVMNWLGEMLGL-PAEFLgqeggGVLQPGSSESNLLALLAARtkwikrmkAAGKPAdssgilaklVAYTSDQAHSSIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 118 KAARYYRMDAKAIPTLPMGEIDYDALQSEIA---KNRDRPVIINVNIGTTVKGAVDNLDRILRILKTLGIPrerfhIHCD 194
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIEedkENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLW-----LHVD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 195 GAL--FAMMMPF-------VDWApevsfqkpiDSIAVSGHKMLGCPMPCGIALTRKEHvkKVEQ----KIDYL----NSV 257
Cdd:pfam00282 235 AAYggSAFICPEfrhwlfgIERA---------DSITFNPHKWMLVLLDCSAVWVKDKE--ALQQafqfNPLYLghtdSAY 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 224006580 258 DT---TIMGSRnGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG 307
Cdd:pfam00282 304 DTghkQIPLSR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDG 355
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
75-236 |
9.32e-08 |
|
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: 53.40 E-value: 9.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 75 PDSYWGYVTTCGTEG-NLHGILLARECHP-DGILYSSREtHYSVF----KAARYYRMDAKAIPTLPMGEIDYDALQSEIa 148
Cdd:pfam00266 59 PSNDEIIFTSGTTEAiNLVALSLGRSLKPgDEIVITEME-HHANLvpwqELAKRTGARVRVLPLDEDGLLDLDELEKLI- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 149 knRDRPVIINVNIGTTVKGAVDNLDRILRILKTLGIprerfHIHCDGALFAMMMPfvdwapeVSFQK-PIDSIAVSGHKM 227
Cdd:pfam00266 137 --TPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGA-----LVLVDAAQAIGHRP-------IDVQKlGVDFLAFSGHKL 202
|
....*....
gi 224006580 228 LGcpmPCGI 236
Cdd:pfam00266 203 YG---PTGI 208
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
80-240 |
5.27e-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: 46.22 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 80 GYVTTCGTEGNLHGILLAREchPDGILYSSRETHYSvfkaaRYYRMDAKA------IPTLPMGEIDYDALQSEIAKNRDR 153
Cdd:cd01494 20 AVFVPSGTGANEAALLALLG--PGDEVIVDANGHGS-----RYWVAAELAgakpvpVPVDDAGYGGLDVAILEELKAKPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 154 PVIINVNIGTTVKGAVDNLDRILRILKTLGIPrerfhIHCDGA--LFAMMMPFVdwapEVSFQkPIDSIAVSGHKMLGCP 231
Cdd:cd01494 93 VALIVITPNTTSGGVLVPLKEIRKIAKEYGIL-----LLVDAAsaGGASPAPGV----LIPEG-GADVVTFSLHKNLGGE 162
|
....*....
gi 224006580 232 MpCGIALTR 240
Cdd:cd01494 163 G-GGVVIVK 170
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
32-305 |
1.22e-04 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 43.93 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 32 LYEFMKYSINNLGDPFITSNygvHSRQFECSVIDFFAKLWKAePDSYW------GYVTTCGTEGNLHGILLARE------ 99
Cdd:PLN02590 147 LGEMLNAGLSVVGFTWLTSP---AATELEIIVLDWLAKLLQL-PDHFLstgnggGVIQGTGCEAVLVVVLAARDrilkkv 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 100 ---CHPDGILYSSRETHYSVFKAA----------RYYRMDAKAIPTLPMGEIDyDALQSEIAKNRdRPVIINVNIGTTVK 166
Cdd:PLN02590 223 gktLLPQLVVYGSDQTHSSFRKACliggiheeniRLLKTDSSTNYGMPPESLE-EAISHDLAKGF-IPFFICATVGTTSS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 167 GAVDNLDRILRILKTLGIprerfHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGI---------- 236
Cdd:PLN02590 301 AAVDPLVPLGNIAKKYGI-----WLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPlwvkdrysli 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224006580 237 -AL-TRKEHVK-KVEQKIDYLNSVDTTIMGSRNGQaALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITE 305
Cdd:PLN02590 376 dALkTNPEYLEfKVSKKDTVVNYKDWQISLSRRFR-SLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQ 446
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
80-232 |
3.33e-04 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 41.93 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 80 GYVTTCGTEGNLhgILLARECHPDGILYSSRETHYSVFKA---ARYYRMDAKAIPTlPMGEIDYDALQSEIAKNRD---- 152
Cdd:cd06502 50 ALFVPSGTAANQ--LALAAHTQPGGSVICHETAHIYTDEAgapEFLSGVKLLPVPG-ENGKLTPEDLEAAIRPRDDihfp 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 153 RPVIINVNIGTTVKG--AVDNLDRILRILKTLGIPrerfhIHCDGALF-----AMMMPFVDWApevsfqKPIDSIAVSGH 225
Cdd:cd06502 127 PPSLVSLENTTEGGTvyPLDELKAISALAKENGLP-----LHLDGARLanaaaALGVALKTYK------SGVDSVSFCLS 195
|
....*..
gi 224006580 226 KMLGCPM 232
Cdd:cd06502 196 KGGGAPV 202
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
81-229 |
7.53e-04 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 41.25 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 81 YVTTCGTEGN---LHGILLARECHPDGILYSSREtHYSVFKAARYYRMDAKAIPTLPM---GEIDYDALQSEIaknrdRP 154
Cdd:PRK02948 64 YFTSGGTESNylaIQSLLNALPQNKKHIITTPME-HASIHSYFQSLESQGYTVTEIPVdksGLIRLVDLERAI-----TP 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224006580 155 VIINVNI--GTTVKGAVDNLDRILRILKTLGIPrerfhIHCDGA-LFAMMmpfvdwaPEVSFQKPIDSIAVSGHKMLG 229
Cdd:PRK02948 138 DTVLASIqhANSEIGTIQPIAEIGALLKKYNVL-----FHSDCVqTFGKL-------PIDVFEMGIDSLSVSAHKIYG 203
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
86-232 |
1.11e-03 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 224919 [Multi-domain] Cd Length: 342 Bit Score: 40.34 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 86 GTEGNLhgILLARECHPDGILYSSRETHYSVFK--AARYYRMDAK-AIPTLPMGEIDYDALQSEIAKN-RDRPV------ 155
Cdd:COG2008 59 GTQANQ--LALAAHCQPGESVICHETAHIYTDEcgAPEFFGGGQKlPIVPGADGKLTPEDVEAAIRPDdIHHAPtplavl 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224006580 156 IINVNIGTTVKgAVDNLDRILRILKTLGIPrerfhIHCDGALFAMMMPFVDwAPEVSFQKPIDSIAVSGHKMLGCPM 232
Cdd:COG2008 137 ENTATEGGTVY-PLDELEAISAVCKEHGLP-----LHMDGARLANALVALG-VALKTIKSYVDSVSFCLTKGGGAPV 206
|
|
| SepCysS |
TIGR02539 |
O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine ... |
100-250 |
5.70e-03 |
|
O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine biosynthesis in the process, happens in Methanocaldococcus jannaschii and several other archaea by misacylation of tRNA(Cys) with O-phosphoserine (Sep), followed by modification of the phosphoserine to cysteine. In some species, direct tRNA-cys aminoacylation also occurs but this pathway is required for Cys biosynthesis. Members of this protein catalyze the second step in this two step pathway, using pyridoxal phosphate and a sulfur donor to synthesize Cys from Sep while attached to the tRNA.
Pssm-ID: 274187 Cd Length: 369 Bit Score: 38.27 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 100 CHPDGILYSSRETHYSVFKAARYYRMDAKAIPTL--PMGEIDYDALQSEIAKNRDRPVIINVNIGTTVKGAVDNL---DR 174
Cdd:TIGR02539 87 CKEGDYVVLDGNAHYTSYVAAERAGLNVAEVPETghPEYKVNPEGYKEVIDEVEDEGKPVGLALLTHVDGEYGNLndaKK 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224006580 175 ILRILKTLGIPrerFHIHCdgALFAMMMPFVDWAPEVSFqkpidsIAVSGHKMLGCPMPCGIALTRKEHVKKVEQK 250
Cdd:TIGR02539 167 VAKICREKGVP---LLLNC--AYTVGRMPVNGKEVKADF------IVGSGHKSMAASAPCGVLAMSEEWEDKVLRT 231
|
|
|