|
Name |
Accession |
Description |
Interval |
E-value |
| am_tr_V_EF2568 |
TIGR01977 |
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal ... |
2-373 |
5.87e-172 |
|
cysteine desulfurase family protein; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family. Related families contain members active as cysteine desulfurases, selenocysteine lyases, or both. The members of this family form a distinct clade and all are shorter at the N-terminus. The function of this subfamily is unknown. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 131032 [Multi-domain] Cd Length: 376 Bit Score: 484.19 E-value: 5.87e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTWPKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEALNLGLK 81
Cdd:TIGR01977 1 IYFDNAATTYPKPDEVYEAMADFYKNYGGSPGRGRYRLALRASREVEETRQLLAKLFNAPSSAHVVFTNNATTALNIALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 82 GLLKPGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLQTSvQEGL-HPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEI 159
Cdd:TIGR01977 81 GLLKEGDHVITTPMEHNSVARPLECLKEQiGVEITIVKCD-NEGLiSPERIKRAIKTNTKLIVVSHASNVTGTILPIEEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 160 GRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQGTGGLYLREDLQLDTLKEGGTGANSEEPFQPEES 239
Cdd:TIGR01977 160 GELAQENGIFFILDAAQTAGVIPIDMTELAIDMLAFTGHKGLLGPQGTGGLYIREGIKLKPLKSGGTGSHSALIDQPSEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 240 PERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVILYGPNPSVERAPVISINLEGREPSEV 319
Cdd:TIGR01977 240 PDRFESGTLNTPGIAGLNAGIKFIEKIGIANIAKKECMLTEKLLNGLREINKVKIYGPADPANRVGVVSFTVEGIDSEEV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 518687961 320 SYLLDKLYGIASRPGLHCAPDAHRTLGTFKQGTVRLSLGYFNTSQEVEKCLDAV 373
Cdd:TIGR01977 320 ADILDEKFDIATRTGLHCAPLAHKTIGTFATGTIRLSLGYFNTEEEIEKLLEAL 373
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
2-373 |
3.19e-161 |
|
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: 456.93 E-value: 3.19e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTWPKPECVYEAVDQClRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEA---LNL 78
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYY-RHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAinlVAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 79 GLKGLLKPGDHVITSSLEHNAVTRPLEKLRS-QGVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIG 157
Cdd:cd06453 80 GLGRANKPGDEIVTSVMEHHSNIVPWQQLAErTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 158 EIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGlLGPQGTGGLYLREDLQLDTLKEGGTGANSE----EP 233
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKM-LGPTGIGVLYGKEELLEEMPPYGGGGEMIEevsfEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 234 FQPEESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVILYGPNPsvERAPVISINLEG 313
Cdd:cd06453 239 TTYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAE--DRAGVVSFNLEG 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 314 REPSEVSYLLDKlYGIASRPGLHCAPDAHRtlGTFKQGTVRLSLGYFNTSQEVEKCLDAV 373
Cdd:cd06453 317 IHPHDVATILDQ-YGIAVRAGHHCAQPLMR--RLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| Sec_lyase_SclA |
NF040779 |
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is ... |
2-378 |
1.96e-126 |
|
selenocysteine lyase SclA; In bacteria, selenocysteine lyase activity (EC 4.4.1.16) usually is seen as a secondary activity of a cysteine desulfurase (EC 2.8.1.7). However, SclA, as studied in Enterococcus faecalis, acts primary on selenocysteine, binding cysteine just as well but acting on cysteine with much lower catalytic efficiency.
Pssm-ID: 468734 [Multi-domain] Cd Length: 378 Bit Score: 368.63 E-value: 1.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTWPKPECVYEAVDQCLR-NKGANPSRSghFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEALNLGL 80
Cdd:NF040779 1 VYLNHAATSNHKFEATIQALCAYLQeNNNLNTNRG--LQGLDELGLAFETRQALADFFHAPDPAHVIFTANATTSLNMVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 81 KGLLKPGDHVITSSLEHNAVTRPLEKLRS-QGVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEI 159
Cdd:NF040779 79 NGLLKPGDHVLTTSVEHNAVARPLHLLETeQNVSVTYLPCEKDGQLDPEQIEAAIRPETKVLVMTHASNVLGTILPVKEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 160 GRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQGTGGLYLREDL--QLDTLKEGGTGANSEEPFQPE 237
Cdd:NF040779 159 FKIAKKHGIITVLDSAQTAGFLPIDMEEMSIDVLAFTGHKSLMGLAGIGGFALAKNIekKIDPWLTGGTGSASLSLEQPD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 238 ESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPgVILYGPNPSVERAPVISINLEGREPS 317
Cdd:NF040779 239 FLPDKFEPGTPNTLGILSLKSSVKAIQELGLEKIQAHERALTARFLTGLKELP-VTILGTKDAAQSVPVVSITAPGIDSG 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518687961 318 EVSYLLDKLYGIASRPGLHCAPDAHRTLGTFKQGTVRLSLGYFNTSQEVEKCLDAVARLSS 378
Cdd:NF040779 318 ELAQQLFDRYGIITRSGLHCAPLAHQTAGTLKTGAVRFSFGWNTTAEEIDYTLSALKEILS 378
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
2-376 |
2.56e-123 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 361.38 E-value: 2.56e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTwPKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEA--LNLG 79
Cdd:COG0520 17 VYLDNAATG-QKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEIIFTRGTTEAinLVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 80 LKGLLKPGDHVITSSLEHNAVTRP-LEKLRSQGVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGE 158
Cdd:COG0520 96 GLGRLKPGDEILITEMEHHSNIVPwQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 159 IGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDLqLDTLK----EGGTGAN-SEEP 233
Cdd:COG0520 176 IAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHK-LYGPTGIGVLYGKREL-LEALPpflgGGGMIEWvSFDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 234 FQPEESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVILYGPNPSVERAPVISINLEG 313
Cdd:COG0520 254 TTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGPADPEDRSGIVSFNVDG 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518687961 314 REPSEVSYLLDKlYGIASRPGLHCAPDAHRTLGTfkQGTVRLSLGYFNTSQEVEKCLDAVARL 376
Cdd:COG0520 334 VHPHDVAALLDD-EGIAVRAGHHCAQPLMRRLGV--PGTVRASFHLYNTEEEIDRLVEALKKL 393
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
2-368 |
1.56e-104 |
|
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: 312.64 E-value: 1.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTwPKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEA---LNL 78
Cdd:pfam00266 1 IYLDSAATT-QKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAinlVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 79 GLKGLLKPGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIG 157
Cdd:pfam00266 80 SLGRSLKPGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 158 EIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDL--QLDTLKEGGTGAN--SEEP 233
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLleKMPPLLGGGGMIEtvSLQE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 234 FQPEESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVILYGPNpsvERAPVISINLEG 313
Cdd:pfam00266 239 STFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE---RRASIISFNFKG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 518687961 314 REPSEVSYLLDKlYGIASRPGLHCAPDAHRTLGtfKQGTVRLSLGYFNTSQEVEK 368
Cdd:pfam00266 316 VHPHDVATLLDE-SGIAVRSGHHCAQPLMVRLG--LGGTVRASFYIYNTQEDVDR 367
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-376 |
3.25e-85 |
|
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: 263.45 E-value: 3.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 1 MIYFDNAATTWPKPEcVYEAVDQCLRNKGANPSrSGHFMALLAGQIVLNARGEIAEFFNIsDPLQVVFTPNATEAL---- 76
Cdd:COG1104 3 MIYLDNAATTPVDPE-VLEAMLPYLTEYFGNPS-SLHSFGREARAALEEAREQVAALLGA-DPEEIIFTSGGTEANnlai 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 77 NLGLKGLLKPGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQTSvQEG-LHPEQVEAAIQNNTKLIVLSHASNVMGLIHP 155
Cdd:COG1104 80 KGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVD-EDGrVDLEALEAALRPDTALVSVMHANNETGTIQP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 156 IGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDLQLDTLKEGGTganseepfQ 235
Cdd:COG1104 159 IAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHK-IYGPKGVGALYVRKGVRLEPLIHGGG--------Q 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 236 peespER-YESGTLNTPGIAGLGAGIEFIKQEgIEKIREKERSLTRQLMLGLSE-IPGVILYGpnPSVERAP-VISINLE 312
Cdd:COG1104 230 -----ERgLRSGTENVPGIVGLGKAAELAAEE-LEEEAARLRALRDRLEEGLLAaIPGVVING--DPENRLPnTLNFSFP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 313 GREPSEVSYLLDkLYGIA-----------SRP-------GLHcAPDAHrtlgtfkqGTVRLSLGYFNTSQEVEKCLDAVA 374
Cdd:COG1104 302 GVEGEALLLALD-LAGIAvssgsacssgsLEPshvllamGLD-EELAH--------GSIRFSLGRFTTEEEIDRAIEALK 371
|
..
gi 518687961 375 RL 376
Cdd:COG1104 372 EI 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
1-372 |
7.64e-73 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 233.10 E-value: 7.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 1 MIYFDNAATTwPKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEALNLGL 80
Cdd:PLN02855 33 LVYLDNAATS-QKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSREIVFTRNATEAINLVA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 81 ----KGLLKPGDHVITSSLEHNAVTRPLEKLRSQG------VEVTKlqtsvQEGLHPEQVEAAIQNNTKLIVLSHASNVM 150
Cdd:PLN02855 112 ytwgLANLKPGDEVILSVAEHHSNIVPWQLVAQKTgavlkfVGLTP-----DEVLDVEQLKELLSEKTKLVATHHVSNVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 151 GLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDLQ------------- 217
Cdd:PLN02855 187 GSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHK-MCGPTGIGFLWGKSDLLesmppflgggemi 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 218 LDTLKEGGTGAnseepfqpeESPERYESGtlnTPGIA---GLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVIL 294
Cdd:PLN02855 266 SDVFLDHSTYA---------PPPSRFEAG---TPAIGeaiGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 295 YGPNPS--VERAPVISINLEGREPSEVSYLLDKLYGIASRPGLHCAPDAHRTLGTfkQGTVRLSLGYFNTSQEVEKCLDA 372
Cdd:PLN02855 334 YGPKPSegVGRAALCAFNVEGIHPTDLSTFLDQQHGVAIRSGHHCAQPLHRYLGV--NASARASLYFYNTKEEVDAFIHA 411
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-376 |
6.19e-62 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 204.21 E-value: 6.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 1 MIYFDNAATTwPKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEALNLGL 80
Cdd:PRK09295 24 LAYLDSAASA-QKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAEELVFVRGTTEGINLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 81 ----KGLLKPGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHP 155
Cdd:PRK09295 103 nswgNSNVRAGDNIIISEMEHHANIVPWQMLCARvGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 156 IGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDLqLDTLK--EGGtGA----- 228
Cdd:PRK09295 183 LAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEAL-LQEMPpwEGG-GSmiatv 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 229 NSEEPFQPEESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVILYGPNpsvERAPVIS 308
Cdd:PRK09295 260 SLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGPQ---NRLGVIA 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 309 INLEGREPSEVSYLLDKlYGIASRPGLHCApdahRTLGTFKQ--GTVRLSLGYFNTSQEVEKCLDAVARL 376
Cdd:PRK09295 337 FNLGKHHAYDVGSFLDN-YGIAVRTGHHCA----MPLMAYYNvpAMCRASLAMYNTHEEVDRLVAGLQRI 401
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
2-367 |
8.36e-58 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 192.18 E-value: 8.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTWPKPEcVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNiSDPLQVVFTPNATE----ALN 77
Cdd:PLN02651 1 LYLDMQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIG-ADPKEIIFTSGATEsnnlAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 78 LGLKGLLKPGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQTSvQEGL-HPEQVEAAIQNNTKLIVLSHASNVMGLIHPI 156
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVK-SDGLvDLDELAAAIRPDTALVSVMAVNNEIGVIQPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 157 GEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLR--EDLQLDTLKEGGTganseepf 234
Cdd:PLN02651 158 EEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHK-IYGPKGVGALYVRrrPRVRLEPLMSGGG-------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 235 qpEESPERyeSGTLNTPGIAGLGAGIEFIKQEGiEKIREKERSLTRQLMLGL-SEIPGVILYGPNPSVERAP-VISINLE 312
Cdd:PLN02651 229 --QERGRR--SGTENTPLVVGLGAACELAMKEM-DYDEKHMKALRERLLNGLrAKLGGVRVNGPRDPEKRYPgTLNLSFA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518687961 313 GREpSEVsyLLDKLYGIASRPGLHC-APDAH-----RTLG---TFKQGTVRLSLGYFNTSQEVE 367
Cdd:PLN02651 304 YVE-GES--LLMGLKEVAVSSGSACtSASLEpsyvlRALGvpeEMAHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
2-373 |
3.89e-56 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 189.00 E-value: 3.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTwPKPECVYEAVDQCLRNKG--ANP-SRSgHFMALLAGQIVLNARGEIAEFFNiSDPLQVVFTPNATE---- 74
Cdd:PRK14012 5 IYLDYSATT-PVDPRVAEKMMPYLTMDGtfGNPaSRS-HRFGWQAEEAVDIARNQIADLIG-ADPREIVFTSGATEsdnl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 75 ALNLGLKGLLKPGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIH 154
Cdd:PRK14012 82 AIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 155 PIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLRED--LQLDTLKEGGtgansee 232
Cdd:PRK14012 162 DIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHK-IYGPKGIGALYVRRKprVRLEAQMHGG------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 233 pfqpeeSPER-YESGTLNTPGIAGLGAGIEFIKQEgIEKIREKERSLTRQLMLGLSEIPGVILygpNPSVE-RAPV---I 307
Cdd:PRK14012 234 ------GHERgMRSGTLPTHQIVGMGEAARIAKEE-MATENERIRALRDRLWNGIKDIEEVYL---NGDLEqRVPGnlnV 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518687961 308 SIN-LEGREpsevsyLLDKLYGIASRPGLHCAPDAH------RTLGT---FKQGTVRLSLGYFNTSQEVEKCLDAV 373
Cdd:PRK14012 304 SFNyVEGES------LIMALKDLAVSSGSACTSASLepsyvlRALGLndeLAHSSIRFSLGRFTTEEEIDYAIELV 373
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
2-375 |
8.91e-54 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 182.93 E-value: 8.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTWpKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEALNLGLK 81
Cdd:PRK10874 21 VYLDSAATAL-KPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPDAKNIVWTRGTTESINLVAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 82 GLL----KPGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLqtSVQEGLHP--EQVEAAIQNNTKLIVLSHASNVMGLIH 154
Cdd:PRK10874 100 SYArprlQPGDEIIVSEAEHHANLVPWLMVAQQtGAKVVKL--PLGADRLPdvDLLPELITPRTRILALGQMSNVTGGCP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 155 PIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDL--QLDTLKEGG---TGAN 229
Cdd:PRK10874 178 DLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHK-LYGPTGIGVLYGKSELleAMSPWQGGGkmlTEVS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 230 SEEpFQPEESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIPGVILYgpnpsveRAP---V 306
Cdd:PRK10874 257 FDG-FTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRSF-------RCQdssL 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518687961 307 ISINLEGREPSEVSYLLDKlYGIASRPGLHCAPDAHRTLGTfkQGTVRLSLGYFNTSQEVEKCLDAVAR 375
Cdd:PRK10874 329 LAFDFAGVHHSDLVTLLAE-YGIALRAGQHCAQPLLAALGV--TGTLRASFAPYNTQSDVDALVNAVDR 394
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
2-373 |
1.37e-51 |
|
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273906 [Multi-domain] Cd Length: 397 Bit Score: 176.87 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTwPKPECVYEAVDQCLRNKGANPSRSgHFMALLAGQIVLNARGEIAEFFNISDPlQVVFTPNATEAL---NL 78
Cdd:TIGR01976 19 VFFDNPAGT-QIPQSVADAVSAALTRSNANRGGA-YESSRRADQVVDDAREAVADLLNADPP-EVVFGANATSLTfllSR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 79 GLKGLLKPGDHVITSSLEHNAVTRP-LEKLRSQGVEVTKLQTSVQEG-LHPEQVEAAIQNNTKLIVLSHASNVMGLIHPI 156
Cdd:TIGR01976 96 AISRRWGPGDEVIVTRLDHEANISPwLQAAERAGAKVKWARVDEATGeLHPDDLASLLSPRTRLVAVTAASNTLGSIVDL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 157 GEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQgTGGLYLREDLqLDTLKeggtgaNSEEPFQP 236
Cdd:TIGR01976 176 AAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYK-FFGPH-MGILWGRPEL-LMNLP------PYKLTFSY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 237 EESPERYESGTLNTPGIAGLGAGIEFIKQ--------------EGIEKIREKERSLTRQLMLGLSEIPGVILYGPNPSVE 302
Cdd:TIGR01976 247 DTGPERFELGTPQYELLAGVVAAVDYLAGlgesangsrrerlvASFQAIDAYENRLAEYLLVGLSDLPGVTLYGVARLAA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518687961 303 RAPVISINLEGREPSEVSYLLDKLyGIASRPGLHCAPDAHRTLG-TFKQGTVRLSLGYFNTSQEVEKCLDAV 373
Cdd:TIGR01976 327 RVPTVSFTVHGLPPQRVVRRLADQ-GIDAWAGHFYAVRLLRRLGlNDEGGVVRVGLAHYNTAEEVDRLLEAL 397
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
2-376 |
1.46e-39 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 148.46 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTwPKPECVYEAVDQCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNISDPLQVVFTPNATEA----LN 77
Cdd:NF041166 247 VWFDNAATT-QKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVDEIIFVRGTTEAinlvAK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 78 LGLKGLLKPGDHVITSSLEHNAVTRPLE--------KLRSQGV---------EVTKLQTSvqeglhpeqveaaiqnNTKL 140
Cdd:NF041166 326 SWGRQNIGAGDEIIVSHLEHHANIVPWQqlaqetgaKLRVIPVddsgqilldEYAKLLNP----------------RTKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 141 IVLSHASNVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDLqLDT 220
Cdd:NF041166 390 VSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHK-VFGPTGIGVVYGKRDL-LEA 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 221 LK--EGgtGAN-------SEEPFQPeeSPERYESGTLNtpgIA---GLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSE 288
Cdd:NF041166 468 MPpwQG--GGNmiadvtfEKTVYQP--APNRFEAGTGN---IAdavGLGAALDYVERIGIENIARYEHDLLEYATAGLAE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 289 IPGVILYGPNPsvERAPVISINLEGREPSEVSYLLDKlYGIASRPGLHCAPDAHRTLGTfkQGTVRLSLGYFNTSQEVEK 368
Cdd:NF041166 541 VPGLRLIGTAA--DKASVLSFVLDGYSTEEVGKALNQ-EGIAVRSGHHCAQPILRRFGV--EATVRPSLAFYNTCEEVDA 615
|
....*...
gi 518687961 369 CLDAVARL 376
Cdd:NF041166 616 LVAVLRRL 623
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
1-381 |
8.53e-35 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 131.78 E-value: 8.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 1 MIYFDNAATTwpkPECVyEAVD--QCLRNKGANPSRSGHFMALLAGQIVLNARGEIAEFFNiSDPLQVVFTPNATE---- 74
Cdd:PRK02948 1 MIYLDYAATT---PMSK-EALQtyQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIG-GEEQGIYFTSGGTEsnyl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 75 ALNLGLKGLLKPGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQTSVQEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIH 154
Cdd:PRK02948 76 AIQSLLNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 155 PIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKgLLGPQGTGGLYLREDLqldtlkeggtganSEEPF 234
Cdd:PRK02948 156 PIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHK-IYGPKGVGAVYINPQV-------------RWKPV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 235 QPEESPER-YESGTLNTPGIAGLGAGIEFIKQEgIEKIREKERSLTRQLMLGLSEIPGVILYGPNPSVERAPVISINLEG 313
Cdd:PRK02948 222 FPGTTHEKgFRPGTVNVPGIAAFLTAAENILKN-MQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKG 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518687961 314 REPSEVSYLLDKlYGIASRPGLHCAPDAHRTLGTFK---------QGTVRLSLGYFNTSQEVEKCLDAVARLSSSNK 381
Cdd:PRK02948 301 IEGQYTMLECNR-RGIAISTGSACQVGKQEPSKTMLaigktyeeaKQFVRFSFGQQTTKDQIDTTIHALETIGNQFY 376
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
111-375 |
1.50e-19 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 88.99 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 111 GVEVTKLQTSVQEGLHPEQVEAAIQNNT--KLIVLSHA--SNvmGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQ 186
Cdd:COG0075 97 GAEVVVLEVPWGEAVDPEEVEEALAADPdiKAVAVVHNetST--GVLNPLEEIGALAKEHGALLIVDAVSSLGGVPLDMD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 187 AMGIDLLVFAGHKGLLGPQGTG------------------GLYLreDL--QLDTLKEGGTganseePFqpeesperyesg 246
Cdd:COG0075 175 EWGIDVVVSGSQKCLMLPPGLAfvavseraleaiearklpSYYL--DLklWLKYWEKGQT------PY------------ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 247 TLNTPGIAGLGAGIEFIKQEGIEKIREKERSLTRQLMLGLSEIpGVILYGPNPSveRAPVI-SINL-EGREPSEV-SYLL 323
Cdd:COG0075 235 TPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEAL-GLELFAEEEY--RSPTVtAVRVpEGVDAAALrKRLK 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518687961 324 DKlYGIASRPGlhcapdahrtLGTFKQGTVRLS-LGYfNTSQEVEKCLDAVAR 375
Cdd:COG0075 312 ER-YGIEIAGG----------LGPLKGKIFRIGhMGY-VNPEDVLRTLAALEE 352
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
54-213 |
8.02e-15 |
|
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: 71.64 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 54 IAEFFNISDPlQVVFTPNATEALNLGLKGLLKPGDHVITSSLEHnaVTRPLEKLRSQGVEVTKLQTSVQE--GLHPEQVE 131
Cdd:cd01494 9 LARLLQPGND-KAVFVPSGTGANEAALLALLGPGDEVIVDANGH--GSRYWVAAELAGAKPVPVPVDDAGygGLDVAILE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 132 -AAIQNNTKLIVLSHASNVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIP---IDVQAMGIDLLVFAGHKGLLGPqGT 207
Cdd:cd01494 86 eLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSLHKNLGGE-GG 164
|
....*.
gi 518687961 208 GGLYLR 213
Cdd:cd01494 165 GVVIVK 170
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
54-336 |
1.56e-13 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 71.17 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 54 IAEFFNISDPLQVVFTPNATEALNLGLKGLLKPGDHVITSSLEHNAvTRPLEKLRSQGVEVTKLQTSVQEGLHPEQVEAA 133
Cdd:cd06451 41 LRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVGVNGVFG-DRWADMAERYGADVDVVEKPWGEAVSPEEIAEA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 134 I-QNNTKLIVLSHASNVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQGTG---- 208
Cdd:cd06451 120 LeQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGpiaf 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 209 ---------------GLYLREDLQLDTLKEGGtganseepfqpeesperyesGTLNTPGIA---GLGAGIEFIKQEGIEK 270
Cdd:cd06451 200 seralerikkktkpkGFYFDLLLLLKYWGEGY--------------------SYPHTPPVNllyALREALDLILEEGLEN 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518687961 271 IREKERSLTRQLMLGLSEIpGVILYgPNPSvERAPVISINL--EGREPSEVSYLLDKLYGIASRPGLH 336
Cdd:cd06451 260 RWARHRRLAKALREGLEAL-GLKLL-AKPE-LRSPTVTAVLvpEGVDGDEVVRRLMKRYNIEIAGGLG 324
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
2-375 |
1.15e-11 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 66.43 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 2 IYFDNAATTWPKPECVYEAVDQCLRNKGANP-SRSGHFMAllAGQIVLNARGEIAEFFNIS-DPLQVVFTPNATEALNLG 79
Cdd:PLN02724 36 VYLDHAGATLYSESQLEAALADFSSNVYGNPhSQSDSSMR--SSDTIESARQQVLEYFNAPpSDYACVFTSGATAALKLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 80 LKGLL-KPGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQ-TSVQEGLHPEQVE-----AAIQNNTKLIVLSHAS----- 147
Cdd:PLN02724 114 GETFPwSSESHFCYTLENHNSVLGIREYALEKGAAAIAVDiEEAANQPTNSQGSvvvksRGLQRRNTSKLQKREDdgeay 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 148 ---------NVMGLIHPIGEIGRI--------AREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQGTGGL 210
Cdd:PLN02724 194 nlfafpsecNFSGAKFPLDLVKLIkdnqhsnfSKSGRWMVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGYPTGLGAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 211 YLRED---LQLDTLKEGGTGANSEEPF----QPEESPERYESGTLNTPGIAGLGAGIEFIKQEGIEKIREKERSLT---R 280
Cdd:PLN02724 274 LVRRDaakLLKKKYFGGGTVAASIADIdfvkRRERVEQRFEDGTISFLSIAALRHGFKLLNRLTISAIAMHTWALThyvA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 281 QLMLGL---SEIPGVILYGPNPSV----ERAPVISINLEGREPSEVSYL----LDKLYGIASRPGLHCAPDA-------- 341
Cdd:PLN02724 354 NSLRNLkhgNGAPVCVLYGNHTFKlefhIQGPIVTFNLKRADGSWVGHRevekLASLSGIQLRTGCFCNPGAcakylgls 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 518687961 342 HRTL-GTFKQ----------------GTVRLSLGYFNTSQEVEKCLDAVAR 375
Cdd:PLN02724 434 HKDLqANFEAghvcwddqdvihgrptGAVRVSFGYMSTFEDCQKFIDFIIS 484
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
53-215 |
1.67e-10 |
|
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.
Pssm-ID: 99745 Cd Length: 361 Bit Score: 62.02 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 53 EIAEFFNISdplQVVFTPNATEALNLGLKGLLKPGDHVITSSLEHNAVTRPLEKlrsQGVEVTKLQTSVQEGLH--PEQV 130
Cdd:cd06452 52 DLAEFLGMD---EARVTPGAREGKFAVMHSLCEKGDWVVVDGLAHYTSYVAAER---AGLNVREVPNTGHPEYHitPEGY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 131 EAAIQN-------NTKLIVLSHASNVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLG 203
Cdd:cd06452 126 AEVIEEvkdefgkPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAA 205
|
170
....*....|..
gi 518687961 204 PQGTGGLYLRED 215
Cdd:cd06452 206 SAPIGVLATTEE 217
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
53-215 |
3.25e-10 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 61.10 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 53 EIAEFFNISdplQVVFTPNATEALNLGLKGLLKPGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQTSvQEGLHPEQVEA 132
Cdd:PRK09331 71 DLAEFLGMD---EARVTHGAREGKFAVMHSLCKKGDYVVLDGLAHYTSYVAAERAGLNVREVPKTGYP-EYKITPEAYAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 133 AIQN-------NTKLIVLSHASNVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQ 205
Cdd:PRK09331 147 KIEEvkeetgkPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHKSMAASA 226
|
170
....*....|
gi 518687961 206 GTGGLYLRED 215
Cdd:PRK09331 227 PSGVLATTEE 236
|
|
| SelA |
COG1921 |
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]; |
126-205 |
2.72e-09 |
|
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441524 Cd Length: 399 Bit Score: 58.21 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 126 HPEQVEAAIQNNTKLIVLSHASN--VMGLIH--PIGEIGRIAREKSVLFMVDSAqtAGSIPI----------DVQ---AM 188
Cdd:COG1921 143 HLRDYEAAITENTAALLKVHTSNyrIVGFTEevSLAELAELAHEHGLPVIVDLG--SGSLVDlskyglphepTVQeylAA 220
|
90
....*....|....*..
gi 518687961 189 GIDLLVFAGHKGLLGPQ 205
Cdd:COG1921 221 GADLVTFSGDKLLGGPQ 237
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
87-203 |
4.93e-09 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 57.39 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 87 GDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQ-TSVQeglhpeQVEAAIQNNTKLIVLSHASNVMGLIHPIGEIGRIARE 165
Cdd:PRK05939 86 GDHLVSSQFLFGNTNSLFGTLRGLGVEVTMVDaTDVQ------NVAAAIRPNTRMVFVETIANPGTQVADLAGIGALCRE 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 518687961 166 KSVLFMVDSAQTAGSI--PIDVQAMgidlLVF-------AGHKGLLG 203
Cdd:PRK05939 160 RGLLYVVDNTMTSPWLfrPKDVGAS----LVInslskyiAGHGNALG 202
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
86-203 |
8.76e-08 |
|
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.
Pssm-ID: 395837 [Multi-domain] Cd Length: 376 Bit Score: 53.39 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLQTSVqeglhPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEIGRIAR 164
Cdd:pfam01053 85 AGDHIVATDDLYGGTYRLFNKVLPRfGIEVTFVDTSD-----PEDLEAAIKPNTKAVYLETPTNPLLKVVDIEAIAKLAK 159
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 518687961 165 EKSVLFMVDSaqTAGSiPIDVQAM--GIDLLVFAGHKGLLG 203
Cdd:pfam01053 160 KHGILVVVDN--TFAS-PYLQRPLdlGADIVVHSATKYIGG 197
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
111-208 |
3.07e-07 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 51.84 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 111 GVEVTKLQTSVQEGLHPEQVEAAIQNNTKL--IVLSHASNVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGSIPIDVQAM 188
Cdd:PRK13479 103 GIAHVVLDTGEDEPPDAAEVEAALAADPRIthVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPIDIAEL 182
|
90 100
....*....|....*....|
gi 518687961 189 GIDLLVFAGHKGLLGPQGTG 208
Cdd:PRK13479 183 GIDALISSANKCIEGVPGFG 202
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
86-174 |
2.49e-06 |
|
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440391 [Multi-domain] Cd Length: 389 Bit Score: 48.89 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSslehNAV---TRPL--EKLRSQGVEVTKLqtsvqEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEIG 160
Cdd:COG0626 96 AGDHVVAS----DDLyggTRRLldKVLARFGIEVTFV-----DPTDLAAVEAAIRPNTKLVFLETPSNPTLEVVDIAAIA 166
|
90
....*....|....
gi 518687961 161 RIAREKSVLFMVDS 174
Cdd:COG0626 167 AIAHAAGALLVVDN 180
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
86-198 |
7.35e-06 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 47.58 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLqtsvqEGLHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEIGRIAR 164
Cdd:cd00614 78 AGDHVVASDDLYGGTYRLFERLLPKlGIEVTFV-----DPDDPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAH 152
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 518687961 165 EKSVLFMVDSaqTAGSiPIDVQAM--GIDLLV------FAGH 198
Cdd:cd00614 153 EHGALLVVDN--TFAT-PYLQRPLelGADIVVhsatkyIGGH 191
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
51-375 |
6.66e-05 |
|
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: 44.64 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 51 RGEIAEFFN-----ISDPLQVVFTPNATEALNLGLKGLLKPGDHVITSS---LEHNAVtrplekLRSQGVEVTKLQTSVQ 122
Cdd:cd00609 42 REAIAEWLGrrggvDVPPEEIVVTNGAQEALSLLLRALLNPGDEVLVPDptyPGYEAA------ARLAGAEVVPVPLDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 123 EG--LHPEQVEAAIQNNTKLIVLSHASNVMGLIHP---IGEIGRIAREKSVLFMVDSA----QTAGSIPIDVQAMGIDLL 193
Cdd:cd00609 116 GGflLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISDEAyaelVYDGEPPPALALLDAYER 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 194 VFAGH---KGLLGPqG--TGGLYLREDLQLDTLKeggtganseepfqpeespeRYESGTLNTPGIAGLGAGIEFIKQEG- 267
Cdd:cd00609 196 VIVLRsfsKTFGLP-GlrIGYLIAPPEELLERLK-------------------KLLPYTTSGPSTLSQAAAAAALDDGEe 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 268 -IEKIREKERSlTRQLML-GLSEIPGVILYGPnpsvERAPVISINL-EGREPSEVSYLLDKlYGIASRPGlhcapdahRT 344
Cdd:cd00609 256 hLEELRERYRR-RRDALLeALKELGPLVVVKP----SGGFFLWLDLpEGDDEEFLERLLLE-AGVVVRPG--------SA 321
|
330 340 350
....*....|....*....|....*....|.
gi 518687961 345 LGTFKQGTVRLSLGyfNTSQEVEKCLDAVAR 375
Cdd:cd00609 322 FGEGGEGFVRLSFA--TPEEELEEALERLAE 350
|
|
| PRK06234 |
PRK06234 |
methionine gamma-lyase; Provisional |
87-203 |
8.15e-05 |
|
methionine gamma-lyase; Provisional
Pssm-ID: 168478 [Multi-domain] Cd Length: 400 Bit Score: 44.43 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 87 GDHVITSSLEHNAVTRPLEK-LRSQGVEVTKLQTSvqeglHPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEIGRIARE 165
Cdd:PRK06234 103 GDHVVASDTLYGCTFALLNHgLTRYGVEVTFVDTS-----NLEEVRNALKANTKVVYLETPANPTLKVTDIKAISNIAHE 177
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 518687961 166 --KSVLFMVDSAQTAGSI--PIDvqaMGIDLLVFAGHKGLLG 203
Cdd:PRK06234 178 nnKECLVFVDNTFCTPYIqrPLQ---LGADVVVHSATKYLNG 216
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
66-206 |
8.30e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 43.74 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 66 VVFTPNATEALNLGLKGLLKPGDHVITSSLEHNAV--TRPLEKLrsQGVEVTKLQTSVQEGLHPEQVEAAI-------QN 136
Cdd:pfam01212 50 ALFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFdeTGGHAEL--GGVQPRPLDGDEAGNMDLEDLEAAIrevgadiFP 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518687961 137 NTKLIVLSHASNVM-GLIHPIG---EIGRIAREKSVLFMVDSAQ---TAGSIPIDVQAM--GIDLLVFAGHKGLLGPQG 206
Cdd:pfam01212 128 PTGLISLENTHNSAgGQVVSLEnlrEIAALAREHGIPVHLDGARfanAAVALGVIVKEItsYADSVTMCLSKGLGAPVG 206
|
|
| PRK07811 |
PRK07811 |
cystathionine gamma-synthase; Provisional |
86-173 |
1.01e-04 |
|
cystathionine gamma-synthase; Provisional
Pssm-ID: 236104 [Multi-domain] Cd Length: 388 Bit Score: 43.87 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSSLEHNAVTRPLEKLRSQ-GVEVTKLQTSVqeglhPEQVEAAIQNNTKLIVLSHASNVMGLIHPIGEIGRIAR 164
Cdd:PRK07811 99 PGDHIVIPNDAYGGTFRLIDKVFTRwGVEYTPVDLSD-----LDAVRAAITPRTKLIWVETPTNPLLSITDIAALAELAH 173
|
....*....
gi 518687961 165 EKSVLFMVD 173
Cdd:PRK07811 174 DAGAKVVVD 182
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
51-173 |
1.97e-04 |
|
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440205 [Multi-domain] Cd Length: 387 Bit Score: 43.20 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 51 RGEIAEF----FNIS-DPLQVVFTPNATEALNLGLKGLLKPGDHVItsslehnaVTRP-----LEKLRSQGVEVTKLQTS 120
Cdd:COG0436 73 REAIAAYykrrYGVDlDPDEILVTNGAKEALALALLALLNPGDEVL--------VPDPgypsyRAAVRLAGGKPVPVPLD 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518687961 121 VQEGLHP--EQVEAAIQNNTKLIVLSHASNvmglihPIG---------EIGRIAREKSVLFMVD 173
Cdd:COG0436 145 EENGFLPdpEALEAAITPRTKAIVLNSPNN------PTGavysreeleALAELAREHDLLVISD 202
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
51-165 |
1.98e-04 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 43.00 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 51 RGEIAEFFNISDPLQVVFTPNATEALNLGLKGLLKPGDHVItsslehnAVTRPLEKL----RSQGVEVTKLQTSVQEGLH 126
Cdd:PRK07324 68 KEAVASLYQNVKPENILQTNGATGANFLVLYALVEPGDHVI-------SVYPTYQQLydipESLGAEVDYWQLKEENGWL 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 518687961 127 P--EQVEAAIQNNTKLIVLSHASNVMGLIHP---IGEIGRIARE 165
Cdd:PRK07324 141 PdlDELRRLVRPNTKLICINNANNPTGALMDrayLEEIVEIARS 184
|
|
| PRK05968 |
PRK05968 |
hypothetical protein; Provisional |
86-203 |
1.02e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168320 [Multi-domain] Cd Length: 389 Bit Score: 40.84 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSSLEHNAVTRPLEK-LRSQGVEVTKLqtsvqEGLHPEQVEAAIqNNTKLIVLSHASNVMGLIHPIGEIGRIAR 164
Cdd:PRK05968 101 PGDRIVAVRHVYPDAFRLFETiLKRMGVEVDYV-----DGRDEEAVAKAL-PGAKLLYLESPTSWVFELQDVAALAALAK 174
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 518687961 165 EKSVLFMVDS--AQTAGSIPIdvqAMGIDLLVFAGHKGLLG 203
Cdd:PRK05968 175 RHGVVTMIDNswASPVFQRPI---TLGVDLVIHSASKYLGG 212
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
65-206 |
1.56e-03 |
|
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: 40.01 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 65 QVVFTPNATEALNLGLKGLLKPGDHVITSSLEHNAV--TRPLEKLrsQGVEVTKLQTSvqEG-LHPEQVEAAIQNN---- 137
Cdd:cd06502 49 AALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTdeAGAPEFL--SGVKLLPVPGE--NGkLTPEDLEAAIRPRddih 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518687961 138 ---TKLIVLSHASNVMGL--IHPIGEIGRIAREKSVLFMVD-----SAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQG 206
Cdd:cd06502 125 fppPSLVSLENTTEGGTVypLDELKAISALAKENGLPLHLDgarlaNAAAALGVALKTYKSGVDSVSFCLSKGGGAPVG 203
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
127-180 |
1.90e-03 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 40.05 E-value: 1.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 518687961 127 PEQVEAAIQNNTKLIVLSHasnVMGLIHPIGEIGRIAREKSVLFMVDSAQTAGS 180
Cdd:COG0399 108 PEALEAAITPRTKAIIPVH---LYGQPADMDAIMAIAKKHGLKVIEDAAQALGA 158
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
86-286 |
2.10e-03 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 39.74 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSSLEHNAVtRPLEKLRSQGVEVTKLQTSVQEGLHPEQVEAAIQNNT----KLIVLSHASNVMGLIHPIGEIGR 161
Cdd:PLN02409 83 PGDKVVSFRIGQFSL-LWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQDTnhkiKAVCVVHNETSTGVTNDLAGVRK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 162 I--AREKSVLFMVDSAQTAGSIPIDVQAMGIDLLVFAGHKGLLGPQGTGGLYLREDlQLDTLKeggTGANSEEPFQPEES 239
Cdd:PLN02409 162 LldCAQHPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPK-ALEASK---TAKSPRVFFDWADY 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 518687961 240 PERYESGTLN--TPGIA---GLGAGIEFIKQEGIEKIREKERSLTRQLMLGL 286
Cdd:PLN02409 238 LKFYKLGTYWpyTPSIQllyGLRAALDLIFEEGLENVIARHARLGEATRLAV 289
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
53-194 |
2.70e-03 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 39.60 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 53 EIAEFFNISDPL------QVVFTPNATEALNLGLKGLLKPGDHVITSSLEHNAVTRpleKLRSQGVEVTKLQTSVQEGLH 126
Cdd:pfam00155 47 ALAKFLGRSPVLkldreaAVVFGSGAGANIEALIFLLANPGDAILVPAPTYASYIR---IARLAGGEVVRYPLYDSNDFH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 127 P--EQVEAAIQNNTKLIVLSHASNVMGLIHPIGE---IGRIAREKSVLFMVDSA--------QTAGSIPIDVqAMGIDLL 193
Cdd:pfam00155 124 LdfDALEAALKEKPKVVLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAyagfvfgsPDAVATRALL-AEGPNLL 202
|
.
gi 518687961 194 V 194
Cdd:pfam00155 203 V 203
|
|
| SelA |
pfam03841 |
L-seryl-tRNA selenium transferase; |
126-205 |
4.09e-03 |
|
L-seryl-tRNA selenium transferase;
Pssm-ID: 309101 Cd Length: 367 Bit Score: 38.86 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 126 HPEQVEAAIQNNTKLIVLSHASN--VMGLIH--PIGEIGRIAREKSVLFMVDsaqtAGS---------------IPIDVQ 186
Cdd:pfam03841 125 HLKDYEQAINENTALLMKVHTSNyrIQGFTKevELAELVELGHEKGLPVYED----LGSgslvdlsqyglpkepTVQELI 200
|
90
....*....|....*....
gi 518687961 187 AMGIDLLVFAGHKGLLGPQ 205
Cdd:pfam03841 201 AQGVDLVSFSGDKLLGGPQ 219
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
86-180 |
6.15e-03 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 38.42 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518687961 86 PGDHVITSSLEHNAVTRPLEKLRSQGVEVTKLQTSVQegLHPEQVEAAIQNNTKLIVLSHasnVMGLIHPIGEIGRIARE 165
Cdd:pfam01041 63 PGDEVITPSFTFVATANAALRLGAKPVFVDIDPDTYN--IDPEAIEAAITPRTKAIIPVH---LYGQPADMDAIRAIAAR 137
|
90
....*....|....*
gi 518687961 166 KSVLFMVDSAQTAGS 180
Cdd:pfam01041 138 HGLPVIEDAAHALGA 152
|
|
| |
