|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
3-404 |
0e+00 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 842.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 3 VKTPVYLDYAATTTVDKRVAEKMIPYLT--ETFGNPASNSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDN 80
Cdd:PRK14012 1 MKLPIYLDYSATTPVDPRVAEKMMPYLTmdGTFGNPASRSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 81 LAIKGAANFYKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVV 160
Cdd:PRK14012 81 LAIKGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 161 QDIPAIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKPRVRLEAQMHGGGHERGFR 240
Cdd:PRK14012 161 QDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 241 SGTLPTHQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGIEGIEEVYINGDLGHRAPNNLNVSFNFVEGESLIMAVKEL 320
Cdd:PRK14012 241 SGTLPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKDIEEVYLNGDLEQRVPGNLNVSFNYVEGESLIMALKDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEVQFAAELIKSKIGKLRELSPLWEMFKDGIDLNSIE 400
Cdd:PRK14012 321 AVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELSPLWEMFKEGVDLNSIE 400
|
....
gi 504393935 401 WAAH 404
Cdd:PRK14012 401 WAHH 404
|
|
| IscS |
TIGR02006 |
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases ... |
3-404 |
0e+00 |
|
cysteine desulfurase IscS; This model represents IscS, one of several cysteine desulfurases from a larger protein family designated (misleadingly, in this case) class V aminotransferases. IscS is one of at least 6 enzymes characteristic of the IscSUA-hscAB-fsx system of iron-sulfur cluster assembly. Scoring almost as well as proteobacterial sequences included in the model are mitochondrial cysteine desulfurases, apparently from an analogous system in eukaryotes. The sulfur, taken from cysteine, may be used in other systems as well, such as tRNA base modification and biosynthesis of other cofactors. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 131061 [Multi-domain] Cd Length: 402 Bit Score: 791.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 3 VKTPVYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLA 82
Cdd:TIGR02006 1 MKLPIYLDYAATTPVDPRVAEKMMPYLTEKFGNPASRSHSFGWEAEEAVENARNQVAELIGADSREIVFTSGATESNNLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 83 IKGAANFYKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQD 162
Cdd:TIGR02006 81 IKGIAHFYKSKGNHIITSKTEHKAVLDTCRYLEREGFEVTYLPPKSNGLIDLEELKAAIRDDTILVSIMHVNNEIGVIQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 163 IPAIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKPRVRLEAQMHGGGHERGFRSG 242
Cdd:TIGR02006 161 IAAIGEICRERKVFFHVDAAQSVGKIPINVNELKVDLMSISGHKIYGPKGIGALYVRRKPRVRLEALIHGGGHERGMRSG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 243 TLPTHQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGIEGIEEVYINGDLGHRAPNNLNVSFNFVEGESLIMAVKELAV 322
Cdd:TIGR02006 241 TLPTHQIVGMGEAFRIAKEEMAQDTAHVLALRDRLLNGIKSIEEVYLNGDLEHRVPGNLNVSFNYVEGESLIMALKDLAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 323 SSGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEVQFAAELIKSKIGKLRELSPLWEMFKDGIDLNSIEWA 402
Cdd:TIGR02006 321 SSGSACTSASLEPSYVLRALGINDELAHSSIRFTIGRFTTEEEIDYAVKLVKSAIDKLRELSPLWEMFKEGVDLNSIEWA 400
|
..
gi 504393935 403 AH 404
Cdd:TIGR02006 401 AH 402
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
4-384 |
0e+00 |
|
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: 645.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 4 KTPVYLDYAATTTVDKRVAEKMIPYLTETFGNPASnSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLAI 83
Cdd:COG1104 1 MMMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 84 KGAANFYKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDI 163
Cdd:COG1104 80 KGAARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 164 PAIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRkpRVRLEAQMHGGGHERGFRSGT 243
Cdd:COG1104 160 AEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRK--GVRLEPLIHGGGQERGLRSGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 244 LPTHQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGI-EGIEEVYINGDLGHRAPNNLNVSFNFVEGESLIMAV--KEL 320
Cdd:COG1104 238 ENVPGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLlAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALdlAGI 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504393935 321 AVSSGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEVQFAAELIKSKIGKLRELS 384
Cdd:COG1104 318 AVSSGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
7-366 |
0e+00 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 573.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLAIKGA 86
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 87 ANFYKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAI 166
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 167 GEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKPRVRLEAQMHGGGHERGFRSGTLPT 246
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 247 HQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGIE-GIEEVYING--DLGHRAPNNLNVSFNFVEGESLIMAVKELAVS 323
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRaKLGGVRVNGprDPEKRYPGTLNLSFAYVEGESLLMGLKEVAVS 320
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 504393935 324 SGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEV 366
Cdd:PLN02651 321 SGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
7-386 |
2.12e-176 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 496.37 E-value: 2.12e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASnSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLAIKGA 86
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSS-MHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 87 ANFYKTKgKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAI 166
Cdd:TIGR03402 80 LAAQPEK-RHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 167 GEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKprVRLEAQMHGGGHERGFRSGTLPT 246
Cdd:TIGR03402 159 GEIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKG--TRFRPLLRGGHQERGRRAGTENV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 247 HQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGI-EGIEEVYINGDLGHRAPNNLNVSFNFVEGESLIMAVKE--LAVS 323
Cdd:TIGR03402 237 PGIVGLGKAAELATEHLEEENTRVRALRDRLEAGLlARIPDARLNGDPTKRLPNTVNISFEYIEGEAILLLLDMegICAS 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504393935 324 SGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEVQFAAELIKSKIGKLRELSPL 386
Cdd:TIGR03402 317 SGSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMSPF 379
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
8-356 |
1.29e-150 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 430.37 E-value: 1.29e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 8 YLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLAIKGAA 87
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRTHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 88 NFYKTKG-KHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAI 166
Cdd:TIGR03235 81 RAGEQKGkKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 167 GEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRR--KPRVRLEAQMHGGGHERGFRSGTL 244
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKrgKPKAPLKPIMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 245 PTHQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGIEGIeEVYINGDLGHRAPNNLNVSFNFVEGESLIMAVKE-LAVS 323
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQTL-GVKLNGDPAETIPHILNFSIDGVNSEALIVNLRAdAAVS 319
|
330 340 350
....*....|....*....|....*....|...
gi 504393935 324 SGSACTSASLEPSYVLRALGRNDELAHSSLRIT 356
Cdd:TIGR03235 320 TGSACSSSKYEPSHVLQAMGLDTDRARGAIRFS 352
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
7-367 |
1.00e-105 |
|
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: 316.50 E-value: 1.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNLAIKG 85
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 86 AANFYKtKGKHLITVKTEHKAVLDTMRELERQ-GFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIP 164
Cdd:pfam00266 81 LGRSLK-PGDEIVITEMEHHANLVPWQELAKRtGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 165 AIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKPRVRLEAQMHGGG-------HER 237
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGmietvslQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 238 G-------FRSGTLPTHQIVGMGEAFR-IAKEELAQDTAHYLKLRDIFLKGIEGIEEVYINGDlgHRAPNNLNVSFNFVE 309
Cdd:pfam00266 240 TfadapwkFEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP--ERRASIISFNFKGVH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 310 GESLIMAVKE--LAVSSGSACTsaslEPSYVLRALgrndelaHSSLRITFGRMTTEEEVQ 367
Cdd:pfam00266 318 PHDVATLLDEsgIAVRSGHHCA----QPLMVRLGL-------GGTVRASFYIYNTQEDVD 366
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
7-395 |
1.08e-98 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 298.95 E-value: 1.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNpASNSHAFGWEAEEAVEKARADIAALINADPKEIVFTSGATESDNLAIKGA 86
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 87 ANFYKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAI 166
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 167 GEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRrkPRVRLEAQMHGGGHERGFRSGTLpt 246
Cdd:PRK02948 161 GALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYIN--PQVRWKPVFPGTTHEKGFRPGTV-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 247 hQIVGMGeAFRIAKEELAQDTA----HYLKLRDIFLKGIEGIE-EVYINGDLGHRAPNNLNVSFNFVEGESLIMAVKE-- 319
Cdd:PRK02948 237 -NVPGIA-AFLTAAENILKNMQeeslRFKELRSYFLEQIQTLPlPIEVEGHSTSCLPHIIGVTIKGIEGQYTMLECNRrg 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504393935 320 LAVSSGSACTSASLEPSYVLRALGRNDELAHSSLRITFGRMTTEEEVQfaaELIKSkigklreLSPLWEMFKDGID 395
Cdd:PRK02948 315 IAISTGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQID---TTIHA-------LETIGNQFYRGVK 380
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
7-374 |
4.55e-72 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 230.80 E-value: 4.55e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNLAIKG 85
Cdd:COG0520 17 VYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLVAYG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 86 AANFykTKGKHLITVKTEHKAVLDTMREL-ERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIP 164
Cdd:COG0520 97 LGRL--KPGDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 165 AIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKprvrLEAQM---HGGGH------ 235
Cdd:COG0520 175 EIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRE----LLEALppfLGGGGmiewvs 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 236 ---------ERGFRSGTLPTHQIVGMGEAF---------RIAKEElaQDTAHYLKLRdifLKGIEGIeEVYINGDLGHRA 297
Cdd:COG0520 251 fdgttyadlPRRFEAGTPNIAGAIGLGAAIdyleaigmeAIEARE--RELTAYALEG---LAAIPGV-RILGPADPEDRS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 298 PnnlNVSFNfVEGE-----SLIMAVKELAVSSGSACTsaslEPsyVLRALGrndelAHSSLRITFGRMTTEEEVQFAAEL 372
Cdd:COG0520 325 G---IVSFN-VDGVhphdvAALLDDEGIAVRAGHHCA----QP--LMRRLG-----VPGTVRASFHLYNTEEEIDRLVEA 389
|
..
gi 504393935 373 IK 374
Cdd:COG0520 390 LK 391
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
7-371 |
3.20e-66 |
|
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: 215.02 E-value: 3.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNLAIKG 85
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 86 AANFYKtKGKHLITVKTEHKAVLDTMREL-ERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIP 164
Cdd:cd06453 81 LGRANK-PGDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 165 AIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRkprvRLEAQM---HGGGH------ 235
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKE----ELLEEMppyGGGGEmieevs 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 236 ----------ERgFRSGTLPTHQIVGMGEAFR----IAKEELAqdtAHYLKLRDIFLKGIEGIEEVYINGDLGHRAPnnl 301
Cdd:cd06453 236 feettyadlpHK-FEAGTPNIAGAIGLGAAIDylekIGMEAIA---AHEHELTAYALERLSEIPGVRVYGDAEDRAG--- 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504393935 302 NVSFNfVEGE-----SLIMAVKELAVSSGSACTsaslEPsyVLRALGRNdelahSSLRITFGRMTTEEEVQFAAE 371
Cdd:cd06453 309 VVSFN-LEGIhphdvATILDQYGIAVRAGHHCA----QP--LMRRLGVP-----GTVRASFGLYNTEEEIDALVE 371
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
7-383 |
1.02e-30 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 121.78 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNLAIK- 84
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINLVAYt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 85 -GAANFyKTKGKHLITVKTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDI 163
Cdd:PLN02855 114 wGLANL-KPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGSILPV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 164 PAIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKPRVRLEAQMhGGGH-------E 236
Cdd:PLN02855 193 EDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFL-GGGEmisdvflD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 237 RG--------FRSGTLPTHQIVGMGEAF---------RIakEELAQDTAHYLKLRdifLKGIEGIeEVY--INGDLGHRA 297
Cdd:PLN02855 272 HStyapppsrFEAGTPAIGEAIGLGAAIdylseigmdRI--HEYEVELGTYLYEK---LSSVPGV-RIYgpKPSEGVGRA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 298 PnnlNVSFNfVEG------ESLIMAVKELAVSSGSACTsaslEPSYvlRALGRNDElAHSSLRItfgrMTTEEEVQFAAE 371
Cdd:PLN02855 346 A---LCAFN-VEGihptdlSTFLDQQHGVAIRSGHHCA----QPLH--RYLGVNAS-ARASLYF----YNTKEEVDAFIH 410
|
410
....*....|..
gi 504393935 372 LIKSKIGKLREL 383
Cdd:PLN02855 411 ALKDTIAFFSSF 422
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
7-255 |
2.96e-27 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 111.77 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNLAIKG 85
Cdd:PRK09295 25 AYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINArSAEELVFVRGTTEGINLVANS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 86 AANFYKTKGKHLITVKTEHKAVLDTMREL-ERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIP 164
Cdd:PRK09295 105 WGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 165 AIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKprvrLEAQM---HGGGH------ 235
Cdd:PRK09295 185 EMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEA----LLQEMppwEGGGSmiatvs 260
|
250 260 270
....*....|....*....|....*....|
gi 504393935 236 -ERG---------FRSGTLPTHQIVGMGEA 255
Cdd:PRK09295 261 lTEGttwakapwrFEAGTPNTGGIIGLGAA 290
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
7-234 |
7.55e-27 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 110.51 E-value: 7.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVAEKMIPYLTETFGNPASNSHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNLAIKG 85
Cdd:PRK10874 21 VYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 86 AANFYKTKGKHLITVKTEHKAVLDTMRELERQ-GFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIP 164
Cdd:PRK10874 101 YARPRLQPGDEIIVSEAEHHANLVPWLMVAQQtGAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGCPDLA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504393935 165 AIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKprvrLEAQM---HGGG 234
Cdd:PRK10874 181 RAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSE----LLEAMspwQGGG 249
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
51-219 |
1.79e-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: 73.57 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 51 VEKARADIAALINADPKEIVFTSGATESDNLAIKgaanFYKTKGKHLITVKTEHKAVldTMRELERQGFE---VTYLGVQ 127
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALL----ALLGPGDEVIVDANGHGSR--YWVAAELAGAKpvpVPVDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 128 ENGLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAIGEICRERKIVFHVDAAQA-----CGKVPVDVEAAkiDLLSM 202
Cdd:cd01494 76 YGGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAggaspAPGVLIPEGGA--DVVTF 153
|
170
....*....|....*..
gi 504393935 203 SAHKVYGPKGIGALYVR 219
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
7-235 |
3.79e-13 |
|
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: 71.04 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYAATTTVDKRVaekmIPYLTETFGNPASN----SHAFGWEAEEAVEKARADIAALINA-DPKEIVFTSGATESDNL 81
Cdd:NF041166 247 VWFDNAATTQKPQAV----IDRLSYFYEHENSNihraAHELAARATDAYEGAREKVRRFIGApSVDEIIFVRGTTEAINL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 82 -AikgaanfyKTKG-KHL-----ITVKT-EHKAVLDTMREL-ERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMW 152
Cdd:NF041166 323 vA--------KSWGrQNIgagdeIIVSHlEHHANIVPWQQLaQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 153 ANNEIGVV---QDIPAIGeicrerkivfH-------VDAAQACGKVPVDVEAAKIDLLSMSAHKVYGPKGIGALYVRRKp 222
Cdd:NF041166 395 VSNALGTVtpvKEIIALA----------HragakvlVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRD- 463
|
250
....*....|....*.
gi 504393935 223 rvrLEAQM---HGGGH 235
Cdd:NF041166 464 ---LLEAMppwQGGGN 476
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-219 |
6.88e-13 |
|
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: 69.15 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 37 ASNSHAFGWEAEEAVEKARADI----AALINADPKEI--VFTSGATESDNLAIKGAANFYKTKGKH----------LITV 100
Cdd:cd06450 22 AKNAIDFTWDESPAATEMEAEVvnwlAKLFGLPSEDAdgVFTSGGSESNLLALLAARDRARKRLKAgggrgidklvIVCS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 101 KTEHKAVLDTMRELERqgfEVTYLGVQENGLIDLEELKAAIRDD------TILVSVMWANNEIGVVQDIPAIGEICRERK 174
Cdd:cd06450 102 DQAHVSVEKAAAYLDV---KVRLVPVDEDGRMDPEALEAAIDEDkaeglnPIMVVATAGTTDTGAIDPLEEIADLAEKYD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504393935 175 IVFHVDAAQACGKVPVD--------VEAAkiDLLSMSAHKvYG--PKGIGALYVR 219
Cdd:cd06450 179 LWLHVDAAYGGFLLPFPeprhldfgIERV--DSISVDPHK-YGlvPLGCSAVLVR 230
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
70-221 |
3.78e-10 |
|
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: 61.39 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 70 VFTSGATESdNL-AIKGA-----ANFYKTKG----KHLITVKTE------HKA--VLDtmreLERQGfeVTYLGVQENGL 131
Cdd:COG0076 129 VFTSGGTEA-NLlALLAArdralARRVRAEGlpgaPRPRIVVSEeahssvDKAarLLG----LGRDA--LRKVPVDEDGR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 132 IDLEELKAAIRDD------TILV-----SVmwannEIGVVQDIPAIGEICRERKIVFHVDAAQACGKVPVD--------V 192
Cdd:COG0076 202 MDPDALEAAIDEDraaglnPIAVvatagTT-----NTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPelrhlldgI 276
|
170 180 190
....*....|....*....|....*....|.
gi 504393935 193 EAAkiDLLSMSAHKvYG--PKGIGALYVRRK 221
Cdd:COG0076 277 ERA--DSITVDPHK-WLyvPYGCGAVLVRDP 304
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
7-234 |
4.35e-10 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 61.42 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 7 VYLDYA-ATTTVDKRVAEKMIPYLTETFGNPASNSHAfGWEAEEAVEKARADIAALINADPKE--IVFTSGATESdnLAI 83
Cdd:PLN02724 36 VYLDHAgATLYSESQLEAALADFSSNVYGNPHSQSDS-SMRSSDTIESARQQVLEYFNAPPSDyaCVFTSGATAA--LKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 84 KGAAnFYKTKGKHLITVKTEHKAVLDtMRE--LERQG--------------------FEVTYLGVQENGLIDLEELKAai 141
Cdd:PLN02724 113 VGET-FPWSSESHFCYTLENHNSVLG-IREyaLEKGAaaiavdieeaanqptnsqgsVVVKSRGLQRRNTSKLQKRED-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 142 RDDTILVSVM----------WANNEIGVVQDIPAIGEICRERKIVFhVDAAQACGKVPVDVEAAKIDLLSMSAHKVYG-P 210
Cdd:PLN02724 189 DGEAYNLFAFpsecnfsgakFPLDLVKLIKDNQHSNFSKSGRWMVL-LDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyP 267
|
250 260
....*....|....*....|....
gi 504393935 211 KGIGALYVRRKPRVRLEAQMHGGG 234
Cdd:PLN02724 268 TGLGALLVRRDAAKLLKKKYFGGG 291
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
114-262 |
5.11e-08 |
|
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: 54.22 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 114 LERQGFEVTYLGVQENGLIDLEELKAAIRDDTIlVSVMWANNE--IGVVQDIPAIGEICRERKIVFHVDAAQACGKVPVD 191
Cdd:cd06451 93 AERYGADVDVVEKPWGEAVSPEEIAEALEQHDI-KAVTLTHNEtsTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 192 VEAAKIDLLSMSAHKVYG-PKGIGALYVRRKPRVRLEA--QMHGG-----------GHERGFRSgTLPTHQIVGMGEAFR 257
Cdd:cd06451 172 MDEWGVDVAYTGSQKALGaPPGLGPIAFSERALERIKKktKPKGFyfdlllllkywGEGYSYPH-TPPVNLLYALREALD 250
|
....*
gi 504393935 258 IAKEE 262
Cdd:cd06451 251 LILEE 255
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
70-287 |
9.48e-08 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 53.58 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 70 VFTSGATESDNLAIKGAA----NFYKTKGKHLITVKTEHKAVLDTMRELERQ--------GFEVTYLGVQENGLIDLEEL 137
Cdd:pfam00282 106 VLQPGSSESNLLALLAARtkwiKRMKAAGKPADSSGILAKLVAYTSDQAHSSiekaalygGVKLREIPSDDNGKMRGMDL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 138 KAAI-RDDTILVSVMWANNEIGVV-----QDIPAIGEICRERKIVFHVDAAQA-----CGKV-PVDVEAAKIDLLSMSAH 205
Cdd:pfam00282 186 EKAIeEDKENGLIPFFVVATLGTTgsgafDDLQELGDICAKHNLWLHVDAAYGgsafiCPEFrHWLFGIERADSITFNPH 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 206 KVYG-PKGIGALYVRRKPRVRLEAQMHGGGHERGFRSGTLPTHQIvGMGEAFRIAKeelaqdtaHYLKLRdifLKGIEGI 284
Cdd:pfam00282 266 KWMLvLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYDTGHKQI-PLSRRFRILK--------LWFVIR---SLGVEGL 333
|
...
gi 504393935 285 EEV 287
Cdd:pfam00282 334 QNQ 336
|
|
| PRK05939 |
PRK05939 |
cystathionine gamma-synthase family protein; |
93-180 |
5.94e-07 |
|
cystathionine gamma-synthase family protein;
Pssm-ID: 235650 [Multi-domain] Cd Length: 397 Bit Score: 51.23 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 93 KGKHLIT---VKTEHKAVLDTMRELerqGFEVTYLGVqenglIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAIGEI 169
Cdd:PRK05939 85 AGDHLVSsqfLFGNTNSLFGTLRGL---GVEVTMVDA-----TDVQNVAAAIRPNTRMVFVETIANPGTQVADLAGIGAL 156
|
90
....*....|.
gi 504393935 170 CRERKIVFHVD 180
Cdd:PRK05939 157 CRERGLLYVVD 167
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
92-177 |
9.05e-07 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 50.52 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 92 TKGKHLITVKT---EHKAVLDTMreLERQGFEVTYLGVqENGLIDLEELKAAIRDDTILVSVmwAN-NEIGVVQDIPAIG 167
Cdd:PRK00451 152 TKRKKVLVSGAvhpEYREVLKTY--LKGQGIEVVEVPY-EDGVTDLEALEAAVDDDTAAVVV--QYpNFFGVIEDLEEIA 226
|
90
....*....|
gi 504393935 168 EICRERKIVF 177
Cdd:PRK00451 227 EIAHAGGALF 236
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
115-234 |
5.53e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 47.60 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 115 ERQGFEVTYLGVQENGLIDLEELKAAIRDDTI-------LVSVMWANNEIG--VV--QDIPAIGEICRERKIVFHVDAAQ 183
Cdd:pfam01212 92 ELGGVQPRPLDGDEAGNMDLEDLEAAIREVGAdifpptgLISLENTHNSAGgqVVslENLREIAALAREHGIPVHLDGAR 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504393935 184 ---ACGKVPVDVE--AAKIDLLSMSAHKVYGpKGIGAL------YVRRKPRVRleaQMHGGG 234
Cdd:pfam01212 172 fanAAVALGVIVKeiTSYADSVTMCLSKGLG-APVGSVlagsddFIAKAIRQR---KYLGGG 229
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
112-180 |
4.46e-05 |
|
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: 45.43 E-value: 4.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504393935 112 RELERQGFEVTYLGvqengLIDLEELKAAIRDDTILV------SVMWAnneigvVQDIPAIGEICRERKIVFHVD 180
Cdd:COG0626 116 KVLARFGIEVTFVD-----PTDLAAVEAAIRPNTKLVfletpsNPTLE------VVDIAAIAAIAHAAGALLVVD 179
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
43-213 |
4.62e-05 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 45.31 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 43 FGW-EAEEAVEKAradIAALI-NADPKEIVFTSGATESDNLAIKGAANfyktKGKHLITVKTEHKAVLDTMRELerqGFE 120
Cdd:PRK07324 58 YGWiEGSPEFKEA---VASLYqNVKPENILQTNGATGANFLVLYALVE----PGDHVISVYPTYQQLYDIPESL---GAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 121 VTYLGV-QENG-LIDLEELKAAIRDDTILVSVMWANNEIGVVQD---IPAIGEICRErkivfhVDAAQACGKV--PVDVE 193
Cdd:PRK07324 128 VDYWQLkEENGwLPDLDELRRLVRPNTKLICINNANNPTGALMDrayLEEIVEIARS------VDAYVLSDEVyrPLDED 201
|
170 180 190
....*....|....*....|....*....|
gi 504393935 194 ---AAKIDLL-------SMSahKVYGPKGI 213
Cdd:PRK07324 202 gstPSIADLYekgistnSMS--KTYSLPGI 229
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
62-374 |
5.85e-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: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 62 INADPKEIVFTSGATEsdnlAIKGAANFYKTKGKHLITVK---TEHKAVldtmreLERQGFEVTYLGVQENG--LIDLEE 136
Cdd:cd00609 55 VDVPPEEIVVTNGAQE----ALSLLLRALLNPGDEVLVPDptyPGYEAA------ARLAGAEVVPVPLDEEGgfLLDLEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 137 LKAAIRDDTILVSVMWANNEIGVV---QDIPAIGEICRERKIVFHVDAA------QACGKVPVDVEAAKIDLL---SMSa 204
Cdd:cd00609 125 LEAAKTPKTKLLYLNNPNNPTGAVlseEELEELAELAKKHGILIISDEAyaelvyDGEPPPALALLDAYERVIvlrSFS- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 205 hKVYGPKG--IGALYVRRKPRVRLEAQMHgggherGFRSGTLPTHQIVGMGEAFRIAKEELAQDTAHYLKLRDIFLKGIE 282
Cdd:cd00609 204 -KTFGLPGlrIGYLIAPPEELLERLKKLL------PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 283 GIeevyinGDLGHRAPNNLNVSFNFVEGESLIMAVKELAvssgsactsasLEPSYVLRALGRNDELAHSSLRITFGrmTT 362
Cdd:cd00609 277 EL------GPLVVVKPSGGFFLWLDLPEGDDEEFLERLL-----------LEAGVVVRPGSAFGEGGEGFVRLSFA--TP 337
|
330
....*....|..
gi 504393935 363 EEEVQFAAELIK 374
Cdd:cd00609 338 EEELEEALERLA 349
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
90-214 |
6.09e-05 |
|
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: 44.91 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 90 YKTKGKHLI--TVKTEHKAVLDTMreLERQGFEVTYLGVQENGLIDLEELKAAIRDDTILVSVMWANNEiGVVQD-IPAI 166
Cdd:cd00613 105 YHKRNKVLVpdSAHPTNPAVARTR--GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNTL-GVFEDlIKEI 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504393935 167 GEICRERKIVFHVDAA--QACG-KVPVDVEAakiDLLSMSAHKVYGPKGIG 214
Cdd:cd00613 182 ADIAHSAGALVYVDGDnlNLTGlKPPGEYGA---DIVVGNLQKTGVPHGGG 229
|
|
| GcvP1 |
COG0403 |
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport ... |
103-181 |
1.08e-04 |
|
Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain [Amino acid transport and metabolism]; Glycine cleavage system protein P (pyridoxal-binding), N-terminal domain is part of the Pathway/BioSystem: Glycine cleavage
Pssm-ID: 440172 [Multi-domain] Cd Length: 442 Bit Score: 44.25 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 103 EHKAVLDTMreLERQGFEVTYLGVqENGLIDLEELKAAIRDDTilVSVMWAN-NEIGVVQDIPAIGEICRERKIVFHVDA 181
Cdd:COG0403 167 QTRAVLKTY--AEPLGIEVVEVPD-EDGVTDLEALKALLDDDV--AGVLVQYpNFFGVIEDLRAIAEAAHAAGALVIVAA 241
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
56-232 |
1.11e-04 |
|
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: 43.92 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 56 ADIAALINADpkEIVFTSGATEsdnlAIKGAANFYKTKGKHLITVK----TEHKAVldtmrelERQGFEVTYLGVQE--N 129
Cdd:cd06452 51 HDLAEFLGMD--EARVTPGARE----GKFAVMHSLCEKGDWVVVDGlahyTSYVAA-------ERAGLNVREVPNTGhpE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 130 GLIDLEELKAAIRDDT-------ILVSVMWANNEIGVVQDIPAIGEICRERKIVFHVDAAQACGKVPVDVEAAKIDLLSM 202
Cdd:cd06452 118 YHITPEGYAEVIEEVKdefgkppALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVG 197
|
170 180 190
....*....|....*....|....*....|...
gi 504393935 203 SAHKVY---GPKGIGALYVRRKPRVRLEAQMHG 232
Cdd:cd06452 198 SGHKSMaasAPIGVLATTEEWADIVFRTSQMFK 230
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
115-234 |
7.24e-04 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 41.21 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 115 ERQGFEVtYLGVQ------ENGLIDLEELKAAIRDDTI------LVSVMWANnEIGVV---QDIPAIGEICRERKIVFHV 179
Cdd:COG2008 89 EGGAPEA-LSGVKllpvpgEDGKLTPEDLEAAIRPGDVhfpqpgLVSLENTT-EGGTVyplEELRAIAAVAREHGLPLHL 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504393935 180 D------AAQACGkVPVDVEAAKIDLLSMSahkvyGPKGIGAL----------YVRRKPRVRleaQMHGGG 234
Cdd:COG2008 167 DgarlfnAAAALG-VSLAEITAGVDSVSFG-----LTKGLGAPggavlagdpeFIEEARRWR---KRLGGL 228
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
114-262 |
1.11e-03 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 40.67 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 114 LERQGFEVTYLGVQENGLIDLEELKAAI-RDDTIL-VSVMWANNEIGVVQDIPAIGEICRERKIVFHVDAAQACGKVPVD 191
Cdd:PRK13479 99 AEYLGIAHVVLDTGEDEPPDAAEVEAALaADPRIThVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAMSSFGAIPID 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 192 VEAAKIDLLSMSAHK-VYGPKGIGALYVRR------KPRVR-----LEAQ---MHGGGHERgFrsgTLPTHQIVGMGEAF 256
Cdd:PRK13479 179 IAELGIDALISSANKcIEGVPGFGFVIARRseleacKGNSRslsldLYDQwayMEKTGQWR-F---TPPTHVVAAFYQAL 254
|
....*.
gi 504393935 257 RIAKEE 262
Cdd:PRK13479 255 LELEEE 260
|
|
| PRK08133 |
PRK08133 |
O-succinylhomoserine sulfhydrylase; Validated |
114-180 |
1.22e-03 |
|
O-succinylhomoserine sulfhydrylase; Validated
Pssm-ID: 181244 [Multi-domain] Cd Length: 390 Bit Score: 40.76 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504393935 114 LERQGFEVTYLGvqengLIDLEELKAAIRDDTILVSVMWANNEIGVVQDIPAIGEICRERKIVFHVD 180
Cdd:PRK08133 121 FARFGIETTFVD-----LTDLDAWRAAVRPNTKLFFLETPSNPLTELADIAALAEIAHAAGALLVVD 182
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
107-262 |
1.36e-03 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 40.51 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 107 VLDTMReleRQGFEVTYLGVQENGLIDLEELKAAIRDDTI--LVSVMWANNE--IGVVQDIPAIGEI--CRERKIVFHVD 180
Cdd:PLN02409 99 WIDQMQ---RLNFDVDVVESPWGQGADLDILKSKLRQDTNhkIKAVCVVHNEtsTGVTNDLAGVRKLldCAQHPALLLVD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 181 AAQACGKVPVDVEAAKIDL-LSMSAHKVYGPKGIG----------ALYVRRKPRVRLEAQMHGGGHERGFRSGTLPTHQI 249
Cdd:PLN02409 176 GVSSIGALDFRMDEWGVDVaLTGSQKALSLPTGLGivcaspkaleASKTAKSPRVFFDWADYLKFYKLGTYWPYTPSIQL 255
|
170
....*....|....
gi 504393935 250 V-GMGEAFRIAKEE 262
Cdd:PLN02409 256 LyGLRAALDLIFEE 269
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
3-180 |
1.41e-03 |
|
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: 40.65 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 3 VKTPVYLdyaATTTVDKRVAEKMIPYLTETF-------GNPASnshafgweaeEAVEKAradIAALINADpKEIVFTSGA 75
Cdd:cd00614 3 VAPPIYQ---TSTFVFPSPAEAADLFALREGgyiysriGNPTV----------DALEKK---LAALEGGE-AALAFSSGM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 76 TesdnlAIKGAANFYKTKGKHLITVKT---EHKAVLDtmRELERQGFEVTYLGVQengliDLEELKAAIRDDTILVSVMW 152
Cdd:cd00614 66 A-----AISTVLLALLKAGDHVVASDDlygGTYRLFE--RLLPKLGIEVTFVDPD-----DPEALEAAIKPETKLVYVES 133
|
170 180
....*....|....*....|....*...
gi 504393935 153 ANNEIGVVQDIPAIGEICRERKIVFHVD 180
Cdd:cd00614 134 PTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
128-206 |
2.27e-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: 39.62 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504393935 128 ENGLIDLEELKAAIR--DD-----TILVSVMWANNEIGV--VQDIPAIGEICRERKIVFHVDAAQ-----ACGKVPVDVE 193
Cdd:cd06502 104 ENGKLTPEDLEAAIRprDDihfppPSLVSLENTTEGGTVypLDELKAISALAKENGLPLHLDGARlanaaAALGVALKTY 183
|
90
....*....|...
gi 504393935 194 AAKIDLLSMSAHK 206
Cdd:cd06502 184 KSGVDSVSFCLSK 196
|
|
| PRK04366 |
PRK04366 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPB; |
118-172 |
4.86e-03 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPB;
Pssm-ID: 235292 Cd Length: 481 Bit Score: 38.94 E-value: 4.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 504393935 118 GFEVTYLGVQENGLIDLEELKAAIRDDTilVSVMWAN-NEIGVV-QDIPAIGEICRE 172
Cdd:PRK04366 182 GFKVVEIPSNEDGLVDLEALKAAVGEDT--AALMLTNpNTLGLFeRNILEIAEIVHE 236
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
128-186 |
7.61e-03 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 38.13 E-value: 7.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504393935 128 ENGLIDLEELKAAIRDDT---ILVSVMwanneiGVVQDIPAIGEICRERKIVFHVDAAQACG 186
Cdd:COG0399 102 DTYNIDPEALEAAITPRTkaiIPVHLY------GQPADMDAIMAIAKKHGLKVIEDAAQALG 157
|
|
| |
