|
Name |
Accession |
Description |
Interval |
E-value |
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
14-414 |
0e+00 |
|
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine desulfurases involved in FeS cluster formation needed for nitrogen fixation among other vital functions. Many cysteine desulfurases are also active as selenocysteine lyase and/or cysteine sulfinate desulfinase. This subfamily is associated with the six-gene SUF system described in E. coli and Erwinia as an FeS cluster formation system during oxidative stress. The active site Cys is this subfamily resembles GHHC with one or both His conserved. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 131034 [Multi-domain] Cd Length: 403 Bit Score: 694.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 14 EAIRRDFPILSRQVHGKTLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNAGSV 93
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 94 DEIVFTKNATEAINTVAYGYGMPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLSERT 173
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 174 KLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMLEK 253
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 254 MRPFQGGGEMIEEVTEENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINSLRIF 333
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 334 G--NAPDKGAIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALEKARK 411
Cdd:TIGR01979 321 GprDAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRK 400
|
...
gi 489053876 412 FFG 414
Cdd:TIGR01979 401 FFG 403
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
33-406 |
0e+00 |
|
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: 653.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 33 VYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNAGSVDEIVFTKNATEAINTVAYG 112
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 113 YGMPFiGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKLVAITHMSNTLGTVVPIK 192
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 193 KIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMLEKMRPFQGGGEMIEEVTEENV 272
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 273 TYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINSLRIFGNAPDKGAIISFALEGIHA 352
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489053876 353 HDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEAL 406
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
12-412 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 646.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 12 DVEAIRRDFPilsrqVHGKTLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNAG 91
Cdd:COG0520 1 DVEAIRADFP-----VLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 92 SVDEIVFTKNATEAINTVAYGYGMpfIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLSE 171
Cdd:COG0520 76 SPDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 172 RTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQML 251
Cdd:COG0520 154 RTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 252 EKMRPFQGGGEMIEEVTEENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINSLR 331
Cdd:COG0520 234 EALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 332 IFGNAP--DKGAIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALEKA 409
Cdd:COG0520 314 ILGPADpeDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393
|
...
gi 489053876 410 RKF 412
Cdd:COG0520 394 AEL 396
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
10-408 |
0e+00 |
|
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: 597.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 10 AYDVEAIRRDFPILSRQVHGKTLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLN 89
Cdd:NF041166 224 PFDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 90 AGSVDEIVFTKNATEAINTVAYGYGMPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRL 169
Cdd:NF041166 304 APSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 170 SERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQ 249
Cdd:NF041166 384 NPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRD 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 250 MLEKMRPFQGGGEMIEEVTEENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINS 329
Cdd:NF041166 464 LLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPG 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053876 330 LRIFGNAPDKGAIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALEK 408
Cdd:NF041166 544 LRLIGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRR 622
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
14-413 |
0e+00 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 512.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 14 EAIRRDFPILSRQVHGKTLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNAGSV 93
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 94 DEIVFTKNATEAINTVAYGYGMPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLSERT 173
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 174 KLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMLEK 253
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 254 MRPFQGGGEMIEEVTEENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINSLRIF 333
Cdd:PLN02855 255 MPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 334 GNAPDKG----AIISFALEGIHAHDVSMVIDRA-GVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALEK 408
Cdd:PLN02855 335 GPKPSEGvgraALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKD 414
|
....*
gi 489053876 409 ARKFF 413
Cdd:PLN02855 415 TIAFF 419
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
33-402 |
0e+00 |
|
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: 508.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 33 VYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNAGSVDEIVFTKNATEAINTVAYG 112
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 113 YGmPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKLVAITHMSNTLGTVVPIK 192
Cdd:pfam00266 81 LG-RSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 193 KIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMLEKMRPFQGGGEMIEEVTEENV 272
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 273 TYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINSLRIFGNaPDKGAIISFALEGIHA 352
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGP-ERRASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489053876 353 HDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDAL 402
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
9-414 |
2.78e-166 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 472.31 E-value: 2.78e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 9 MAYDVEAIRRDFPILSRQVHGKTLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFL 88
Cdd:PRK09295 1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 89 NAGSVDEIVFTKNATEAINTVAYGYGMPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKR 168
Cdd:PRK09295 81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 169 LSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRA 248
Cdd:PRK09295 161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 249 QMLEKMRPFQGGGEMIEEVT-EENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRI 327
Cdd:PRK09295 241 ALLQEMPPWEGGGSMIATVSlTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 328 NSLRIFGNAPDKGaIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALE 407
Cdd:PRK09295 321 PDLTLYGPQNRLG-VIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQ 399
|
....*..
gi 489053876 408 KARKFFG 414
Cdd:PRK09295 400 RIHRLLG 406
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
9-409 |
1.86e-143 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 414.05 E-value: 1.86e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 9 MAYDVEAIRRDFPILSRQvhgktLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFL 88
Cdd:PRK10874 2 NVFNPAQFRAQFPALQDA-----GVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 89 NAGSVDEIVFTKNATEAINTVAYGYGMPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKR 168
Cdd:PRK10874 77 NAPDAKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 169 LSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRA 248
Cdd:PRK10874 157 ITPRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 249 QMLEKMRPFQGGGEMIEEVTEENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRIN 328
Cdd:PRK10874 237 ELLEAMSPWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 329 SLRIFgNAPDKgAIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALEK 408
Cdd:PRK10874 317 GFRSF-RCQDS-SLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDR 394
|
.
gi 489053876 409 A 409
Cdd:PRK10874 395 A 395
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
11-413 |
3.93e-133 |
|
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This protein, found Escherichia coli, Yersinia pestis, Photorhabdus luminescens, and related species, and related to SufS, works together with and physically interacts with CsdE (a paralog of SufE). CsdA has cysteine desulfurase activity that is enhanced by CsdE, a sulfur acceptor protein. This gene pair, although involved in FeS cluster biosynthesis, is not found next to other such genes as are its paralogs from the Suf or Isc systems. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274558 [Multi-domain] Cd Length: 398 Bit Score: 388.04 E-value: 3.93e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 11 YDVEAIRRDFPILSRQvhgktLVYLDNGASAQKPQSVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNA 90
Cdd:TIGR03392 1 FNPAQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 91 GSVDEIVFTKNATEAINTVAYGYGMPFIGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLS 170
Cdd:TIGR03392 76 PDAENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 171 ERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQM 250
Cdd:TIGR03392 156 PRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 251 LEKMRPFQGGGEMIEEVTEENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGRHAILAHEADLRDYAHERLGRINSL 330
Cdd:TIGR03392 236 LEAMPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 331 RIFgNAPDKgAIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTSTCRASFALYNTRAEVDALAEALEKAR 410
Cdd:TIGR03392 316 RSF-RCQGS-SLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRAL 393
|
...
gi 489053876 411 KFF 413
Cdd:TIGR03392 394 ELL 396
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
11-406 |
1.62e-75 |
|
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: 240.42 E-value: 1.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 11 YDVEAIRRDFPILSRQVhgktLVYLDNGASAQKPQSVIDAVTHAYANEYANvhRGLHFLSNAATDAY-EKSRETVRRFLN 89
Cdd:TIGR01976 1 FDVEAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAALTRSNAN--RGGAYESSRRADQVvDDAREAVADLLN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 90 AGSvDEIVFTKNATEAINTVAYGYGMPFiGEGDEILLSIMEHHSNIVPWHFIRERQGAKLVFTPVD-DNGVFHIEEFEKR 168
Cdd:TIGR01976 75 ADP-PEVVFGANATSLTFLLSRAISRRW-GPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDeATGELHPDDLASL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 169 LSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSgIGVLYGRA 248
Cdd:TIGR01976 153 LSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 249 QMLEKMRPFQgggemieevteENVTYNHPPHRFEAGTPPIVQAIGLGAALEYMEKIGR--------------HAILAHEA 314
Cdd:TIGR01976 232 ELLMNLPPYK-----------LTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGEsangsrrerlvasfQAIDAYEN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 315 DLRDYAHERLGRINSLRIFG--NAPDKGAIISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFGVTS---TCRAS 389
Cdd:TIGR01976 301 RLAEYLLVGLSDLPGVTLYGvaRLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDeggVVRVG 380
|
410
....*....|....*..
gi 489053876 390 FALYNTRAEVDALAEAL 406
Cdd:TIGR01976 381 LAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
33-409 |
3.46e-73 |
|
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: 233.79 E-value: 3.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 33 VYLDNGASAQKPQSVIDAVTHAYANEYANVHRgLHFLSNAATDAYEKSRETVRRFLNAGSvDEIVFTKNATEAINTVAYG 112
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAMLPYLTEYFGNPSS-LHSFGREARAALEEAREQVAALLGADP-EEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 113 YGMPFIGEGDEILLSIMEHHS--NIVPWHfirERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKLVAITHMSNTLGTVVP 190
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAvlETARFL---EKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 191 IKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMleKMRPFQGGGEMieevtEE 270
Cdd:COG1104 159 IAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGGQ-----ER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 271 NvtynhppHRfeAGTPPIVQAIGLGAALEYMEKiGRHAILAHEADLRDYAHERL-GRINSLRIFGnAPDKGA--IISFAL 347
Cdd:COG1104 232 G-------LR--SGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLlAAIPGVVING-DPENRLpnTLNFSF 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053876 348 EGIHAHDVSMVIDRAGVAVRAGTHCAQ------PLLKRFGVT-----STCRASFALYNTRAEVDALAEALEKA 409
Cdd:COG1104 301 PGVEGEALLLALDLAGIAVSSGSACSSgslepsHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEALKEI 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
33-400 |
7.66e-38 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 140.56 E-value: 7.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 33 VYLD-NGASAQKPQsVIDAVTHAYANEYANVHRGLHFLSNAATDAYEKSRETVRRFLNAGSvDEIVFTKNATEAINTVAY 111
Cdd:PLN02651 1 LYLDmQATTPIDPR-VLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADP-KEIIFTSGATESNNLAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 112 GYGMPFIGEGDEILLSIMEHhSNIVPWHFIRERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKLVAITHMSNTLGTVVPI 191
Cdd:PLN02651 79 GVMHFYKDKKKHVITTQTEH-KCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 192 KKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMLEKMRP-FQGGGEmieevtee 270
Cdd:PLN02651 158 EEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPlMSGGGQ-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 271 nvtynhpPHRFEAGTPPIVQAIGLGAALEYMEKIGRHaILAHEADLRDYAHERL-GRINSLRIFGNA-PDKGAI--ISFA 346
Cdd:PLN02651 230 -------ERGRRSGTENTPLVVGLGAACELAMKEMDY-DEKHMKALRERLLNGLrAKLGGVRVNGPRdPEKRYPgtLNLS 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053876 347 LEGIHAHDVSMVIdrAGVAVRAGTHC----AQP--LLKRFGV-----TSTCRASFALYNTRAEVD 400
Cdd:PLN02651 302 FAYVEGESLLMGL--KEVAVSSGSACtsasLEPsyVLRALGVpeemaHGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
73-409 |
1.18e-32 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 126.98 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 73 ATDAYEKSRETVRRFLNAGSvDEIVFTKNATE----AINTVAYGYGmpfiGEGDEILLSIMEHHSNIVPWHFIrERQGAK 148
Cdd:PRK14012 47 AEEAVDIARNQIADLIGADP-REIVFTSGATEsdnlAIKGAAHFYQ----KKGKHIITSKTEHKAVLDTCRQL-EREGFE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 149 LVFTPVDDNGVFHIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWY 228
Cdd:PRK14012 121 VTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 229 VFTGHKVYGPSGIGVLYGR--------AQMlekmrpfQGGGemieevteenvtynhppHR--FEAGTPPIVQAIGLGAAL 298
Cdd:PRK14012 201 SFSAHKIYGPKGIGALYVRrkprvrleAQM-------HGGG-----------------HErgMRSGTLPTHQIVGMGEAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 299 ----EYMEKIGRHaILAheadLRDYAHERLGRINSLRIFGNApDKGAI----ISFA-LEGihahdVSMVIDRAGVAVRAG 369
Cdd:PRK14012 257 riakEEMATENER-IRA----LRDRLWNGIKDIEEVYLNGDL-EQRVPgnlnVSFNyVEG-----ESLIMALKDLAVSSG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489053876 370 THCA----QP--LLKRFGVT-----STCRASFALYNTRAEVDALAEALEKA 409
Cdd:PRK14012 326 SACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEEIDYAIELVRKS 376
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
77-247 |
9.96e-31 |
|
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: 115.94 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 77 YEKSRETVRRFLNAGsVDEIVFTKNATEAINTVAYGYGMPfigeGDEILLSIMEHHSNIVpwhFIRERQGAKLVFTPVDD 156
Cdd:cd01494 2 LEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLALLGP----GDEVIVDANGHGSRYW---VAAELAGAKPVPVPVDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 157 NGVFHIE--EFEKRLSERTKLVAITHMSNTLGTV-VPIKKIVELAHARGVPVLVDGSQGAVHLP---VDVQDLGCDWYVF 230
Cdd:cd01494 74 AGYGGLDvaILEELKAKPNVALIVITPNTTSGGVlVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTF 153
|
170
....*....|....*..
gi 489053876 231 TGHKVYGPSGIGVLYGR 247
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
32-407 |
3.90e-29 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 116.75 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 32 LVYLDNGASAQKPQSVIDAVTHAYANEYANvHRGLHFLSNAATDAYEKSRETVRRFLNaGSVDEIVFTKNATE----AIN 107
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKAASQYFGN-ESSLHDIGGTASSLLQVCRKTFAEMIG-GEEQGIYFTSGGTEsnylAIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 108 TVAYGYGMpfigEGDEILLSIMEHHSNIVPWHFIrERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKLVAITHMSNTLGT 187
Cdd:PRK02948 79 SLLNALPQ----NKKHIITTPMEHASIHSYFQSL-ESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 188 VVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSGIGVLYGRAQMLEKMrpfqgggeMIEEV 267
Cdd:PRK02948 154 IQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKP--------VFPGT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 268 TEENvtynhpphRFEAGTppiVQAIGLGAALEYMEKIGRHAILAHE--ADLRDYAHERLgRINSLRI--FGNAPDKGA-I 342
Cdd:PRK02948 226 THEK--------GFRPGT---VNVPGIAAFLTAAENILKNMQEESLrfKELRSYFLEQI-QTLPLPIevEGHSTSCLPhI 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053876 343 ISFALEGIHAHDVSMVIDRAGVAVRAGTHCAQPL------LKRFGVTST-----CRASFALYNTRAEVDALAEALE 407
Cdd:PRK02948 294 IGVTIKGIEGQYTMLECNRRGIAISTGSACQVGKqepsktMLAIGKTYEeakqfVRFSFGQQTTKDQIDTTIHALE 369
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
94-244 |
4.50e-15 |
|
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: 75.89 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 94 DEIVFTKNATEAINTVAYGYGMPfigeGDEILLSIMEHHSNIVPwhfiRERQGAKLVFTPVDDNGVFH---------IEE 164
Cdd:cd06452 60 DEARVTPGAREGKFAVMHSLCEK----GDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGHPEYHitpegyaevIEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 165 FEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSG-IGV 243
Cdd:cd06452 132 VKDEFGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASApIGV 211
|
.
gi 489053876 244 L 244
Cdd:cd06452 212 L 212
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
56-406 |
7.51e-15 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 75.42 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 56 ANEYANVHRGLHFLSNaaTDAYEKSRETVRRFLNAGSV------DEIVFTKNATEAINTVAYGYGMPfigeGDEILLSIM 129
Cdd:pfam00155 22 AEKDALAGGTRNLYGP--TDGHPELREALAKFLGRSPVlkldreAAVVFGSGAGANIEALIFLLANP----GDAILVPAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 130 EH--HSNIVPWHfirerqGAKLVFTPVDDNGVFHI--EEFEKRLSERTKLVAITHMSNTLGTVVP---IKKIVELAHARG 202
Cdd:pfam00155 96 TYasYIRIARLA------GGEVVRYPLYDSNDFHLdfDALEAALKEKPKVVLHTSPHNPTGTVATleeLEKLLDLAKEHN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 203 VPVLVD--------GSQGAVHLPVDVQDLGCDWYVFTGHKVYGPSG--IGVLYGRAQMLEKMRPFQGGGemieevteenv 272
Cdd:pfam00155 170 ILLLVDeayagfvfGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrVGYILGNAAVISQLRKLARPF----------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 273 tynhpphRFEAGTPPIVQAIgLGAALEYMEKIgrHAILAHEADLRDYAHERLGRINslriFGNAPDKGAIISFA-LEGIH 351
Cdd:pfam00155 239 -------YSSTHLQAAAAAA-LSDPLLVASEL--EEMRQRIKERRDYLRDGLQAAG----LSVLPSQAGFFLLTgLDPET 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053876 352 AHDVSMV-IDRAGVAVRAGTHcaqpllkrFGVTSTCRASFALYnTRAEVDALAEAL 406
Cdd:pfam00155 305 AKELAQVlLEEVGVYVTPGSS--------PGVPGWLRITVAGG-TEEELEELLEAI 351
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
82-244 |
4.97e-14 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 73.04 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 82 ETVRRFLNagsVDEIVFTKNATEAINTVAYGYGmpfiGEGDEILLSIMEHHSNIVPwhfiRERQGAKLVFTPVDDNGVFH 161
Cdd:PRK09331 70 EDLAEFLG---MDEARVTHGAREGKFAVMHSLC----KKGDYVVLDGLAHYTSYVA----AERAGLNVREVPKTGYPEYK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 162 ---------IEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLGCDWYVFTG 232
Cdd:PRK09331 139 itpeayaekIEEVKEETGKPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSG 218
|
170
....*....|...
gi 489053876 233 HKVYGPSG-IGVL 244
Cdd:PRK09331 219 HKSMAASApSGVL 231
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
44-408 |
1.58e-11 |
|
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: 65.06 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 44 PQSVIDAVTHAYANEYANVH---RGLHFLSNAATDAYEksretvRRFLNAGSVDEIVFTKNATEAINTVAygygMPFIGE 120
Cdd:cd00609 13 PPEVLEALAAAALRAGLLGYypdPGLPELREAIAEWLG------RRGGVDVPPEEIVVTNGAQEALSLLL----RALLNP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 121 GDEILLSImehhsnivP-WHFIR---ERQGAKLVFTPVDDNGVF--HIEEFEKRLSERTKLVAITHMSNTLGTVVP---I 191
Cdd:cd00609 83 GDEVLVPD--------PtYPGYEaaaRLAGAEVVPVPLDEEGGFllDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 192 KKIVELAHARGVPVLVD------GSQGAVHLPVD-VQDLGCDWYVFTGHKVYGPSG--IGVLYGRAqmlekmrpfqggge 262
Cdd:cd00609 155 EELAELAKKHGILIISDeayaelVYDGEPPPALAlLDAYERVIVLRSFSKTFGLPGlrIGYLIAPP-------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 263 miEEVTEENVTYnhppHRFEAGTPPIVQAIGLGAALEYMEKIgRHAILAHEADLRDYAHERLGRINSLRIFgnaPDKGAI 342
Cdd:cd00609 221 --EELLERLKKL----LPYTTSGPSTLSQAAAAAALDDGEEH-LEELRERYRRRRDALLEALKELGPLVVV---KPSGGF 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053876 343 ISFA--LEGIHAHDVSMVIDRAGVAVRAGTHCAQPLLKRFgvtstcRASFAlyNTRAEVDALAEALEK 408
Cdd:cd00609 291 FLWLdlPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFV------RLSFA--TPEEELEEALERLAE 350
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
71-265 |
3.60e-10 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 60.31 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 71 NAATDAYEKSReTVRRFLNAGS----VDEIVFTKNATEAiNTVAYgygMPFIGEGDEILLsimEHHSNIvpwHF-----I 141
Cdd:pfam01212 22 MVGDEVYGGDP-TVNRLEDRVAelfgKEAALFVPSGTAA-NQLAL---MAHCQRGDEVIC---GEPAHI---HFdetggH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 142 RERQGAKLVFTPVDDNGVFHIEEFEKRLSE-------RTKLVAITHMSNTL-GTVVP---IKKIVELAHARGVPVLVDG- 209
Cdd:pfam01212 91 AELGGVQPRPLDGDEAGNMDLEDLEAAIREvgadifpPTGLISLENTHNSAgGQVVSlenLREIAALAREHGIPVHLDGa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053876 210 --SQGAVHLPVDVQDL--GCDWYVFTGHKVYG-PSGiGVLYGRAQMLEKMRPFQG--GGEMIE 265
Cdd:pfam01212 171 rfANAAVALGVIVKEItsYADSVTMCLSKGLGaPVG-SVLAGSDDFIAKAIRQRKylGGGLRQ 232
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
44-413 |
3.04e-09 |
|
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: 58.22 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 44 PQSVIDAVTHAYANE---YANVhRGLHFLSNAATDAYeksretvRRFLNAG-SVDEIVFTKNATEAINTVAygygMPFIG 119
Cdd:COG0436 45 PDHIREAAIEALDDGvtgYTPS-AGIPELREAIAAYY-------KRRYGVDlDPDEILVTNGAKEALALAL----LALLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 120 EGDEILLsimehhsnIVPW-----HFIReRQGAKLVFTPVDDNGVFHI--EEFEKRLSERTKLVAITHMSNTLGTVVP-- 190
Cdd:COG0436 113 PGDEVLV--------PDPGypsyrAAVR-LAGGKPVPVPLDEENGFLPdpEALEAAITPRTKAIVLNSPNNPTGAVYSre 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 191 -IKKIVELAHARGVPVLVD------GSQGAVHLPV-DVQDLGCDWYVFTGH-KVYGPSG--IGVLYGRAQMLEKMRPFQG 259
Cdd:COG0436 184 eLEALAELAREHDLLVISDeiyeelVYDGAEHVSIlSLPGLKDRTIVINSFsKSYAMTGwrIGYAVGPPELIAALLKLQS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 260 ggemieevteeNVTYNhpphrfeagTPPIVQAiglgAALEYMEkiGRHAILAHEADL----RDYAHERLGRINslriFGN 335
Cdd:COG0436 264 -----------NLTSC---------APTPAQY----AAAAALE--GPQDYVEEMRAEyrrrRDLLVEGLNEIG----LSV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 336 APDKGAIISFA-LEGIHAHDVSMV---IDRAGVAVRAGTHcaqpllkrFGVTSTC--RASFAlyntrAEVDALAEALEKA 409
Cdd:COG0436 314 VKPEGAFYLFAdVPELGLDSEEFAerlLEEAGVAVVPGSA--------FGPAGEGyvRISYA-----TSEERLEEALERL 380
|
....
gi 489053876 410 RKFF 413
Cdd:COG0436 381 ARFL 384
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
66-411 |
1.30e-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: 56.14 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 66 LHFLSNAATDAYEKSRETVRRFLNAGSVDEIVFTKNATEAINTVAYGygmpFIGEGDEILLSIMEHHSNIvpWHFIRERQ 145
Cdd:cd06451 23 LGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSN----LLEPGDKVLVGVNGVFGDR--WADMAERY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 146 GAKLVFTPVDDNGVFHIEEFEKRLSERT-KLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAVHLPVDVQDLG 224
Cdd:cd06451 97 GADVDVVEKPWGEAVSPEEIAEALEQHDiKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVDAVSSLGGEPFRMDEWG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 225 CDwYVFTG-HKVYG-PSGIGVL------YGRAQMLEKMRPFQGGGEMIEEVTEENVTYNHpphrfeagTPPIVQAIGLGA 296
Cdd:cd06451 177 VD-VAYTGsQKALGaPPGLGPIafseraLERIKKKTKPKGFYFDLLLLLKYWGEGYSYPH--------TPPVNLLYALRE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 297 ALEYMEKIGRHAILAHEADLRDYAHERLGRInSLRIFGNAPDKGAIISFAL--EGIHAHDV-SMVIDRAGVAVRAGTHCA 373
Cdd:cd06451 248 ALDLILEEGLENRWARHRRLAKALREGLEAL-GLKLLAKPELRSPTVTAVLvpEGVDGDEVvRRLMKRYNIEIAGGLGPT 326
|
330 340 350
....*....|....*....|....*....|....*...
gi 489053876 374 QPLLKRFGVTStcrasfalYNTRAEVDALAEALEKARK 411
Cdd:cd06451 327 AGKVFRIGHMG--------EATREDVLGVLSALEEALK 356
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
143-311 |
3.27e-08 |
|
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: 55.10 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 143 ERQGAKLVFTPVDDNGVFHIEEFEKRLSE--RTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDG--SQGAVhlPV 218
Cdd:COG0075 94 ERYGAEVVVLEVPWGEAVDPEEVEEALAAdpDIKAVAVVHNETSTGVLNPLEEIGALAKEHGALLIVDAvsSLGGV--PL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 219 DVQDLGCDWYVFTGHKVY-GPSGIGVLYGRAQMLEKMRPFQGGG-----EMIEEVTEENVTynhpPHrfeagTPPIVQAI 292
Cdd:COG0075 172 DMDEWGIDVVVSGSQKCLmLPPGLAFVAVSERALEAIEARKLPSyyldlKLWLKYWEKGQT----PY-----TPPVSLLY 242
|
170 180
....*....|....*....|....*
gi 489053876 293 GLGAALEYMEKIG------RHAILA 311
Cdd:COG0075 243 ALREALDLILEEGlenrfaRHRRLA 267
|
|
| SelA |
COG1921 |
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]; |
161-255 |
5.87e-08 |
|
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441524 Cd Length: 399 Bit Score: 54.36 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 161 HIEEFEKRLSERTKLVAITHMSNT--LGTV--VPIKKIVELAHARGVPVLVD-GSQ--------GAVHLPvDVQDL---G 224
Cdd:COG1921 143 HLRDYEAAITENTAALLKVHTSNYriVGFTeeVSLAELAELAHEHGLPVIVDlGSGslvdlskyGLPHEP-TVQEYlaaG 221
|
90 100 110
....*....|....*....|....*....|...
gi 489053876 225 CDWYVFTGHKVY-GP-SGIGVlyGRAQMLEKMR 255
Cdd:COG1921 222 ADLVTFSGDKLLgGPqAGIIV--GKKELIERIK 252
|
|
| SelA |
pfam03841 |
L-seryl-tRNA selenium transferase; |
141-255 |
1.56e-07 |
|
L-seryl-tRNA selenium transferase;
Pssm-ID: 309101 Cd Length: 367 Bit Score: 53.11 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 141 IRERQGAKLVftPVDDNGVFHIEEFEKRLSERTKLVAITHMSN--TLGTV--VPIKKIVELAHARGVPVLVD-GSQGAVH 215
Cdd:pfam03841 107 VMKQAGVKLV--EVGTTNRTHLKDYEQAINENTALLMKVHTSNyrIQGFTkeVELAELVELGHEKGLPVYEDlGSGSLVD 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489053876 216 L-----PVD--VQDL---GCDWYVFTGHKVYGPSGIGVLYGRAQMLEKMR 255
Cdd:pfam03841 185 LsqyglPKEptVQELiaqGVDLVSFSGDKLLGGPQAGIIVGKKELIERIK 234
|
|
| Cys_Met_Meta_PP |
pfam01053 |
Cys/Met metabolism PLP-dependent enzyme; This family includes enzymes involved in cysteine and ... |
144-226 |
1.70e-07 |
|
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: 53.01 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 144 RQGAKLVFTPVDDngvfhIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAvhlPVDVQ-- 221
Cdd:pfam01053 109 RFGIEVTFVDTSD-----PEDLEAAIKPNTKAVYLETPTNPLLKVVDIEAIAKLAKKHGILVVVDNTFAS---PYLQRpl 180
|
....*
gi 489053876 222 DLGCD 226
Cdd:pfam01053 181 DLGAD 185
|
|
| MET17 |
COG2873 |
O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid ... |
144-208 |
2.87e-06 |
|
O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; O-acetylhomoserine/O-acetylserine sulfhydrylase, pyridoxal phosphate-dependent is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 442120 [Multi-domain] Cd Length: 428 Bit Score: 49.26 E-value: 2.87e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053876 144 RQGAKLVFTPVDDngvfhIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVD 208
Cdd:COG2873 125 RLGIEVRFVDPDD-----PEAFEAAIDPNTKAIFGETIGNPALDVLDIEAIAEIAHEHGVPLIVD 184
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
146-208 |
3.54e-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: 48.74 E-value: 3.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053876 146 GAKLVFTPVDDngvfhIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVD 208
Cdd:cd00614 104 GIEVTFVDPDD-----PEALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| PRK05994 |
PRK05994 |
O-acetylhomoserine aminocarboxypropyltransferase; Validated |
146-208 |
5.38e-05 |
|
O-acetylhomoserine aminocarboxypropyltransferase; Validated
Pssm-ID: 180344 [Multi-domain] Cd Length: 427 Bit Score: 45.09 E-value: 5.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053876 146 GAKLVFTPVDDngvfhIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVD 208
Cdd:PRK05994 127 GWQVRWADADD-----PASFERAITPRTKAIFIESIANPGGTVTDIAAIAEVAHRAGLPLIVD 184
|
|
| WecE |
COG0399 |
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis]; |
118-215 |
1.29e-04 |
|
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440168 Cd Length: 364 Bit Score: 43.90 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 118 IGEGDEIllsimehhsnIVP-------WHFIReRQGAKLVFtpVD-DNGVFHI--EEFEKRLSERTKLVAITHMsntLGT 187
Cdd:COG0399 67 IGPGDEV----------ITPaftfvatANAIL-YVGATPVF--VDiDPDTYNIdpEALEAAITPRTKAIIPVHL---YGQ 130
|
90 100 110
....*....|....*....|....*....|
gi 489053876 188 VVPIKKIVELAHARGVPVLVDGSQ--GAVH 215
Cdd:COG0399 131 PADMDAIMAIAKKHGLKVIEDAAQalGATY 160
|
|
| PRK07568 |
PRK07568 |
pyridoxal phosphate-dependent aminotransferase; |
44-198 |
1.85e-04 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181036 Cd Length: 397 Bit Score: 43.30 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 44 PQSVIDAVTHaYANE---YANvHRGLHFLSNAATDAYEKSRETVrrflnagSVDEIVFTKNATEAINTVAygygMPFIGE 120
Cdd:PRK07568 45 PEVFFEAIKN-YDEEvlaYSH-SQGIPELREAFAKYYKKWGIDV-------EPDEILITNGGSEAILFAM----MAICDP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 121 GDEIllsimehhsnIVPWHF------IRERQGAKLV--FTPVDDNgvFH---IEEFEKRLSERTKLVAITHMSNTLGTVV 189
Cdd:PRK07568 112 GDEI----------LVPEPFyanyngFATSAGVKIVpvTTKIEEG--FHlpsKEEIEKLITPKTKAILISNPGNPTGVVY 179
|
170
....*....|..
gi 489053876 190 P---IKKIVELA 198
Cdd:PRK07568 180 TkeeLEMLAEIA 191
|
|
| PLN02242 |
PLN02242 |
methionine gamma-lyase |
139-264 |
2.86e-04 |
|
methionine gamma-lyase
Pssm-ID: 215134 Cd Length: 418 Bit Score: 42.83 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 139 HFIRERQGAKLVFTPVDDngvfhIEEFEKRLSE-RTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAvhLP 217
Cdd:PLN02242 134 HFLPRKCNITTTFVDITD-----LEAVKKAVVPgKTKVLYFESISNPTLTVADIPELARIAHEKGVTVVVDNTFAP--MV 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489053876 218 VDVQDLGCDWYVFTGHK-VYGPSGI--GVLYGRAQMLEKMRPFQGGGEMI 264
Cdd:PLN02242 207 LSPARLGADVVVHSISKfISGGADIiaGAVCGPAELVNSMMDLHHGALML 256
|
|
| MetC |
COG0626 |
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ... |
141-208 |
4.54e-04 |
|
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: 41.96 E-value: 4.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053876 141 IRERQGAKLVFTPVDDngvfhIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVD 208
Cdd:COG0626 117 VLARFGIEVTFVDPTD-----LAAVEAAIRPNTKLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
|
|
| PLN02509 |
PLN02509 |
cystathionine beta-lyase |
161-253 |
5.25e-04 |
|
cystathionine beta-lyase
Pssm-ID: 178125 [Multi-domain] Cd Length: 464 Bit Score: 41.94 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 161 HIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGSqgaVHLPVDVQ--DLGCDWYVFTGHK-VYG 237
Cdd:PLN02509 206 NLDEVAAAIGPQTKLVWLESPTNPRQQISDIRKIAEMAHAQGALVLVDNS---IMSPVLSRplELGADIVMHSATKfIAG 282
|
90
....*....|....*...
gi 489053876 238 PSGI--GVLYGRAQMLEK 253
Cdd:PLN02509 283 HSDVmaGVLAVKGEKLAK 300
|
|
| PRK05764 |
PRK05764 |
aspartate aminotransferase; Provisional |
146-208 |
5.26e-04 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 235596 Cd Length: 393 Bit Score: 42.03 E-value: 5.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053876 146 GAKLVFTPVD-DNGvFHI--EEFEKRLSERTKLVAITHMSNTLGTVVP---IKKIVELAHARGVPVLVD 208
Cdd:PRK05764 136 GGVPVFVPTGeENG-FKLtvEQLEAAITPKTKALILNSPSNPTGAVYSpeeLEAIADVAVEHDIWVLSD 203
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
145-408 |
5.53e-04 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 41.55 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 145 QGAKLVftPVD-DNGVFHIEEFEKRL-------SERTKLVAITHMSNtLGTVVP---IKKIVELAHARGVPVLVDGSQ-- 211
Cdd:cd06502 94 SGVKLL--PVPgENGKLTPEDLEAAIrprddihFPPPSLVSLENTTE-GGTVYPldeLKAISALAKENGLPLHLDGARla 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 212 -GAVHLPVDVQDL--GCDWYVFTGHKVYGPSGIGVLYGRAQMLEKMRPFQ---GGGemieevteenvtynhpphrfeagt 285
Cdd:cd06502 171 nAAAALGVALKTYksGVDSVSFCLSKGGGAPVGAVVVGNRDFIARARRRRkqaGGG------------------------ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 286 ppIVQAIGLGAALEYMekigrhaiLAHEADLR--DYAHErlgriNSLRIFGNAPDKGAIISFALEGIHAHDVSMVidrAG 363
Cdd:cd06502 227 --MRQSGFLAAAGLAA--------LENDLWLRrlRHDHE-----MARRLAEALEELGGLESEVQTNIVLLDPVEA---NA 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489053876 364 VAVRAGTHCAQPLLKRFGV----TSTCRASFALYNTRAEVDALAEALEK 408
Cdd:cd06502 289 VFVELSKEAIERRGEGVLFyawgEGGVRFVTHWDTTEEDVDELLSALKA 337
|
|
| PRK06084 |
PRK06084 |
bifunctional O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase; |
144-210 |
6.26e-04 |
|
bifunctional O-acetylhomoserine aminocarboxypropyltransferase/cysteine synthase;
Pssm-ID: 180392 [Multi-domain] Cd Length: 425 Bit Score: 41.81 E-value: 6.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053876 144 RQGAKLVFTPVDDngvfhIEEFEKRLSERTKLVAITHMSNTLGTVVPIKKIVELAHARGVPVLVDGS 210
Cdd:PRK06084 120 RIGIETRFAAHDD-----IAALEALIDERTKAVFCESIGNPAGNIIDIQALADAAHRHGVPLIVDNT 181
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
143-242 |
1.68e-03 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 40.29 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 143 ERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKLVAITHmSNTLGTVVP-IKKIVELAHARGVPVLVDGSqgavhlPVDVQ 221
Cdd:cd00613 130 EPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQY-PNTLGVFEDlIKEIADIAHSAGALVYVDGD------NLNLT 202
|
90 100
....*....|....*....|....*..
gi 489053876 222 ------DLGCDWYVFTGHKVYGPSGIG 242
Cdd:cd00613 203 glkppgEYGADIVVGNLQKTGVPHGGG 229
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
103-219 |
3.52e-03 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 39.15 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 103 TEAINTVaygyGMPFIGEGDEILLSIMEHHSNIvpwHFIrERQGAKLVFTPVDDNGVFHI------EEFEKRLSERT--K 174
Cdd:cd00615 85 SSSNKAV----ILAVCGPGDKILIDRNCHKSVI---NGL-VLSGAVPVYLKPERNPYYGIaggippETFKKALIEHPdaK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489053876 175 LVAITHmSNTLGTVVPIKKIVELAHARGVPVLVDGSQGAvHLPVD 219
Cdd:cd00615 157 AAVITN-PTYYGICYNLRKIVEEAHHRGLPVLVDEAHGA-HFRFH 199
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
141-253 |
4.07e-03 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 39.13 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 141 IRERQGAKLVFTPVDDNGVFHIEEFEKRLSERTKL--VAITHMSNTLGTVVPIKKIVELAHARGVPVLVDG--SQGAVhl 216
Cdd:PRK13479 98 IAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRIthVALVHCETTTGILNPLDEIAAVAKRHGKRLIVDAmsSFGAI-- 175
|
90 100 110
....*....|....*....|....*....|....*...
gi 489053876 217 PVDVQDLGCDWYVFTGHK-VYGPSGIGVLYGRAQMLEK 253
Cdd:PRK13479 176 PIDIAELGIDALISSANKcIEGVPGFGFVIARRSELEA 213
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
275-406 |
4.87e-03 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 38.99 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053876 275 NHPPHRFEAGTPPIVqAIGLGAALEYMEKIGRHAiLAHEADLRDYAHERLGRinslrifgNAPDKGAIISfaLEGIHAHD 354
Cdd:PRK05937 234 NSPPLRYSTGLPPHL-LISIQVAYDFLSQEGELA-RKQLFRLKEYFAQKFSS--------AAPGCVQPIF--LPGISEQE 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489053876 355 VSMVIDRAGVAVRAGTHCAQPLLkrfgvtstcRASFALYNTRAEVDALAEAL 406
Cdd:PRK05937 302 LYSKLVETGIRVGVVCFPTGPFL---------RVNLHAFNTEDEVDILVSVL 344
|
|
| |
