|
Name |
Accession |
Description |
Interval |
E-value |
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
14-405 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 594.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 14 NYRSDFPAIPENWSYLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANEIVFV 93
Cdd:COG0520 4 AIRADFPVLGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAASPDEIIFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 94 RGATEAINLVAQIWGatHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLA 173
Cdd:COG0520 84 RGTTEAINLVAYGLG--RLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 174 HISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAPWQG 253
Cdd:COG0520 162 HVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLEALPPFLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 254 GGAMIDQVTFEKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFG---AD 330
Cdd:COG0520 242 GGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRILGpadPE 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540327402 331 DSAAILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSRVVSI 405
Cdd:COG0520 322 DRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
28-399 |
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: 590.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 28 YLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANEIVFVRGATEAINLVAQIW 107
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 108 GATHlNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLAHISNVLGSVLDVSK 187
Cdd:cd06453 82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 188 ARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAPWQGGGAMIDQVTFEKTT 267
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEETT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 268 YLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFG-ADDSAAILSFSMDGIHPH 346
Cdd:cd06453 241 YADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGdAEDRAGVVSFNLEGIHPH 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2540327402 347 DIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGL 399
Cdd:cd06453 321 DVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
14-406 |
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: 581.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 14 NYRSDFPAIPEN-----WSYLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSAN 88
Cdd:TIGR01979 2 NIRADFPILKRKingkpLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 89 EIVFVRGATEAINLVAQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHK 168
Cdd:TIGR01979 82 EIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKTK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 169 LLSLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSM 248
Cdd:TIGR01979 162 LVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 249 APWQGGGAMIDQVTFEKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFG 328
Cdd:TIGR01979 242 PPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIYG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 329 ---ADDSAAILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSRVVSI 405
Cdd:TIGR01979 322 prdAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVRKF 401
|
.
gi 2540327402 406 F 406
Cdd:TIGR01979 402 F 402
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
28-395 |
2.21e-174 |
|
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: 490.99 E-value: 2.21e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 28 YLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANEIVFVRGATEAINLVAQIW 107
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 108 GAtHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLAHISNVLGSVLDVSK 187
Cdd:pfam00266 82 GR-SLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 188 ARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAPWQGGGAMIDQVTFEKTT 267
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQEST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 268 YLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFGADDSAAILSFSMDGIHPHD 347
Cdd:pfam00266 241 FADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNFKGVHPHD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2540327402 348 IGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERL 395
Cdd:pfam00266 321 VATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
16-401 |
9.75e-172 |
|
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: 493.99 E-value: 9.75e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 16 RSDFPAIPE--N-----WsyLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSAN 88
Cdd:NF041166 231 RRDFPILQErvNgkplvW--FDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGAPSVD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 89 EIVFVRGATEAINLVAQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHK 168
Cdd:NF041166 309 EIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLNPRTK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 169 LLSLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSM 248
Cdd:NF041166 389 LVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDLLEAM 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 249 APWQGGGAMIDQVTFEKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFG 328
Cdd:NF041166 469 PPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPGLRLIG 548
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540327402 329 -ADDSAAILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSR 401
Cdd:NF041166 549 tAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRR 622
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
16-406 |
7.35e-170 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 481.94 E-value: 7.35e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 16 RSDFPAIPENWS-----YLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANEI 90
Cdd:PLN02855 18 RPDFPILDQTVNgsklvYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTSREI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 91 VFVRGATEAINLVAQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLL 170
Cdd:PLN02855 98 VFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 171 SLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAP 250
Cdd:PLN02855 178 ATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 251 WQGGGAMIDQVTFEKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFG-- 328
Cdd:PLN02855 258 FLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRIYGpk 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 329 ---ADDSAAILSFSMDGIHPHDIGTILDEE-GVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSRVVS 404
Cdd:PLN02855 338 pseGVGRAALCAFNVEGIHPTDLSTFLDQQhGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALKDTIA 417
|
..
gi 2540327402 405 IF 406
Cdd:PLN02855 418 FF 419
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
16-402 |
4.20e-161 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 458.83 E-value: 4.20e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 16 RSDFPAIPEN-----WSYLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANEI 90
Cdd:PRK09295 9 RADFPVLSREvnglpLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINARSAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 91 VFVRGATEAINLVAQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLL 170
Cdd:PRK09295 89 VFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDERTRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 171 SLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAP 250
Cdd:PRK09295 169 AITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 251 WQGGGAMIDQVTF-EKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFGA 329
Cdd:PRK09295 249 WEGGGSMIATVSLtEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGP 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540327402 330 DDSAAILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSRV 402
Cdd:PRK09295 329 QNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQRI 401
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
13-406 |
1.08e-147 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 424.84 E-value: 1.08e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 13 FN---YRSDFPAIPENWSYLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANE 89
Cdd:PRK10874 4 FNpaqFRAQFPALQDAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPDAKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 90 IVFVRGATEAINLVAQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKL 169
Cdd:PRK10874 84 IVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPRTRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 170 LSLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMA 249
Cdd:PRK10874 164 LALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 250 PWQGGGAMIDQVTFEKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFGA 329
Cdd:PRK10874 244 PWQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPGFRSFRC 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540327402 330 DDSaAILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSRVVSIF 406
Cdd:PRK10874 324 QDS-SLLAFDFAGVHHSDLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRALELL 399
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
15-406 |
7.59e-137 |
|
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: 396.90 E-value: 7.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 15 YRSDFPAIPENWSYLDSAATAQKPKAVIDAVYKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAKSANEIVFVR 94
Cdd:TIGR03392 6 FRRQFPALQDATVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDAENIVWTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 95 GATEAINLVAQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLAH 174
Cdd:TIGR03392 86 GTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRTRILALGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 175 ISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAPWQGG 254
Cdd:TIGR03392 166 MSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEAMPPWQGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 255 GAMIDQVTFEKTTYLDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIKGLRLFGADDSaA 334
Cdd:TIGR03392 246 GKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSFRCQGS-S 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540327402 335 ILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPATARASFGLYNEEQDIERLAAGLSRVVSIF 406
Cdd:TIGR03392 325 LLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRALELL 396
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
28-403 |
1.28e-67 |
|
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: 219.15 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 28 YLDSAATAQKPKAVIDAVYKAYAVDYA---TVHRgvYSRSAdmtKEK-EKARETVARFIGAKsANEIVFVRGATEAINLV 103
Cdd:COG1104 5 YLDNAATTPVDPEVLEAMLPYLTEYFGnpsSLHS--FGREA---RAAlEEAREQVAALLGAD-PEEIIFTSGGTEANNLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 104 aqIWGATHLNQ--GDRILISQLEHHSNIVPWQLLRdRMGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLAHISNVLGS 181
Cdd:COG1104 79 --IKGAARAYRkkGKHIITSAIEHPAVLETARFLE-KEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 182 VLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDIldSMAPWQGGGAmidQv 261
Cdd:COG1104 156 IQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGG---Q- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 262 tfEKttyldppaRFEAGTPHIVGTLGLAAAIEYLENiGMEKVACHEAALTKMARKRLKD-IKGLRLFGADDSAA--ILSF 338
Cdd:COG1104 230 --ER--------GLRSGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLLAaIPGVVINGDPENRLpnTLNF 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540327402 339 SMDGIHPHDIGTILDEEGVAIRAGHHCA----QP---LMAhLNVPATA-----RASFGLYNEEQDIERLAAGLSRVV 403
Cdd:COG1104 299 SFPGVEGEALLLALDLAGIAVSSGSACSsgslEPshvLLA-MGLDEELahgsiRFSLGRFTTEEEIDRAIEALKEIV 374
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
16-399 |
2.49e-63 |
|
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: 208.45 E-value: 2.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 16 RSDFPAIPE-NWSYLDSAATAQKPKAVIDAVyKAYAVDYATVHRGVYSRSADMTKEKEKARETVARFIGAkSANEIVFVR 94
Cdd:TIGR01976 7 RGQFPALADgDRVFFDNPAGTQIPQSVADAV-SAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNA-DPPEVVFGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 95 GATEAINLVAQIWGAThLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLDEE-GRIDLDAAARMIRPEHKLLSLA 173
Cdd:TIGR01976 85 NATSLTFLLSRAISRR-WGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtGELHPDDLASLLSPRTRLVAVT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 174 HISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTgIGVLWAKSDILDSMAPwqg 253
Cdd:TIGR01976 164 AASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPELLMNLPP--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 254 ggamiDQVTFEKTTyldPPARFEAGTPHIVGTLGLAAAIEYLENIG--------------MEKVACHEAALTKMARKRLK 319
Cdd:TIGR01976 240 -----YKLTFSYDT---GPERFELGTPQYELLAGVVAAVDYLAGLGesangsrrerlvasFQAIDAYENRLAEYLLVGLS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 320 DIKGLRLFGADDSAA---ILSFSMDGIHPHDIGTILDEEGVAIRAGHHCAQPLMAHLNVPA---TARASFGLYNEEQDIE 393
Cdd:TIGR01976 312 DLPGVTLYGVARLAArvpTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDeggVVRVGLAHYNTAEEVD 391
|
....*.
gi 2540327402 394 RLAAGL 399
Cdd:TIGR01976 392 RLLEAL 397
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
28-393 |
9.95e-30 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 118.22 E-value: 9.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 28 YLDSAATAQKPKAVIDAVYKAYAVDYATVH-RG-VYSRSADmtKEKEKARETVARFIGAkSANEIVFVRGATEAINLVaq 105
Cdd:PLN02651 2 YLDMQATTPIDPRVLDAMLPFLIEHFGNPHsRThLYGWESE--DAVEKARAQVAALIGA-DPKEIIFTSGATESNNLA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 106 IWGATHLNQGDR--ILISQLEHHSNIVPWQLLRDRmGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLAHISNVLGSVL 183
Cdd:PLN02651 77 IKGVMHFYKDKKkhVITTQTEHKCVLDSCRHLQQE-GFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 184 DVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDILDSMAPWQGGGAMidqvtf 263
Cdd:PLN02651 156 PVEEIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLMSGGGQ------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 264 ekttyldpparfEAG-------TPHIVGtLGLAAAIEYLEnigMEKVACHEAALTKMARKRLKD-IKGLRLFGADDSAA- 334
Cdd:PLN02651 230 ------------ERGrrsgtenTPLVVG-LGAACELAMKE---MDYDEKHMKALRERLLNGLRAkLGGVRVNGPRDPEKr 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540327402 335 ---ILSFSMDGIHPhdiGTILDE-EGVAIRAGHHC----AQP---LMAhLNVP-----ATARASFGLYNEEQDIE 393
Cdd:PLN02651 294 ypgTLNLSFAYVEG---ESLLMGlKEVAVSSGSACtsasLEPsyvLRA-LGVPeemahGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
72-321 |
3.18e-28 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 114.65 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 72 EKARETVARFIGAKSaNEIVFVRGATEAINLVaqIWGATHL--NQGDRILISQLEHHSNIVPWQLLrDRMGFAIDVIPLD 149
Cdd:PRK14012 52 DIARNQIADLIGADP-REIVFTSGATESDNLA--IKGAAHFyqKKGKHIITSKTEHKAVLDTCRQL-EREGFEVTYLDPQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 150 EEGRIDLDAAARMIRPEHKLLSLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKL 229
Cdd:PRK14012 128 SNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 230 YAPTGIGVLWAKSDILDSMAPWQGGGAMidqvtfEKTtyldpparFEAGT---PHIVGtLGLAAAIEYLEnigMEKVACH 306
Cdd:PRK14012 208 YGPKGIGALYVRRKPRVRLEAQMHGGGH------ERG--------MRSGTlptHQIVG-MGEAARIAKEE---MATENER 269
|
250
....*....|....*
gi 2540327402 307 EAALTKMARKRLKDI 321
Cdd:PRK14012 270 IRALRDRLWNGIKDI 284
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
28-402 |
5.80e-26 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 107.89 E-value: 5.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 28 YLDSAATAQKPKAVIDAVYKAyAVDY----ATVHrGVYSRSADMTkekEKARETVARFIGAKsANEIVFVRGATEAINLV 103
Cdd:PRK02948 3 YLDYAATTPMSKEALQTYQKA-ASQYfgneSSLH-DIGGTASSLL---QVCRKTFAEMIGGE-EQGIYFTSGGTESNYLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 104 AQIWGATHLNQGDRILISQLEHHSNIVPWQLLRDRmGFAIDVIPLDEEGRIDLDAAARMIRPEHKLLSLAHISNVLGSVL 183
Cdd:PRK02948 77 IQSLLNALPQNKKHIITTPMEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 184 DVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSGHKLYAPTGIGVLWAKSDIldsmaPWQgggamidQVtF 263
Cdd:PRK02948 156 PIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RWK-------PV-F 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 264 EKTTYLDPparFEAGTPHIVGTLGLAAAIEYLENiGMEKVACHEAALtkmaRKRLKD-IKGLRL----FGADDS--AAIL 336
Cdd:PRK02948 223 PGTTHEKG---FRPGTVNVPGIAAFLTAAENILK-NMQEESLRFKEL----RSYFLEqIQTLPLpievEGHSTSclPHII 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540327402 337 SFSMDGIHPHDIGTILDEEGVAIRAGHHC-------AQPLMAHLNVPATA----RASFGLYNEEQDIERLAAGLSRV 402
Cdd:PRK02948 295 GVTIKGIEGQYTMLECNRRGIAISTGSACqvgkqepSKTMLAIGKTYEEAkqfvRFSFGQQTTKDQIDTTIHALETI 371
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
72-241 |
1.50e-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: 73.96 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 72 EKARETVARFIGaKSANEIVFVRGATEAINLVAQiwgaTHLNQGDRILISQLEHHSNIVpwqLLRDRMGFAIDVIPLDEE 151
Cdd:cd01494 3 EELEEKLARLLQ-PGNDKAVFVPSGTGANEAALL----ALLGPGDEVIVDANGHGSRYW---VAAELAGAKPVPVPVDDA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 152 GRIDLDAAA---RMIRPEHKLLSLAHISNvLGSVLDVSKA-RKIADSVGAKLLIDGCQSAPHLPINVSEL---GCDFFVF 224
Cdd:cd01494 75 GYGGLDVAIleeLKAKPNVALIVITPNTT-SGGVLVPLKEiRKIAKEYGILLLVDAASAGGASPAPGVLIpegGADVVTF 153
|
170
....*....|....*..
gi 2540327402 225 SGHKLYAPTGIGVLWAK 241
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
76-243 |
1.51e-12 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 68.42 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 76 ETVARFIGAksaNEIVFVRGATEAINLVAQiwgaTHLNQGDRILISQLEHHSNIVPWQllrdRMGFAIDVIPL--DEEGR 153
Cdd:PRK09331 70 EDLAEFLGM---DEARVTHGAREGKFAVMH----SLCKKGDYVVLDGLAHYTSYVAAE----RAGLNVREVPKtgYPEYK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 154 IDLDAAARMI----RPEHKLLSLAHISNV---LGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSG 226
Cdd:PRK09331 139 ITPEAYAEKIeevkEETGKPPALALLTHVdgnYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSG 218
|
170
....*....|....*...
gi 2540327402 227 HKLYAPTG-IGVLWAKSD 243
Cdd:PRK09331 219 HKSMAASApSGVLATTEE 236
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
76-243 |
1.07e-11 |
|
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: 65.88 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 76 ETVARFIGAKSANeivFVRGATEAINLVAQiwgaTHLNQGDRILISQLEHHSNIVPwqllRDRMGFAIDVIPLDE--EGR 153
Cdd:cd06452 51 HDLAEFLGMDEAR---VTPGAREGKFAVMH----SLCEKGDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGhpEYH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 154 IDLDAAARMIRP-------EHKLLSLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPHLPINVSELGCDFFVFSG 226
Cdd:cd06452 120 ITPEGYAEVIEEvkdefgkPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSG 199
|
170
....*....|....*...
gi 2540327402 227 HKLYAPTG-IGVLWAKSD 243
Cdd:cd06452 200 HKSMAASApIGVLATTEE 217
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
112-331 |
2.68e-10 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 61.70 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 112 LNQGDRILISQLEHHSNIvpWQLLRDRMGFAIDVIPLDEEGRIDLDAAARMIR--PEH--KLLSLAHISNVLGSVLDVSK 187
Cdd:PLN02409 81 LSPGDKVVSFRIGQFSLL--WIDQMQRLNFDVDVVESPWGQGADLDILKSKLRqdTNHkiKAVCVVHNETSTGVTNDLAG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 188 ARKIADSV--GAKLLIDGCQSAPHLPINVSELGCDFFVFSGHK-LYAPTGIGVLWAKSDILDSMApwqggGAMIDQVTFE 264
Cdd:PLN02409 159 VRKLLDCAqhPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKaLSLPTGLGIVCASPKALEASK-----TAKSPRVFFD 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540327402 265 KTTYLD--PPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHEAALTKMARKRLKDIkGLRLFGADD 331
Cdd:PLN02409 234 WADYLKfyKLGTYWPYTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAW-GLKLCTKKP 301
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
28-322 |
1.64e-08 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 56.80 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 28 YLDSAATAQKPKAVIDAVYKAYAVD-YATVHR--GVYSRSADMTkekEKARETVARFIGAKSAN-EIVFVRGATEAINLV 103
Cdd:PLN02724 37 YLDHAGATLYSESQLEAALADFSSNvYGNPHSqsDSSMRSSDTI---ESARQQVLEYFNAPPSDyACVFTSGATAALKLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 104 AQI--WgathlNQGDRILISQLEHHS--NIVPWQLLRDRMGFAIDV-----IPLDEEGRIDLDAAARMIRPEHK------ 168
Cdd:PLN02724 114 GETfpW-----SSESHFCYTLENHNSvlGIREYALEKGAAAIAVDIeeaanQPTNSQGSVVVKSRGLQRRNTSKlqkred 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 169 ------LLSLAHISNVLGSVLDVSKARKIADSVGAK--------LLIDGCQSAPHLPINVSELGCDFFVFSGHKLYA-PT 233
Cdd:PLN02724 189 dgeaynLFAFPSECNFSGAKFPLDLVKLIKDNQHSNfsksgrwmVLLDAAKGCGTSPPDLSRYPADFVVVSFYKIFGyPT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 234 GIGVLWAKSD---ILDSMapWQGGG---AMIDQVTFEKTTYlDPPARFEAGTPHIVGTLGLAAAIEYLENIGMEKVACHE 307
Cdd:PLN02724 269 GLGALLVRRDaakLLKKK--YFGGGtvaASIADIDFVKRRE-RVEQRFEDGTISFLSIAALRHGFKLLNRLTISAIAMHT 345
|
330
....*....|....*
gi 2540327402 308 AALTKMARKRLKDIK 322
Cdd:PLN02724 346 WALTHYVANSLRNLK 360
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
73-255 |
5.87e-08 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 54.23 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 73 KARETVARFIGA------KSANEIVFVRGATEAINLVAQIWgathLNQGDRILISQLEH--HSNIVPWqllrdrMGFAID 144
Cdd:pfam00155 43 ELREALAKFLGRspvlklDREAAVVFGSGAGANIEALIFLL----ANPGDAILVPAPTYasYIRIARL------AGGEVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 145 VIPLDEE--GRIDLDAAARMIRPEHKLLSLAHISNVLGSVLDVSKARKIADSV---GAKLLID--------GCQSAPHLP 211
Cdd:pfam00155 113 RYPLYDSndFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLLDLAkehNILLLVDeayagfvfGSPDAVATR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2540327402 212 INVSELGCDFFVFSGHKLYAPTG--IGVLWAKSDILDSMAPWQGGG 255
Cdd:pfam00155 193 ALLAEGPNLLVVGSFSKAFGLAGwrVGYILGNAAVISQLRKLARPF 238
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
99-202 |
1.28e-06 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 50.07 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 99 AINLVAQIWGATH-------------------LNQGDRILISQLEH-----HS----------NIVPWqllrdrmgfaid 144
Cdd:PRK00011 76 AIDRAKELFGAEYanvqphsgsqanaavyfalLKPGDTILGMDLAHgghltHGspvnfsgklyNVVSY------------ 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540327402 145 viPLDEE-GRIDLDAAARMIRpEH--KLLslahisnVLGS-----VLDVSKARKIADSVGAKLLID 202
Cdd:PRK00011 144 --GVDEEtGLIDYDEVEKLAL-EHkpKLI-------IAGAsaysrPIDFKRFREIADEVGAYLMVD 199
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
75-193 |
1.67e-06 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 49.65 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 75 RETVARFIGAK-----SANEIVFVRGATEAINLVAQIWgathLNQGDRILISQLEHHSNIVPWQLlrdrMGFAIDVIPLD 149
Cdd:cd00609 42 REAIAEWLGRRggvdvPPEEIVVTNGAQEALSLLLRAL----LNPGDEVLVPDPTYPGYEAAARL----AGAEVVPVPLD 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2540327402 150 EEGRI--DLDAAARMIRPEHKLLSLAHISNVLGSVLDVSKARKIAD 193
Cdd:cd00609 114 EEGGFllDLELLEAAKTPKTKLLYLNNPNNPTGAVLSEEELEELAE 159
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
99-202 |
1.93e-06 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 49.64 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 99 AINLVAQIWGATH-------------------LNQGDRIL---ISQ---LEHHS---------NIVPWqllrdrmgfaid 144
Cdd:COG0112 75 AIERAKELFGAEHanvqphsgsqanlavyfalLKPGDTILgmdLAHgghLTHGSpvnfsgkgyNVVSY------------ 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540327402 145 viPLDEE-GRIDLDAAARMIRpEH--KLLslahisnVLGS-----VLDVSKARKIADSVGAKLLID 202
Cdd:COG0112 143 --GVDPEtGLIDYDEVRKLAL-EHkpKLI-------IAGAsayprPIDFARFREIADEVGAYLMVD 198
|
|
| PRK08133 |
PRK08133 |
O-succinylhomoserine sulfhydrylase; Validated |
111-228 |
6.23e-06 |
|
O-succinylhomoserine sulfhydrylase; Validated
Pssm-ID: 181244 [Multi-domain] Cd Length: 390 Bit Score: 48.07 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 111 HLNQGDRILISQLEHHSNIVPWQLLRDRMGFAIDVIPLdeegrIDLDAAARMIRPEHKLLSLAHISNVLGSVLDVSKARK 190
Cdd:PRK08133 96 LLQAGDHVVSSRSLFGSTVSLFEKIFARFGIETTFVDL-----TDLDAWRAAVRPNTKLFFLETPSNPLTELADIAALAE 170
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2540327402 191 IADSVGAKLLIDGCQSAPHL--PInvsELGCDFFVFSGHK 228
Cdd:PRK08133 171 IAHAAGALLVVDNCFCTPALqqPL---KLGADVVIHSATK 207
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
75-193 |
1.30e-05 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 47.13 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 75 RETVARFIGAK----SANEIVFVRGATEAINLVAQiwgaTHLNQGDRILISQLeHHSNIvpWQLLRdRMGFAIDVIPLDE 150
Cdd:COG1167 154 REAIARYLARRgvpaSPDQILITSGAQQALDLALR----ALLRPGDTVAVESP-TYPGA--LAALR-AAGLRLVPVPVDE 225
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2540327402 151 EGrIDLDAAARMIRPEH-KLLSL-AHISNVLGSVLDVSKARKIAD 193
Cdd:COG1167 226 DG-LDLDALEAALRRHRpRAVYVtPSHQNPTGATMSLERRRALLE 269
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
75-202 |
1.66e-05 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 46.47 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 75 RETVARFIGAKSANEIVFVRGATEAINLVAQiwgaTHLNQGDRIlISQL----EHHSniVPWQLlrdrmGFAIDVIPLDE 150
Cdd:PRK07324 68 KEAVASLYQNVKPENILQTNGATGANFLVLY----ALVEPGDHV-ISVYptyqQLYD--IPESL-----GAEVDYWQLKE 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540327402 151 EGRI--DLDAAARMIRPEHKLLSLAHISNVLGSVLDVSKARK---IADSVGAKLLID 202
Cdd:PRK07324 136 ENGWlpDLDELRRLVRPNTKLICINNANNPTGALMDRAYLEEiveIARSVDAYVLSD 192
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
115-363 |
2.83e-05 |
|
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: 45.74 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 115 GDRILISQLEHHSnivpwQLLRD---RMGFAIDVIPLDEEGRIDLDAAARMIR-PEHKLLSLAHISNVLGSVLDVSKARK 190
Cdd:cd06451 74 GDKVLVGVNGVFG-----DRWADmaeRYGADVDVVEKPWGEAVSPEEIAEALEqHDIKAVTLTHNETSTGVLNPLEGIGA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 191 IADSVGAKLLIDGCQSAPHLPINVSELGCDfFVFSGHK--LYAPTGIGVLWAKSDILD------SMAPWQgggamidqvt 262
Cdd:cd06451 149 LAKKHDALLIVDAVSSLGGEPFRMDEWGVD-VAYTGSQkaLGAPPGLGPIAFSERALErikkktKPKGFY---------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 263 FEKTTYLDPPARFEaGTPHIVGT---LGLAAAIEYLENIGMEKV-ACHEaALTKMARKRLKDIkGLRLFGAD-------- 330
Cdd:cd06451 218 FDLLLLLKYWGEGY-SYPHTPPVnllYALREALDLILEEGLENRwARHR-RLAKALREGLEAL-GLKLLAKPelrsptvt 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2540327402 331 --------DSAAILSFSMD--------GIHPHdigtildeEGVAIRAGH 363
Cdd:cd06451 295 avlvpegvDGDEVVRRLMKrynieiagGLGPT--------AGKVFRIGH 335
|
|
| PRK07504 |
PRK07504 |
O-succinylhomoserine sulfhydrylase; Reviewed |
155-228 |
2.43e-04 |
|
O-succinylhomoserine sulfhydrylase; Reviewed
Pssm-ID: 168979 [Multi-domain] Cd Length: 398 Bit Score: 42.82 E-value: 2.43e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540327402 155 DLDAAARMIRPEHKLLSLAHISNVLGSVLDVSKARKIADSVGAKLLIDGCQSAPhLPINVSELGCDFFVFSGHK 228
Cdd:PRK07504 139 DLDNWEKAVRPNTKVFFLESPTNPTLEVIDIAAVAKIANQAGAKLVVDNVFATP-LFQKPLELGAHIVVYSATK 211
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
112-228 |
7.17e-04 |
|
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: 41.42 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 112 LNQGDRILIS-QLEHHSNIVPWQLLRdRMGfaIDVIPLDEEGRIDLDAAarmIRPEHKLLSLAHISNVLGSVLDVSKARK 190
Cdd:cd00614 76 LKAGDHVVASdDLYGGTYRLFERLLP-KLG--IEVTFVDPDDPEALEAA---IKPETKLVYVESPTNPTLKVVDIEAIAE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2540327402 191 IADSVGAKLLIDGCQSAPHL--PInvsELGCDFFVFSGHK 228
Cdd:cd00614 150 LAHEHGALLVVDNTFATPYLqrPL---ELGADIVVHSATK 186
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
91-326 |
1.94e-03 |
|
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: 40.20 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 91 VFVRGATEAiNLVA-----QIWGATHLNQGD-------RILISQLEHHSNivpwqllrDR----MGF---AIDVIPLDEE 151
Cdd:COG0076 129 VFTSGGTEA-NLLAllaarDRALARRVRAEGlpgaprpRIVVSEEAHSSV--------DKaarlLGLgrdALRKVPVDED 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 152 GRIDLDAAARMIRPehkllSLAHISNVL-----------GSVLDVSKARKIADSVGAKLLIDGCQSAPHLPinvSELGCD 220
Cdd:COG0076 200 GRMDPDALEAAIDE-----DRAAGLNPIavvatagttntGAIDPLAEIADIAREHGLWLHVDAAYGGFALP---SPELRH 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 221 FF---------VFSGHK-LYAPTGIG-VLWAKSDILDSmapwqgggAMIDQVtfektTYLDPPAR--FEAGTPHIVGT-- 285
Cdd:COG0076 272 LLdgieradsiTVDPHKwLYVPYGCGaVLVRDPELLRE--------AFSFHA-----SYLGPADDgvPNLGDYTLELSrr 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2540327402 286 ---LGLAAAIEYLeniGMEKV-ACHEA--ALTKMARKRLKDIKGLRL 326
Cdd:COG0076 339 fraLKLWATLRAL---GREGYrELIERciDLARYLAEGIAALPGFEL 382
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
113-236 |
3.90e-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: 39.14 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 113 NQGDRILISQLEHHSNIvpwQLLRDRM---GFAIDVIPLDEEGRIDLDAAARMIRPEhkllsLAHI----SNVLGSVLDV 185
Cdd:cd00613 106 HKRNKVLVPDSAHPTNP---AVARTRGeplGIEVVEVPSDEGGTVDLEALKEEVSEE-----VAALmvqyPNTLGVFEDL 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540327402 186 SKA-RKIADSVGAKLLIDGCqsaphlPINVS------ELGCDFFVFSGHKLYAPTGIG 236
Cdd:cd00613 178 IKEiADIAHSAGALVYVDGD------NLNLTglkppgEYGADIVVGNLQKTGVPHGGG 229
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
38-401 |
5.66e-03 |
|
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: 38.57 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 38 PKAVIDAVYKAYAvdyATVHRgvYSRSADMtkekEKARETVARFIGAK-----SANEIVFVRGATEAINLVAQiwgaTHL 112
Cdd:COG0436 45 PDHIREAAIEALD---DGVTG--YTPSAGI----PELREAIAAYYKRRygvdlDPDEILVTNGAKEALALALL----ALL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 113 NQGDRILI---------SQLEHHS-NIVPwqllrdrmgfaidvIPLDEEG--RIDLDAAARMIRPEHKLLSLAHISNVLG 180
Cdd:COG0436 112 NPGDEVLVpdpgypsyrAAVRLAGgKPVP--------------VPLDEENgfLPDPEALEAAITPRTKAIVLNSPNNPTG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 181 SVLD-------VSKARK-----IADSVGAKLLIDGcqsAPHLPI-NVSELGCDFFVFSGH-KLYAPTG--IGVLWAKSDI 244
Cdd:COG0436 178 AVYSreelealAELAREhdllvISDEIYEELVYDG---AEHVSIlSLPGLKDRTIVINSFsKSYAMTGwrIGYAVGPPEL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 245 LDSMApwqgggAMIDQVTFekttyldpparfeaGTPHIVgtlgLAAAIEYLENigmeKVACHEAALTKMARKR------L 318
Cdd:COG0436 255 IAALL------KLQSNLTS--------------CAPTPA----QYAAAAALEG----PQDYVEEMRAEYRRRRdllvegL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 319 KDIkGLRLF---GA-----------DDSAAilsFSMDgihphdigtILDEEGVAIraghhcaqplmahlnVPATArasFG 384
Cdd:COG0436 307 NEI-GLSVVkpeGAfylfadvpelgLDSEE---FAER---------LLEEAGVAV---------------VPGSA---FG 355
|
410 420
....*....|....*....|....
gi 2540327402 385 LYNEE-------QDIERLAAGLSR 401
Cdd:COG0436 356 PAGEGyvrisyaTSEERLEEALER 379
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
73-238 |
6.05e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 38.35 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 73 KARETVARFIGAKSAneiVFVRGATEAiNLVAQiwgATHLNQGDRILisqLEHHSNIVPW-----QLLRDRMgfAIDVIP 147
Cdd:pfam01212 36 RLEDRVAELFGKEAA---LFVPSGTAA-NQLAL---MAHCQRGDEVI---CGEPAHIHFDetgghAELGGVQ--PRPLDG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540327402 148 lDEEGRIDLDAAARMIR-------PEHKLLSLAHISNVLG----SVLDVSKARKIADSVGAKLLIDGCQ---SAPHLPIN 213
Cdd:pfam01212 104 -DEAGNMDLEDLEAAIRevgadifPPTGLISLENTHNSAGgqvvSLENLREIAALAREHGIPVHLDGARfanAAVALGVI 182
|
170 180
....*....|....*....|....*...
gi 2540327402 214 VSEL--GCDFFVFSGHK-LYAPTGiGVL 238
Cdd:pfam01212 183 VKEItsYADSVTMCLSKgLGAPVG-SVL 209
|
|
| |
