|
Name |
Accession |
Description |
Interval |
E-value |
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
27-506 |
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: 849.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 27 APGGWPGEADDAPSARDYGLPDARD-LQGLLSDTPArprgvetayAPRVVPLGQEGRAD---ITPRGFATLPAFGSRPAP 102
Cdd:NF041166 146 AAPSAAAAPPDLVAPQAFGLPGEDAaLRALLPAASP---------APPSAPSAAAAESSyyfLDERAAPSPAAAPPGSPP 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 103 AARVGQIP--VERIRADFPILAEQVEGHPLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAARE 180
Cdd:NF041166 217 ALASAHPPfdVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGARE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 181 KVSRFIGARGPENIIFVRGTTEGLNLIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIV 260
Cdd:NF041166 297 KVRRFIGAPSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 261 EEYIRLFNDKTRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIG 340
Cdd:NF041166 377 DEYAKLLNPRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIG 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 341 VIYGKQEVLEAARPYQGGGNMIADVTFELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIA 420
Cdd:NF041166 457 VVYGKRDLLEAMPPWQGGGNMIADVTFEKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATA 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 421 KLSAIPGLTLVGTAANKTSVLSFVLAGHENEAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFL 500
Cdd:NF041166 537 GLAEVPGLRLIGTAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDAL 616
|
....*.
gi 1738373870 501 AEQVAR 506
Cdd:NF041166 617 VAVLRR 622
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
111-510 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 597.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 111 VERIRADFPILaeqveGHPLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARG 190
Cdd:COG0520 2 VEAIRADFPVL-----GKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 191 PENIIFVRGTTEGLNLIAHSYvkPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFNDK 270
Cdd:COG0520 77 PDEIIFTRGTTEAINLVAYGL--GRLKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 271 TRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLE 350
Cdd:COG0520 155 TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 351 AARPYQGGGNMIADVTFELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGLTL 430
Cdd:COG0520 235 ALPPFLGGGGMIEWVSFDGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGVRI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 431 VGTA--ANKTSVLSFVLAGHENEAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFLAEQVARFA 508
Cdd:COG0520 315 LGPAdpEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKKLA 394
|
..
gi 1738373870 509 AR 510
Cdd:COG0520 395 EL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
131-502 |
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: 596.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 131 VWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARGPENIIFVRGTTEGLNLIAHS 210
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 211 YVKPLlRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFNDKTRFVSATHVSNALGTVTPVQ 290
Cdd:cd06453 81 LGRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 291 ELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLEAARPYQGGGNMIADVTFELT 370
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSFEET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 371 RYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGLTLVGTAANKTSVLSFVLAGHEN 450
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGDAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1738373870 451 EAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFLAE 502
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVE 371
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
112-502 |
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: 578.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 112 ERIRADFPILAEQVEGHPLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARGP 191
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 192 ENIIFVRGTTEGLNLIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFNDKT 271
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 272 RFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLEA 351
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 352 ARPYQGGGNMIADVTFELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGLTLV 431
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSFEETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRIY 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1738373870 432 GT--AANKTSVLSFVLAGHENEAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFLAE 502
Cdd:TIGR01979 321 GPrdAEDRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVE 393
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
131-500 |
5.12e-175 |
|
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: 496.77 E-value: 5.12e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 131 VWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARGPENIIFVRGTTEGLNLIAHS 210
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 211 YvKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFNDKTRFVSATHVSNALGTVTPVQ 290
Cdd:pfam00266 81 L-GRSLKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 291 ELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLEAARPYQGGGNMIADVTFELT 370
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSLQES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 371 RYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGLTLVGTAANkTSVLSFVLAGHEN 450
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERR-ASIISFNFKGVHP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1738373870 451 EAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFL 500
Cdd:pfam00266 319 HDVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
100-498 |
1.56e-166 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 477.70 E-value: 1.56e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 100 PAPAARVGQIPV-ERIRADFPILAEQVEGHPLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAA 178
Cdd:PLN02855 2 SAPAASAASVSLgAETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 179 REKVSRFIGARGPENIIFVRGTTEGLNLIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQL 258
Cdd:PLN02855 82 RKKVAAFINASTSREIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 259 IVEEYIRLFNDKTRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTG 338
Cdd:PLN02855 162 DVEQLKELLSEKTKLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 339 IGVIYGKQEVLEAARPYQGGGNMIADVTFELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYG 418
Cdd:PLN02855 242 IGFLWGKSDLLESMPPFLGGGEMISDVFLDHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 419 IAKLSAIPGLTLVG----TAANKTSVLSFVLAG-HENEaVGRYLSQ-VGIAVRSGHHCAQPILRRLGYESTVRPSLAFYN 492
Cdd:PLN02855 322 YEKLSSVPGVRIYGpkpsEGVGRAALCAFNVEGiHPTD-LSTFLDQqHGVAIRSGHHCAQPLHRYLGVNASARASLYFYN 400
|
....*.
gi 1738373870 493 TPQEID 498
Cdd:PLN02855 401 TKEEVD 406
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
110-506 |
4.96e-166 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 475.78 E-value: 4.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 110 PVERIRADFPILAEQVEGHPLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGAR 189
Cdd:PRK09295 4 SVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFINAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 190 GPENIIFVRGTTEGLNLIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFND 269
Cdd:PRK09295 84 SAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPALFDE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 270 KTRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVL 349
Cdd:PRK09295 164 RTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 350 EAARPYQGGGNMIADVTF-ELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGL 428
Cdd:PRK09295 244 QEMPPWEGGGSMIATVSLtEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESVPDL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738373870 429 TLVGtAANKTSVLSFVLAGHENEAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFLAEQVAR 506
Cdd:PRK09295 324 TLYG-PQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
115-506 |
1.70e-130 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 384.78 E-value: 1.70e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 115 RADFPILAeqvegHPLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARGPENI 194
Cdd:PRK10874 10 RAQFPALQ-----DAGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNAPDAKNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 195 IFVRGTTEGLNLIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFNDKTRFV 274
Cdd:PRK10874 85 VWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELITPRTRIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 275 SATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLEAARP 354
Cdd:PRK10874 165 ALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSELLEAMSP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 355 YQGGGNMIADVTFELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGltLVGTA 434
Cdd:PRK10874 245 WQGGGKMLTEVSFDGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPG--FRSFR 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1738373870 435 ANKTSVLSFVLAG-HENEAVgRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFLAEQVAR 506
Cdd:PRK10874 323 CQDSSLLAFDFAGvHHSDLV-TLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDR 394
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
112-506 |
5.33e-123 |
|
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: 365.70 E-value: 5.33e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 112 ERIRADFPILAEQveghpLVWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARGP 191
Cdd:TIGR03392 4 AQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNAPDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 192 ENIIFVRGTTEGLNLIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEHGQLIVEEYIRLFNDKT 271
Cdd:TIGR03392 79 ENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLTPRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 272 RFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLEA 351
Cdd:TIGR03392 159 RILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTELLEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 352 ARPYQGGGNMIADVTFELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAIPGLTLV 431
Cdd:TIGR03392 239 MPPWQGGGKMLSHVSFDGFTPQAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPGFRSF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1738373870 432 GTAanKTSVLSFVLAGHENEAVGRYLSQVGIAVRSGHHCAQPILRRLGYESTVRPSLAFYNTPQEIDFLAEQVAR 506
Cdd:TIGR03392 319 RCQ--GSSLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGR 391
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
109-504 |
5.01e-73 |
|
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: 236.96 E-value: 5.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 109 IPVERIRADFPILAEQVeghpLVWLDNAATTQRPKQVIDRISHYYLHENSNvhRAAHTLAARSTDAY-EAAREKVSRFIG 187
Cdd:TIGR01976 1 FDVEAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAALTRSNAN--RGGAYESSRRADQVvDDAREAVADLLN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 188 ARGPEnIIFVRGTTEGLNLIAHSYVKpLLRPGDEIILTQLEHHANIVPWQLIAQETGATIRVAPVDEH-GQLIVEEYIRL 266
Cdd:TIGR01976 75 ADPPE-VVFGANATSLTFLLSRAISR-RWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDEAtGELHPDDLASL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 267 FNDKTRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTgIGVIYGKQ 346
Cdd:TIGR01976 153 LSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 347 EVLEAARPYQgggnmiadvtfELTRYQPSPNKFEAGTGNIADAVGLGAAIDYVTSLGIEN--------------IAQYEH 412
Cdd:TIGR01976 232 ELLMNLPPYK-----------LTFSYDTGPERFELGTPQYELLAGVVAAVDYLAGLGESAngsrrerlvasfqaIDAYEN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 413 ALLEYGIAKLSAIPGLTLVG--TAANKTSVLSFVLAGHENEAVGRYLSQVGIAVRSGHHCAQPILRRLGYES---TVRPS 487
Cdd:TIGR01976 301 RLAEYLLVGLSDLPGVTLYGvaRLAARVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDeggVVRVG 380
|
410
....*....|....*..
gi 1738373870 488 LAFYNTPQEIDFLAEQV 504
Cdd:TIGR01976 381 LAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
133-510 |
2.01e-61 |
|
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: 206.05 E-value: 2.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 133 LDNAATTQRPKQVIDRISHYYLHENSN---VHRAAhtLAARStdAYEAAREKVSRFIGARgPENIIFVRGTTEGLNLIAH 209
Cdd:COG1104 6 LDNAATTPVDPEVLEAMLPYLTEYFGNpssLHSFG--REARA--ALEEAREQVAALLGAD-PEEIIFTSGGTEANNLAIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 210 SYVKPLLRPGDEIILTQLEHHA--NIVPWqliAQETGATIRVAPVDEHGQLIVEEYIRLFNDKTRFVSATHVSNALGTVT 287
Cdd:COG1104 81 GAARAYRKKGKHIITSAIEHPAvlETARF---LEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 288 PVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVleAARPYQGGGNMiadvtf 367
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGV--RLEPLIHGGGQ------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 368 EltryqpspNKFEAGTGNIADAVGLGAAIDYVTSLGIENIAQYEhALLEYGIAKLSA-IPGLTLVGTAANKT-SVLSFVL 445
Cdd:COG1104 230 E--------RGLRSGTENVPGIVGLGKAAELAAEELEEEAARLR-ALRDRLEEGLLAaIPGVVINGDPENRLpNTLNFSF 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738373870 446 AGHENEAVGRYLSQVGIAVRSGHHCAQ------PILRRLGYE-----STVRPSLAFYNTPQEIDFLAEQVARFAAR 510
Cdd:COG1104 301 PGVEGEALLLALDLAGIAVSSGSACSSgslepsHVLLAMGLDeelahGSIRFSLGRFTTEEEIDRAIEALKEIVAR 376
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
131-498 |
1.75e-38 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 144.03 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 131 VWLDNAATTQRPKQVIDRISHYYLHENSNVHRAAHTLAARSTDAYEAAREKVSRFIGARGPEnIIFVRGTTEGLNLIAHS 210
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGADPKE-IIFTSGATESNNLAIKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 211 YVKPLLRPGDEIILTQLEHHANIVPWQLIAQEtGATIRVAPVDEHGQLIVEEYIRLFNDKTRFVSATHVSNALGTVTPVQ 290
Cdd:PLN02651 80 VMHFYKDKKKHVITTQTEHKCVLDSCRHLQQE-GFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 291 ELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVLEAARPY-QGGGNmiadvtfEL 369
Cdd:PLN02651 159 EIGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPLmSGGGQ-------ER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 370 TRyqpspnkfEAGTGNIADAVGLGAAIDYVTSLG---IENIAQYEHALLEyGIAklSAIPGLTLVGT---AANKTSVLSF 443
Cdd:PLN02651 232 GR--------RSGTENTPLVVGLGAACELAMKEMdydEKHMKALRERLLN-GLR--AKLGGVRVNGPrdpEKRYPGTLNL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1738373870 444 VLAGHENEAVGRYLSqvGIAVRSGHHC----AQP--ILRRLGYE-----STVRPSLAFYNTPQEID 498
Cdd:PLN02651 301 SFAYVEGESLLMGLK--EVAVSSGSACtsasLEPsyVLRALGVPeemahGSLRLGVGRFTTEEEVD 364
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
131-504 |
4.91e-30 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 121.20 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 131 VWLDNAATTQRPKQVIDRISHYYLHEN--SNVHRAAHTLAARSTDAYEAAREKVSRFIGArGPENIIFVRGTTEGLNL-- 206
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMPYLTMDGtfGNPASRSHRFGWQAEEAVDIARNQIADLIGA-DPREIVFTSGATESDNLai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 207 --IAHSYVKPllrpGDEIILTQLEHHANIVPWQLIAQEtGATIRVAPVDEHGQL---IVEEYIRlfnDKTRFVSATHVSN 281
Cdd:PRK14012 84 kgAAHFYQKK----GKHIITSKTEHKAVLDTCRQLERE-GFEVTYLDPQSNGIIdleKLEAAMR---DDTILVSIMHVNN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 282 ALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIY--GKQEV-LEAArpYQGG 358
Cdd:PRK14012 156 EIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYvrRKPRVrLEAQ--MHGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 359 GNmiadvtfeltryqpsPNKFEAGTGNIADAVGLGAAIdyvtslgieNIAQYE--------HALLEYGIAKLSAIPGLTL 430
Cdd:PRK14012 234 GH---------------ERGMRSGTLPTHQIVGMGEAA---------RIAKEEmateneriRALRDRLWNGIKDIEEVYL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 431 VGTAANKTS---VLSFvlAGHENEAVGRYLSQvgIAVRSGHHCA----QP--ILRRLGYE-----STVRPSLAFYNTPQE 496
Cdd:PRK14012 290 NGDLEQRVPgnlNVSF--NYVEGESLIMALKD--LAVSSGSACTsaslEPsyVLRALGLNdelahSSIRFSLGRFTTEEE 365
|
....*...
gi 1738373870 497 IDFLAEQV 504
Cdd:PRK14012 366 IDYAIELV 373
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
130-508 |
6.02e-25 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 106.35 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 130 LVWLDNAATTQRPKQVIDRISH----YYLHENSnvhraAHTLAARSTDAYEAAREKVSRFIGARGpENIIFVRGTTEGLN 205
Cdd:PRK02948 1 MIYLDYAATTPMSKEALQTYQKaasqYFGNESS-----LHDIGGTASSLLQVCRKTFAEMIGGEE-QGIYFTSGGTESNY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 206 LIAHSYVKPLLRPGDEIILTQLEHHANIVPWQLIAQEtGATIRVAPVDEHGQLIVEEYIRLFNDKTRFVSATHVSNALGT 285
Cdd:PRK02948 75 LAIQSLLNALPQNKKHIITTPMEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 286 VTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTGIGVIYGKQEVleaarPYQgggnmiadV 365
Cdd:PRK02948 154 IQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RWK--------P 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 366 TFELTRYQpspNKFEAGTGNIADAVGLGAAIDYVtslgIENIAQYEHALLEYGIAKLSAIPGLTL-VGTAANKTSVLSFV 444
Cdd:PRK02948 221 VFPGTTHE---KGFRPGTVNVPGIAAFLTAAENI----LKNMQEESLRFKELRSYFLEQIQTLPLpIEVEGHSTSCLPHI 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738373870 445 L----AGHENEAVGRYLSQVGIAVRSGHHCaqpilrRLGYESTVRPSLAFYNTPQEidflAEQVARFA 508
Cdd:PRK02948 294 IgvtiKGIEGQYTMLECNRRGIAISTGSAC------QVGKQEPSKTMLAIGKTYEE----AKQFVRFS 351
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
175-345 |
5.30e-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: 72.80 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 175 YEAAREKVSRFIGArGPENIIFVRGTTEGLNLIAHSyvkpLLRPGDEIILTQLEHHANIVPWQLIAqetGATIRVAPVDE 254
Cdd:cd01494 2 LEELEEKLARLLQP-GNDKAVFVPSGTGANEAALLA----LLGPGDEVIVDANGHGSRYWVAAELA---GAKPVPVPVDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 255 HGQLIVEEYIRLFNDKTRFVS--ATHVSNALGTVT-PVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALD---ADFFVF 328
Cdd:cd01494 74 AGYGGLDVAILEELKAKPNVAliVITPNTTSGGVLvPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVTF 153
|
170
....*....|....*..
gi 1738373870 329 SGHKIFGPTGIGVIYGK 345
Cdd:cd01494 154 SLHKNLGGEGGGVVIVK 170
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
196-347 |
2.82e-14 |
|
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: 74.35 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 196 FVRGTTEGLNLIAHSYVKPllrpGDEIILTQLEHHANIVPwqliAQETGATIRVAPVDEHGQLIV---------EEYIRL 266
Cdd:cd06452 64 VTPGAREGKFAVMHSLCEK----GDWVVVDGLAHYTSYVA----AERAGLNVREVPNTGHPEYHItpegyaeviEEVKDE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 267 FNDKTRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFVFSGHKIFGPTG-IGVIYGK 345
Cdd:cd06452 136 FGKPPALALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASApIGVLATT 215
|
..
gi 1738373870 346 QE 347
Cdd:cd06452 216 EE 217
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
180-339 |
4.53e-13 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 70.73 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 180 EKVSRFIG---ARgpeniiFVRGTTEGLNLIAHSYVKPllrpGDEIILTQLEHHANIVPwqliAQETGATIRVAPVDEHG 256
Cdd:PRK09331 70 EDLAEFLGmdeAR------VTHGAREGKFAVMHSLCKK----GDYVVLDGLAHYTSYVA----AERAGLNVREVPKTGYP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 257 QLIV---------EEYIRLFNDKTRFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSISHIPTNVTALDADFFV 327
Cdd:PRK09331 136 EYKItpeayaekiEEVKEETGKPPALALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIV 215
|
170
....*....|....*
gi 1738373870 328 FSGHKIF---GPTGI 339
Cdd:PRK09331 216 GSGHKSMaasAPSGV 230
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
107-425 |
5.87e-10 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 61.81 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 107 GQIPVERIRA-DFPILAEqveghpLVWLDNAATTQRPKQVIDRISHYYlheNSNVHRAAHT---LAARSTDAYEAAREKV 182
Cdd:PLN02724 17 GPKPIDELRAtEFARLKG------VVYLDHAGATLYSESQLEAALADF---SSNVYGNPHSqsdSSMRSSDTIESARQQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 183 SRFIGARGPE-NIIFVRGTTEGLNLIAHSYvkPLlRPGDEIILTqLEHHANIVPWQLIAQETGAT-----IRVA---PVD 253
Cdd:PLN02724 88 LEYFNAPPSDyACVFTSGATAALKLVGETF--PW-SSESHFCYT-LENHNSVLGIREYALEKGAAaiavdIEEAanqPTN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 254 EHGQLIVE-------------------EYIRLFndktRFVSATHVSNALGTVTPVQELVQIAHRFGVR-----IAIDGAQ 309
Cdd:PLN02724 164 SQGSVVVKsrglqrrntsklqkreddgEAYNLF----AFPSECNFSGAKFPLDLVKLIKDNQHSNFSKsgrwmVLLDAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 310 SISHIPTNVTALDADFFVFSGHKIFG-PTGIGVIYGKQEVLEA-ARPYQGGGNM---IADVTFeLTRYQPSPNKFEAGTG 384
Cdd:PLN02724 240 GCGTSPPDLSRYPADFVVVSFYKIFGyPTGLGALLVRRDAAKLlKKKYFGGGTVaasIADIDF-VKRRERVEQRFEDGTI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1738373870 385 NIADAVGLGAAIDYVTSLGIENIAQYEHALLEYGIAKLSAI 425
Cdd:PLN02724 319 SFLSIAALRHGFKLLNRLTISAIAMHTWALTHYVANSLRNL 359
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
175-352 |
2.96e-09 |
|
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: 58.51 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 175 YEAAREKVSRFIGARG-----PENIIFVRGTTEGLNLIAHSyvkpLLRPGDEIILTQLEHHanivPWQLIAQETGATIRV 249
Cdd:cd00609 38 LPELREAIAEWLGRRGgvdvpPEEIVVTNGAQEALSLLLRA----LLNPGDEVLVPDPTYP----GYEAAARLAGAEVVP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 250 APVDEHG--QLIVEEYIRLFNDKTRFVSATHVSNALGTVTP---VQELVQIAHRFGVRIAIDGA----QSISHIPTNVTA 320
Cdd:cd00609 110 VPLDEEGgfLLDLELLEAAKTPKTKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISDEAyaelVYDGEPPPALAL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1738373870 321 LDADFFVFSGH---KIFGPTG--IGVIYGKQEVLEAA 352
Cdd:cd00609 190 LDAYERVIVLRsfsKTFGLPGlrIGYLIAPPEELLER 226
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
190-359 |
5.60e-08 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 54.14 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 190 GPENIIFV-RGTteGLNLIAHSYvkpLLRPGDEIILtqlEHHANIVPWQL--IAQETGATIRVAPVDEHGQLIVE----- 261
Cdd:pfam01212 46 GKEAALFVpSGT--AANQLALMA---HCQRGDEVIC---GEPAHIHFDETggHAELGGVQPRPLDGDEAGNMDLEdleaa 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 262 --EYIRLFNDKTRFVSATHVSN-ALGTVTPVQELVQI---AHRFGVRIAIDGAQ------SISHIPTNVTAlDADFFVFS 329
Cdd:pfam01212 118 irEVGADIFPPTGLISLENTHNsAGGQVVSLENLREIaalAREHGIPVHLDGARfanaavALGVIVKEITS-YADSVTMC 196
|
170 180 190
....*....|....*....|....*....|....
gi 1738373870 330 GHK-IFGPTGiGVIYGKQEVLEAA---RPYQGGG 359
Cdd:pfam01212 197 LSKgLGAPVG-SVLAGSDDFIAKAirqRKYLGGG 229
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
162-303 |
9.28e-08 |
|
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: 54.45 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 162 RAAHTLAARSTDAYEAA-----REKVSRFIGARG----PENIIFVRGTTEGLNLIAHSyvkpLLRPGDEIILTQLEHHAN 232
Cdd:COG1167 132 RALRRLPPALLGYGDPQglpelREAIARYLARRGvpasPDQILITSGAQQALDLALRA----LLRPGDTVAVESPTYPGA 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738373870 233 IvpwqLIAQETGATIRVAPVDEHGqLIVEEyIRLFNDKTR----FVSATHvSNALGTVTPV---QELVQIAHRFGVRI 303
Cdd:COG1167 208 L----AALRAAGLRLVPVPVDEDG-LDLDA-LEAALRRHRpravYVTPSH-QNPTGATMSLerrRALLELARRHGVPI 278
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
172-353 |
1.74e-07 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 53.08 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 172 TDAYEAAREKVSRFIG-----ARGPE-NIIFVRGTTEGLNLIAHSyvkpLLRPGDEIILTQLEH--HANIVPWqliaqeT 243
Cdd:pfam00155 38 TDGHPELREALAKFLGrspvlKLDREaAVVFGSGAGANIEALIFL----LANPGDAILVPAPTYasYIRIARL------A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 244 GATIRVAPVD--EHGQLIVEEYIRLFNDKTRFVSATHVSNALGTVTPVQELVQIA---HRFGVRIAID--------GAQS 310
Cdd:pfam00155 108 GGEVVRYPLYdsNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVATLEELEKLLdlaKEHNILLLVDeayagfvfGSPD 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1738373870 311 ISHIPTNVTALDADFFVFSGHKIFGPTG--IGVIYGKQEVLEAAR 353
Cdd:pfam00155 188 AVATRALLAEGPNLLVVGSFSKAFGLAGwrVGYILGNAAVISQLR 232
|
|
| PRK06836 |
PRK06836 |
pyridoxal phosphate-dependent aminotransferase; |
142-296 |
2.60e-05 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 180720 Cd Length: 394 Bit Score: 46.34 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 142 PKQVIDRISHYYLHENSNVHRaaHTLAArstdAYEAAREKVSRFIGAR-----GPENIIFVRGTTEGLNLIahsyVKPLL 216
Cdd:PRK06836 48 PAAVKEALRELAEEEDPGLHG--YMPNA----GYPEVREAIAESLNRRfgtplTADHIVMTCGAAGALNVA----LKAIL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 217 RPGDE-IILTQLehhanIVPWQLIAQETGATIRVAPVDEHG-QLIVEEYIRLFNDKTRFVSATHVSNALGTVTPVQELVQ 294
Cdd:PRK06836 118 NPGDEvIVFAPY-----FVEYRFYVDNHGGKLVVVPTDTDTfQPDLDALEAAITPKTKAVIINSPNNPTGVVYSEETLKA 192
|
..
gi 1738373870 295 IA 296
Cdd:PRK06836 193 LA 194
|
|
| AspB |
COG0436 |
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ... |
103-353 |
2.70e-05 |
|
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: 46.28 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 103 AARVGQIPVERIRADFPILAE-QVEGHPLVWL-----DNAAttqrPKQVIDRISHYYlheNSNVHR---AAHTLAARstd 173
Cdd:COG0436 4 SSRLARLPPSPIREVSALAAElKAAGEDVIDLgigepDFPT----PDHIREAAIEAL---DDGVTGytpSAGIPELR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 174 ayEAAREKVSRFIGAR-GPENIIFVRGTTEGLNLIAHSyvkpLLRPGDEIILTQ---LEHHAnivpwqlIAQETGATIRV 249
Cdd:COG0436 74 --EAIAAYYKRRYGVDlDPDEILVTNGAKEALALALLA----LLNPGDEVLVPDpgyPSYRA-------AVRLAGGKPVP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 250 APVDE--HGQLIVEEYIRLFNDKTRFVSATHVSNALGTVTP---VQELVQIAHRFGVRIAID-----------GAQSISH 313
Cdd:COG0436 141 VPLDEenGFLPDPEALEAAITPRTKAIVLNSPNNPTGAVYSreeLEALAELAREHDLLVISDeiyeelvydgaEHVSILS 220
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1738373870 314 IPtnvtALDADFFVFSGH-KIFGPTG--IGVIYGKQEVLEAAR 353
Cdd:COG0436 221 LP----GLKDRTIVINSFsKSYAMTGwrIGYAVGPPELIAALL 259
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
215-371 |
4.75e-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: 42.57 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 215 LLRPGDEIILTQLEHHANIvpwQLIAQETGAT-IRVAPVDehgQLIVEEYIRLFNDKTRFVSATHVSNALGTVTPVQELV 293
Cdd:cd00614 75 LLKAGDHVVASDDLYGGTY---RLFERLLPKLgIEVTFVD---PDDPEALEAAIKPETKLVYVESPTNPTLKVVDIEAIA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 294 QIAHRFGVRIAIDGAQSishIPTNVTALD--ADFFVFSGHKIFGPTG---IGVIYGKQE-VLEAARPYQG--GGNMIADV 365
Cdd:cd00614 149 ELAHEHGALLVVDNTFA---TPYLQRPLElgADIVVHSATKYIGGHSdviAGVVVGSGEaLIQRLRFLRLalGTILSPFD 225
|
....*.
gi 1738373870 366 TFELTR 371
Cdd:cd00614 226 AWLLLR 231
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
240-340 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 240 AQETGATIRVAPVDEHGQLIVEEYIRLFNDKTRFVSATHVsNALGTVTP-VQELVQIAHRFGVRIAIDGAqsishiPTNV 318
Cdd:cd00613 129 GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYP-NTLGVFEDlIKEIADIAHSAGALVYVDGD------NLNL 201
|
90 100
....*....|....*....|....*...
gi 1738373870 319 TALD------ADFFVFSGHKIFGPTGIG 340
Cdd:cd00613 202 TGLKppgeygADIVVGNLQKTGVPHGGG 229
|
|
| PRK05957 |
PRK05957 |
pyridoxal phosphate-dependent aminotransferase; |
142-340 |
3.90e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 235654 Cd Length: 389 Bit Score: 39.67 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 142 PKQVIDRISHYYLHENSNVHRAAHTLAarstDAYEAAREKVSRFIGAR-GPENIIFVrgtTEGLNLIAHSYVKPLLRPGD 220
Cdd:PRK05957 42 PPEAIEALNNFLANPENHKYQAVQGIP----PLLEAITQKLQQDNGIElNNEQAIVV---TAGSNMAFMNAILAITDPGD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 221 EIILtQLEHHANivPWQLIAQETGATIRVaPVDEHGQLIVEEYIRLFNDKTRFVSATHVSNALGTVTP---VQELVQIAH 297
Cdd:PRK05957 115 EIIL-NTPYYFN--HEMAITMAGCQPILV-PTDDNYQLQPEAIEQAITPKTRAIVTISPNNPTGVVYPealLRAVNQICA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1738373870 298 RFGvriaidgaqsISHIPTNVTaldaDFFVFSGHKIFGPTGIG 340
Cdd:PRK05957 191 EHG----------IYHISDEAY----EYFTYDGVKHFSPGSIP 219
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
171-355 |
6.40e-03 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 38.70 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 171 STDAYEAAREKVSRFIGArgPENIIFVRGTTEGLNLIAHsyvkpLLRPGDEIILTQLeHHANIVpwqLIAQETGATIRVA 250
Cdd:cd06454 44 TSDLHEELEEELAEFHGK--EAALVFSSGYAANDGVLST-----LAGKGDLIISDSL-NHASII---DGIRLSGAKKRIF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 251 P---VDEHGQLIvEEYIRLFNDKtrFVSATHVSNALGTVTPVQELVQIAHRFGVRIAIDGAQSI---------SHIPTNV 318
Cdd:cd06454 113 KhndMEDLEKLL-REARRPYGKK--LIVTEGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVgvygphgrgVEEFGGL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1738373870 319 TAlDADFFVFSGHKIFGPTGiGVIYGKQEVLE----AARPY 355
Cdd:cd06454 190 TD-DVDIIMGTLGKAFGAVG-GYIAGSKELIDylrsYARGF 228
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
162-308 |
8.33e-03 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 38.47 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 162 RAAHTLAARSTDAY---EAAREKVSRFIGARGPENIIFVRGTTEGlNLIAhsyVKPLLRPGDEIILTQLEHhanIVPWQL 238
Cdd:cd06502 15 LEAMAAANVGDDVYgedPTTAKLEARAAELFGKEAALFVPSGTAA-NQLA---LAAHTQPGGSVICHETAH---IYTDEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738373870 239 IAQETGATIRVAPVD-EHGQLI---VEEYIRLFND----KTRFVSATHVSNaLGTVTPVQELVQI---AHRFGVRIAIDG 307
Cdd:cd06502 88 GAPEFLSGVKLLPVPgENGKLTpedLEAAIRPRDDihfpPPSLVSLENTTE-GGTVYPLDELKAIsalAKENGLPLHLDG 166
|
.
gi 1738373870 308 A 308
Cdd:cd06502 167 A 167
|
|
| |
