|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
1-406 |
0e+00 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 885.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 1 MIFSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFI 80
Cdd:PRK09295 1 MTFSVEKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKQAALFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTL 160
Cdd:PRK09295 81 NARSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISEMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 161 FDEKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
Cdd:PRK09295 161 FDERTRLLAITHVSNVLGTENPLAEMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 241 ALLQEMPPWEGGGSMIATVSLSEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESV 320
Cdd:PRK09295 241 ALLQEMPPWEGGGSMIATVSLTEGTTWAKAPWRFEAGTPNTGGIIGLGAALDYVSALGLNNIAEYEQNLMHYALSQLESV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQR 400
Cdd:PRK09295 321 PDLTLYGPQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVAGLQR 400
|
....*.
gi 259511796 401 IHRLLG 406
Cdd:PRK09295 401 IHRLLG 406
|
|
| sufS |
TIGR01979 |
cysteine desulfurases, SufSfamily; This model represents a subfamily of NifS-related cysteine ... |
6-406 |
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: 709.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 6 DKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINARSA 85
Cdd:TIGR01979 1 KNIRADFPILKRKINGKPLVYLDSAATSQKPQQVIDAVAEYYRNSNANVHRGIHTLSVRATEAYEAVREKVAKFINAASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 86 EELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKT 165
Cdd:TIGR01979 81 EEIVFTRGTTESINLVAYSWGDSNLKAGDEIVISEMEHHANIVPWQLLAERTGATLKFIPLDDDGTLDLDDLEKLLTEKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 166 RLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQE 245
Cdd:TIGR01979 161 KLVAITHVSNVLGTVNPVEEIAKLAHQVGAKVLVDGAQAVPHMPVDVQALDCDFYVFSGHKMYGPTGIGVLYGKEELLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 246 MPPWEGGGSMIATVSLsEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPDLTL 325
Cdd:TIGR01979 241 MPPFLGGGEMIAEVSF-EETTYNEAPHKFEAGTPNIAGVIGLGAAIDYLEAIGLENIEAHEHELTAYALERLGEIPGLRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 326 YGPQN---RLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIH 402
Cdd:TIGR01979 320 YGPRDaedRGGIISFNVEGVHPHDVGTILDEEGIAVRSGHHCAQPLMRRFGVPATCRASFYIYNTEEDIDALVEALKKVR 399
|
....
gi 259511796 403 RLLG 406
Cdd:TIGR01979 400 KFFG 403
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
4-404 |
0e+00 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 633.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 4 SVDKVRADFPVlsrevNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINAR 83
Cdd:COG0520 1 DVEAIRADFPV-----LGKPLVYLDNAATGQKPRPVIDAIRDYYEPYNANVHRGAHELSAEATDAYEAAREKVARFIGAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 84 SAEELVFVRGTTEGINLVANSWGNsnVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDE 163
Cdd:COG0520 76 SPDEIIFTRGTTEAINLVAYGLGR--LKPGDEILITEMEHHSNIVPWQELAERTGAEVRVIPLDEDGELDLEALEALLTP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 164 KTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALL 243
Cdd:COG0520 154 RTKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 244 QEMPPWEGGGSMIATVSLsEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPDL 323
Cdd:COG0520 234 EALPPFLGGGGMIEWVSF-DGTTYADLPRRFEAGTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIPGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 324 TLYGP---QNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQR 400
Cdd:COG0520 313 RILGPadpEDRSGIVSFNVDGVHPHDVAALLDDEGIAVRAGHHCAQPLMRRLGVPGTVRASFHLYNTEEEIDRLVEALKK 392
|
....
gi 259511796 401 IHRL 404
Cdd:COG0520 393 LAEL 396
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
26-398 |
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: 602.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 26 YLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSW 105
Cdd:cd06453 2 YLDNAATSQKPQPVIDAIVDYYRHYNANVHRGVHELSARATDAYEAAREKVARFINAPSPDEIIFTRNTTEAINLVAYGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 106 GNSNvRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTENPLAE 185
Cdd:cd06453 82 GRAN-KPGDEIVTSVMEHHSNIVPWQQLAERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 186 MITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGGSMIATVSLsEGT 265
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPPYGGGGEMIEEVSF-EET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 266 TWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYG-PQNRLGVIAFNLGKHHA 344
Cdd:cd06453 240 TYADLPHKFEAGTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIPGVRVYGdAEDRAGVVSFNLEGIHP 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 259511796 345 YDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGL 398
Cdd:cd06453 320 HDVATILDQYGIAVRAGHHCAQPLMRRLGVPGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
3-401 |
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: 577.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 3 FSVDKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINA 82
Cdd:NF041166 225 FDVNAVRRDFPILQERVNGKPLVWFDNAATTQKPQAVIDRLSYFYEHENSNIHRAAHELAARATDAYEGAREKVRRFIGA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 83 RSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFD 162
Cdd:NF041166 305 PSVDEIIFVRGTTEAINLVAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLAQETGAKLRVIPVDDSGQILLDEYAKLLN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 163 EKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEAL 242
Cdd:NF041166 385 PRTKLVSVTQVSNALGTVTPVKEIIALAHRAGAKVLVDGAQSVSHMPVDVQALDADFFVFSGHKVFGPTGIGVVYGKRDL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 243 LQEMPPWEGGGSMIATVSLsEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPD 322
Cdd:NF041166 465 LEAMPPWQGGGNMIADVTF-EKTVYQPAPNRFEAGTGNIADAVGLGAALDYVERIGIENIARYEHDLLEYATAGLAEVPG 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 323 LTLYG-PQNRLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRI 401
Cdd:NF041166 544 LRLIGtAADKASVLSFVLDGYSTEEVGKALNQEGIAVRSGHHCAQPILRRFGVEATVRPSLAFYNTCEEVDALVAVLRRL 623
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
26-394 |
0e+00 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 573.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 26 YLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINARSAEELVFVRGTTEGINLVANSW 105
Cdd:pfam00266 2 YLDSAATTQKPQEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTEAINLVALSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 106 GNSnVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTENPLAE 185
Cdd:pfam00266 82 GRS-LKPGDEIVITEMEHHANLVPWQELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 186 MITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPPWEGGGSMIATVSLsEGT 265
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDLLEKMPPLLGGGGMIETVSL-QES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 266 TWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPDLTLYGPQNRLGVIAFNLGKHHAY 345
Cdd:pfam00266 240 TFADAPWKFEAGTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNFKGVHPH 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 259511796 346 DVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRL 394
Cdd:pfam00266 320 DVATLLDESGIAVRSGHHCAQPLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
6-399 |
0e+00 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 520.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 6 DKVRADFPVLSREVNGLPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINARSA 85
Cdd:PLN02855 15 AETRPDFPILDQTVNGSKLVYLDNAATSQKPAAVLDALQDYYEEYNSNVHRGIHALSAKATDAYELARKKVAAFINASTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 86 EELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKT 165
Cdd:PLN02855 95 REIVFTRNATEAINLVAYTWGLANLKPGDEVILSVAEHHSNIVPWQLVAQKTGAVLKFVGLTPDEVLDVEQLKELLSEKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 166 RLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQE 245
Cdd:PLN02855 175 KLVATHHVSNVLGSILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLES 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 246 MPPWEGGGSMIATVSLsEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPDLTL 325
Cdd:PLN02855 255 MPPFLGGGEMISDVFL-DHSTYAPPPSRFEAGTPAIGEAIGLGAAIDYLSEIGMDRIHEYEVELGTYLYEKLSSVPGVRI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 326 YGP-----QNRLGVIAFNLGKHHAYDVGSFLD-NYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQ 399
Cdd:PLN02855 334 YGPkpsegVGRAALCAFNVEGIHPTDLSTFLDqQHGVAIRSGHHCAQPLHRYLGVNASARASLYFYNTKEEVDAFIHALK 413
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
3-405 |
1.62e-152 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 436.78 E-value: 1.62e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 3 FSVDKVRADFPVLSRevnglPLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINA 82
Cdd:PRK10874 4 FNPAQFRAQFPALQD-----AGVYLDSAATALKPQAVIEATQQFYSLSAGNVHRSQFAAAQRLTARYEAAREQVAQLLNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 83 RSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFD 162
Cdd:PRK10874 79 PDAKNIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLVPWLMVAQQTGAKVVKLPLGADRLPDVDLLPELIT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 163 EKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEAL 242
Cdd:PRK10874 159 PRTRILALGQMSNVTGGCPDLARAITLAHQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKSEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 243 LQEMPPWEGGGSMIATVSLsEGTTWTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPD 322
Cdd:PRK10874 239 LEAMSPWQGGGKMLTEVSF-DGFTPQSAPWRFEAGTPNVAGVIGLSAALEWLADIDINQAESWSRSLATLAEDALAKLPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 323 LTLYGPQNRlGVIAFNL-GKHHAyDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRI 401
Cdd:PRK10874 318 FRSFRCQDS-SLLAFDFaGVHHS-DLVTLLAEYGIALRAGQHCAQPLLAALGVTGTLRASFAPYNTQSDVDALVNAVDRA 395
|
....
gi 259511796 402 HRLL 405
Cdd:PRK10874 396 LELL 399
|
|
| FeS_syn_CsdA |
TIGR03392 |
cysteine desulfurase, catalytic subunit CsdA; Members of this protein family are CsdS. This ... |
3-405 |
6.36e-141 |
|
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: 407.30 E-value: 6.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 3 FSVDKVRADFPVLSREvnglpLAYLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINA 82
Cdd:TIGR03392 1 FNPAQFRRQFPALQDA-----TVYLDSAATALKPQAVIDATQQFYRLSSGTVHRSQHQEAQSLTARYEAAREQVAQLLNA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 83 RSAEELVFVRGTTEGINLVANSWGNSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLNPDGTLQLETLPTLFD 162
Cdd:TIGR03392 76 PDAENIVWTRGTTESINLVAQSYARPRLQPGDEIIVSEAEHHANLIPWLMVAQQTGAKVVKLPIGADLLPDIDQLPELLT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 163 EKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEAL 242
Cdd:TIGR03392 156 PRTRILALGQMSNVTGGCPDLARAITLAHQYGCVVVVDGAQGVVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKTEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 243 LQEMPPWEGGGSMIATVSLSEGTTwTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHYALSQLESVPD 322
Cdd:TIGR03392 236 LEAMPPWQGGGKMLSHVSFDGFTP-QAVPWRFEAGTPNIAGVIGLSAALEWLADIDINAAESWSVSLATLAEEALAQLPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 323 LTLYGPQNRlGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPAMCRASLAMYNTHEEVDRLVTGLQRIH 402
Cdd:TIGR03392 315 FRSFRCQGS-SLLAFDFAGVHHSDLVTLLAEQGIALRAGQHCAQPLMAALGVSGTLRASFAPYNTQQDVDALVNAVGRAL 393
|
...
gi 259511796 403 RLL 405
Cdd:TIGR03392 394 ELL 396
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
3-398 |
6.15e-74 |
|
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: 235.80 E-value: 6.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 3 FSVDKVRADFPVLSREVnglpLAYLDSAASAQKPSQVIDAEAE-FYRHGyaaVHRGIHTLSAQATEKM-ENVRKRASLFI 80
Cdd:TIGR01976 1 FDVEAVRGQFPALADGD----RVFFDNPAGTQIPQSVADAVSAaLTRSN---ANRGGAYESSRRADQVvDDAREAVADLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 81 NArSAEELVFVRGTTEGINLVANSWGnSNVRAGDNIIISQMEHHANIVPWQMLCARVGAELRVIPLN-PDGTLQLETLPT 159
Cdd:TIGR01976 74 NA-DPPEVVFGANATSLTFLLSRAIS-RRWGPGDEVIVTRLDHEANISPWLQAAERAGAKVKWARVDeATGELHPDDLAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 160 LFDEKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTgIGILYVK 239
Cdd:TIGR01976 152 LLSPRTRLVAVTAASNTLGSIVDLAAITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 240 EALLQEMPPWEgggsmiatVSLSEGTtwtkAPWRFEAGTPNTGGIIGLGAALEYVSALGLNN--------------IAEY 305
Cdd:TIGR01976 231 PELLMNLPPYK--------LTFSYDT----GPERFELGTPQYELLAGVVAAVDYLAGLGESAngsrrerlvasfqaIDAY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 306 EQNLMHYALSQLESVPDLTLYGPQN---RLGVIAFNLGKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYNVPA---MCR 379
Cdd:TIGR01976 299 ENRLAEYLLVGLSDLPGVTLYGVARlaaRVPTVSFTVHGLPPQRVVRRLADQGIDAWAGHFYAVRLLRRLGLNDeggVVR 378
|
410
....*....|....*....
gi 259511796 380 ASLAMYNTHEEVDRLVTGL 398
Cdd:TIGR01976 379 VGLAHYNTAEEVDRLLEAL 397
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
26-401 |
4.16e-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: 202.20 E-value: 4.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 26 YLDSAASAQKPSQVIDAEAEFYRHGYaavhrG----IHTLSAQATEKMENVRKRASLFINARsAEELVFVRGTTEGINLV 101
Cdd:COG1104 5 YLDNAATTPVDPEVLEAMLPYLTEYF-----GnpssLHSFGREARAALEEAREQVAALLGAD-PEEIIFTSGGTEANNLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 102 ANSWGNSNVRAGDNIIISQMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTEN 181
Cdd:COG1104 79 IKGAARAYRKKGKHIITSAIEHPAVLETARFL-EKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 182 PLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEmPPWEGGGsmiatvsl 261
Cdd:COG1104 158 PIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLE-PLIHGGG-------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 262 SEGTtwtkapWRfeAGTPNTGGIIGLGAALEYVSAlGLNNIAEYEQNLMHYALSQL-ESVPDLTLYG-PQNRL-GVIAFN 338
Cdd:COG1104 229 QERG------LR--SGTENVPGIVGLGKAAELAAE-ELEEEAARLRALRDRLEEGLlAAIPGVVINGdPENRLpNTLNFS 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259511796 339 LGKHHAYDVGSFLDNYGIAVRTGHHC------------AMPLMAYYNVPAMcRASLAMYNTHEEVDRLVTGLQRI 401
Cdd:COG1104 300 FPGVEGEALLLALDLAGIAVSSGSACssgslepshvllAMGLDEELAHGSI-RFSLGRFTTEEEIDRAIEALKEI 373
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
26-292 |
8.75e-29 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 115.52 E-value: 8.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 26 YLDSAASAQKPSQVIDAEAEFYRHGYAAVHRGIHTLSAQATEKMENVRKRASLFINArSAEELVFVRGTTEGINLVANSW 105
Cdd:PLN02651 2 YLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRTHLYGWESEDAVEKARAQVAALIGA-DPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 106 GNSNVRAGDNIIISQMEHHANIVPWQMLCARvGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTENPLAE 185
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQE-GFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 186 MITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALLQEMPP-WEGGGsmiatvslSEG 264
Cdd:PLN02651 160 IGELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRRRPRVRLEPlMSGGG--------QER 231
|
250 260
....*....|....*....|....*...
gi 259511796 265 TtwtkapwrFEAGTPNTGGIIGLGAALE 292
Cdd:PLN02651 232 G--------RRSGTENTPLVVGLGAACE 251
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
22-290 |
3.20e-28 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 114.65 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 22 LPLaYLDSAAS-------AQKPSQVIDAEAEFyrhGYAAVHRgiHTLSAQATEKMENVRKRASLFINArSAEELVFVRGT 94
Cdd:PRK14012 3 LPI-YLDYSATtpvdprvAEKMMPYLTMDGTF---GNPASRS--HRFGWQAEEAVDIARNQIADLIGA-DPREIVFTSGA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 95 TEGINL----VANSWGNSnvraGDNIIISQMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAI 170
Cdd:PRK14012 76 TESDNLaikgAAHFYQKK----GKHIITSKTEHKAVLDTCRQL-EREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 171 THVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVK-------EALL 243
Cdd:PRK14012 151 MHVNNEIGVIQDIAAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVRrkprvrlEAQM 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 259511796 244 QemppweGGGSmiatvslSEGttwtkapwrFEAGTPNTGGIIGLGAA 290
Cdd:PRK14012 231 H------GGGH-------ERG---------MRSGTLPTHQIVGMGEA 255
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
26-401 |
1.81e-22 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 97.88 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 26 YLDSAASAQKPSQVIDAEAEFYRHgYAAVHRGIHTLSAQATEKMENVRKRASLFINARsAEELVFVRGTTEGINLVANSW 105
Cdd:PRK02948 3 YLDYAATTPMSKEALQTYQKAASQ-YFGNESSLHDIGGTASSLLQVCRKTFAEMIGGE-EQGIYFTSGGTESNYLAIQSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 106 GNSNVRAGDNIIISQMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVSNVLGTENPLAE 185
Cdd:PRK02948 81 LNALPQNKKHIITTPMEHASIHSYFQSL-ESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 186 MITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEALlqempPWEgggsmiatvSLSEGT 265
Cdd:PRK02948 160 IGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQV-----RWK---------PVFPGT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 266 TWTKApwrFEAGTPNTGGIIGLGAALEYVsalgLNNIAEYE---QNLMHYALSQLESVPdltlygpqnrLGVIAFNLGKH 342
Cdd:PRK02948 226 THEKG---FRPGTVNVPGIAAFLTAAENI----LKNMQEESlrfKELRSYFLEQIQTLP----------LPIEVEGHSTS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 343 H-AYDVGSFLDNY------------GIAVRTGHHCAmplmAYYNVP--AM-------------CRASLAMYNTHEEVDRL 394
Cdd:PRK02948 289 ClPHIIGVTIKGIegqytmlecnrrGIAISTGSACQ----VGKQEPskTMlaigktyeeakqfVRFSFGQQTTKDQIDTT 364
|
....*..
gi 259511796 395 VTGLQRI 401
Cdd:PRK02948 365 IHALETI 371
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
68-239 |
5.04e-16 |
|
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: 75.11 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 68 KMENVRKRASLFINArSAEELVFVRGTTEGINLVANSWgnsnVRAGDNIIISQMEHHANIvpWQMLcARVGAELRVIPLN 147
Cdd:cd01494 1 KLEELEEKLARLLQP-GNDKAVFVPSGTGANEAALLAL----LGPGDEVIVDANGHGSRY--WVAA-ELAGAKPVPVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 148 P--DGTLQLETLP-TLFDEKTRLLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALD---CDFYV 221
Cdd:cd01494 73 DagYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPeggADVVT 152
|
170
....*....|....*...
gi 259511796 222 FSGHKLYGPTGIGILYVK 239
Cdd:cd01494 153 FSLHKNLGGEGGGVVIVK 170
|
|
| SepCysS |
cd06452 |
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ... |
90-240 |
5.13e-12 |
|
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: 66.65 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 90 FVRGTTEGINLVANSWgnsnVRAGDNIIISQMEHHANIVPWQmlcaRVGAELRVIPLN--PDGTLQLETLPTLFDEKTR- 166
Cdd:cd06452 64 VTPGAREGKFAVMHSL----CEKGDWVVVDGLAHYTSYVAAE----RAGLNVREVPNTghPEYHITPEGYAEVIEEVKDe 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 167 ------LLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTG-IGILYVK 239
Cdd:cd06452 136 fgkppaLALLTHVDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAASApIGVLATT 215
|
.
gi 259511796 240 E 240
Cdd:cd06452 216 E 216
|
|
| PRK09331 |
PRK09331 |
Sep-tRNA:Cys-tRNA synthetase; Provisional |
90-240 |
1.10e-10 |
|
Sep-tRNA:Cys-tRNA synthetase; Provisional
Pssm-ID: 236469 Cd Length: 387 Bit Score: 62.64 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 90 FVRGTTEGINLVANSWGNsnvrAGDNIIISQMEHHANIVPWQmlcaRVGAELRVIPL--NPDGTLQLETLPTLFDEKTR- 166
Cdd:PRK09331 83 VTHGAREGKFAVMHSLCK----KGDYVVLDGLAHYTSYVAAE----RAGLNVREVPKtgYPEYKITPEAYAEKIEEVKEe 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 167 ------LLAITHVSNVLGTENPLAEMITLAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTG-IGILYVK 239
Cdd:PRK09331 155 tgkppaLALLTHVDGNYGNLADAKKVAKVAHEYGIPFLLNGAYTVGRMPVDGKKLGADFIVGSGHKSMAASApSGVLATT 234
|
.
gi 259511796 240 E 240
Cdd:PRK09331 235 E 235
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
130-308 |
5.05e-09 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 57.41 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 130 WQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKT--RLLAITHV--SNvlGTENPLAEMITLAHQHGAKVLVDG--AQ 203
Cdd:COG0075 89 WAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPdiKAVAVVHNetST--GVLNPLEEIGALAKEHGALLIVDAvsSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 204 AVMhhPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEALLQEMppwegGGSMIATVSLS---EGTTWTKAPWRFeagTP 279
Cdd:COG0075 167 GGV--PLDMDEWGIDVVVSGSQKcLMLPPGLAFVAVSERALEAI-----EARKLPSYYLDlklWLKYWEKGQTPY---TP 236
|
170 180 190
....*....|....*....|....*....|
gi 259511796 280 NTGGIIGLGAALEYVSALGLNN-IAEYEQN 308
Cdd:COG0075 237 PVSLLYALREALDLILEEGLENrFARHRRL 266
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
138-326 |
1.56e-08 |
|
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: 56.09 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 138 GAELRVIPLNPDGTLQLETLPTLFDEKTRLLAITHVsNVLGT-ENPLAEMITLAHQHGAKVLVDGAQ---AVMHHPVDVQ 213
Cdd:cd00613 133 GIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYP-NTLGVfEDLIKEIADIAHSAGALVYVDGDNlnlTGLKPPGEYG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 214 AldcDFYVFSGHKLYGPTG-----IGILYVKEALLQEMPpweggGSMIATVSLSEGTT-------WTKAPWRFEAGTPN- 280
Cdd:cd00613 212 A---DIVVGNLQKTGVPHGgggpgAGFFAVKKELVRFLP-----GRLVGVTKDAEGNRafrlalqTREQHIRREKATSNi 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 259511796 281 -TGGIIGLGAALEYVSALG---LNNIAEYEQNLMHYALSQLESVPDLTLY 326
Cdd:cd00613 284 cTGQALLALMAAMYIVYLGpegLKEIAERAHLNANYLAKRLKEVGGVLPF 333
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
110-246 |
1.64e-08 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 55.76 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 110 VRAGDNIIISQMEHHANIvpWQMLCARVGAELRVIPLNPDGTLQLETLPTLFDEKT-RLLAITHVSNVLGTENPLAEMIT 188
Cdd:cd06451 71 LEPGDKVLVGVNGVFGDR--WADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDiKAVTLTHNETSTGVLNPLEGIGA 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 189 LAHQHGAKVLVDGAQAVMHHPVDVQALDCDfYVFSGHK--LYGPTGIGILYVKEALLQEM 246
Cdd:cd06451 149 LAKKHDALLIVDAVSSLGGEPFRMDEWGVD-VAYTGSQkaLGAPPGLGPIAFSERALERI 207
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
84-403 |
2.11e-07 |
|
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: 52.34 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 84 SAEELVFVRGTTEGINLVANSWgnsnVRAGDNIIISQmehhanivP-WQM---LCARVGAELRVIPLNPDGTLQL--ETL 157
Cdd:cd00609 58 PPEEIVVTNGAQEALSLLLRAL----LNPGDEVLVPD--------PtYPGyeaAARLAGAEVVPVPLDEEGGFLLdlELL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 158 PTLFDEKTRLLAITHVSNVLG---TENPLAEMITLAHQHGAKVLVDGA-------QAVMHHPVDVQALDCDFYVFSGHKL 227
Cdd:cd00609 126 EAAKTPKTKLLYLNNPNNPTGavlSEEELEELAELAKKHGILIISDEAyaelvydGEPPPALALLDAYERVIVLRSFSKT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 228 YGPTG--IGILYVKEALLQEMppwegggsmiatvslsegttwTKAPWRFEAGTPNTGGIIGLGAALEYVSALGLNNIAEY 305
Cdd:cd00609 206 FGLPGlrIGYLIAPPEELLER---------------------LKKLLPYTTSGPSTLSQAAAAAALDDGEEHLEELRERY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 306 EQNlMHYALSQLESVPDLTLYGPQNrlgviAFNL-----GKHHAYDVGSFLDNYGIAVRTGHHCAMPLMAYYnvpamcRA 380
Cdd:cd00609 265 RRR-RDALLEALKELGPLVVVKPSG-----GFFLwldlpEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFV------RL 332
|
330 340
....*....|....*....|...
gi 259511796 381 SLAmyNTHEEVDRlvtGLQRIHR 403
Cdd:cd00609 333 SFA--TPEEELEE---ALERLAE 350
|
|
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
4-364 |
6.75e-07 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 51.41 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 4 SVDKVRA-DFPVLSREVnglplaYLDSA-ASAQKPSQVIDAEAEFYRHGYAAVHRGIHTlSAQATEKMENVRKRASLFIN 81
Cdd:PLN02724 20 PIDELRAtEFARLKGVV------YLDHAgATLYSESQLEAALADFSSNVYGNPHSQSDS-SMRSSDTIESARQQVLEYFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 82 ARSAE-ELVFVRGTTEGINLVANSWGNSNvragDNIIISQMEHHANIVPWQMLCARVGA--------------------- 139
Cdd:PLN02724 93 APPSDyACVFTSGATAALKLVGETFPWSS----ESHFCYTLENHNSVLGIREYALEKGAaaiavdieeaanqptnsqgsv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 140 --ELRVIPLNPDGTLQLETLPtlfDEKTRLLAITHVSNVLGTENPLaEMITL----AHQHGAK-----VLVDGAQAVMHH 208
Cdd:PLN02724 169 vvKSRGLQRRNTSKLQKREDD---GEAYNLFAFPSECNFSGAKFPL-DLVKLikdnQHSNFSKsgrwmVLLDAAKGCGTS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 209 PVDVQALDCDFYVFSGHKLYG-PTGIGILYVKE---ALLQEMppWEGGGSMIATV----------SLSEgttwtkapwRF 274
Cdd:PLN02724 245 PPDLSRYPADFVVVSFYKIFGyPTGLGALLVRRdaaKLLKKK--YFGGGTVAASIadidfvkrreRVEQ---------RF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 275 EAGTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMHY------ALSQLESVPDLTLYGPQN------RLG-VIAFNL-- 339
Cdd:PLN02724 314 EDGTISFLSIAALRHGFKLLNRLTISAIAMHTWALTHYvanslrNLKHGNGAPVCVLYGNHTfklefhIQGpIVTFNLkr 393
|
410 420
....*....|....*....|....*...
gi 259511796 340 --GKHHAY-DVGSFLDNYGIAVRTGHHC 364
Cdd:PLN02724 394 adGSWVGHrEVEKLASLSGIQLRTGCFC 421
|
|
| PRK13479 |
PRK13479 |
2-aminoethylphosphonate--pyruvate transaminase; Provisional |
133-245 |
1.38e-06 |
|
2-aminoethylphosphonate--pyruvate transaminase; Provisional
Pssm-ID: 184076 [Multi-domain] Cd Length: 368 Bit Score: 49.91 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 133 LCARVGAELRVIPLNpdgtlqlETLPTLFDEKTRLLA----ITHVSNV-----LGTENPLAEMITLAHQHGAKVLVDGAQ 203
Cdd:PRK13479 98 IAEYLGIAHVVLDTG-------EDEPPDAAEVEAALAadprITHVALVhcettTGILNPLDEIAAVAKRHGKRLIVDAMS 170
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 259511796 204 AVMHHPVDVQALDCDFYVFSGHK-LYGPTGIGILYVKEALLQE 245
Cdd:PRK13479 171 SFGAIPIDIAELGIDALISSANKcIEGVPGFGFVIARRSELEA 213
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
130-311 |
4.33e-05 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 45.52 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 130 WQMLCARVGAELRVIPLNPDGTLQLETLPTLFDE----KTRLLAITHVSNVLGTENPLAEM--ITLAHQHGAKVLVDGAQ 203
Cdd:PLN02409 99 WIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnhKIKAVCVVHNETSTGVTNDLAGVrkLLDCAQHPALLLVDGVS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 204 AV--MHHPVDVQALDCdFYVFSGHKLYGPTGIGILYVKEALLQEM-----PP----WeggGSMIATVSLseGTTWtkaPW 272
Cdd:PLN02409 179 SIgaLDFRMDEWGVDV-ALTGSQKALSLPTGLGIVCASPKALEASktaksPRvffdW---ADYLKFYKL--GTYW---PY 249
|
170 180 190
....*....|....*....|....*....|....*....
gi 259511796 273 rfeagTPNTGGIIGLGAALEYVSALGLNNIAEYEQNLMH 311
Cdd:PLN02409 250 -----TPSIQLLYGLRAALDLIFEEGLENVIARHARLGE 283
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
87-246 |
4.73e-05 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 44.99 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 87 ELVFVRGTTEGINLVANSWGNsnvrAGDNIIISQMEH--HANIVPWqmlcarVGAELRVIPLNP--DGTLQLETLPTLFD 162
Cdd:pfam00155 65 AVVFGSGAGANIEALIFLLAN----PGDAILVPAPTYasYIRIARL------AGGEVVRYPLYDsnDFHLDFDALEAALK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 163 EKTRLLAITHVSNVLGTENPLAE---MITLAHQHGAKVLVD--------GAQAVMHHPVDVQALDCDFYVFSGHKLYGPT 231
Cdd:pfam00155 135 EKPKVVLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDeayagfvfGSPDAVATRALLAEGPNLLVVGSFSKAFGLA 214
|
170
....*....|....*..
gi 259511796 232 G--IGILYVKEALLQEM 246
Cdd:pfam00155 215 GwrVGYILGNAAVISQL 231
|
|
| tyr_amTase_E |
TIGR01264 |
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ... |
85-200 |
2.37e-04 |
|
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273529 [Multi-domain] Cd Length: 401 Bit Score: 42.85 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 85 AEELVFVRGTTEGINLVANSWGNsnvrAGDNIIISqmehHANIVPWQMLCARVGAELRVIPLNPDGTLQ--LETLPTLFD 162
Cdd:TIGR01264 95 ADDVVLCSGCSHAIEMCIAALAN----AGQNILVP----RPGFPLYETLAESMGIEVKLYNLLPDKSWEidLKQLESLID 166
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 259511796 163 EKTRLLAITHVSNVLG---TENPLAEMITLAHQHGAKVLVD 200
Cdd:TIGR01264 167 EKTAALIVNNPSNPCGsvfSRQHLEEILAVAERQCLPIIAD 207
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
89-241 |
1.11e-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: 40.97 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 89 VFVRGTTEGiNLVA-----NSWGNSNVRAGD-------NIIISQMEHHAnivpWQMLCA--RVGAE-LRVIPLNPDGTLQ 153
Cdd:COG0076 129 VFTSGGTEA-NLLAllaarDRALARRVRAEGlpgaprpRIVVSEEAHSS----VDKAARllGLGRDaLRKVPVDEDGRMD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 154 LETLPTLFDEKTRLLAITH-VSNVLGTEN-----PLAEMITLAHQHGAKVLVDGA-----QAVMHHPVDVQALD-CDFYV 221
Cdd:COG0076 204 PDALEAAIDEDRAAGLNPIaVVATAGTTNtgaidPLAEIADIAREHGLWLHVDAAyggfaLPSPELRHLLDGIErADSIT 283
|
170 180
....*....|....*....|.
gi 259511796 222 FSGHK-LYGPTGIGILYVKEA 241
Cdd:COG0076 284 VDPHKwLYVPYGCGAVLVRDP 304
|
|
| SelA |
COG1921 |
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis]; |
162-233 |
3.26e-03 |
|
Seryl-tRNA(Sec) selenium transferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441524 Cd Length: 399 Bit Score: 39.33 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 162 DEKTRLLAITHVSN--VLG--TENPLAEMITLAHQH--------GAKVLVDGAQAVMHHPVDVQ---ALDCDFYVFSGHK 226
Cdd:COG1921 152 TENTAALLKVHTSNyrIVGftEEVSLAELAELAHEHglpvivdlGSGSLVDLSKYGLPHEPTVQeylAAGADLVTFSGDK 231
|
....*....
gi 259511796 227 LY-GPT-GI 233
Cdd:COG1921 232 LLgGPQaGI 240
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
89-239 |
6.88e-03 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 38.34 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 89 VFVRGTTE----GINLVANSWGNSNVRAGD------NIIISQMEHHAnivpWQMLCARVGAELRVIPLNPDGTLQLETLP 158
Cdd:cd06450 61 VFTSGGSEsnllALLAARDRARKRLKAGGGrgidklVIVCSDQAHVS----VEKAAAYLDVKVRLVPVDEDGRMDPEALE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259511796 159 TLFDEKTRLLAIT-HVSNVLGTEN-----PLAEMITLAHQHGAKVLVDGAQAVMHHPvdvqALDCDFYVF---------- 222
Cdd:cd06450 137 AAIDEDKAEGLNPiMVVATAGTTDtgaidPLEEIADLAEKYDLWLHVDAAYGGFLLP----FPEPRHLDFgiervdsisv 212
|
170
....*....|....*...
gi 259511796 223 SGHKLYG-PTGIGILYVK 239
Cdd:cd06450 213 DPHKYGLvPLGCSAVLVR 230
|
|
| AmyAc_bac1_AmyA |
cd11315 |
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ... |
175-208 |
9.49e-03 |
|
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
Pssm-ID: 200454 [Multi-domain] Cd Length: 352 Bit Score: 38.03 E-value: 9.49e-03
10 20 30
....*....|....*....|....*....|....
gi 259511796 175 NVLGTENPLAEMITLAHQHGAKVLVDgaqAVMHH 208
Cdd:cd11315 62 NQLGTEDDFKALCAAAHKYGIKIIVD---VVFNH 92
|
|
| |
