|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
5-424 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 781.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 5 FRYQDLATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERA 84
Cdd:PRK00011 1 FFMDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 85 KEVFGAKFANVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGMKINFSGRLYNVAAYEVEKDTHLIDMAKLREQ 164
Cdd:PRK00011 81 KELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 165 AREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPRSGFILT 244
Cdd:PRK00011 161 ALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 245 NDEELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLTSEdakaaGIDVVSGGTDVHL 324
Cdd:PRK00011 241 NDEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAER-----GFRVVSGGTDNHL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 325 VLVDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDPRPPKVTSGLRIGTSALATRGFGEEDFREVSDIIAETLI-QGEKAD 403
Cdd:PRK00011 316 VLVDLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDnPDDEAV 395
|
410 420
....*....|....*....|.
gi 1317637751 404 IPALRARVEALAEKYPLYPGL 424
Cdd:PRK00011 396 IEEVKEEVKELCKRFPLYKYL 416
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
7-424 |
0e+00 |
|
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine hydroxymethyltransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439882 Cd Length: 414 Bit Score: 761.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 7 YQDLATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKE 86
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 87 VFGAKFANVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGMKINFSGRLYNVAAYEVEKDTHLIDMAKLREQAR 166
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 167 EVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPRSGFILTNd 246
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCN- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 247 EELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLtsedaKAAGIDVVSGGTDVHLVL 326
Cdd:COG0112 241 EELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEAL-----AERGFRVVSGGTDNHLVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 327 VDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDPRPPKVTSGLRIGTSALATRGFGEEDFREVSDIIAETLIQGE-KADIP 405
Cdd:COG0112 316 VDLRSKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEdEAVLA 395
|
410
....*....|....*....
gi 1317637751 406 ALRARVEALAEKYPLYPGL 424
Cdd:COG0112 396 EVREEVKELCKRFPLYPDL 414
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
5-421 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 665.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 5 FRYQDLATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERA 84
Cdd:PRK13034 4 FFSDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 85 KEVFGAKFANVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGMKINFSGRLYNVAAYEVEKDTHLIDMAKLREQ 164
Cdd:PRK13034 84 KQLFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 165 AREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPRSGFILT 244
Cdd:PRK13034 164 AKEHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 245 NDEELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLtsedaKAAGIDVVSGGTDVHL 324
Cdd:PRK13034 244 NDEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVL-----KERGYDLVSGGTDNHL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 325 VLVDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDPRPPKVTSGLRIGTSALATRGFGEEDFREVSDIIAETLIQGEKADI 404
Cdd:PRK13034 319 LLVDLRPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAAL 398
|
410
....*....|....*...
gi 1317637751 405 PA-LRARVEALAEKYPLY 421
Cdd:PRK13034 399 EQrVRKEVKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
14-414 |
0e+00 |
|
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). SHMT carries out interconversion of serine and glycine; it catalyzes the transfer of hydroxymethyl group of N5, N10-methylene tetrahydrofolate to glycine resulting in the formation of serine and tetrahydrofolate. Both eukaryotic and prokaryotic SHMT enzymes form tight obligate homodimers; the mammalian enzyme forms a homotetramer comprising four pyridoxal phosphate-bound active sites.
Pssm-ID: 99733 Cd Length: 402 Bit Score: 626.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 14 DPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKEVFGAKFA 93
Cdd:cd00378 4 DPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 94 NVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGM--KINFSGRLYNVAAYEVEKDTHLIDMAKLREQAREVKPK 171
Cdd:cd00378 84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 172 VIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPRSGFILTNDEELNK 251
Cdd:cd00378 164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGELAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 252 KINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLTSEdakaaGIDVVSGGTDVHLVLVDLRN 331
Cdd:cd00378 244 KINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKER-----GFKVVSGGTDNHLVLVDLRP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 332 SPMDGQQAEDLLHAAGITVNRNAVPFDPRPPKVTSGLRIGTSALATRGFGEEDFREVSDIIAETLIQGEKADIP-ALRAR 410
Cdd:cd00378 319 KGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAeEVRKE 398
|
....
gi 1317637751 411 VEAL 414
Cdd:cd00378 399 VAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
10-392 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 563.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 10 LATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKEVFG 89
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 90 AK----FANVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHG-----MKINFSGRLYNVAAYEVEKDTHLIDMAK 160
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGypvnsKKISASSKFFESMPYGVDPETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 161 LREQAREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPRSG 240
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 241 FILTND-------------EELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLTSEd 307
Cdd:pfam00464 241 MIFYRKgvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTER- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 308 akaaGIDVVSGGTDVHLVLVDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDpRPPKVTSGLRIGTSALATRGFGEEDFRE 387
Cdd:pfam00464 320 ----GYKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEK 394
|
....*
gi 1317637751 388 VSDII 392
Cdd:pfam00464 395 VAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
8-424 |
5.25e-171 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 486.80 E-value: 5.25e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 8 QDLATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKEV 87
Cdd:PTZ00094 13 QSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 88 FGAKF----ANVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGM-----KINFSGRLYNVAAYEVEKDThLIDM 158
Cdd:PTZ00094 93 FGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGFytakkKVSATSIYFESLPYQVNEKG-LIDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 159 AKLREQAREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPR 238
Cdd:PTZ00094 172 DKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 239 SGFILTN---DEELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLTSEdakaaGIDV 315
Cdd:PTZ00094 252 SGLIFYRkkvKPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKR-----GYDL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 316 VSGGTDVHLVLVDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDPRPPkVTSGLRIGTSALATRGFGEEDFREVSDIIAET 395
Cdd:PTZ00094 327 VTGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSAL-NPSGVRLGTPALTTRGAKEKDFKFVADFLDRA 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1317637751 396 L-----IQGEKA--------------DIPALRARVEALAEKYPlYPGL 424
Cdd:PTZ00094 406 VklaqeIQKQVGkklvdfkkaleknpELQKLRQEVVEFASQFP-FPGI 452
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
10-425 |
3.45e-163 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 468.37 E-value: 3.45e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 10 LATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKEVFG 89
Cdd:PRK13580 30 ILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 90 AKFANVQPHSGAQANAAVLMAL------------------------------AEPGD-TILGLNLAHGGHLTHGMKINFS 138
Cdd:PRK13580 110 AEHAYVQPHSGADANLVAFWAIlahkvespaleklgaktvndlteedwealrAELGNqRLLGMSLDSGGHLTHGFRPNIS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 139 GRLYNVAAYEVEKDTHLIDMAKLREQAREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGL--- 215
Cdd:PRK13580 190 GKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftg 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 216 HPSPVPHAHVVSSTVHKTLGGPRSGFILTnDEELNKKINSAVfPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDG 295
Cdd:PRK13580 270 DEDPVPHADIVTTTTHKTLRGPRGGLVLA-KKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 296 AKILAERLTSEDAKaagidVVSGGTDVHLVLVDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDPRPPKVTSGLRIGTSAL 375
Cdd:PRK13580 348 ARALAEGFLKRGAR-----LVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPAL 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317637751 376 ATRGFGEEDFREVSDIIAETL---------------IQGEKADIPA--LRARVEALAEKYPLYPGLE 425
Cdd:PRK13580 423 TTLGMGSDEMDEVAELIVKVLsnttpgttaegapskAKYELDEGVAqeVRARVAELLARFPLYPEID 489
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-425 |
4.16e-153 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 442.11 E-value: 4.16e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 8 QDLATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKEV 87
Cdd:PLN03226 13 APLEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 88 FGAKFA----NVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGM-----KINFSGRLYNVAAYEVEKDTHLIDM 158
Cdd:PLN03226 93 FRLDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYqtdgkKISATSIYFESMPYRLDESTGLIDY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 159 AKLREQAREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGPR 238
Cdd:PLN03226 173 DKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 239 SGFIL-------------TNDEELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKILAERLTS 305
Cdd:PLN03226 253 GGMIFfrkgpkppkgqgeGAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 306 EdakaaGIDVVSGGTDVHLVLVDLRNSPMDGQQAEDLLHAAGITVNRNAVPFDpRPPKVTSGLRIGTSALATRGFGEEDF 385
Cdd:PLN03226 333 K-----GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDF 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317637751 386 REVSDIIAETL-----IQGE-----------------KADIPALRARVEALAEKYPLyPGLE 425
Cdd:PLN03226 407 EKVAEFLHRAVtialkIQKEhgkklkdfkkglesndfSKDIEALRAEVEEFATSFPM-PGFD 467
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
8-425 |
4.65e-105 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 322.91 E-value: 4.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 8 QDLATFDPEVHAAIVDELARQRNTLEMIASENFVPRAVLEAQGSVLTNKYAEGYPGKRYYGGCEHVDVVETLAQERAKEV 87
Cdd:PLN02271 127 QPLPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 88 FG---AKFA-NVQPHSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGM------KINFSGRLYNVAAYEVEKDTHLID 157
Cdd:PLN02271 207 FGldsEKWGvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGYytpggkKVSGASIFFESLPYKVNPQTGYID 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 158 MAKLREQAREVKPKVIIAGWSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVHKTLGGP 237
Cdd:PLN02271 287 YDKLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 238 RSGFIL-------------------TNDEELNKKINSAVFPGQQGGPLMHVIAAKATAFKIAGMEEFKDRQQRTIDGAKI 298
Cdd:PLN02271 367 RGGIIFyrkgpklrkqgmllshgddNSHYDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQA 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 299 LAERLTSEDAKaagidVVSGGTDVHLVLVDLRNSPMDGQQAEDLLHAAGITVNRNAVpFDPRPPKVTSGLRIGTSALATR 378
Cdd:PLN02271 447 LASALLRRKCR-----LVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSR 520
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317637751 379 GFGEEDFREVSDIIAE-----TLIQGEKA--------------DIPALRARVEALAEKYPLyPGLE 425
Cdd:PLN02271 521 GCLESDFETIADFLLRaaqiaSAVQREHGklqkeflkglqnnkDIVELRNRVEAFASQFAM-PGFD 585
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
77-245 |
1.05e-20 |
|
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: 88.59 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 77 ETLAQERAKEVF--GAKFANVQPhSGAQANAAVLMALAEPGDTILGLNLAHGGHLTHGMKINFsgrlYNVAAYEVEKDTH 154
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAG----AKPVPVPVDDAGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 155 -LIDMAKLREQAREVKPKVIIAGWSAYPR--HEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVSSTVH 231
Cdd:cd01494 77 gGLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 1317637751 232 KTLGGPRSGFILTN 245
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
99-394 |
1.86e-13 |
|
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: 71.22 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 99 SGA-QANAAVLMALAEPGDTILGLNLAHGGHLTHgmkINFSGRlyNVAAYEVEKDTHLIDMAKLREQAREVKPKVII--- 174
Cdd:cd00609 66 NGAqEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAGA--EVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYlnn 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 175 ------AGWSAyprhEDFAEFRSIADEVGAYLWVDMAHfAGLVVAGLHPSPVPHAH-----VVSSTVHKTLGGP--RSGF 241
Cdd:cd00609 141 pnnptgAVLSE----EELEELAELAKKHGILIISDEAY-AELVYDGEPPPALALLDayervIVLRSFSKTFGLPglRIGY 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 242 ILTNDEELNKKINSAVfPGQQGGPLMHVIAAKATAFKiAGMEEFKDRQQRTIDGAKILAERLtsedaKAAGIDVVSGGTD 321
Cdd:cd00609 216 LIAPPEELLERLKKLL-PYTTSGPSTLSQAAAAAALD-DGEEHLEELRERYRRRRDALLEAL-----KELGPLVVVKPSG 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317637751 322 VHLVLVDLRNsPMDGQQAEDLLHAAGITVnrnaVPFDPRPPKVTSGLRIGTSALatrgfgEEDFREVSDIIAE 394
Cdd:cd00609 289 GFFLWLDLPE-GDDEEFLERLLLEAGVVV----RPGSAFGEGGEGFVRLSFATP------EEELEEALERLAE 350
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
67-375 |
1.47e-12 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 68.49 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 67 YGGCEHVDVVETLAQERAKEVFGAKF---ANVQPHSGAQANAAVL-MALAEPGDTILGLNLAHGGHlTHGMKINfSGRLY 142
Cdd:pfam00155 35 YGPTDGHPELREALAKFLGRSPVLKLdreAAVVFGSGAGANIEALiFLLANPGDAILVPAPTYASY-IRIARLA-GGEVV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 143 NVaAYEVEKDTHlIDMAKLrEQAREVKPKVIIA-------GwsAYPRHEDFAEFRSIADEVGAYLWVDMAHfAGLVVAGL 215
Cdd:pfam00155 113 RY-PLYDSNDFH-LDFDAL-EAALKEKPKVVLHtsphnptG--TVATLEELEKLLDLAKEHNILLLVDEAY-AGFVFGSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 216 HP-------SPVPHAHVVsSTVHKTLG--GPRSGFILTNDEELN--KKINSAVF---PGQQggplmhvIAAKATAFKIAG 281
Cdd:pfam00155 187 DAvatrallAEGPNLLVV-GSFSKAFGlaGWRVGYILGNAAVISqlRKLARPFYsstHLQA-------AAAAALSDPLLV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 282 MEEFKDRQQRTIDGAKILAERLTsedakAAGIDVVSGGTDVhLVLVDLRNSPMDgQQAEDLLHAAGITVNRNavpfdpRP 361
Cdd:pfam00155 259 ASELEEMRQRIKERRDYLRDGLQ-----AAGLSVLPSQAGF-FLLTGLDPETAK-ELAQVLLEEVGVYVTPG------SS 325
|
330
....*....|....
gi 1317637751 362 PKVTSGLRIGTSAL 375
Cdd:pfam00155 326 PGVPGWLRITVAGG 339
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
72-374 |
5.11e-09 |
|
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: 57.57 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 72 HVDVVETLAQERAKE---VFGakfanvqphSGAQANAAVLMALAEPGDTILGLNLAHgghlthgMKINFSGRLYNvAAYE 148
Cdd:cd06454 48 HEELEEELAEFHGKEaalVFS---------SGYAANDGVLSTLAGKGDLIISDSLNH-------ASIIDGIRLSG-AKKR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 149 VEKDTHLIDMAKLREQAREVKPKVIIAGWSAYPRHEDFA---EFRSIADEVGAYLWVDMAHFAGLV---VAGLHPSPVPH 222
Cdd:cd06454 111 IFKHNDMEDLEKLLREARRPYGKKLIVTEGVYSMDGDIAplpELVDLAKKYGAILFVDEAHSVGVYgphGRGVEEFGGLT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 223 AHV--VSSTVHKTLGGpRSGFILTNDEELNKKIN--------SAVFPgqqggplmHVIAAKATAFKIagMEEFKDRQQRT 292
Cdd:cd06454 191 DDVdiIMGTLGKAFGA-VGGYIAGSKELIDYLRSyargfifsTSLPP--------AVAAAALAALEV--LQGGPERRERL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 293 IDGAKILAERLtsedaKAAGIDVvsGGTDVHLVLVDLRNSPMDGQQAEDLLHAAGITVnrNAVPFdPRPPKVTSGLRIGT 372
Cdd:cd06454 260 QENVRYLRRGL-----KELGFPV--GGSPSHIIPPLIGDDPAKAVAFSDALLERGIYV--QAIRY-PTVPRGTARLRISL 329
|
..
gi 1317637751 373 SA 374
Cdd:cd06454 330 SA 331
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
80-252 |
7.10e-05 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 44.55 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 80 AQERAKEVFGAK--FANVQPHSGAqaNAAVLMALAEPGDTILGLNLAHGGHlTHGMKINFSGRLYNVAayEVEKDTHLI- 156
Cdd:cd00615 64 AQELAARAFGAKhtFFLVNGTSSS--NKAVILAVCGPGDKILIDRNCHKSV-INGLVLSGAVPVYLKP--ERNPYYGIAg 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 157 -----DMAKLREQAREVKPKVIIagwsaYPRHEDF-AEFRSIADEVGA---YLWVDMAHFAGLVVAGLHPSPVPHA---H 224
Cdd:cd00615 139 gippeTFKKALIEHPDAKAAVIT-----NPTYYGIcYNLRKIVEEAHHrglPVLVDEAHGAHFRFHPILPSSAAMAgadI 213
|
170 180
....*....|....*....|....*....
gi 1317637751 225 VVSSTvHKTLGGPRSG-FILTNDEELNKK 252
Cdd:cd00615 214 VVQST-HKTLPALTQGsMIHVKGDLVNPD 241
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
81-329 |
1.75e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.97 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 81 QERAKEVFGAKFAnVQPHSGAQANAAVLMALAEPGDTILGLNLAH------GGHLTHGmkinfSGRLYNVaayeVEKDTH 154
Cdd:pfam01212 38 EDRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHihfdetGGHAELG-----GVQPRPL----DGDEAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 155 LIDMAKLREQAREV------KPKVI-------IAGWSAYPRhEDFAEFRSIADEVGAYLWVDMAHFAGLVVA-GLHPSPV 220
Cdd:pfam01212 108 NMDLEDLEAAIREVgadifpPTGLIslenthnSAGGQVVSL-ENLREIAALAREHGIPVHLDGARFANAAVAlGVIVKEI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 221 -PHAHVVSSTVHKTLGGPRSGFILTNDEELNKKINsavFPGQQGGPL--MHVIAAKAtafkIAGMEEFKDRQQRTIDGAK 297
Cdd:pfam01212 187 tSYADSVTMCLSKGLGAPVGSVLAGSDDFIAKAIR---QRKYLGGGLrqAGVLAAAG----LRALEEGVARLARDHATAR 259
|
250 260 270
....*....|....*....|....*....|..
gi 1317637751 298 ILAERLtsedAKAAGIDVVSGGTDVHLVLVDL 329
Cdd:pfam01212 260 RLAEGL----ELLRLAIPRRVYTNTHMVYVAA 287
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
80-307 |
2.05e-04 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 43.26 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 80 AQERAKEVFGA--KFANVQPHSGAqaNAAVLMALAEPGDTILGLNLAHGGhLTHGMKI------------NFSGRLYNVA 145
Cdd:pfam01276 71 AQKYAARVFGAdkSYFVVNGTSGS--NKTVGMAVCTPGDTILIDRNCHKS-IHHALMLsgatpvylepsrNAYGIIGGIP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 146 AYEVEKDThlidmakLREQAREVKPK------VIIAGwsAYPRHedFAEFRSIADEVGA---YLWVDMAHFAglvVAGLH 216
Cdd:pfam01276 148 LHEFQEET-------LKEAIAEVPDAkgprlaVITNP--TYDGV--LYNAKEIVDTLHHlsdPILFDSAWVG---YEQFI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 217 PSPVPH-----------AHVVSSTVHKTLGGPRSGFILTNDEELN---KKINSAVFPGQQGGPLMHVIAAKATAFKIAGM 282
Cdd:pfam01276 214 PIYADAspmggenengpGIFVTQSVHKLLAALSQASYIHKKEGHIvnhDRFNEAFMMHATTSPSYPIFASLDVAAKMLEG 293
|
250 260
....*....|....*....|....*
gi 1317637751 283 EEFKDRQQRTIDGAKILAERLTSED 307
Cdd:pfam01276 294 NSGRRLWNECVERAIEFRKAIDTLN 318
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
148-253 |
1.15e-03 |
|
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.
Pssm-ID: 395827 Cd Length: 360 Bit Score: 40.73 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317637751 148 EVEKDTHLIDMAKLrEQAREVKPKVIIAGwSAYPRHEDFAEFRSIADEVGAYLWVDMAHFAGLVVAGLHPSPVPHAHVVS 227
Cdd:pfam01041 92 DIDPDTYNIDPEAI-EAAITPRTKAIIPV-HLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQGKKVGTLGDAATFS 169
|
90 100
....*....|....*....|....*.
gi 1317637751 228 STVHKTLGGPRSGFILTNDEELNKKI 253
Cdd:pfam01041 170 FHPTKNLTTGEGGAVVTNDPELAEKA 195
|
|
| |
