|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
6-417 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 822.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 6 MNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKEL 85
Cdd:PRK00011 4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 86 FGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDA-TGHIDYADLEKQAKE 164
Cdd:PRK00011 84 FGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEeTGLIDYDEVEKLALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 165 HKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKgg 244
Cdd:PRK00011 164 HKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTN-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 245 SEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLV 324
Cdd:PRK00011 242 DEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 325 DKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKG 404
Cdd:PRK00011 322 SKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKE 401
|
410
....*....|...
gi 56480132 405 KVLDICARYPVYA 417
Cdd:PRK00011 402 EVKELCKRFPLYK 414
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
6-417 |
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: 798.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 6 MNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKEL 85
Cdd:COG0112 3 SSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 86 FGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDA-TGHIDYADLEKQAKE 164
Cdd:COG0112 83 FGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPeTGLIDYDEVRKLALE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 165 HKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKgg 244
Cdd:COG0112 163 HKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCN-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 245 sEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLV 324
Cdd:COG0112 241 -EELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 325 DKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKG 404
Cdd:COG0112 320 SKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVRE 399
|
410
....*....|...
gi 56480132 405 KVLDICARYPVYA 417
Cdd:COG0112 400 EVKELCKRFPLYP 412
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
5-416 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 717.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 5 EMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKE 84
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 85 LFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDA-TGHIDYADLEKQAK 163
Cdd:PRK13034 86 LFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRlTGLIDYDEVEELAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 164 EHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKg 243
Cdd:PRK13034 166 EHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTN- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 244 gSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDL 323
Cdd:PRK13034 245 -DEEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 324 VDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIK 403
Cdd:PRK13034 324 RPKGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVR 403
|
410
....*....|...
gi 56480132 404 GKVLDICARYPVY 416
Cdd:PRK13034 404 KEVKALCSRFPIY 416
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
8-386 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 659.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 88 AD----YANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNF-----SGKLYNIVPYGID-ATGHIDYAD 157
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDpETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 158 LEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGG 237
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 238 LILA-----------KGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERG 306
Cdd:pfam00464 241 MIFYrkgvksvdktgKEILYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 307 YKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWM 386
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
9-409 |
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: 651.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 9 ADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGA 88
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 89 DYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSP--VNFSGKLYNIVPYGID-ATGHIDYADLEKQAKEH 165
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDpETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 166 KPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGs 245
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 246 eELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLVD 325
Cdd:cd00378 240 -ELAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 326 KNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGK 405
Cdd:cd00378 319 KGITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKE 398
|
....
gi 56480132 406 VLDI 409
Cdd:cd00378 399 VAEL 402
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
1-391 |
4.46e-175 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 496.43 E-value: 4.46e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 1 MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAID 80
Cdd:PTZ00094 8 VLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 81 RAKELFGADY----ANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHG-----SPVNFSGKLYNIVPYGIDATG 151
Cdd:PTZ00094 88 RALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 152 HIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTL 231
Cdd:PTZ00094 168 LIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 232 AGPRGGLILAKGGSEELYK-KLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVV 310
Cdd:PTZ00094 248 RGPRSGLIFYRKKVKPDIEnKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 311 SGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRVGTPAITRRGFKEAEAKELAgwmcDVL 390
Cdd:PTZ00094 328 TGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVA----DFL 402
|
.
gi 56480132 391 D 391
Cdd:PTZ00094 403 D 403
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
17-416 |
1.15e-163 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 469.14 E-value: 1.15e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 17 QAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPH 96
Cdd:PRK13580 39 EAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQPH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 97 SGSQANFAVYTALL------------------------------EPGDTV-LGMNLAHGGHLTHGSPVNFSGKLYNIVPY 145
Cdd:PRK13580 119 SGADANLVAFWAILahkvespaleklgaktvndlteedwealraELGNQRlLGMSLDSGGHLTHGFRPNISGKMFHQRSY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 146 GID-ATGHIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYP---NPVPHAH 221
Cdd:PRK13580 199 GVDpDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHAD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 222 VVTTTTHKTLAGPRGGLILAKggsEELYKKLNSAVfPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEV 301
Cdd:PRK13580 279 IVTTTTHKTLRGPRGGLVLAK---KEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 302 FLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKE 381
Cdd:PRK13580 355 FLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDE 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 56480132 382 LAGWMCDVLDSIN----------------DEAVIERIKGKVLDICARYPVY 416
Cdd:PRK13580 435 VAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLY 485
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-378 |
4.40e-160 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 459.45 E-value: 4.40e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 88 ADYA----NVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNfSGKL------YNIVPYGID-ATGHIDYA 156
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTD-GKKIsatsiyFESMPYRLDeSTGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 157 DLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRG 236
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 237 GLIL--------AKGGSEELY---KKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLER 305
Cdd:PLN03226 254 GMIFfrkgpkppKGQGEGAVYdyeDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56480132 306 GYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDpKSPFVTSGIRVGTPAITRRGFKEAE 378
Cdd:PLN03226 334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKD 405
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
8-383 |
1.56e-111 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 339.09 E-value: 1.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 8 IADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFG 87
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 88 ADYA----NVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHG--SP----VNFSGKLYNIVPYGIDA-TGHIDYA 156
Cdd:PLN02271 209 LDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNPqTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 157 DLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRG 236
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 237 GLILAKGGSE-----------------ELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMV 299
Cdd:PLN02271 369 GIIFYRKGPKlrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 300 EVFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSV--PNDPKSPfvtSGIRVGTPAITRRGFKEA 377
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIfgDNGTISP---GGVRIGTPAMTSRGCLES 525
|
....*.
gi 56480132 378 EAKELA 383
Cdd:PLN02271 526 DFETIA 531
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-242 |
9.00e-19 |
|
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: 83.20 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 75 EQLAIDRAKELF--GADYANVQPhSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGspVNFSGKLYNIVPYGIDATGH 152
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 153 IDYADLEKQAKEHKPKMII--GGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKT 230
Cdd:cd01494 79 LDVAILEELKAKPNVALIVitPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKN 158
|
170
....*....|..
gi 56480132 231 LAGPRGGLILAK 242
Cdd:cd01494 159 LGGEGGGVVIVK 170
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
91-383 |
2.07e-09 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 58.86 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 91 ANVQPHSGSQAN-FAVYTALLEPGDTVLGMNLAHGGHLT----HGSPVNFsgklyniVPYGIDATGHIDYADLEKQAKEh 165
Cdd:pfam00155 64 AAVVFGSGAGANiEALIFLLANPGDAILVPAPTYASYIRiarlAGGEVVR-------YPLYDSNDFHLDFDALEAALKE- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 166 KPKMII-GGFSAYSGVV----DWAKMREIADSIGAYLFVDMAHvaglvAAGVYPNPVPHAHVVTTTTHKT---------- 230
Cdd:pfam00155 136 KPKVVLhTSPHNPTGTVatleELEKLLDLAKEHNILLLVDEAY-----AGFVFGSPDAVATRALLAEGPNllvvgsfska 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 231 --LAGPRGGLILakgGSEELYKKLNSAVFPG---GQGGPlmhvIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLER 305
Cdd:pfam00155 211 fgLAGWRVGYIL---GNAAVISQLRKLARPFyssTHLQA----AAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAA 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56480132 306 GYKVVsgGTDNHLFLVDLVDKNLTGKEADAALGRANITVnknsVPNdpKSPFVTSGIRVGTPAITrrgfkEAEAKELA 383
Cdd:pfam00155 284 GLSVL--PSQAGFFLLTGLDPETAKELAQVLLEEVGVYV----TPG--SSPGVPGWLRITVAGGT-----EEELEELL 348
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
96-320 |
1.38e-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: 53.11 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 96 HSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHgspVNFSGklYNIVPYGIDATGHIDY-ADLEKQAKEHKPKMIIggF 174
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG--AEVVPVPLDEEGGFLLdLELLEAAKTPKTKLLY--L 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 175 SAYS---GVV----DWAKMREIADSIGAYLFVDMAHvAGLvaagVYPNPVPHAHVVTTTTHK-----------TLAGPRG 236
Cdd:cd00609 139 NNPNnptGAVlseeELEELAELAKKHGILIISDEAY-AEL----VYDGEPPPALALLDAYERvivlrsfsktfGLPGLRI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 237 GLILAkggSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAmEPEFKTYQQQVAKNAKAMVEVFLERGYKVV---SGG 313
Cdd:cd00609 214 GYLIA---PPEELLERLKKLLPYTTSGPSTLSQAAAAAALDDG-EEHLEELRERYRRRRDALLEALKELGPLVVvkpSGG 289
|
....*..
gi 56480132 314 tdNHLFL 320
Cdd:cd00609 290 --FFLWL 294
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
96-208 |
1.71e-06 |
|
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: 49.48 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 96 HSGSQANFAVYTALLEPGDTVLGMNLAHG----GHLTHGSPvnfsgklynIVPYGidatgHIDYADLEKQAKE----HKP 167
Cdd:cd06454 68 SSGYAANDGVLSTLAGKGDLIISDSLNHAsiidGIRLSGAK---------KRIFK-----HNDMEDLEKLLREarrpYGK 133
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 56480132 168 KMII--GGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLV 208
Cdd:cd06454 134 KLIVteGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
80-205 |
4.21e-05 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 44.90 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 80 DRAKELFGADYAnVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSG-KLYNIVpygIDATGHIDYADL 158
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGGvQPRPLD---GDEAGNMDLEDL 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56480132 159 EKQAKEH------KPKMI-------IGGFSAYSgvVDW-AKMREIADSIGAYLFVDMAHVA 205
Cdd:pfam01212 115 EAAIREVgadifpPTGLIslenthnSAGGQVVS--LENlREIAALAREHGIPVHLDGARFA 173
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
80-205 |
2.48e-04 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 43.18 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 80 DRAKELFGADYA----NvqphsG-SQANFAVYTALLEPGDTVL-GMN----LAHGGHLTHGSPVNFSGKLYNivPYGIda 149
Cdd:COG1982 73 ELAAEAFGADRTfflvN-----GtSSGNKAMILAVCGPGDKVLvPRNchksVIHGLILSGAIPVYLNPEIDN--ELGI-- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56480132 150 TGHIDYADLEKQAKEHKPkmiiggFSA-------YSGVV-DWAKMREIADSIGAYLFVDMAHVA 205
Cdd:COG1982 144 IGGITPEAVEEALIEHPD------AKAvlitnptYYGVCyDLKAIAELAHEHGIPVLVDEAHGA 201
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
78-257 |
4.12e-04 |
|
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: 41.85 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 78 AIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGM-----NLAHGGHLTHGSPVnfsgklYnIVPY---GIDA 149
Cdd:cd00615 64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDrnchkSVINGLVLSGAVPV------Y-LKPErnpYYGI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 150 TGHIDYADLEKQAKEHK-PKMIIGGFSAYSGVV-DWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPH--AHVVTT 225
Cdd:cd00615 137 AGGIPPETFKKALIEHPdAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSSAAMagADIVVQ 216
|
170 180 190
....*....|....*....|....*....|..
gi 56480132 226 TTHKTLAGPRGGLILAKGGSEELYKKLNSAVF 257
Cdd:cd00615 217 STHKTLPALTQGSMIHVKGDLVNPDRVNEALN 248
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
97-213 |
7.04e-04 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 41.68 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 97 SGSQANFAVYTALLEPGDTVLGMNLAH-----GGHLthgSPVNFSgklynivpygidATGHIDYADLEKQ--AKEHKPKM 169
Cdd:PRK05958 107 SGYAANLAVLTALAGKGDLIVSDKLNHaslidGARL---SRARVR------------RYPHNDVDALEALlaKWRAGRAL 171
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 56480132 170 II--GGFSAYSGVVDWAKMREIADSIGAYLFVDMAHvaglvAAGVY 213
Cdd:PRK05958 172 IVteSVFSMDGDLAPLAELVALARRHGAWLLVDEAH-----GTGVL 212
|
|
| OKR_DC_1 |
pfam01276 |
Orn/Lys/Arg decarboxylase, major domain; |
78-205 |
1.05e-03 |
|
Orn/Lys/Arg decarboxylase, major domain;
Pssm-ID: 396025 [Multi-domain] Cd Length: 417 Bit Score: 40.95 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 78 AIDRAKELFGAD--YANVQPHSGSqaNFAVYTALLEPGDTVL-----GMNLAHGGHLTHGSPVNFSGKlYNivPYGIdaT 150
Cdd:pfam01276 71 AQKYAARVFGADksYFVVNGTSGS--NKTVGMAVCTPGDTILidrncHKSIHHALMLSGATPVYLEPS-RN--AYGI--I 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56480132 151 GHID-----YADLEKQAKEHK----PKMIIGGFSAYSGVVdwAKMREI---ADSIGAYLFVDMAHVA 205
Cdd:pfam01276 144 GGIPlhefqEETLKEAIAEVPdakgPRLAVITNPTYDGVL--YNAKEIvdtLHHLSDPILFDSAWVG 208
|
|
| GLY1 |
COG2008 |
Threonine aldolase [Amino acid transport and metabolism]; |
34-212 |
2.10e-03 |
|
Threonine aldolase [Amino acid transport and metabolism];
Pssm-ID: 441611 [Multi-domain] Cd Length: 333 Bit Score: 40.05 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 34 ASENYT--SPRVMQAqgsqLTNkyAEGypGKRYYGGCEYVDIVEQlaidRAKELFGAdyANVQP-HSGSQANFAVYTALL 110
Cdd:COG2008 6 RSDTVTgpHPEMLEA----MAA--ANV--GDDVYGEDPTVNRLEE----RVAELFGK--EAALFvPSGTMANQLALRAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 111 EPGDTVLgmnLAHGGHL-TH--GSPVNFSGKLYNIVPygiDATGHIDYADLEKQAKEH-----KPKMI-----IGGFSAY 177
Cdd:COG2008 72 RPGDEVI---CHETAHIyVDegGAPEALSGVKLLPVP---GEDGKLTPEDLEAAIRPGdvhfpQPGLVslentTEGGTVY 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 56480132 178 SgvvdWAKMREI---ADSIGAYLFVDMAHVA-GLVAAGV 212
Cdd:COG2008 146 P----LEELRAIaavAREHGLPLHLDGARLFnAAAALGV 180
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
71-200 |
4.03e-03 |
|
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: 39.11 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 71 VDIVEQ-LAidrakELFGADYANVQPhSGSQANFAVYTALLEPGDTVLGMNLAHGGhlTHgspvNFSGKLynIVPYGIDA 149
Cdd:cd00614 42 VDALEKkLA-----ALEGGEAALAFS-SGMAAISTVLLALLKAGDHVVASDDLYGG--TY----RLFERL--LPKLGIEV 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 56480132 150 TgHIDYADLEKQAK--EHKPKMI----IGgfSAYSGVVDWAKMREIADSIGAYLFVD 200
Cdd:cd00614 108 T-FVDPDDPEALEAaiKPETKLVyvesPT--NPTLKVVDIEAIAELAHEHGALLVVD 161
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
41-202 |
6.27e-03 |
|
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: 38.38 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 41 PRVMQAQGSQLTNKYAEGYPGKRYYGGcEYVDIVEQlAIDRAKELFGADYAN--VQPHSGSQANFAV---YTALLEPGDT 115
Cdd:pfam00266 13 QEVLDAIQEYYTDYNGNVHRGVHTLGK-EATQAYEE-AREKVAEFINAPSNDeiIFTSGTTEAINLValsLGRSLKPGDE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56480132 116 VLGMNLAHgghltHGSPV------NFSGklYNIVPYGIDATGHIDYADLEKQAKEhKPKMI-IGGFSAYSGVV-DWAKMR 187
Cdd:pfam00266 91 IVITEMEH-----HANLVpwqelaKRTG--ARVRVLPLDEDGLLDLDELEKLITP-KTKLVaITHVSNVTGTIqPVPEIG 162
|
170
....*....|....*
gi 56480132 188 EIADSIGAYLFVDMA 202
Cdd:pfam00266 163 KLAHQYGALVLVDAA 177
|
|
| |
