|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
6-416 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 802.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 6 MNIADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACEL 85
Cdd:PRK00011 4 DNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 86 FGAQYANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNFSGKLYNIIPYGID-EAGQIDYEEMEALAIE 164
Cdd:PRK00011 84 FGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDeETGLIDYDEVEKLALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 165 HKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILSNEg 244
Cdd:PRK00011 164 HKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTND- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 245 EDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARGYNIVSGSTENHLFLVDLID 324
Cdd:PRK00011 243 EELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 325 KDITGKEADAALGAANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFSEADAKELAGWICDILDNMGDESVIEATKAK 404
Cdd:PRK00011 323 KGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEE 402
|
410
....*....|..
gi 857910092 405 VLNICKRLPVYA 416
Cdd:PRK00011 403 VKELCKRFPLYK 414
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
5-416 |
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: 772.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 5 DMNIADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACE 84
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 85 LFGAQYANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNFSGKLYNIIPYGID-EAGQIDYEEMEALAI 163
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDpETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 164 EHKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAhvvtttthktLAGPRGGLILSNE 243
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGAdvvtttthktLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 244 geDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARGYNIVSGSTENHLFLVDLI 323
Cdd:COG0112 242 --ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 324 DKDITGKEADAALGAANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFSEADAKELAGWICDILDNMGDESVIEATKA 403
Cdd:COG0112 320 SKGLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVRE 399
|
410
....*....|...
gi 857910092 404 KVLNICKRLPVYA 416
Cdd:COG0112 400 EVKELCKRFPLYP 412
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
6-415 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 706.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 6 MNIADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACEL 85
Cdd:PRK13034 7 DSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 86 FGAQYANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNFSGKLYNIIPYGIDEA-GQIDYEEMEALAIE 164
Cdd:PRK13034 87 FGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLtGLIDYDEVEELAKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 165 HKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILSNEg 244
Cdd:PRK13034 167 HKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTND- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 245 EDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARGYNIVSGSTENHLFLVDLID 324
Cdd:PRK13034 246 EEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 325 KDITGKEADAALGAANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFSEADAKELAGWICDILDNMGDESVIEATKAK 404
Cdd:PRK13034 326 KGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKE 405
|
410
....*....|.
gi 857910092 405 VLNICKRLPVY 415
Cdd:PRK13034 406 VKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
9-405 |
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: 621.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 9 ADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACELFGA 88
Cdd:cd00378 1 ADVDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 89 QYANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSP--VNFSGKLYNIIPYGID-EAGQIDYEEMEALAIEH 165
Cdd:cd00378 81 EYANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDpETGLIDYDALEKMALEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 166 KPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILSNEGE 245
Cdd:cd00378 161 KPKLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 246 dLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARGYNIVSGSTENHLFLVDLIDK 325
Cdd:cd00378 241 -LAKKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 326 DITGKEADAALGAANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFSEADAKELAGWICDILDNMGDESVIEATKAKV 405
Cdd:cd00378 320 GITGKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEV 399
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
8-385 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 600.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 8 IADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACELFG 87
Cdd:pfam00464 1 LEDSDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 88 AQ----YANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNF-----SGKLYNIIPYGID-EAGQIDYEE 157
Cdd:pfam00464 81 LDpakwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDpETGYIDYDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 158 MEALAIEHKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRGG 237
Cdd:pfam00464 161 LEKNAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 238 LILSNEG------------EDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARG 305
Cdd:pfam00464 241 MIFYRKGvksvdktgkeilYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 306 YNIVSGSTENHLFLVDLIDKDITGKEADAALGAANITVNKNSVPNDpRSPFVTSGIRIGSPSITRRGFSEADAKELAGWI 385
Cdd:pfam00464 321 YKLVSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
1-414 |
3.71e-169 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 481.40 E-value: 3.71e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 1 MLKRDMNIADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIE 80
Cdd:PTZ00094 8 VLPLNQSLKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 81 RACELFGAQY----ANVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHG-----SPVNFSGKLYNIIPYGIDEAG 151
Cdd:PTZ00094 88 RALEAFGLDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 152 QIDYEEMEALAIEHKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTL 231
Cdd:PTZ00094 168 LIDYDKLEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 232 AGPRGGLILSNEG--EDLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLARGYNIV 309
Cdd:PTZ00094 248 RGPRSGLIFYRKKvkPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 310 SGSTENHLFLVDLIDKDITGKEADAALGAANITVNKNSVPNDpRSPFVTSGIRIGSPSITRRGFSEADAKELAGWI---- 385
Cdd:PTZ00094 328 TGGTDNHLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGD-KSALNPSGVRLGTPALTTRGAKEKDFKFVADFLdrav 406
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 857910092 386 --------------CDILDNMGDESVIEATKAKVLNICKRLPV 414
Cdd:PTZ00094 407 klaqeiqkqvgkklVDFKKALEKNPELQKLRQEVVEFASQFPF 449
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
17-415 |
2.39e-149 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 432.54 E-value: 2.39e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 17 AAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACELFGAQYANVQPH 96
Cdd:PRK13580 39 EAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAYVQPH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 97 SGSQANNAVYMALLNA------------------------------GDTV-LGMSLAHGGHLTHGSPVNFSGKLYNIIPY 145
Cdd:PRK13580 119 SGADANLVAFWAILAHkvespaleklgaktvndlteedwealraelGNQRlLGMSLDSGGHLTHGFRPNISGKMFHQRSY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 146 GID-EAGQIDYEEMEALAIEHKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYP---NPVPHAH 221
Cdd:PRK13580 199 GVDpDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVFTgdeDPVPHAD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 222 VVTTTTHKTLAGPRGGLILSneGEDLYKKLNSAVfPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEF 301
Cdd:PRK13580 279 IVTTTTHKTLRGPRGGLVLA--KKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAEGF 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 302 LARGYNIVSGSTENHLFLVDLIDKDITGKEADAALGAANITVNKNSVPNDPRSPFVTSGIRIGSPSITRRGFSEADAKEL 381
Cdd:PRK13580 356 LKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMDEV 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 857910092 382 AGWICDILDNMG----------------DESVIEATKAKVLNICKRLPVY 415
Cdd:PRK13580 436 AELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLY 485
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-385 |
1.10e-146 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 425.16 E-value: 1.10e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 8 IADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACELFG 87
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 88 AQYA----NVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNfSGKL------YNIIPYGIDEA-GQIDYE 156
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGYQTD-GKKIsatsiyFESMPYRLDEStGLIDYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 157 EMEALAIEHKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRG 236
Cdd:PLN03226 174 KLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 237 GLILSNEGE------------DLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMVAEFLAR 304
Cdd:PLN03226 254 GMIFFRKGPkppkgqgegavyDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 305 GYNIVSGSTENHLFLVDLIDKDITGKEADAALGAANITVNKNSVPNDpRSPFVTSGIRIGSPSITRRGFSEADAKELAGW 384
Cdd:PLN03226 334 GYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD-SSALVPGGVRIGTPAMTSRGLVEKDFEKVAEF 412
|
.
gi 857910092 385 I 385
Cdd:PLN03226 413 L 413
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
8-382 |
1.36e-97 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 303.26 E-value: 1.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 8 IADYDADLFAAIQEETLRQEEHIELIASENYTSPRVMEAQGSQLTNKYAEGYPGKRYYGGCEYVDKVETLAIERACELFG 87
Cdd:PLN02271 129 LPEADPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 88 AQYA----NVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHG--SP----VNFSGKLYNIIPYGID-EAGQIDYE 156
Cdd:PLN02271 209 LDSEkwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyyTPggkkVSGASIFFESLPYKVNpQTGYIDYD 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 157 EMEALAIEHKPKMIIGGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKTLAGPRG 236
Cdd:PLN02271 289 KLEEKALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRG 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 237 GLI-------------LSNEGE-----DLYKKLNSAVFPGGQGGPLMHVIAGKAVAFKEALEPEFKEYQARVVANAKAMV 298
Cdd:PLN02271 369 GIIfyrkgpklrkqgmLLSHGDdnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 299 AEFLARGYNIVSGSTENHLFLVDLIDKDITGKEADAALGAANITVNKNSV--PNDPRSPfvtSGIRIGSPSITRRGFSEA 376
Cdd:PLN02271 449 SALLRRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIfgDNGTISP---GGVRIGTPAMTSRGCLES 525
|
....*.
gi 857910092 377 DAKELA 382
Cdd:PLN02271 526 DFETIA 531
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-239 |
1.05e-17 |
|
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: 80.12 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 75 ETLAIERACELF--GAQYANVQPhSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGspVNFSGKLYNIIPYGIDEAGQ 152
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVA--AELAGAKPVPVPVDDAGYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 153 IDYEEMEALAIEHKPKMII--GGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNPVPHAHVVTTTTHKT 230
Cdd:cd01494 79 LDVAILEELKAKPNVALIVitPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKN 158
|
....*....
gi 857910092 231 LAGPRGGLI 239
Cdd:cd01494 159 LGGEGGGVV 167
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
65-363 |
3.63e-09 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 58.09 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 65 YGGCEYVDKVEtlaiERACELFGAQY-------ANVQPHSGSQANN-AVYMALLNAGDTVLGMSLAHGGHLT----HGSP 132
Cdd:pfam00155 35 YGPTDGHPELR----EALAKFLGRSPvlkldreAAVVFGSGAGANIeALIFLLANPGDAILVPAPTYASYIRiarlAGGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 133 VNFsgklyniIPYGIDEAGQIDYEEMEAlAIEHKPKMII--GGFSAYSQVC---DWKRMREIADKVGAYFFVDMAHvagl 207
Cdd:pfam00155 111 VVR-------YPLYDSNDFHLDFDALEA-ALKEKPKVVLhtSPHNPTGTVAtleELEKLLDLAKEHNILLLVDEAY---- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 208 iAAGVYPNPVPHAHVVTTTTHKT------------LAGPRGGLILSNEG-EDLYKKLNSAVFPGGQGGPlmhvIAGKAVA 274
Cdd:pfam00155 179 -AGFVFGSPDAVATRALLAEGPNllvvgsfskafgLAGWRVGYILGNAAvISQLRKLARPFYSSTHLQA----AAAAALS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 275 FKEALEPEFKEYQARVVANAKAMVAEFLARGYNIVSGstENHLFLVDLIDKDITGKEADAALGAANITVnknsVPNdpRS 354
Cdd:pfam00155 254 DPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPS--QAGFFLLTGLDPETAKELAQVLLEEVGVYV----TPG--SS 325
|
....*....
gi 857910092 355 PFVTSGIRI 363
Cdd:pfam00155 326 PGVPGWLRI 334
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
96-319 |
1.05e-06 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 50.42 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 96 HSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHgspVNFSGklYNIIPYGIDEAGQIDYE-EMEALAIEHKPKMIIggf 174
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG--AEVVPVPLDEEGGFLLDlELLEAAKTPKTKLLY--- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 175 saysqVC-------------DWKRMREIADKVGAYFFVDMAHvAGLiaagVYPNPVPHAHVVTTTTHK-----------T 230
Cdd:cd00609 138 -----LNnpnnptgavlseeELEELAELAKKHGILIISDEAY-AEL----VYDGEPPPALALLDAYERvivlrsfsktfG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 231 LAGPRGGLILSNEgEDLYKKLNSAVfPGGQGGPLMHVIAGKAVAFKEALEpEFKEYQARVVANAKAMVAEFLARGYNIV- 309
Cdd:cd00609 208 LPGLRIGYLIAPP-EELLERLKKLL-PYTTSGPSTLSQAAAAAALDDGEE-HLEELRERYRRRRDALLEALKELGPLVVv 284
|
250
....*....|..
gi 857910092 310 --SGSteNHLFL 319
Cdd:cd00609 285 kpSGG--FFLWL 294
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
78-216 |
1.87e-06 |
|
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: 49.17 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 78 AIERACELFGAQYANVQPHSGSQANNAVYMALLNAGDTVLGM-----SLAHGGHLTHGSPVnfsgKLYNIIPYGIDEAGQ 152
Cdd:cd00615 64 AQELAARAFGAKHTFFLVNGTSSSNKAVILAVCGPGDKILIDrnchkSVINGLVLSGAVPV----YLKPERNPYYGIAGG 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857910092 153 IDYEEMEALAIEHK-PKMIIGGFSAYSQVC-DWKRMREIADKVGAYFFVDMAHVAGLIAAGVYPNP 216
Cdd:cd00615 140 IPPETFKKALIEHPdAKAAVITNPTYYGICyNLRKIVEEAHHRGLPVLVDEAHGAHFRFHPILPSS 205
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
65-205 |
3.53e-06 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 48.37 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 65 YGGCEYVDKVEtlaiERACELFGAQYAnVQPHSGSQANNAVYMALLNAGDTVLGMSLAHGGHLTHGSPVNFSG-KLYNII 143
Cdd:pfam01212 28 YGGDPTVNRLE----DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGGvQPRPLD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857910092 144 pygIDEAGQIDYEEMEALAIEH------KPKMI-------IGGFSAYSQvcDW-KRMREIADKVGAYFFVDMAHVA 205
Cdd:pfam01212 103 ---GDEAGNMDLEDLEAAIREVgadifpPTGLIslenthnSAGGQVVSL--ENlREIAALAREHGIPVHLDGARFA 173
|
|
| DegT_DnrJ_EryC1 |
pfam01041 |
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ... |
75-211 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 75 ETLAIERA-CELFGAQYAnVQPHSGSQANNAVYMAL-LNAGDTVLGMSLahgGHLTHGSPVNFSGklYNIIPYGID-EAG 151
Cdd:pfam01041 25 YVREFERAfAAYLGVKHA-IAVSSGTAALHLALRALgVGPGDEVITPSF---TFVATANAALRLG--AKPVFVDIDpDTY 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 152 QIDYEEMEAlAIEHKPKMIIGgFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLIAAG 211
Cdd:pfam01041 99 NIDPEAIEA-AITPRTKAIIP-VHLYGQPADMDAIRAIAARHGLPVIEDAAHALGATYQG 156
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
96-208 |
3.65e-03 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 39.08 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 96 HSGSQANNAVYMALLNAGDTVLGMSLAH-----GGHLTHGSPVNFsgkLYNiipygideagqiDYEEMEALAIE----HK 166
Cdd:cd06454 68 SSGYAANDGVLSTLAGKGDLIISDSLNHasiidGIRLSGAKKRIF---KHN------------DMEDLEKLLREarrpYG 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 857910092 167 PKMII--GGFSAYSQVCDWKRMREIADKVGAYFFVDMAHVAGLI 208
Cdd:cd06454 133 KKLIVteGVYSMDGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
107-206 |
7.85e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.20 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857910092 107 MALLNAGDTVLgMSlahggHLTHGSpvnfsgklyNIIPY--------------GIDEAGQIDYEEMEALaIEHKPKMIIg 172
Cdd:COG0520 97 LGRLKPGDEIL-IT-----EMEHHS---------NIVPWqelaertgaevrviPLDEDGELDLEALEAL-LTPRTKLVA- 159
|
90 100 110
....*....|....*....|....*....|....*...
gi 857910092 173 gFSAYS----QVCDWKRMREIADKVGAYFFVDMAHVAG 206
Cdd:COG0520 160 -VTHVSnvtgTVNPVKEIAALAHAHGALVLVDGAQSVP 196
|
|
| |
