|
Name |
Accession |
Description |
Interval |
E-value |
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
8-414 |
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: 812.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 8 VKPIDPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFG 87
Cdd:COG0112 5 LAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 88 AEHANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVNISGKYFNIVDYGVNRDTESIDYEQLREVALKAR 167
Cdd:COG0112 85 AEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLALEHK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 168 PQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILCRQEWA 247
Cdd:COG0112 165 PKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNEELA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 248 TKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLVDLRPKGFT 327
Cdd:COG0112 245 KKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 328 GRDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEEAKGIVKGL 407
Cdd:COG0112 325 GKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKEL 404
|
....*..
gi 2544104406 408 CDKYPLY 414
Cdd:COG0112 405 CKRFPLY 411
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-414 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 806.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 1 MDYIQKYvkpiDPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARD 80
Cdd:PRK00011 3 MDNLAEY----DPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 81 RVKKIFGAEHANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVNISGKYFNIVDYGVNRDTESIDYEQLR 160
Cdd:PRK00011 79 RAKELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 161 EVALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFI 240
Cdd:PRK00011 159 KLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 241 LCR-QEWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLV 319
Cdd:PRK00011 239 LTNdEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 320 DLRPKGFTGRDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEE 399
Cdd:PRK00011 319 DLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEE 398
|
410
....*....|....*
gi 2544104406 400 AKGIVKGLCDKYPLY 414
Cdd:PRK00011 399 VKEEVKELCKRFPLY 413
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
12-407 |
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: 647.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 12 DPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAEHA 91
Cdd:cd00378 4 DPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 92 NVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGS--KVNISGKYFNIVDYGVNRDTESIDYEQLREVALKARPQ 169
Cdd:cd00378 84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 170 MIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILCRQ-EWAT 248
Cdd:cd00378 164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKgELAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 249 KIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLVDLRPKGFTG 328
Cdd:cd00378 244 KINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITG 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544104406 329 RDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEEAKGIVKGL 407
Cdd:cd00378 324 KAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
12-381 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 614.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 12 DPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAE-- 89
Cdd:pfam00464 5 DPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDpa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 90 --HANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVN-----ISGKYFNIVDYGVNRDTESIDYEQLREV 162
Cdd:pfam00464 85 kwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNskkisASSKFFESMPYGVDPETGYIDYDQLEKN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 163 ALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILC 242
Cdd:pfam00464 165 AKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 243 RQ--------------EWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLV 308
Cdd:pfam00464 245 RKgvksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKLV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2544104406 309 SGGTDNHLMLVDLRPKGFTGRDAEAILEAVNITVNKNAIPFDpEKPTITSGIRVGTPAVTSRGLKGEDMRELA 381
Cdd:pfam00464 325 SGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVA 396
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
8-414 |
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: 812.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 8 VKPIDPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFG 87
Cdd:COG0112 5 LAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKELFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 88 AEHANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVNISGKYFNIVDYGVNRDTESIDYEQLREVALKAR 167
Cdd:COG0112 85 AEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLALEHK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 168 PQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILCRQEWA 247
Cdd:COG0112 165 PKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNEELA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 248 TKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLVDLRPKGFT 327
Cdd:COG0112 245 KKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSKGLT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 328 GRDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEEAKGIVKGL 407
Cdd:COG0112 325 GKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEVKEL 404
|
....*..
gi 2544104406 408 CDKYPLY 414
Cdd:COG0112 405 CKRFPLY 411
|
|
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-414 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 806.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 1 MDYIQKYvkpiDPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARD 80
Cdd:PRK00011 3 MDNLAEY----DPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 81 RVKKIFGAEHANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVNISGKYFNIVDYGVNRDTESIDYEQLR 160
Cdd:PRK00011 79 RAKELFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 161 EVALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFI 240
Cdd:PRK00011 159 KLALEHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 241 LCR-QEWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLV 319
Cdd:PRK00011 239 LTNdEELAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 320 DLRPKGFTGRDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEE 399
Cdd:PRK00011 319 DLRSKGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEE 398
|
410
....*....|....*
gi 2544104406 400 AKGIVKGLCDKYPLY 414
Cdd:PRK00011 399 VKEEVKELCKRFPLY 413
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
12-414 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 699.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 12 DPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAEHA 91
Cdd:PRK13034 13 DDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQLFGCDYA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 92 NVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVNISGKYFNIVDYGVNRDTESIDYEQLREVALKARPQMI 171
Cdd:PRK13034 93 NVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAKEHKPKLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 172 VAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILCR-QEWATKI 250
Cdd:PRK13034 173 IAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNdEEIAKKI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 251 DKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLVDLRPKGFTGRD 330
Cdd:PRK13034 253 NSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRPKGLSGKD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 331 AEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEEAKGIVKGLCDK 410
Cdd:PRK13034 333 AEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKEVKALCSR 412
|
....
gi 2544104406 411 YPLY 414
Cdd:PRK13034 413 FPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
12-407 |
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: 647.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 12 DPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAEHA 91
Cdd:cd00378 4 DPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEYA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 92 NVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGS--KVNISGKYFNIVDYGVNRDTESIDYEQLREVALKARPQ 169
Cdd:cd00378 84 NVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSftKVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 170 MIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILCRQ-EWAT 248
Cdd:cd00378 164 LIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTRKgELAK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 249 KIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDNHLMLVDLRPKGFTG 328
Cdd:cd00378 244 KINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGITG 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544104406 329 RDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMRELARAMTLVLDKPGSEEVKEEAKGIVKGL 407
Cdd:cd00378 324 KAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
12-381 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 614.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 12 DPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAE-- 89
Cdd:pfam00464 5 DPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDpa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 90 --HANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHGSKVN-----ISGKYFNIVDYGVNRDTESIDYEQLREV 162
Cdd:pfam00464 85 kwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNskkisASSKFFESMPYGVDPETGYIDYDQLEKN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 163 ALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFILC 242
Cdd:pfam00464 165 AKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIFY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 243 RQ--------------EWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLV 308
Cdd:pfam00464 245 RKgvksvdktgkeilyELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKLV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2544104406 309 SGGTDNHLMLVDLRPKGFTGRDAEAILEAVNITVNKNAIPFDpEKPTITSGIRVGTPAVTSRGLKGEDMRELA 381
Cdd:pfam00464 325 SGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVA 396
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
8-407 |
0e+00 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 542.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 8 VKPIDPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFG 87
Cdd:PTZ00094 15 LKEADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 88 AEH----ANVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHG-----SKVNISGKYFNIVDYGVNRDTEsIDYEQ 158
Cdd:PTZ00094 95 LDPeewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVNEKGL-IDYDK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 159 LREVALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGG 238
Cdd:PTZ00094 174 LEELAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 239 FILCR----QEWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQGLRLVSGGTDN 314
Cdd:PTZ00094 254 LIFYRkkvkPDIENKINEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 315 HLMLVDLRPKGFTGRDAEAILEAVNITVNKNAIPFDPEKPtITSGIRVGTPAVTSRGLKGEDMRELA----RAMTLVLDK 390
Cdd:PTZ00094 334 HLVLVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDKSAL-NPSGVRLGTPALTTRGAKEKDFKFVAdfldRAVKLAQEI 412
|
410
....*....|....*..
gi 2544104406 391 pgSEEVKEEAKGIVKGL 407
Cdd:PTZ00094 413 --QKQVGKKLVDFKKAL 427
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
13-414 |
0e+00 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 518.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 13 PEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAEHAN 92
Cdd:PRK13580 35 PRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKELFGAEHAY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 93 VQPHSGAQANTAVYFAAL-----QPG--------------------------QTIMGMNLNHGGHLTHGSKVNISGKYFN 141
Cdd:PRK13580 115 VQPHSGADANLVAFWAILahkveSPAleklgaktvndlteedwealraelgnQRLLGMSLDSGGHLTHGFRPNISGKMFH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 142 IVDYGVNRDTESIDYEQLREVALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGL---HPSPV 218
Cdd:PRK13580 195 QRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKVftgDEDPV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 219 PYADFVSSTTHKTLRGPRGGFILCRQEWATKIDKAVfPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAK 298
Cdd:PRK13580 275 PHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQVVDNARALAE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 299 ALLEQGLRLVSGGTDNHLMLVDLRPKGFTGRDAEAILEAVNITVNKNAIPFDPEKPTITSGIRVGTPAVTSRGLKGEDMR 378
Cdd:PRK13580 354 GFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALTTLGMGSDEMD 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2544104406 379 ELARAMTLVLD--KPG--------------SEEVKEEAKGIVKGLCDKYPLY 414
Cdd:PRK13580 434 EVAELIVKVLSntTPGttaegapskakyelDEGVAQEVRARVAELLARFPLY 485
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
8-405 |
7.96e-179 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 506.83 E-value: 7.96e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 8 VKPIDPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFG 87
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 88 AEHA----NVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHG---SKVNISGK--YFNIVDYGVNRDTESIDYEQ 158
Cdd:PLN03226 95 LDPEkwgvNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtDGKKISATsiYFESMPYRLDESTGLIDYDK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 159 LREVALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGG 238
Cdd:PLN03226 175 LEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLRGPRGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 239 FILCR---------QEWAT-----KIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALLEQG 304
Cdd:PLN03226 255 MIFFRkgpkppkgqGEGAVydyedKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANRLMSKG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 305 LRLVSGGTDNHLMLVDLRPKGFTGRDAEAILEAVNITVNKNAIPFDpekptiTS-----GIRVGTPAVTSRGLKGEDMRE 379
Cdd:PLN03226 335 YKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGD------SSalvpgGVRIGTPAMTSRGLVEKDFEK 408
|
410 420 430
....*....|....*....|....*....|
gi 2544104406 380 LA----RAMTLVLDkpgseeVKEEAKGIVK 405
Cdd:PLN03226 409 VAeflhRAVTIALK------IQKEHGKKLK 432
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
12-381 |
9.75e-134 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 396.10 E-value: 9.75e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 12 DPEVAEAIEKEEARQNNKLELIASENFVSRAVMAAQGSVMTNKYAEGLPGARYYGGCEYVDIVEELARDRVKKIFGAEHA 91
Cdd:PLN02271 133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 92 ----NVQPHSGAQANTAVYFAALQPGQTIMGMNLNHGGHLTHG------SKVNISGKYFNIVDYGVNRDTESIDYEQLRE 161
Cdd:PLN02271 213 kwgvNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpggKKVSGASIFFESLPYKVNPQTGYIDYDKLEE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 162 VALKARPQMIVAGASAYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTHKTLRGPRGGFIL 241
Cdd:PLN02271 293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIF 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 242 CRQ--------------------EWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALMPEFKAYQQAIVNNAATLAKALL 301
Cdd:PLN02271 373 YRKgpklrkqgmllshgddnshyDFEEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 302 EQGLRLVSGGTDNHLMLVDLRPKGFTGRDAEAILEAVNITVNKNAIPFDpeKPTIT-SGIRVGTPAVTSRGLKGEDMREL 380
Cdd:PLN02271 453 RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAIFGD--NGTISpGGVRIGTPAMTSRGCLESDFETI 530
|
.
gi 2544104406 381 A 381
Cdd:PLN02271 531 A 531
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
75-240 |
4.80e-22 |
|
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: 92.06 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 75 EELARDRVKKIF--GAEHANVQPhSGAQANTAVYFAALQPGQTIMGMNLNHGGHltHGSKVNISGkyFNIVDYGVNRDTE 152
Cdd:cd01494 2 LEELEEKLARLLqpGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSR--YWVAAELAG--AKPVPVPVDDAGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 153 -SIDYEQLREVALKARPQMIVAGASAYPR--ILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSPVPYADFVSSTTH 229
Cdd:cd01494 77 gGLDVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|.
gi 2544104406 230 KTLRGPRGGFI 240
Cdd:cd01494 157 KNLGGEGGGVV 167
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
62-383 |
7.70e-15 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 75.42 E-value: 7.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 62 ARYYGGCEYVDIVEElardrvkkifgaehANVQPHSGAQAN-TAVYFAALQPGQTIMGMNLNHGGHLT----HGSKVnis 136
Cdd:pfam00155 49 AKFLGRSPVLKLDRE--------------AAVVFGSGAGANiEALIFLLANPGDAILVPAPTYASYIRiarlAGGEV--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 137 gKYFNIVDygvnRDTESIDYEQLREvALKARPQMIVAG------ASAYPRiLDFQKFREIADEAGALLFVDMAHIAGLVA 210
Cdd:pfam00155 112 -VRYPLYD----SNDFHLDFDALEA-ALKEKPKVVLHTsphnptGTVATL-EELEKLLDLAKEHNILLLVDEAYAGFVFG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 211 AGLHPSPVPYAD-----FVSSTTHKT--LRGPRGGFILCRQEWATKIDKAVFPGIQGGPLMHvIAAKAVCFKEALMPEFK 283
Cdd:pfam00155 185 SPDAVATRALLAegpnlLVVGSFSKAfgLAGWRVGYILGNAAVISQLRKLARPFYSSTHLQA-AAAAALSDPLLVASELE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 284 AYQQAIVNNAATLAKALLEQGLRLVSGGTdNHLMLVDLRPKGFTgRDAEAILEAVNItvnkNAIPFDPekPTITSGIRVG 363
Cdd:pfam00155 264 EMRQRIKERRDYLRDGLQAAGLSVLPSQA-GFFLLTGLDPETAK-ELAQVLLEEVGV----YVTPGSS--PGVPGWLRIT 335
|
330 340
....*....|....*....|
gi 2544104406 364 TPAVTSrglkgEDMRELARA 383
Cdd:pfam00155 336 VAGGTE-----EELEELLEA 350
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
63-384 |
2.50e-07 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 52.34 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 63 RYYGGCEYVDIVEELA-RDRVKKIFGAEHANVQPHSGA-QANTAVYFAALQPGQTIMGMNLNHGGHLTHgskVNISGkyF 140
Cdd:cd00609 31 GYYPDPGLPELREAIAeWLGRRGGVDVPPEEIVVTNGAqEALSLLLRALLNPGDEVLVPDPTYPGYEAA---ARLAG--A 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 141 NIVDYGVNRDTESIDYEQLREVALKARPQMIVAGASAYP--RILDFQKFREIADEA---GALLFVDMAHiAGLVAAGLHP 215
Cdd:cd00609 106 EVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPtgAVLSEEELEELAELAkkhGILIISDEAY-AELVYDGEPP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 216 SPVPYAD-----FVSSTTHKTLRGP--RGGFILCRQEWATKIDKAVFPGIQGGPLMHVIAAKAVCFKEALmPEFKAYQQA 288
Cdd:cd00609 185 PALALLDayervIVLRSFSKTFGLPglRIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAAAALDDGE-EHLEELRER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 289 IVNNAATLAKALLEQGLRLVSGGTDNHLMLVDLrPKGFTGRDAEAILEAVNITVNKNAIPFDPEKptitSGIRVGTpavt 368
Cdd:cd00609 264 YRRRRDALLEALKELGPLVVVKPSGGFFLWLDL-PEGDDEEFLERLLLEAGVVVRPGSAFGEGGE----GFVRLSF---- 334
|
330
....*....|....*.
gi 2544104406 369 srGLKGEDMRELARAM 384
Cdd:cd00609 335 --ATPEEELEEALERL 348
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
75-245 |
3.94e-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: 48.33 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 75 EELArdrvkKIFGAEHANVQpHSGAQANTAVYFAALQPGQTIMGMNLNHG----GHLTHGSKVNIsgkyFNivdygvNRD 150
Cdd:cd06454 53 EELA-----EFHGKEAALVF-SSGYAANDGVLSTLAGKGDLIISDSLNHAsiidGIRLSGAKKRI----FK------HND 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 151 TESIDyEQLREVALKARPQMIVA-------GASAyprilDFQKFREIADEAGALLFVDMAH--------IAGLVAAGLHP 215
Cdd:cd06454 117 MEDLE-KLLREARRPYGKKLIVTegvysmdGDIA-----PLPELVDLAKKYGAILFVDEAHsvgvygphGRGVEEFGGLT 190
|
170 180 190
....*....|....*....|....*....|
gi 2544104406 216 SPVpyaDFVSSTTHKTLrGPRGGFILCRQE 245
Cdd:cd06454 191 DDV---DIIMGTLGKAF-GAVGGYIAGSKE 216
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
76-246 |
1.79e-05 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 46.67 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 76 ELARDRVKKIFGAEHanvqPH-----SGAQA--NTAVY-FAALQPGQTIMGMNLNHGGHLT--------HGSKVnisgKY 139
Cdd:COG0520 62 EAAREKVARFIGAAS----PDeiiftRGTTEaiNLVAYgLGRLKPGDEILITEMEHHSNIVpwqelaerTGAEV----RV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 140 FNIVDYGVnrdtesIDYEQLREvALKARPQMI-VAGAS-AYPRILDFQKFREIADEAGALLFVDMAHIAGLVAAGLHPSp 217
Cdd:COG0520 134 IPLDEDGE------LDLEALEA-LLTPRTKLVaVTHVSnVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQAL- 205
|
170 180 190
....*....|....*....|....*....|
gi 2544104406 218 vpYADFVSSTTHKtLRGPRG-GFILCRQEW 246
Cdd:COG0520 206 --GCDFYAFSGHK-LYGPTGiGVLYGKREL 232
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
72-245 |
4.96e-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: 38.77 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 72 DIVEElARDRVKKIFGAEHAN--VQPHSGAQANTAV---YFAALQPGQTIMGMNLNHGGHL--------THGSKVnisgK 138
Cdd:pfam00266 43 QAYEE-AREKVAEFINAPSNDeiIFTSGTTEAINLValsLGRSLKPGDEIVITEMEHHANLvpwqelakRTGARV----R 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544104406 139 YFNIVDYGvnrdteSIDYEQLREvALKARPQM--IVAGASAYPRILDFQKFREIADEAGALLFVDMAHiaglvAAGLHPS 216
Cdd:pfam00266 118 VLPLDEDG------LLDLDELEK-LITPKTKLvaITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQ-----AIGHRPI 185
|
170 180 190
....*....|....*....|....*....|..
gi 2544104406 217 PVPY--ADFVSSTTHKTLrGPRG-GFILCRQE 245
Cdd:pfam00266 186 DVQKlgVDFLAFSGHKLY-GPTGiGVLYGRRD 216
|
|
| |
