|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-412 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 749.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 1 MEELLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKA 80
Cdd:PRK00011 3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 81 LFDCDYVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFSGKLYNVVHYGVTRETQTIDYDQVEALAK 160
Cdd:PRK00011 83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 161 EHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILSTE 240
Cdd:PRK00011 163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTND 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 241 DQ-SKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTN 319
Cdd:PRK00011 243 EElAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 320 KDITGKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANE 399
Cdd:PRK00011 323 KGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEE 402
|
410
....*....|...
gi 516841597 400 VEEFAREFPLFAW 412
Cdd:PRK00011 403 VKELCKRFPLYKY 415
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
1-412 |
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: 743.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 1 MEELLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKA 80
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 81 LFDCDYVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFSGKLYNVVHYGVTRETQTIDYDQVEALAK 160
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 161 EHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILSTE 240
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 241 DQSKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTNK 320
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 321 DITGKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANEV 400
Cdd:COG0112 322 GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEV 401
|
410
....*....|..
gi 516841597 401 EEFAREFPLFAW 412
Cdd:COG0112 402 KELCKRFPLYPD 413
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
7-403 |
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: 606.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 7 QDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFDCDY 86
Cdd:cd00378 3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 87 VNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGAS--VNFSGKLYNVVHYGVTRETQTIDYDQVEALAKEHRP 164
Cdd:cd00378 83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 165 AMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILS-TEDQS 243
Cdd:cd00378 163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGELA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 244 KTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTNKDIT 323
Cdd:cd00378 243 KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 324 GKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANEVEEF 403
Cdd:cd00378 323 GKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
7-380 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 565.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 7 QDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFDCD- 85
Cdd:pfam00464 4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 86 ---YVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNF-----SGKLYNVVHYGVTRETQTIDYDQVEA 157
Cdd:pfam00464 84 akwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 158 LAKEHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMIL 237
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 238 S--------------TEDQSKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFEL 303
Cdd:pfam00464 244 YrkgvksvdktgkeiLYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516841597 304 VSGGTDNHLLMIDLTNKDITGKDAEHALDLAGITANKNTIPFEtRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAI 380
Cdd:pfam00464 324 VSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glyA |
PRK00011 |
serine hydroxymethyltransferase; Reviewed |
1-412 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 234571 Cd Length: 416 Bit Score: 749.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 1 MEELLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKA 80
Cdd:PRK00011 3 MDNLAEYDPEIADAIEQELKRQEEHIELIASENFVSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEYVDVVEQLAIDRAKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 81 LFDCDYVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFSGKLYNVVHYGVTRETQTIDYDQVEALAK 160
Cdd:PRK00011 83 LFGAEYANVQPHSGSQANAAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKLYNVVSYGVDEETGLIDYDEVEKLAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 161 EHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILSTE 240
Cdd:PRK00011 163 EHKPKLIIAGASAYSRPIDFKRFREIADEVGAYLMVDMAHIAGLVAAGVHPSPVPHADVVTTTTHKTLRGPRGGLILTND 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 241 DQ-SKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTN 319
Cdd:PRK00011 243 EElAKKINSAVFPGIQGGPLMHVIAAKAVAFKEALEPEFKEYAQQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 320 KDITGKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANE 399
Cdd:PRK00011 323 KGLTGKEAEAALEEANITVNKNAVPFDPRSPFVTSGIRIGTPAITTRGFKEAEMKEIAELIADVLDNPDDEAVIEEVKEE 402
|
410
....*....|...
gi 516841597 400 VEEFAREFPLFAW 412
Cdd:PRK00011 403 VKELCKRFPLYKY 415
|
|
| GlyA |
COG0112 |
Glycine/serine hydroxymethyltransferase [Amino acid transport and metabolism]; Glycine/serine ... |
1-412 |
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: 743.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 1 MEELLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKA 80
Cdd:COG0112 2 LSSLAEVDPEIAEAIEKELERQEEGIELIASENFVSPAVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDEVEQLAIERAKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 81 LFDCDYVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFSGKLYNVVHYGVTRETQTIDYDQVEALAK 160
Cdd:COG0112 82 LFGAEHANVQPHSGSQANLAVYFALLKPGDTILGMDLAHGGHLTHGSPVNFSGKGYNVVSYGVDPETGLIDYDEVRKLAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 161 EHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILSTE 240
Cdd:COG0112 162 EHKPKLIIAGASAYPRPIDFARFREIADEVGAYLMVDMAHIAGLVAGGLHPSPVPGADVVTTTTHKTLRGPRGGLILCNE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 241 DQSKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTNK 320
Cdd:COG0112 242 ELAKKIDSAVFPGLQGGPLMHVIAAKAVAFKEALTPEFKEYAKQVVKNAKALAEALAERGFRVVSGGTDNHLVLVDLRSK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 321 DITGKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANEV 400
Cdd:COG0112 322 GLTGKEAEKALERAGITVNKNAIPFDPRSPFVTSGIRIGTPAVTTRGMKEAEMEEIAELIADVLDNPEDEAVLAEVREEV 401
|
410
....*....|..
gi 516841597 401 EEFAREFPLFAW 412
Cdd:COG0112 402 KELCKRFPLYPD 413
|
|
| PRK13034 |
PRK13034 |
serine hydroxymethyltransferase; Reviewed |
1-410 |
0e+00 |
|
serine hydroxymethyltransferase; Reviewed
Pssm-ID: 237280 Cd Length: 416 Bit Score: 661.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 1 MEELLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKA 80
Cdd:PRK13034 6 SDSLEEYDDEVFAAINKELERQQDHLELIASENFTSPAVMEAQGSVLTNKYAEGYPGKRYYGGCEFVDEVEALAIERAKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 81 LFDCDYVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFSGKLYNVVHYGVTRETQTIDYDQVEALAK 160
Cdd:PRK13034 86 LFGCDYANVQPHSGSQANGAVYLALLKPGDTILGMSLSHGGHLTHGAKVSLSGKWYNAVQYGVDRLTGLIDYDEVEELAK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 161 EHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILST- 239
Cdd:PRK13034 166 EHKPKLIIAGFSAYPRELDFARFREIADEVGALLMVDMAHIAGLVAAGEHPNPFPHAHVVTTTTHKTLRGPRGGMILTNd 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 240 EDQSKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTN 319
Cdd:PRK13034 246 EEIAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKTYAKQVIANAQALAEVLKERGYDLVSGGTDNHLLLVDLRP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 320 KDITGKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANE 399
Cdd:PRK13034 326 KGLSGKDAEQALERAGITVNKNTVPGDTESPFVTSGIRIGTPAGTTRGFGEAEFREIANWILDVLDDLGNAALEQRVRKE 405
|
410
....*....|.
gi 516841597 400 VEEFAREFPLF 410
Cdd:PRK13034 406 VKALCSRFPIY 416
|
|
| SHMT |
cd00378 |
Serine-glycine hydroxymethyltransferase (SHMT). This family belongs to pyridoxal phosphate ... |
7-403 |
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: 606.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 7 QDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFDCDY 86
Cdd:cd00378 3 VDPEIAEIIKKENERQRETLELIASENFTSPAVMEAMGSDLTNKYAEGYPGKRYYGGCEYVDEIEDLAIERAKKLFGAEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 87 VNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGAS--VNFSGKLYNVVHYGVTRETQTIDYDQVEALAKEHRP 164
Cdd:cd00378 83 ANVQPHSGSQANLAVYFALLEPGDTIMGLDLSHGGHLTHGSFtkVSASGKLFESVPYGVDPETGLIDYDALEKMALEFKP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 165 AMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMILS-TEDQS 243
Cdd:cd00378 163 KLIVAGASAYPRPIDFKRFREIADEVGAYLLVDMAHVAGLVAGGVFPNPLPGADVVTTTTHKTLRGPRGGLILTrKGELA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 244 KTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTNKDIT 323
Cdd:cd00378 243 KKINSAVFPGLQGGPHLHVIAAKAVALKEALEPEFKAYAKQVVENAKALAEALKERGFKVVSGGTDNHLVLVDLRPKGIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 324 GKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAIDNWQNEKALEEIANEVEEF 403
Cdd:cd00378 323 GKAAEDALEEAGITVNKNTLPWDPSSPFVPSGIRIGTPAMTTRGMGEEEMEEIADFIARALKDAEDVAVAEEVRKEVAEL 402
|
|
| SHMT |
pfam00464 |
Serine hydroxymethyltransferase; |
7-380 |
0e+00 |
|
Serine hydroxymethyltransferase;
Pssm-ID: 395372 Cd Length: 399 Bit Score: 565.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 7 QDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFDCD- 85
Cdd:pfam00464 4 SDPEVFDIIKKEKERQREGIELIASENFTSRAVMEALGSVLTNKYSEGYPGKRYYGGCEHVDEIETLCQDRALEAFGLDp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 86 ---YVNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNF-----SGKLYNVVHYGVTRETQTIDYDQVEA 157
Cdd:pfam00464 84 akwGVNVQPLSGSPANLAVYTALLEPGDRIMGLDLPHGGHLTHGYPVNSkkisaSSKFFESMPYGVDPETGYIDYDQLEK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 158 LAKEHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMIL 237
Cdd:pfam00464 164 NAKLFRPKLIVAGTSAYSRLIDYARFREIADEVGAYLMVDMAHISGLVAAGVIPSPFPYADVVTTTTHKTLRGPRGGMIF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 238 S--------------TEDQSKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFEL 303
Cdd:pfam00464 244 YrkgvksvdktgkeiLYELEKKINSAVFPGLQGGPHNHVIAAKAVALKQALTPEFKEYQQQVVKNAKALAEALTERGYKL 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516841597 304 VSGGTDNHLLMIDLTNKDITGKDAEHALDLAGITANKNTIPFEtRSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAI 380
Cdd:pfam00464 324 VSGGTDNHLVLVDLRPKGLDGARAEKVLEAANITANKNTIPGD-KSAFVPSGLRLGTPALTSRGFGEADFEKVAGFI 399
|
|
| PTZ00094 |
PTZ00094 |
serine hydroxymethyltransferase; Provisional |
7-409 |
7.45e-174 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 240264 Cd Length: 452 Bit Score: 493.35 E-value: 7.45e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 7 QDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFDCDY 86
Cdd:PTZ00094 18 ADPELYELIEKEKERQIEGLELIASENFTSRAVLECLGSCFTNKYAEGLPGNRYYGGNEVVDKIENLCQKRALEAFGLDP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 87 ----VNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHG-----ASVNFSGKLYNVVHYGVTrETQTIDYDQVEA 157
Cdd:PTZ00094 98 eewgVNVQPYSGSPANFAVYTALLQPHDRIMGLDLPSGGHLTHGfytakKKVSATSIYFESLPYQVN-EKGLIDYDKLEE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 158 LAKEHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMIL 237
Cdd:PTZ00094 177 LAKAFRPKLIIAGASAYPRDIDYKRFREICDSVGAYLMADIAHTSGLVAAGVLPSPFPYADVVTTTTHKSLRGPRSGLIF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 238 STEDQSKTL----NSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLL 313
Cdd:PTZ00094 257 YRKKVKPDIenkiNEAVFPGLQGGPHNHQIAAIAVQLKEVQSPEWKEYAKQVLKNAKALAAALEKRGYDLVTGGTDNHLV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 314 MIDLTNKDITGKDAEHALDLAGITANKNTIPFETrSPFVTSGIRLGTPALTTRGMIEEDMIVVAEAITAAI--------- 384
Cdd:PTZ00094 337 LVDLRPFGITGSKMEKLLDAVNISVNKNTIPGDK-SALNPSGVRLGTPALTTRGAKEKDFKFVADFLDRAVklaqeiqkq 415
|
410 420 430
....*....|....*....|....*....|....
gi 516841597 385 ---------DNWQNEKALEEIANEVEEFAREFPL 409
Cdd:PTZ00094 416 vgkklvdfkKALEKNPELQKLRQEVVEFASQFPF 449
|
|
| PLN03226 |
PLN03226 |
serine hydroxymethyltransferase; Provisional |
4-408 |
5.12e-159 |
|
serine hydroxymethyltransferase; Provisional
Pssm-ID: 215639 Cd Length: 475 Bit Score: 456.37 E-value: 5.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 4 LLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFD 83
Cdd:PLN03226 15 LEEVDPEIADIIEKEKRRQWKGLELIASENFTSRAVMEALGSCLTNKYSEGLPGARYYGGNEYIDQIETLCQKRALEAFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 84 CDY----VNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHG----------ASVNFSGklynvVHYGVTRETQT 149
Cdd:PLN03226 95 LDPekwgVNVQPLSGSPANFAVYTALLQPHDRIMGLDLPHGGHLSHGyqtdgkkisaTSIYFES-----MPYRLDESTGL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 150 IDYDQVEALAKEHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLR 229
Cdd:PLN03226 170 IDYDKLEKKAMLFRPKLIIAGASAYPRDWDYARMRKIADKVGALLMCDMAHISGLVAAQEAASPFEYCDVVTTTTHKSLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 230 GPRGGMIL--------------STEDQSKTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANS 295
Cdd:PLN03226 250 GPRGGMIFfrkgpkppkgqgegAVYDYEDKINFAVFPGLQGGPHNHTIAALAVALKQAMTPEFKAYQKQVKANAAALANR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 296 LEESGFELVSGGTDNHLLMIDLTNKDITGKDAEHALDLAGITANKNTIPFETrSPFVTSGIRLGTPALTTRGMIEEDMIV 375
Cdd:PLN03226 330 LMSKGYKLVTGGTDNHLVLWDLRPLGLTGSRVEKVLDLAHITLNKNAVPGDS-SALVPGGVRIGTPAMTSRGLVEKDFEK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 516841597 376 VAE----AITAAID-----------------NWQNEKALEEIANEVEEFAREFP 408
Cdd:PLN03226 409 VAEflhrAVTIALKiqkehgkklkdfkkgleSNDFSKDIEALRAEVEEFATSFP 462
|
|
| PRK13580 |
PRK13580 |
glycine hydroxymethyltransferase; |
1-410 |
3.39e-148 |
|
glycine hydroxymethyltransferase;
Pssm-ID: 184161 Cd Length: 493 Bit Score: 429.46 E-value: 3.39e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 1 MEELLIQDPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKA 80
Cdd:PRK13580 27 LDVILHVEPRIAEAIRQELADQRSSLKLIASENYSSLAVQLAMGNLLTDKYAEGTPGHRFYAGCQNVDTVEWEAAEHAKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 81 LFDCDYVNVQPHSGSQANMAVY---------------FGYCKPGD----------------TILTMELSHGGHLTHGASV 129
Cdd:PRK13580 107 LFGAEHAYVQPHSGADANLVAFwailahkvespalekLGAKTVNDlteedwealraelgnqRLLGMSLDSGGHLTHGFRP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 130 NFSGKLYNVVHYGVTRETQTIDYDQVEALAKEHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAG- 208
Cdd:PRK13580 187 NISGKMFHQRSYGVDPDTGLLDYDEIAALAREFKPLILVAGYSAYPRRVNFAKLREIADEVGAVLMVDMAHFAGLVAGKv 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 209 ----EHPscIPHAHITTTTTHKTLRGPRGGMILSTEDQSKTLNSQIfPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQ 284
Cdd:PRK13580 267 ftgdEDP--VPHADIVTTTTHKTLRGPRGGLVLAKKEYADAVDKGC-PLVLGGPLPHVMAAKAVALAEARTPEFQKYAQQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 285 VVKNAKVLANSLEESGFELVSGGTDNHLLMIDLTNKDITGKDAEHALDLAGITANKNTIPFETRSPFVTSGIRLGTPALT 364
Cdd:PRK13580 344 VVDNARALAEGFLKRGARLVTGGTDNHLVLIDVTSFGLTGRQAESALLDAGIVTNRNSIPSDPNGAWYTSGIRLGTPALT 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516841597 365 TRGMIEEDMIVVAEAITAAIDNWQ----------------NEKALEEIANEVEEFAREFPLF 410
Cdd:PRK13580 424 TLGMGSDEMDEVAELIVKVLSNTTpgttaegapskakyelDEGVAQEVRARVAELLARFPLY 485
|
|
| PLN02271 |
PLN02271 |
serine hydroxymethyltransferase |
8-407 |
3.57e-104 |
|
serine hydroxymethyltransferase
Pssm-ID: 215153 Cd Length: 586 Bit Score: 320.21 E-value: 3.57e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 8 DPEVAAAIAAEADRQVSKLELIASENFVSTAVRQAQGSIMTHKYAEGYPHKRYYGGCEFVDIAEDIARDRAKALFDCDY- 86
Cdd:PLN02271 133 DPDIHELMEKEKQRQFKGIELIASENFVCRAVMEALGSHLTNKYSEGMPGARYYTGNQYIDQIERLCCERALAAFGLDSe 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 87 ---VNVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHG------ASVNFSGKLYNVVHYGVTRETQTIDYDQVEA 157
Cdd:PLN02271 213 kwgVNVQPYSCTSANFAVYTGLLLPGDRIMGLDSPSGGHMSHGyytpggKKVSGASIFFESLPYKVNPQTGYIDYDKLEE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 158 LAKEHRPAMIVAGASAYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTLRGPRGGMI- 236
Cdd:PLN02271 293 KALDFRPKILICGGSSYPREWDYARFRQIADKCGAVLMCDMAHISGLVAAKECVNPFDYCDIVTSTTHKSLRGPRGGIIf 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 237 -------------LSTEDQS------KTLNSQIFPGIQGGPLMHVIAAKAAAFGEALREGFVEYQKQVVKNAKVLANSLE 297
Cdd:PLN02271 373 yrkgpklrkqgmlLSHGDDNshydfeEKINFAVFPSLQGGPHNNHIAALAIALKQVATPEYKAYMQQVKKNAQALASALL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 298 ESGFELVSGGTDNHLLMIDLTNKDITGKDAEHALDLAGITANKNTIpFETRSPFVTSGIRLGTPALTTRGMIEEDMIVVA 377
Cdd:PLN02271 453 RRKCRLVTGGTDNHLLLWDLTTLGLTGKNYEKVCEMCHITLNKTAI-FGDNGTISPGGVRIGTPAMTSRGCLESDFETIA 531
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 516841597 378 E------AITAAI------------DNWQNEKALEEIANEVEEFAREF 407
Cdd:PLN02271 532 DfllraaQIASAVqrehgklqkeflKGLQNNKDIVELRNRVEAFASQF 579
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
74-236 |
2.68e-18 |
|
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: 81.66 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 74 ARDRAKALFD--CDYVNVQPhSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFsgklYNVVHYGVTRETQ-TI 150
Cdd:cd01494 5 LEEKLARLLQpgNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAG----AKPVPVPVDDAGYgGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 151 DYDQVEALAKEHRPAMIVAGASAYPR--IIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCIPHAHITTTTTHKTL 228
Cdd:cd01494 80 DVAILEELKAKPNVALIVITPNTTSGgvLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEGGADVVTFSLHKNL 159
|
....*...
gi 516841597 229 RGPRGGMI 236
Cdd:cd01494 160 GGEGGGVV 167
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
76-202 |
3.78e-04 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 42.20 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 76 DRAKALFDCDYVnVQPHSGSQANMAVYFGYCKPGDTILTMELSHGGHLTHGASVNFSG-KLYNVvhygVTRETQTIDYDQ 154
Cdd:pfam01212 39 DRVAELFGKEAA-LFVPSGTAANQLALMAHCQRGDEVICGEPAHIHFDETGGHAELGGvQPRPL----DGDEAGNMDLED 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516841597 155 VEALAKEH------RPAMIV-------AGASAYPrIIDFARFRAIADEVGAKLMVDMAHIA 202
Cdd:pfam01212 114 LEAAIREVgadifpPTGLISlenthnsAGGQVVS-LENLREIAALAREHGIPVHLDGARFA 173
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
78-380 |
4.15e-04 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 42.29 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 78 AKALFDCDYV------NVQPHSGSQANM-AVYFGYCKPGDTILTMELSHGGHLThgaSVNFSG-KLYnVVHYgVTRETQT 149
Cdd:pfam00155 49 AKFLGRSPVLkldreaAVVFGSGAGANIeALIFLLANPGDAILVPAPTYASYIR---IARLAGgEVV-RYPL-YDSNDFH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 150 IDYDQVEALAKEHRPAMIVAGAS----AYPRIIDFARFRAIADEVGAKLMVDMAHIAGLIAAGEHPSCI------PHAHI 219
Cdd:pfam00155 124 LDFDALEAALKEKPKVVLHTSPHnptgTVATLEELEKLLDLAKEHNILLLVDEAYAGFVFGSPDAVATRallaegPNLLV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 220 TTTTThKT--LRGPRGGMILSTEDQSKTLNSQIFPGIQGGPLMHVIAAKAAafGEALREGFV-EYQKQVVKNAKVLANSL 296
Cdd:pfam00155 204 VGSFS-KAfgLAGWRVGYILGNAAVISQLRKLARPFYSSTHLQAAAAAALS--DPLLVASELeEMRQRIKERRDYLRDGL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 297 EESGFELVsgGTDNHLLMidltnkdITGKDAEHALDLAGITANK---NTIPFetRSPFVTSGIRLgTPALTTRGMIEEdm 373
Cdd:pfam00155 281 QAAGLSVL--PSQAGFFL-------LTGLDPETAKELAQVLLEEvgvYVTPG--SSPGVPGWLRI-TVAGGTEEELEE-- 346
|
....*..
gi 516841597 374 ivVAEAI 380
Cdd:pfam00155 347 --LLEAI 351
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
92-380 |
5.36e-04 |
|
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: 41.94 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 92 HSGSQANMAVYFGYCKPGDTILTMELSHGGHLthgASVNFSGklYNVVHYGVTRETQTIDYDQVEALAKEHRPAMIVAGA 171
Cdd:cd00609 66 NGAQEALSLLLRALLNPGDEVLVPDPTYPGYE---AAARLAG--AEVVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 172 SAYP--RIIDFARFRAIAD---EVGAKLMVDMAHiAGLIAAGEHPSCIPHAHITTTTTH-----KTLRGP--RGGMILST 239
Cdd:cd00609 141 PNNPtgAVLSEEELEELAElakKHGILIISDEAY-AELVYDGEPPPALALLDAYERVIVlrsfsKTFGLPglRIGYLIAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 240 EDQSKTLNSQIFPGIQGGPLMHVIAAKAaafgEALREG---FVEYQKQVVKNAKVLANSLEESGFELVSGGTDNHLLMID 316
Cdd:cd00609 220 PEELLERLKKLLPYTTSGPSTLSQAAAA----AALDDGeehLEELRERYRRRRDALLEALKELGPLVVVKPSGGFFLWLD 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516841597 317 LtNKDITGKDAEHALDLAGITANKNTIPFETRSPFvtsgIRLGTpalttrGMIEEDMIVVAEAI 380
Cdd:cd00609 296 L-PEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGF----VRLSF------ATPEEELEEALERL 348
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
92-210 |
1.89e-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: 40.24 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516841597 92 HSGSQANMAVYFGYCKPGDTILTMELSHgghlthgASVNFSGKLYNVVhygvTRETQTIDYDQVEALAKE----HRPAMI 167
Cdd:cd06454 68 SSGYAANDGVLSTLAGKGDLIISDSLNH-------ASIIDGIRLSGAK----KRIFKHNDMEDLEKLLREarrpYGKKLI 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516841597 168 VA-------GASA-YPRIIDfarfraIADEVGAKLMVDMAHIAGLIaaGEH 210
Cdd:cd06454 137 VTegvysmdGDIApLPELVD------LAKKYGAILFVDEAHSVGVY--GPH 179
|
|
| |
