|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05355 |
PRK05355 |
3-phosphoserine/phosphohydroxythreonine transaminase; |
1-362 |
0e+00 |
|
3-phosphoserine/phosphohydroxythreonine transaminase;
Pssm-ID: 235428 Cd Length: 360 Bit Score: 723.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 1 MAQVFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQF 80
Cdd:PRK05355 1 MMRVYNFSAGPAMLPEEVLEQAQQELLDWNGSGMSVMEISHRSKEFEAVAEEAEADLRELLNIPDNYKVLFLQGGASLQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 81 AGVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKiTVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAID 160
Cdd:PRK05355 81 AMVPMNLLGGGKKADYVDTGSWSKKAIKEAKKYGEVNVAASS-EDDGFTYIPPLDEWQLSDDAAYVHYTSNETIDGTEFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 161 ETPDFGPeVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNT 240
Cdd:PRK05355 160 ELPDTGD-VPLVADMSSDILSRPIDVSKFGLIYAGAQKNIGPAGLTIVIVREDLLGRALPSIPSMLDYKTHADNDSMYNT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 241 PPTFAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAA 320
Cdd:PRK05355 239 PPTFAIYLAGLVFKWLKEQGGVAAMEKRNQEKAALLYDAIDSSDFYRNPVAPEDRSRMNVPFTLADEELDKKFLAEAKAA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446001735 321 GLHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRHG 362
Cdd:PRK05355 319 GLVGLKGHRSVGGMRASIYNAMPLEGVQALVDFMKEFERRHG 360
|
|
| SerC |
COG1932 |
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ... |
2-361 |
0e+00 |
|
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]; Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 441535 Cd Length: 358 Bit Score: 640.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 2 AQVFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFA 81
Cdd:COG1932 1 MRVYNFSAGPAKLPEEVLEQAQAELLDWNGSGMSVMEMSHRSKPFKAIVEEAEADLRELLGIPDGYEVLFLQGGATAQFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 82 GVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKITvDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDE 161
Cdd:COG1932 81 MVPMNLLRGGKKADYLVTGEWSKKAIKEAKKYGEVNVVASSED-DNFGYIPKPEEWQLSPDADYVHYTSNETITGVEFHE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 162 TPDFGpEVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTP 241
Cdd:COG1932 160 LPDVG-DVPLVADMSSDILSRPVDVSKFGLIYAGAQKNIGPAGLTVVIVRPDLLGRAERAIPSMLDYKTHADNDSMYNTP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 242 PTFAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAG 321
Cdd:COG1932 239 PTFAIYLAGLVLKWLKEQGGLAAMEKRNAEKAALLYDWIDASDFYTNPVDPEDRSRMNVTFDLADEELDAAFLAEAKAAG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446001735 322 LHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRH 361
Cdd:COG1932 319 LVGLKGHRSVGGMRASIYNAMPLEGVEALVDFMDEFERRH 358
|
|
| PSAT_like |
cd00611 |
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ... |
5-359 |
0e+00 |
|
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine.
Pssm-ID: 99736 [Multi-domain] Cd Length: 355 Bit Score: 599.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 5 FNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVP 84
Cdd:cd00611 1 INFSAGPAALPEEVLEQAQKELLDFNGLGMSVMEMSHRSKDFEAIVNEAESDLRELLNIPDNYKVLFLQGGATGQFAAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 85 LNLLGDKTTADYVDAGYWAASAIKEAKKYC-APQIIDAKITvDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETP 163
Cdd:cd00611 81 LNLLGDKGTADYVVTGAWSAKAAKEAKRYGgVVVIVAAKEE-GKYTKIPDVETWDLAPDAAYVHYCSNETIHGVEFDEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 164 DFGPeVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPT 243
Cdd:cd00611 160 DTGG-VPLVADMSSNILSRPIDVSKFGVIYAGAQKNLGPAGVTVVIVRKDLLGKARKITPSMLNYKTHADNNSLYNTPPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 244 FAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNS-DFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAGL 322
Cdd:cd00611 239 FAIYMMGLVLKWLKEQGGVEAMEKRNRQKAQLLYDTIDNSnGFYRGPVDKRARSRMNVPFRLGKEELEKEFLKEAEAAGM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 446001735 323 HALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFER 359
Cdd:cd00611 319 IGLKGHRSVGGIRASIYNALSLEGVQALADFMKEFQK 355
|
|
| serC_1 |
TIGR01364 |
phosphoserine aminotransferase; This model represents the common form of the phosphoserine ... |
12-361 |
0e+00 |
|
phosphoserine aminotransferase; This model represents the common form of the phosphoserine aminotransferase SerC. The phosphoserine aminotransferase of the archaeon Methanosarcina barkeri and putative phosphoserine aminotransferase of Mycobacterium tuberculosis are represented by separate models. All are members of the class V aminotransferases (pfam00266). [Amino acid biosynthesis, Serine family]
Pssm-ID: 130431 Cd Length: 349 Bit Score: 548.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 12 AMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVPLNLLGDK 91
Cdd:TIGR01364 1 AALPEEVLEQAQKELLNFNGTGMSVMEISHRSKEFEAVANEAESDLRELLNIPDNYEVLFLQGGATGQFAAVPLNLLAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 92 TTADYVDAGYWAASAIKEAKKYCAPqIIDAKITVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETPDFGPEVVV 171
Cdd:TIGR01364 81 KVADYIVTGAWSKKAAKEAKKYGVV-NVVASGKEGNYTKIPDPSTWEISEDAAYVHYCANETIHGVEFRELPDVKNAPLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 172 tADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPTFAWYLSGL 251
Cdd:TIGR01364 160 -ADMSSNILSRPIDVSKFGLIYAGAQKNIGPAGLTVVIVRKDLLGRASRITPSMLNYKIHAENDSMYNTPPTFAIYVSGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 252 VFKWLKAQGGVAAMHKINQQKAELLYGVIDNS-DFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAGLHALKGHRV 330
Cdd:TIGR01364 239 VFKWLKEQGGVKAIEKRNQAKAQLLYDTIDNSnGFYRNPVDPRNRSRMNVVFTLGNEELEKRFLKEAEERGLVSLKGHRS 318
|
330 340 350
....*....|....*....|....*....|.
gi 446001735 331 VGGMRASIYNAMPIEGVKALTDFMIDFERRH 361
Cdd:TIGR01364 319 VGGMRASIYNAMPLEGVQALVDFMKEFQKKH 349
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
4-350 |
1.67e-89 |
|
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: 273.35 E-value: 1.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 4 VFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSvmEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRgQFAGV 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHR--GVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTE-AINLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 84 PLNL---LGDKTTADYVDAGYWAAS-AIKEAKKYCAPQIIDAKITVDGKRAVKPMrEWQLSDNAAYLHYCPNETIDGIaI 159
Cdd:pfam00266 78 ALSLgrsLKPGDEIVITEMEHHANLvPWQELAKRTGARVRVLPLDEDGLLDLDEL-EKLITPKTKLVAITHVSNVTGT-I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 160 DETPDFGPE-----VVVTADFSSTILSAPLDVSRYGV--IYAGAQKNIGPAGLTLVIVREDLLGKAHE--------SCPS 224
Cdd:pfam00266 156 QPVPEIGKLahqygALVLVDAAQAIGHRPIDVQKLGVdfLAFSGHKLYGPTGIGVLYGRRDLLEKMPPllggggmiETVS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 225 iLDYTVLNDNDSMFN--TPPTFAWYLSGLVFKWLKAqGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPF 302
Cdd:pfam00266 236 -LQESTFADAPWKFEagTPNIAGIIGLGAALEYLSE-IGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNF 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446001735 303 QLADNALDKVFLEESFAA---GLH----ALKGHRVVGGMRASIYNAMPIEGVKAL 350
Cdd:pfam00266 314 KGVHPHDVATLLDESGIAvrsGHHcaqpLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05355 |
PRK05355 |
3-phosphoserine/phosphohydroxythreonine transaminase; |
1-362 |
0e+00 |
|
3-phosphoserine/phosphohydroxythreonine transaminase;
Pssm-ID: 235428 Cd Length: 360 Bit Score: 723.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 1 MAQVFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQF 80
Cdd:PRK05355 1 MMRVYNFSAGPAMLPEEVLEQAQQELLDWNGSGMSVMEISHRSKEFEAVAEEAEADLRELLNIPDNYKVLFLQGGASLQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 81 AGVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKiTVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAID 160
Cdd:PRK05355 81 AMVPMNLLGGGKKADYVDTGSWSKKAIKEAKKYGEVNVAASS-EDDGFTYIPPLDEWQLSDDAAYVHYTSNETIDGTEFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 161 ETPDFGPeVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNT 240
Cdd:PRK05355 160 ELPDTGD-VPLVADMSSDILSRPIDVSKFGLIYAGAQKNIGPAGLTIVIVREDLLGRALPSIPSMLDYKTHADNDSMYNT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 241 PPTFAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAA 320
Cdd:PRK05355 239 PPTFAIYLAGLVFKWLKEQGGVAAMEKRNQEKAALLYDAIDSSDFYRNPVAPEDRSRMNVPFTLADEELDKKFLAEAKAA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446001735 321 GLHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRHG 362
Cdd:PRK05355 319 GLVGLKGHRSVGGMRASIYNAMPLEGVQALVDFMKEFERRHG 360
|
|
| SerC |
COG1932 |
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and ... |
2-361 |
0e+00 |
|
Phosphoserine aminotransferase [Coenzyme transport and metabolism, Amino acid transport and metabolism]; Phosphoserine aminotransferase is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 441535 Cd Length: 358 Bit Score: 640.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 2 AQVFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFA 81
Cdd:COG1932 1 MRVYNFSAGPAKLPEEVLEQAQAELLDWNGSGMSVMEMSHRSKPFKAIVEEAEADLRELLGIPDGYEVLFLQGGATAQFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 82 GVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKITvDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDE 161
Cdd:COG1932 81 MVPMNLLRGGKKADYLVTGEWSKKAIKEAKKYGEVNVVASSED-DNFGYIPKPEEWQLSPDADYVHYTSNETITGVEFHE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 162 TPDFGpEVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTP 241
Cdd:COG1932 160 LPDVG-DVPLVADMSSDILSRPVDVSKFGLIYAGAQKNIGPAGLTVVIVRPDLLGRAERAIPSMLDYKTHADNDSMYNTP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 242 PTFAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAG 321
Cdd:COG1932 239 PTFAIYLAGLVLKWLKEQGGLAAMEKRNAEKAALLYDWIDASDFYTNPVDPEDRSRMNVTFDLADEELDAAFLAEAKAAG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446001735 322 LHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRH 361
Cdd:COG1932 319 LVGLKGHRSVGGMRASIYNAMPLEGVEALVDFMDEFERRH 358
|
|
| PSAT_like |
cd00611 |
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP) ... |
5-359 |
0e+00 |
|
Phosphoserine aminotransferase (PSAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major group in this CD corresponds to phosphoserine aminotransferase (PSAT). PSAT is active as a dimer and catalyzes the conversion of phosphohydroxypyruvate to phosphoserine.
Pssm-ID: 99736 [Multi-domain] Cd Length: 355 Bit Score: 599.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 5 FNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVP 84
Cdd:cd00611 1 INFSAGPAALPEEVLEQAQKELLDFNGLGMSVMEMSHRSKDFEAIVNEAESDLRELLNIPDNYKVLFLQGGATGQFAAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 85 LNLLGDKTTADYVDAGYWAASAIKEAKKYC-APQIIDAKITvDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETP 163
Cdd:cd00611 81 LNLLGDKGTADYVVTGAWSAKAAKEAKRYGgVVVIVAAKEE-GKYTKIPDVETWDLAPDAAYVHYCSNETIHGVEFDEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 164 DFGPeVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPT 243
Cdd:cd00611 160 DTGG-VPLVADMSSNILSRPIDVSKFGVIYAGAQKNLGPAGVTVVIVRKDLLGKARKITPSMLNYKTHADNNSLYNTPPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 244 FAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNS-DFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAGL 322
Cdd:cd00611 239 FAIYMMGLVLKWLKEQGGVEAMEKRNRQKAQLLYDTIDNSnGFYRGPVDKRARSRMNVPFRLGKEELEKEFLKEAEAAGM 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 446001735 323 HALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFER 359
Cdd:cd00611 319 IGLKGHRSVGGIRASIYNALSLEGVQALADFMKEFQK 355
|
|
| serC_1 |
TIGR01364 |
phosphoserine aminotransferase; This model represents the common form of the phosphoserine ... |
12-361 |
0e+00 |
|
phosphoserine aminotransferase; This model represents the common form of the phosphoserine aminotransferase SerC. The phosphoserine aminotransferase of the archaeon Methanosarcina barkeri and putative phosphoserine aminotransferase of Mycobacterium tuberculosis are represented by separate models. All are members of the class V aminotransferases (pfam00266). [Amino acid biosynthesis, Serine family]
Pssm-ID: 130431 Cd Length: 349 Bit Score: 548.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 12 AMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVPLNLLGDK 91
Cdd:TIGR01364 1 AALPEEVLEQAQKELLNFNGTGMSVMEISHRSKEFEAVANEAESDLRELLNIPDNYEVLFLQGGATGQFAAVPLNLLAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 92 TTADYVDAGYWAASAIKEAKKYCAPqIIDAKITVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETPDFGPEVVV 171
Cdd:TIGR01364 81 KVADYIVTGAWSKKAAKEAKKYGVV-NVVASGKEGNYTKIPDPSTWEISEDAAYVHYCANETIHGVEFRELPDVKNAPLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 172 tADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPTFAWYLSGL 251
Cdd:TIGR01364 160 -ADMSSNILSRPIDVSKFGLIYAGAQKNIGPAGLTVVIVRKDLLGRASRITPSMLNYKIHAENDSMYNTPPTFAIYVSGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 252 VFKWLKAQGGVAAMHKINQQKAELLYGVIDNS-DFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAGLHALKGHRV 330
Cdd:TIGR01364 239 VFKWLKEQGGVKAIEKRNQAKAQLLYDTIDNSnGFYRNPVDPRNRSRMNVVFTLGNEELEKRFLKEAEERGLVSLKGHRS 318
|
330 340 350
....*....|....*....|....*....|.
gi 446001735 331 VGGMRASIYNAMPIEGVKALTDFMIDFERRH 361
Cdd:TIGR01364 319 VGGMRASIYNAMPLEGVQALVDFMKEFQKKH 349
|
|
| PLN02452 |
PLN02452 |
phosphoserine transaminase |
4-361 |
0e+00 |
|
phosphoserine transaminase
Pssm-ID: 178071 Cd Length: 365 Bit Score: 507.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 4 VFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGV 83
Cdd:PLN02452 8 VFNFSAGPATLPANVLAKAQAELYNWEGSGMSVMEMSHRGKEFLSIIQKAEADLRELLDIPDNYEVLFLQGGASTQFAAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 84 PLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIdAKITVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETP 163
Cdd:PLN02452 88 PLNLCKPGDKADFVVTGSWSKKAAKEAKKYCKTNVI-ASGKDEKYTKIPSVSEWELTPDAKFVHICANETIHGVEFKDYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 164 DFGPEVVVtADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPT 243
Cdd:PLN02452 167 DVGNVPLV-ADMSSNFLSKPVDVSKYGVIYAGAQKNVGPSGVTIVIIRKDLIGNARPITPGMLDYKIHAENDSLYNTPPC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 244 FAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSD-FYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAGL 322
Cdd:PLN02452 246 FGIYMCGLVFEDLLAQGGLKAMEKRNIRKADLLYDAIDESNgFYVCPVEKSVRSLMNVPFTLGGSELEAEFVKEAAKAGM 325
|
330 340 350
....*....|....*....|....*....|....*....
gi 446001735 323 HALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRH 361
Cdd:PLN02452 326 VQLKGHRSVGGMRASIYNAMPLAGVEKLVAFMKDFQAKH 364
|
|
| PRK12462 |
PRK12462 |
phosphoserine aminotransferase; Provisional |
6-362 |
2.69e-118 |
|
phosphoserine aminotransferase; Provisional
Pssm-ID: 183540 Cd Length: 364 Bit Score: 346.80 E-value: 2.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 6 NFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVPL 85
Cdd:PRK12462 7 NFSGGPGALPDTVLEQVRQAVVELPETGLSVLGMSHRSSWFSSLLAQAEADLRDLLGIPDEYGVVFLQGGSSLQFSMIPM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 86 NLLGDKTT-ADYVDAGYWAASAIKEAKKYCAPQII-DAKitVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETP 163
Cdd:PRK12462 87 NFSRPGAAaPEYVTTGYWSRKAIGEASRVAAMRVVwDGA--ASGYRTLPSLAELDWDARAPFRHYVSNETVEGLQFPDAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 164 DFgPEVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPT 243
Cdd:PRK12462 165 GL-PDSPLIADMSSDFMSRPFDVEAYGMVYAHAQKNLGPAGVTVAIIRRALLERVPDTLPPMLDFRTHVEHRSNYNTPPV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 244 FAWYLSGLVFKWLKAQ-GGVAAMHKINQQKAELLYGVIDNSD-FYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAG 321
Cdd:PRK12462 244 FAIYVMALVLRWIRDEiGGVHAMRDINARKAAMLYATLDALNeVIDCHAHRAARSTMNVAFRFRQPRLDTLFKEQSTEAG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446001735 322 LHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRHG 362
Cdd:PRK12462 324 FCGLSGHRSIGGIRASLYNAVSEQAVSRLCAFLKDFAIRHA 364
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
4-350 |
1.67e-89 |
|
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: 273.35 E-value: 1.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 4 VFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSvmEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRgQFAGV 83
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVHR--GVHTLGKEATQAYEEAREKVAEFINAPSNDEIIFTSGTTE-AINLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 84 PLNL---LGDKTTADYVDAGYWAAS-AIKEAKKYCAPQIIDAKITVDGKRAVKPMrEWQLSDNAAYLHYCPNETIDGIaI 159
Cdd:pfam00266 78 ALSLgrsLKPGDEIVITEMEHHANLvPWQELAKRTGARVRVLPLDEDGLLDLDEL-EKLITPKTKLVAITHVSNVTGT-I 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 160 DETPDFGPE-----VVVTADFSSTILSAPLDVSRYGV--IYAGAQKNIGPAGLTLVIVREDLLGKAHE--------SCPS 224
Cdd:pfam00266 156 QPVPEIGKLahqygALVLVDAAQAIGHRPIDVQKLGVdfLAFSGHKLYGPTGIGVLYGRRDLLEKMPPllggggmiETVS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 225 iLDYTVLNDNDSMFN--TPPTFAWYLSGLVFKWLKAqGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPF 302
Cdd:pfam00266 236 -LQESTFADAPWKFEagTPNIAGIIGLGAALEYLSE-IGLEAIEKHEHELAQYLYERLLSLPGIRLYGPERRASIISFNF 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446001735 303 QLADNALDKVFLEESFAA---GLH----ALKGHRVVGGMRASIYNAMPIEGVKAL 350
Cdd:pfam00266 314 KGVHPHDVATLLDESGIAvrsGHHcaqpLMVRLGLGGTVRASFYIYNTQEDVDRL 368
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
50-211 |
4.13e-25 |
|
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: 99.76 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 50 AEEAEQDFRDLLNiPSNYKVLFCHGGgRGQFAGVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKITVDGKR 129
Cdd:cd01494 2 LEELEEKLARLLQ-PGNDKAVFVPSG-TGANEAALLALLGPGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAGYGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 130 AVKPMREWQLSDNAAYLHYCPNETIDGIAID----ETPDFGPEVVVTADFSSTILSAP-----LDVSRYGVIYAGAQKNI 200
Cdd:cd01494 80 DVAILEELKAKPNVALIVITPNTTSGGVLVPlkeiRKIAKEYGILLLVDAASAGGASPapgvlIPEGGADVVTFSLHKNL 159
|
170
....*....|.
gi 446001735 201 GPAGLTLVIVR 211
Cdd:cd01494 160 GGEGGGVVIVK 170
|
|
| PRK03080 |
PRK03080 |
phosphoserine transaminase; |
6-325 |
3.23e-07 |
|
phosphoserine transaminase;
Pssm-ID: 235103 Cd Length: 378 Bit Score: 51.73 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 6 NFSSGPAMLPAEvlklaqqelRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVPL 85
Cdd:PRK03080 15 RFSSGPCKKRPG---------WQLEALADALLGRSHRQKPVKALLKRVIEGTRELLSLPEGYEVGIVPGSDTGAWEMALW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 86 NLLGdkttADYVDAGYWA------ASAIKEAKKYCAPQIIDAK-------ITVDGKRAVkpmrewqlsdnaAYLHycpNE 152
Cdd:PRK03080 86 SLLG----ARRVDHLAWEsfgskwATDVVKQLKLEDPRVLEADygslpdlSAVDFDRDV------------VFTW---NG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 153 TIDGIAIdetPDFGP-----EVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIG-PAGLTLVIVR----EDLLG-KAHES 221
Cdd:PRK03080 147 TTTGVRV---PVARWigadrEGLTICDATSAAFALPLDWSKLDVYTFSWQKVLGgEGGHGMAILSpravERLESyTPARP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 222 CPSILDYT---VLNDN---DSMFNTPP--TFAWYLSGLvfKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVA-Q 292
Cdd:PRK03080 224 IPKFFRLTkggKAIENsfkGQTINTPSmlTVEDYLDQL--DWANSIGGLDALIARTAANASVLYDWAEKTPWATPLVAdP 301
|
330 340 350
....*....|....*....|....*....|...
gi 446001735 293 ANRSRMNVPFQLADnaldkvfLEESFAAGLHAL 325
Cdd:PRK03080 302 ATRSNTSVTLDFVD-------AQAAVDAAAVAK 327
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
10-218 |
5.97e-04 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 41.51 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 10 GPAMLPAEVLKLAQQELrdwhglgtsvmeISHRGKEFIQVAEEAEQDFRDLLnIPSNYKVLFCHGGGRGQFAGVPLNLL- 88
Cdd:cd06451 6 GPSNVPPRVLKAMNRPM------------LGHRSPEFLALMDEILEGLRYVF-QTENGLTFLLSGSGTGAMEAALSNLLe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446001735 89 -GDKTTAdyVDAGYWAASAIKEAKKYCA--------------PQIIDAKITVDGKRAVkpmrewqlsdnaAYLHycpNET 153
Cdd:cd06451 73 pGDKVLV--GVNGVFGDRWADMAERYGAdvdvvekpwgeavsPEEIAEALEQHDIKAV------------TLTH---NET 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446001735 154 -------IDGIAIDETpdfGPEVVVTADFSSTILSAPLDVSRYGV--IYAGAQKNIG-PAGLTLVIVREDLLGKA 218
Cdd:cd06451 136 stgvlnpLEGIGALAK---KHDALLIVDAVSSLGGEPFRMDEWGVdvAYTGSQKALGaPPGLGPIAFSERALERI 207
|
|
| |
