|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-592 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1122.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQID 80
Cdd:PRK05222 125 FDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPVTFLWLSKSKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQID 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 81 EPALVLELPQAWRAAFRAAYDTLEGE---VKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPADWLL 157
Cdd:PRK05222 205 EPALVLDLPQEWLEAFKRAYEALAAAkprPKLLLATYFGSLNDALDLLASLPVDGLHLDLVRGPEQLAALLKYFPADKVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 158 SLGVINGRNVWRADLHSWFVRLQPIAGKRQQLWIGSSCSLLHSPIDLSVETRLDKEVKSWFAFALQKCVELGLLTRALNQ 237
Cdd:PRK05222 285 SAGVIDGRNIWRADLEAALALLEPLAAKVDRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 238 ---NDSALLEEWSAPIRARRHSRRVHNAVVTQRLAAITGKDSQRNNAYPQRAAAQRARFRLPLWPTTTIGSFPQTTEIRR 314
Cdd:PRK05222 365 grgAVAEALAANRAAIAARRTSPRVHNPAVRARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRK 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 315 LRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPVI 394
Cdd:PRK05222 445 ARAAFKKGELSEEEYEAFIREEIARAIRLQEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPII 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 395 IGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEKAGIGIIQIDEPA 474
Cdd:PRK05222 525 YGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 475 LREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIETSRSDMELLESFKEFDY 554
Cdd:PRK05222 605 LREGLPLRRSDWDAYLDWAVEAFRLATSGVKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGY 684
|
570 580 590
....*....|....*....|....*....|....*...
gi 693735264 555 PNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:PRK05222 685 PNEIGPGVYDIHSPRVPSVEEIEELLRKALEVIPAERL 722
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
1-592 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273583 [Multi-domain] Cd Length: 750 Bit Score: 930.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQID 80
Cdd:TIGR01371 119 LSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLSKAVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQID 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 81 EPALVLELPQAWRAAFRAAYDTLEGE---VKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPADWLL 157
Cdd:TIGR01371 199 EPALVTDLSKEDLAAFKEAYTELSEAlsgLKLLLQTYFDSVGDALEALVSLPVKGIGLDFVHGKGTLELVKAGFPEDKVL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 158 SLGVINGRNVWRADLHSWFVRLQPIAGKRQQLWIGSSCSLLHSPIDLSVETRLDKEVKSWFAFALQKCVELGLLTRALNQ 237
Cdd:TIGR01371 279 SAGVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 238 NDSAL---LEEWSAPIRARRHSRRVHNAVVTQRLAAITGKDSQRNNAYPQRAAAQRARFRLPLWPTTTIGSFPQTTEIRR 314
Cdd:TIGR01371 359 NDDAVafaLEANAAAIAARKSSPRVNDAQVKARLANLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRK 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 315 LRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPVI 394
Cdd:TIGR01371 439 ARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLDVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPII 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 395 IGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEKAGIGIIQIDEPA 474
Cdd:TIGR01371 519 YGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPA 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 475 LREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIETSRSDMELLESFKE-FD 553
Cdd:TIGR01371 599 LREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQIHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNgFG 678
|
570 580 590
....*....|....*....|....*....|....*....
gi 693735264 554 YPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:TIGR01371 679 YPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPAERL 717
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
298-592 |
1.60e-174 |
|
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent methionine synthases or 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferases, EC:2.1.1.14 from bacteria and plants. Plants are the only higher eukaryotes that have the required enzymes for methionine synthesis. This enzyme catalyzes the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to homocysteine. The aligned region makes up the carboxy region of the approximately 750 amino acid protein except in some hypothetical archaeal proteins present in the family, where this region corresponds to the entire length. This domain contains the catalytic residues of the enzyme.
Pssm-ID: 366771 [Multi-domain] Cd Length: 323 Bit Score: 496.96 E-value: 1.60e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 298 WPTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQ 377
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 378 NGWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEV 457
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 458 ADLEKAGIGIIQIDEPALREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIE 537
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 693735264 538 TSRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERL 295
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
299-592 |
2.24e-137 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 402.60 E-value: 2.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQN 378
Cdd:COG0620 2 PTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFARN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 379 GWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVA 458
Cdd:COG0620 82 GWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 459 DLEKAGIGIIQIDEPALREGLPlhradwDNYLAWAVEAFRLNAAVVRDeTQIHTHMCYCEFNDIMDVIAALDADVITIET 538
Cdd:COG0620 162 ALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLEF 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 693735264 539 SRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:COG0620 235 VRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERL 288
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
299-592 |
1.31e-124 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the C-terminal barrel, and a few single-barrel sequences most similar to the C-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Sidechains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239427 [Multi-domain] Cd Length: 332 Bit Score: 370.02 E-value: 1.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQn 378
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 379 gWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTD-KPVKGMLTGPVTILCWSFPRE---DVSRETIAKQIALALR 454
Cdd:cd03311 80 -WVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 455 DEVADLEKAGIGIIQIDEPALREGLPLHR-ADWDNYLAWAVEAFRLnaavVRDETQIHTHMCYCEF----------NDIM 523
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALAD----RPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693735264 524 DVIAALDADVITIETSRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQL 303
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-592 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1122.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQID 80
Cdd:PRK05222 125 FDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPVTFLWLSKSKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQID 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 81 EPALVLELPQAWRAAFRAAYDTLEGE---VKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPADWLL 157
Cdd:PRK05222 205 EPALVLDLPQEWLEAFKRAYEALAAAkprPKLLLATYFGSLNDALDLLASLPVDGLHLDLVRGPEQLAALLKYFPADKVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 158 SLGVINGRNVWRADLHSWFVRLQPIAGKRQQLWIGSSCSLLHSPIDLSVETRLDKEVKSWFAFALQKCVELGLLTRALNQ 237
Cdd:PRK05222 285 SAGVIDGRNIWRADLEAALALLEPLAAKVDRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 238 ---NDSALLEEWSAPIRARRHSRRVHNAVVTQRLAAITGKDSQRNNAYPQRAAAQRARFRLPLWPTTTIGSFPQTTEIRR 314
Cdd:PRK05222 365 grgAVAEALAANRAAIAARRTSPRVHNPAVRARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRK 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 315 LRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPVI 394
Cdd:PRK05222 445 ARAAFKKGELSEEEYEAFIREEIARAIRLQEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPII 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 395 IGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEKAGIGIIQIDEPA 474
Cdd:PRK05222 525 YGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 475 LREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIETSRSDMELLESFKEFDY 554
Cdd:PRK05222 605 LREGLPLRRSDWDAYLDWAVEAFRLATSGVKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGY 684
|
570 580 590
....*....|....*....|....*....|....*...
gi 693735264 555 PNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:PRK05222 685 PNEIGPGVYDIHSPRVPSVEEIEELLRKALEVIPAERL 722
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
1-592 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273583 [Multi-domain] Cd Length: 750 Bit Score: 930.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQID 80
Cdd:TIGR01371 119 LSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLSKAVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQID 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 81 EPALVLELPQAWRAAFRAAYDTLEGE---VKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPADWLL 157
Cdd:TIGR01371 199 EPALVTDLSKEDLAAFKEAYTELSEAlsgLKLLLQTYFDSVGDALEALVSLPVKGIGLDFVHGKGTLELVKAGFPEDKVL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 158 SLGVINGRNVWRADLHSWFVRLQPIAGKRQQLWIGSSCSLLHSPIDLSVETRLDKEVKSWFAFALQKCVELGLLTRALNQ 237
Cdd:TIGR01371 279 SAGVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNG 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 238 NDSAL---LEEWSAPIRARRHSRRVHNAVVTQRLAAITGKDSQRNNAYPQRAAAQRARFRLPLWPTTTIGSFPQTTEIRR 314
Cdd:TIGR01371 359 NDDAVafaLEANAAAIAARKSSPRVNDAQVKARLANLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRK 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 315 LRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPVI 394
Cdd:TIGR01371 439 ARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLDVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPII 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 395 IGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEKAGIGIIQIDEPA 474
Cdd:TIGR01371 519 YGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPA 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 475 LREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIETSRSDMELLESFKE-FD 553
Cdd:TIGR01371 599 LREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQIHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNgFG 678
|
570 580 590
....*....|....*....|....*....|....*....
gi 693735264 554 YPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:TIGR01371 679 YPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPAERL 717
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
6-582 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 677.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 6 KFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGK-VKGEP--FDRLTLLNEILPVYKQILTALAQRNIEWVQIDEP 82
Cdd:PLN02475 129 KFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKpAKGVDksFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEP 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 83 ALVLELPQAWRAAFRAAYDTLE---GEVKLLLTTYFDSIG-QNLDLIRTLP-VQGIHVDLVHGNDDLASLNDQ-LPADWL 156
Cdd:PLN02475 209 ALVMDLESHKLQAFKTAYAELEstlSGLNVLVETYFADVPaEAYKTLTSLKgVTAFGFDLVRGTKTLDLIKKAgFPSGKY 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 157 LSLGVINGRNVWRADLHSWFVRLQPIAGK--RQQLWIGSSCSLLHSPIDLSVETRLDKEVKSWFAFALQKCVELGLLTRA 234
Cdd:PLN02475 289 LFAGVVDGRNIWANDLAASLATLQALEGIvgKDKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 235 L-NQNDSALLEEWSAPIRARRHSRRVHNAVVTQRLAAITGKDSQRNNAYPQRAAAQRARFRLPLWPTTTIGSFPQTTEIR 313
Cdd:PLN02475 369 LaGQKDEAFFSANAAAQASRRSSPRVTNEAVQKAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 314 RLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPV 393
Cdd:PLN02475 449 RVRREYKAKKISEEDYVKAIKEEIAKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPI 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 394 IIGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEKAGIGIIQIDEP 473
Cdd:PLN02475 529 IYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEA 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 474 ALREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIETSRSDMELLESFKE-F 552
Cdd:PLN02475 609 ALREGLPLRKSEHAFYLDWAVHSFRITNCGVQDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgV 688
|
570 580 590
....*....|....*....|....*....|
gi 693735264 553 DYPNEIGPGVYDIHSPNVPDVTWMETLLQK 582
Cdd:PLN02475 689 KYGAGIGPGVYDIHSPRIPSTEEIADRINK 718
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
298-592 |
1.60e-174 |
|
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent methionine synthases or 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferases, EC:2.1.1.14 from bacteria and plants. Plants are the only higher eukaryotes that have the required enzymes for methionine synthesis. This enzyme catalyzes the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to homocysteine. The aligned region makes up the carboxy region of the approximately 750 amino acid protein except in some hypothetical archaeal proteins present in the family, where this region corresponds to the entire length. This domain contains the catalytic residues of the enzyme.
Pssm-ID: 366771 [Multi-domain] Cd Length: 323 Bit Score: 496.96 E-value: 1.60e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 298 WPTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQ 377
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 378 NGWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEV 457
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 458 ADLEKAGIGIIQIDEPALREGLPLHRADWDNYLAWAVEAFRLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADVITIE 537
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 693735264 538 TSRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERL 295
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
299-592 |
2.24e-137 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 402.60 E-value: 2.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQN 378
Cdd:COG0620 2 PTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFARN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 379 GWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVA 458
Cdd:COG0620 82 GWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 459 DLEKAGIGIIQIDEPALREGLPlhradwDNYLAWAVEAFRLNAAVVRDeTQIHTHMCYCEFNDIMDVIAALDADVITIET 538
Cdd:COG0620 162 ALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLEF 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 693735264 539 SRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:COG0620 235 VRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERL 288
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
299-592 |
1.31e-124 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the C-terminal barrel, and a few single-barrel sequences most similar to the C-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Sidechains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239427 [Multi-domain] Cd Length: 332 Bit Score: 370.02 E-value: 1.31e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQn 378
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 379 gWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTD-KPVKGMLTGPVTILCWSFPRE---DVSRETIAKQIALALR 454
Cdd:cd03311 80 -WVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 455 DEVADLEKAGIGIIQIDEPALREGLPLHR-ADWDNYLAWAVEAFRLnaavVRDETQIHTHMCYCEF----------NDIM 523
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALAD----RPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693735264 524 DVIAALDADVITIETSRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQL 303
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
1-234 |
4.46e-123 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 367.24 E-value: 4.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQID 80
Cdd:cd03312 123 LSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFLKLSKAKGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQID 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 81 EPALVLELPQAWRAAFRAAYDTLEGE---VKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPADWLL 157
Cdd:cd03312 203 EPALVLDLPEEWLAAFKRAYEELAKAapgLKLLLATYFGSLGENLDLLASLPVDGLHLDLVRGPENLEAVLKAGFADKVL 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 693735264 158 SLGVINGRNVWRADLHSWFVRLQPIAGK-RQQLWIGSSCSLLHSPIDLSVETRLDKEVKSWFAFALQKCVELGLLTRA 234
Cdd:cd03312 283 SAGVVDGRNIWRADLAASLALLETLAAIlGDRLVVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
1-186 |
1.05e-92 |
|
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal domains of cobalamin-independent synthases together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilize a loop from the C-terminal domain.
Pssm-ID: 400526 [Multi-domain] Cd Length: 310 Bit Score: 287.17 E-value: 1.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQID 80
Cdd:pfam08267 122 LDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFLKLSKGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQID 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 81 EPALVLELPQAWRAAFRAAYDTLE---GEVKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPADWLL 157
Cdd:pfam08267 202 EPALVLDLPPEWLAAFKEAYQELAsakPGPKLLLATYFGSVADALELLASLPVAGLGLDLVRGPENLAALKKGFPADKVL 281
|
170 180
....*....|....*....|....*....
gi 693735264 158 SLGVINGRNVWRADLHSWFVRLQPIAGKR 186
Cdd:pfam08267 282 SAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
295-592 |
1.12e-60 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 204.44 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 295 LPLWPTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDGFV 374
Cdd:PRK04326 6 LPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 375 FtqNGWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLT-DKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALAL 453
Cdd:PRK04326 86 F--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKVI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 454 RDEVADLEKAGIGIIQIDEPAlregLPLHRADwdnyLAWAVEAfrLNAAVVRDETQIHTHMCYCEFNDIMDVIAALDADV 533
Cdd:PRK04326 164 NEEIKNLVEAGAKYIQIDEPA----LATHPED----VEIAVEA--LNRIVKGINAKLGLHVCYGDYSRIAPYILEFPVDQ 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 693735264 534 ITIETSRSDMELLESFKEFDYPNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:PRK04326 234 FDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKL 292
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
1-224 |
1.05e-56 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 193.82 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 1 FTSGQKFKLSWLqlLEEVDEALAL-GHRVKPVLLGPVTYLWLGKVKGEPfDRLTLLNEILPVYKQILTALAQRNIEWVQI 79
Cdd:COG0620 97 ITGDVSFSGPMT--VEEFRFAKSLtGKPVKPVLPGPVTLLLLSKVRDYK-DREELLDDLAPAYREELKALEAAGARWIQI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 80 DEPALVLELPQAWRAAFRAAYD-TLEG--EVKLLLTTYFDSIGQNLDLIRTLPVQGIHVDLVHGN-DDLASLNDqLPADW 155
Cdd:COG0620 174 DEPALAEDLPDEYLDWAVEAYNrAAAGvpDTKIHLHTCYGGYEDILEALAALPVDGIHLEFVRSRaGLLEPLKE-LPYDK 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 693735264 156 LLSLGVINGRNVWRADLHSWFVRLQPIAGK--RQQLWIGSSCSLLHSPIDLSVETrLDKEVKSWFAFALQK 224
Cdd:COG0620 253 VLGLGVIDGRNPWVEDPEEVAARIEEALKYvpPERLWVSPDCGLKHRPVDLTREE-AWAKLRNMVAFAREV 322
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
299-552 |
1.50e-28 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 116.37 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERnDMVEYFGEHLDGFVFtqn 378
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 379 GWVQSYGSRCVKPPVIIGDIS-RPEAITAEWAKYAQSLTdKPVKGMLTGPVTILCWSF--PREDVSRETIAKQIALALRD 455
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFlPLELDYLEEVAEAYKEA-LKVKVVVTGPLTLALLAFlpNGEPDAYEDLAKSLAEFLRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 456 EVADLEKAGIGIIQIDEPALREGLPLHRADWDNYLAWaveafrLNAAVVRDETQIHTHMCYcefNDIMDVIAALDADVIT 535
Cdd:cd03310 156 QVKELKNRGIVVVQIDEPSLGAVGAGAFEDLEIVDAA------LEEVSLKSGGDVEVHLCA---PLDYEALLELGVDVIG 226
|
250
....*....|....*..
gi 693735264 536 IETSRSDMELLESFKEF 552
Cdd:cd03310 227 FDAAALPSKYLEDLKKL 243
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
299-585 |
8.60e-28 |
|
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc.
Pssm-ID: 238261 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 8.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFPQTTEIRRlrldfkrERIDGSHYRTGIAQHIKQAItEQELLGLDVLVHGEAERNDMVEYFGehldgfvftqn 378
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPGETSKAEWGITLV-EPEEIPLDVIPVHEDDVLKVAQALG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 379 GWVQSYGSRCVKPPVIIGD-ISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSR---------ETIAKQ 448
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEeDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDALMalyerpeamHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 449 IALALRDEVADLEKAGIGIIQIDEPALREGLPLhrADWDNYLAWAVEAFRLNA-AVVRDETQIHTHMCYcEFNDIMDVIA 527
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSF--LGPKMFKKFALPAYKKVAeYKAAGEVPIVHHSCY-DAADLLEEMI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 693735264 528 ALDADVITIETSRSdmELLESFKEFDYPNEIGPGVYDIHSPNVPdvtwmETLLQKAAQ 585
Cdd:cd00465 219 QLGVDVISFDMTVN--EPKEAIEKVGEKKTLVGGVDPGYLPATD-----EECIAKVEE 269
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
296-592 |
8.03e-23 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 99.76 E-value: 8.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 296 PLWPTTTIGSFPQTT---EIRRLRLDFKREridGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDG 372
Cdd:PRK09121 1 TLLPTSTAGSLPKPSwlaEPETLWSPWKLQ---GEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 373 FVFTQNGWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALA 452
Cdd:PRK09121 78 VDFEKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 453 LRDEVADLEKAGIGIIQIDEPALREGLPlHRADWD-NYLAWAVEAFRLNAAVvrdetqihtHMCY--------------- 516
Cdd:PRK09121 158 LNQEAKELEAAGVDIIQFDEPAFNVFFD-EVNDWGvAALERAIEGLKCETAV---------HICYgygikantdwkktlg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 517 CEFNDIMDVIAALDA---DVITIE--TSRSDMELLESFKEfdypNEIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTER 591
Cdd:PRK09121 228 SEWRQYEEAFPKLQKsniDIISLEchNSRVPMDLLELIRG----KKVMVGAIDVASDTIETPEEVADTLRKALQFVDADK 303
|
.
gi 693735264 592 L 592
Cdd:PRK09121 304 L 304
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
299-592 |
2.95e-21 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 94.67 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 299 PTTTIGSFP---QTTEIRRLRLDFKRERIDGSHYRtgiaqhIKQAITEQELLGLDVLVHGEAeRNDMVEYFGEHLDGFvf 375
Cdd:PRK00957 3 ITTVVGSYPvvkGEPETLKDKIKGFFGLYDPYKPA------IEEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGF-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 376 tqngwvqsYGSRcvkppvIIGDISRPE-AITAEWAKYAQSLT-----DKPVKGMLTGPVTIlCWSFPRE----DVSRETI 445
Cdd:PRK00957 74 --------DGKR------VIGRVEPPAkPITLKDLKYAKKVAkkkdpNKGVKGIITGPSTL-AYSLRVEpfysDNKDEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 446 AKQIALALRDEVADLEKAGIGIIQIDEPALREGLplhrADwdnyLAWAVEAFRLNAAVVRDETQIHThmcyC-EFNDIMD 524
Cdd:PRK00957 139 IYDLARALRKEAEALEKAGVAMIQIDEPILSTGA----YD----LEVAKKAIDIITKGLNVPVAMHV----CgDVSNIID 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 525 VIAALDADVITIE--TSRSDMELLESFKEFDYPneIGPGVYDIHSPNVPDVTWMETLLQKAAQRIPTERL 592
Cdd:PRK00957 207 DLLKFNVDILDHEfaSNKKNLEILEEKDLIGKK--IGFGCVDTKSKSVESVDEIKALIEEGIEILGAENI 274
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
348-587 |
1.30e-15 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 78.42 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 348 GLD-VLVHGEAERNDMVEYFGEHLDGFVFTqnGWVQSYGSRCVKPPVIIGDISRPEAITAEWAKYAQSLTDKPVKGMLTG 426
Cdd:PRK01207 50 GLDnIGIGGEMFRWEMYEHPAERIKGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 427 PVTILCWSFPREDVSRETIAKQIALALRDEVADLEKAGIGI-------IQIDEPALREglplHRADWDnylawaVEAFRL 499
Cdd:PRK01207 128 PYTMMDWSFNDFYRDRYDLAMEFARIINEELKDIKSAWDRKspgrkleIQIDEPATTT----HPDEMD------IVVDSI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 500 NAAVVRDETQIHTHMCYC-EFNDIMDVIAALDADVITIETSRSDM-------ELLESFKEFDYPNE----------IGPG 561
Cdd:PRK01207 198 NKSVYGIDNEFSIHVCYSsDYRLLYDRIPELNIDGYNLEYSNRDTlepgtsdEKRPGFQDLKYFAEhneslqrkkfIGLG 277
|
250 260
....*....|....*....|....*.
gi 693735264 562 VYDIHSPNVPDVTWMETLLQKAAQRI 587
Cdd:PRK01207 278 VTDVHIDYVEPVKLIEDRIRYALKII 303
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
12-204 |
4.35e-09 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 58.21 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 12 LQLLEEVDEALALGHRVKPVLLGPVT-YLWLGKVKGEPFDRLTLLNEILPVYKQILTALAQRNIEWVQIDEPALVL---- 86
Cdd:cd03310 102 LDYLEEVAEAYKEALKVKVVVTGPLTlALLAFLPNGEPDAYEDLAKSLAEFLREQVKELKNRGIVVVQIDEPSLGAvgag 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 87 --ELPQAWRAAFRAAYDTLEGEVKLLLTTYFDsigqnLDLIRTLPVQGIHVDLV----HGNDDLASLNDQLPADWLLSLG 160
Cdd:cd03310 182 afEDLEIVDAALEEVSLKSGGDVEVHLCAPLD-----YEALLELGVDVIGFDAAalpsKYLEDLKKLLRIGVRTLILGLV 256
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 693735264 161 VIN----GRNVWR-ADLHSWFVRLQPIAG--KRQQLWIGSSCSLLHSPIDL 204
Cdd:cd03310 257 VTDneakGRNAWKeIERLEKLVRRLEEPGevLDEILYLTPDCGLAFLPPQE 307
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
9-166 |
1.36e-07 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 53.59 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 9 LSWLQLLEEVDEALALGHRVKPVLLGPVTYLWLGkvKGEPFDRltlLNEILPVYKQILTALAQ---RNIEWVQIDEPALV 85
Cdd:PRK08575 111 LQWLESAREIKEEVSLESKLKAVLPGPLTYAVLS--DNEYYKN---LIELMEDYASVVNSLIKelsSVVDAVEIHEPSIF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 86 L-ELPQAWRAAFRAAYDTLEGEVKL--LLTTYFD--SIGQnLDLIRTLPVQGIHVDLVHGNDDLASLNDQLPaDWLLSLG 160
Cdd:PRK08575 186 AkGIKRDTLEKLPEVYKTMAKNVNIekHLMTYFEinNLKR-LDILFSLPVTYFGIDVIENLKKLGRVYTYLK-GRKVYLG 263
|
....*.
gi 693735264 161 VINGRN 166
Cdd:PRK08575 264 ILNARN 269
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
303-477 |
2.57e-04 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 43.57 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 303 IGSFPQTTEIRRLRLDFKRERIDGSHYRTGIAQHIKQAITEQELLGLDVLVHGEAERNDMVEYFGEHLDG------FVFT 376
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGvekgglQRFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693735264 377 QNGWVqsYGSrcvkpPVIIGDIS-RPEAITAEWAKYAQSLTDK-----PVKGMLTGPVTILCWSFPREDVSRETIAKQIA 450
Cdd:PRK08575 88 DNNFY--YRQ-----PVIKEKINlKEENPYLQWLESAREIKEEvslesKLKAVLPGPLTYAVLSDNEYYKNLIELMEDYA 160
|
170 180
....*....|....*....|....*..
gi 693735264 451 LALRDEVADLeKAGIGIIQIDEPALRE 477
Cdd:PRK08575 161 SVVNSLIKEL-SSVVDAVEIHEPSIFA 186
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
410-475 |
2.42e-03 |
|
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal domains of cobalamin-independent synthases together define a catalytic cleft in the enzyme. The N-terminal domain is thought to bind the substrate, in particular, the negatively charged polyglutamate chain. The N-terminal domain is also thought to stabilize a loop from the C-terminal domain.
Pssm-ID: 400526 [Multi-domain] Cd Length: 310 Bit Score: 40.26 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693735264 410 KYAQSLTD--KPVkgmLTGPVTILCWS-FPREDVSRETIAKQIALALRDEVADLEKAGIGIIQIDEPAL 475
Cdd:pfam08267 140 KEAKALGIetKPV---LLGPVTFLKLSkGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPAL 205
|
|
| |
