|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
4-762 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1328.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 4 AISSNLGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPK 83
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 84 RFQHDGGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPEL-ADAEPKVLDNRALYYYEEAKkELGIEGKPVLVGPI 162
Cdd:PRK05222 82 RFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFdPDTQFKLTSNKLLDEFEEAK-ALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 163 TYLKLGKGS-DAKSFEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQT 241
Cdd:PRK05222 161 TFLWLSKSKgEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 242 YFESL-DYYEEVVNLPVAAIGIDFVHDHGDsIKALKAHgFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVadGKL 320
Cdd:PRK05222 241 YFGSLnDALDLLASLPVDGLHLDLVRGPEQ-LAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV--DRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 321 IVQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKALTNGAESVAAELEESRAAVTALNESSHRNNLEVQE 400
Cdd:PRK05222 317 WVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVHNPAVRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 401 AIANLKNVRVDRELPFAERIKLQHAWLKLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQED 480
Cdd:PRK05222 397 RLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 481 LDIDVLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTA 560
Cdd:PRK05222 477 LGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 561 PVTIINWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTASVQN 640
Cdd:PRK05222 557 PVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGVKD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 641 DTQIHTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRA 720
Cdd:PRK05222 637 ETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALEV 716
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1254433488 721 IDAKQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAEYQV 762
Cdd:PRK05222 717 IPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
9-759 |
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: 1121.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 9 LGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRFQHD 88
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 89 GGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPELADAEPKVLD-NRALYYYEEAKkELGIEGKPVLVGPITYLKL 167
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTsNKPLEEYLEAK-ELGIETKPVLLGPITFLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 168 GKGSDaKSFEVL--LDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQTYFES 245
Cdd:TIGR01371 160 SKAVE-EPFEPLslLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 246 L-DYYEEVVNLPVAAIGIDFVHDHGDsiKALKAHGFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVadGKLIVQP 324
Cdd:TIGR01371 239 VgDALEALVSLPVKGIGLDFVHGKGT--LELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHV--GKLVVST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 325 SNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKALTNGAESVAAELEESRAAVTALNESSHRNNLEVQEAIAN 404
Cdd:TIGR01371 315 SCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIAARKSSPRVNDAQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 405 LKNVRVDRELPFAERIKLQHAWLKLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDID 484
Cdd:TIGR01371 395 LKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 485 VLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTI 564
Cdd:TIGR01371 475 VLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 565 INWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTASVQNDTQI 644
Cdd:TIGR01371 555 LNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 645 HTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVT-YDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDA 723
Cdd:TIGR01371 635 HTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFgYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPA 714
|
730 740 750
....*....|....*....|....*....|....*.
gi 1254433488 724 KQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAE 759
Cdd:TIGR01371 715 ERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
5-365 |
0e+00 |
|
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: 552.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 5 ISSNLGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPKR 84
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 85 FQHDGGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPEL-ADAEPKVLDNRALYYYEEAkKELGIEGKPVLVGPIT 163
Cdd:cd03312 81 FGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELsPDTEFKLASNKLLDEYLEA-KALGINTKPVLLGPVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 164 YLKLGKGSDAKS-FEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQTY 242
Cdd:cd03312 160 FLKLSKAKGGGFdRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLATY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 243 FESL-DYYEEVVNLPVAAIGIDFVHDhGDSIKALKAHGFPeDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVADgKLI 321
Cdd:cd03312 240 FGSLgENLDLLASLPVDGLHLDLVRG-PENLEAVLKAGFA-DKVLSAGVVDGRNIWRADLAASLALLETLAAILGD-RLV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1254433488 322 VQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKA 365
Cdd:cd03312 317 VSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
432-754 |
2.16e-171 |
|
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: 495.42 E-value: 2.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 592 EALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTASVQNDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTRKEPETIAALQDMIK 751
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMVD 320
|
...
gi 1254433488 752 ATK 754
Cdd:pfam01717 321 AAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-759 |
4.96e-138 |
|
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: 409.92 E-value: 4.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 592 EALERNGIKVIQVDEPALREGLPlkqarwQKYLDDAVYSFKLTTASVQnDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVP-DTKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTR----KEPETIAALQ 747
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKLR 313
|
330
....*....|..
gi 1254433488 748 DMIKATKEVRAE 759
Cdd:COG0620 314 NMVAFAREVRGE 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
4-762 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1328.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 4 AISSNLGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPK 83
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 84 RFQHDGGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPEL-ADAEPKVLDNRALYYYEEAKkELGIEGKPVLVGPI 162
Cdd:PRK05222 82 RFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFdPDTQFKLTSNKLLDEFEEAK-ALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 163 TYLKLGKGS-DAKSFEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQT 241
Cdd:PRK05222 161 TFLWLSKSKgEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 242 YFESL-DYYEEVVNLPVAAIGIDFVHDHGDsIKALKAHgFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVadGKL 320
Cdd:PRK05222 241 YFGSLnDALDLLASLPVDGLHLDLVRGPEQ-LAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV--DRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 321 IVQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKALTNGAESVAAELEESRAAVTALNESSHRNNLEVQE 400
Cdd:PRK05222 317 WVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVHNPAVRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 401 AIANLKNVRVDRELPFAERIKLQHAWLKLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQED 480
Cdd:PRK05222 397 RLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 481 LDIDVLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTA 560
Cdd:PRK05222 477 LGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 561 PVTIINWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTASVQN 640
Cdd:PRK05222 557 PVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGVKD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 641 DTQIHTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRA 720
Cdd:PRK05222 637 ETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALEV 716
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1254433488 721 IDAKQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAEYQV 762
Cdd:PRK05222 717 IPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
9-759 |
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: 1121.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 9 LGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRFQHD 88
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 89 GGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPELADAEPKVLD-NRALYYYEEAKkELGIEGKPVLVGPITYLKL 167
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTsNKPLEEYLEAK-ELGIETKPVLLGPITFLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 168 GKGSDaKSFEVL--LDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQTYFES 245
Cdd:TIGR01371 160 SKAVE-EPFEPLslLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 246 L-DYYEEVVNLPVAAIGIDFVHDHGDsiKALKAHGFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVadGKLIVQP 324
Cdd:TIGR01371 239 VgDALEALVSLPVKGIGLDFVHGKGT--LELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHV--GKLVVST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 325 SNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKALTNGAESVAAELEESRAAVTALNESSHRNNLEVQEAIAN 404
Cdd:TIGR01371 315 SCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIAARKSSPRVNDAQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 405 LKNVRVDRELPFAERIKLQHAWLKLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDID 484
Cdd:TIGR01371 395 LKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 485 VLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTI 564
Cdd:TIGR01371 475 VLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 565 INWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTASVQNDTQI 644
Cdd:TIGR01371 555 LNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 645 HTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVT-YDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDA 723
Cdd:TIGR01371 635 HTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFgYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPA 714
|
730 740 750
....*....|....*....|....*....|....*.
gi 1254433488 724 KQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAE 759
Cdd:TIGR01371 715 ERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
6-761 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 869.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 6 SSNLGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRF 85
Cdd:PLN02475 3 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPPRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 86 QHDGGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPELA-DAEPKVLDNRALYYYEEAKkELGIEGKPVLVGPITY 164
Cdd:PLN02475 83 GWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGpEVKFSYASHKAVNEYKEAK-ALGVDTVPVLVGPVSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 165 LKLGKGSD--AKSFEV--LLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQ 240
Cdd:PLN02475 162 LLLSKPAKgvDKSFDLlsLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 241 TYFESL--DYYEEVVNLP-VAAIGIDFVHDHgDSIKALKAHGFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVAD 317
Cdd:PLN02475 242 TYFADVpaEAYKTLTSLKgVTAFGFDLVRGT-KTLDLIKKAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 318 GKLIVQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKALtngAESVAAELEESRAAVTALNESSHR-NNL 396
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKAL---AGQKDEAFFSANAAAQASRRSSPRvTNE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 397 EVQEAIANLKNVRVDRELPFAERIKLQHAWLKLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIK 476
Cdd:PLN02475 398 AVQKAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 477 IQEDLDIDVLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKG 556
Cdd:PLN02475 478 LQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKG 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 557 MLTAPVTIINWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTA 636
Cdd:PLN02475 558 MLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNC 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 637 SVQNDTQIHTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEE-VTYDKEIGLGVYDIHSPRVPTVTEIQDNIR 715
Cdd:PLN02475 638 GVQDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRIN 717
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1254433488 716 RALRAIDAKQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAEYQ 761
Cdd:PLN02475 718 KMLAVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLA 763
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
5-365 |
0e+00 |
|
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: 552.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 5 ISSNLGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPKR 84
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 85 FQHDGGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPEL-ADAEPKVLDNRALYYYEEAkKELGIEGKPVLVGPIT 163
Cdd:cd03312 81 FGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELsPDTEFKLASNKLLDEYLEA-KALGINTKPVLLGPVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 164 YLKLGKGSDAKS-FEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQTY 242
Cdd:cd03312 160 FLKLSKAKGGGFdRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLATY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 243 FESL-DYYEEVVNLPVAAIGIDFVHDhGDSIKALKAHGFPeDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVADgKLI 321
Cdd:cd03312 240 FGSLgENLDLLASLPVDGLHLDLVRG-PENLEAVLKAGFA-DKVLSAGVVDGRNIWRADLAASLALLETLAAILGD-RLV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1254433488 322 VQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLEEITILTKA 365
Cdd:cd03312 317 VSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
432-754 |
2.16e-171 |
|
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: 495.42 E-value: 2.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 592 EALERNGIKVIQVDEPALREGLPLKQARWQKYLDDAVYSFKLTTASVQNDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTRKEPETIAALQDMIK 751
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMVD 320
|
...
gi 1254433488 752 ATK 754
Cdd:pfam01717 321 AAK 323
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
6-315 |
2.61e-168 |
|
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: 487.09 E-value: 2.61e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 6 SSNLGYPRLGEKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRF 85
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 86 QHDGGKVSLNTYFDIARGKNDAVASEMTKWFNTNYHYIVPEL-ADAEPKVLDNRALYYYEEAkKELGIEGKPVLVGPITY 164
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELdKDTEFKLNSNKLLDEYKEA-KALGIETKPVLLGPVTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 165 LKLGKGSDAK-SFEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQTYF 243
Cdd:pfam08267 160 LKLSKGKGGSfDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLATYF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1254433488 244 ESL-DYYEEVVNLPVAAIGIDFVHdHGDSIKALKAhGFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYV 315
Cdd:pfam08267 240 GSVaDALELLASLPVAGLGLDLVR-GPENLAALKK-GFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-759 |
4.96e-138 |
|
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: 409.92 E-value: 4.96e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 592 EALERNGIKVIQVDEPALREGLPlkqarwQKYLDDAVYSFKLTTASVQnDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVP-DTKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTR----KEPETIAALQ 747
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKLR 313
|
330
....*....|..
gi 1254433488 748 DMIKATKEVRAE 759
Cdd:COG0620 314 NMVAFAREVRGE 325
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
433-755 |
4.44e-128 |
|
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: 384.66 E-value: 4.44e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 433 PTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQKLAGFQATkf 512
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTK-RPVKGMLTAPVTIINWSFVRD---DVPESVVANQVGLALR 588
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 589 KEVEALERNGIKVIQVDEPALREGLPL-KQARWQKYLDDAVYSFKLTtasvQNDTQIHTHMCYSDF----------DDII 657
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLePDDLAADYLKWANEALADR----PDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 658 DTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTR 737
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATR 314
|
330
....*....|....*...
gi 1254433488 738 KEPETIAALQDMIKATKE 755
Cdd:cd03311 315 ERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
6-358 |
9.72e-88 |
|
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: 279.72 E-value: 9.72e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 6 SSNLGYPRLgekREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDtsvtfgiIPKRF 85
Cdd:COG0620 4 TTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGY-------FPERL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 86 qhDGgkvslntyFDIARGKNDavasemtKWFNTNYHYiVPELAD----AEPKVLDnralyYYEEAKKELGIEGKPVLVGP 161
Cdd:COG0620 74 --DG--------YAFARNGWV-------EWFDTNYHY-VPEITGdvsfSGPMTVE-----EFRFAKSLTGKPVKPVLPGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 162 ITYLKLGKGSDAKSFEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQT 241
Cdd:COG0620 131 VTLLLLSKVRDYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHLHT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 242 YFESLDY-YEEVVNLPVAAIGIDFVHDHGDSIKALKAhgFPEDKYLAAGVVDGRNVWRSDLDAKLELLTEIANYVADGKL 320
Cdd:COG0620 211 CYGGYEDiLEALAALPVDGIHLEFVRSRAGLLEPLKE--LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERL 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 1254433488 321 IVQPSNSLLHVPVTkLSEPDLDEVILGGLSFADQKLEE 358
Cdd:COG0620 289 WVSPDCGLKHRPVD-LTREEAWAKLRNMVAFAREVRGE 325
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
424-760 |
7.64e-69 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 229.86 E-value: 7.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 424 HAWLKLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQK 503
Cdd:PRK04326 1 MDHDKLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 504 LAGFqatKF-GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLT-KRPVKGMLTAPVTIINWSF--VRDDVPESVV 579
Cdd:PRK04326 81 IEGF---KFyGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFneYYKDKEELVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 580 AnqvgLA--LRKEVEALERNGIKVIQVDEPAL---REGLPLkqarwqkylddAVYSFKLTTASVqnDTQIHTHMCYSDFD 654
Cdd:PRK04326 158 D----LAkvINEEIKNLVEAGAKYIQIDEPALathPEDVEI-----------AVEALNRIVKGI--NAKLGLHVCYGDYS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 655 DIIDTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGL 734
Cdd:PRK04326 221 RIAPYILEFPVDQFDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGL 300
|
330 340
....*....|....*....|....*.
gi 1254433488 735 KTRKEPETIAALQDMIKATKEVRAEY 760
Cdd:PRK04326 301 KLLPREIAYQKLVNMVKATREVREEL 326
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
431-757 |
3.89e-37 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 141.28 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 431 LFPTTTIGSFPQSPEVRKTRADWLKGNI-TDAEYNAFIEKEtarwIKIQEDLDIDVLVHGEFeRTDMVEYFGQKLAGFQA 509
Cdd:PRK00957 1 IMITTVVGSYPVVKGEPETLKDKIKGFFgLYDPYKPAIEEA----VADQVKAGIDIISDGQV-RGDMVEIFASNMPGFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 510 tkfgwvQSYGSRaVRPPliygdvafTEEITVKESVYAQSLTK-----RPVKGMLTAPVTIINWS----FVRDDVPESVVA 580
Cdd:PRK00957 76 ------KRVIGR-VEPP--------AKPITLKDLKYAKKVAKkkdpnKGVKGIITGPSTLAYSLrvepFYSDNKDEELIY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 581 NqVGLALRKEVEALERNGIKVIQVDEPALREGLP-LKQARwqKYLDDAVYSFKLTTAsvqndtqihTHMCySDFDDIIDT 659
Cdd:PRK00957 141 D-LARALRKEAEALEKAGVAMIQIDEPILSTGAYdLEVAK--KAIDIITKGLNVPVA---------MHVC-GDVSNIIDD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 660 ISALDADVISIETSrSHGEIISTFEEVTY-DKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLktRK 738
Cdd:PRK00957 208 LLKFNVDILDHEFA-SNKKNLEILEEKDLiGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGM--RM 284
|
330 340
....*....|....*....|.
gi 1254433488 739 EPETIA--ALQDMIKATKEVR 757
Cdd:PRK00957 285 LPRDVAfeKLKNMVEAAREIR 305
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
433-751 |
3.35e-36 |
|
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: 138.79 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 433 PTTTIGSFPQSPEVRKTRadwlkgnITDAEYNAFIEKETARWIKiQEDLDIDVLVHGEFERTDMVEYFGqklagfqatkf 512
Cdd:cd00465 1 PVQCEGQTGIMEASETMA-------ISEEPGETSKAEWGITLVE-PEEIPLDVIPVHEDDVLKVAQALG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESV-YAQSLTKRPVKGMLTAPVTIINWSFVRDDV---------PESVVANQ 582
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEDPFREAPALEHItAVRSLEEFPTAGAAGGPFTFTHHSMSMGDAlmalyerpeAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 583 VGLALRKEVEALERNGIKVIQVDEPALREGLPLkqARWQKYLDDAVYSFKLTTASVQN-DTQIHTHMCYSDFDDiIDTIS 661
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSF--LGPKMFKKFALPAYKKVAEYKAAgEVPIVHHSCYDAADL-LEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 662 ALDADVISIETSRshGEIISTFEEVTYDKEIGLGVYDIHSPRvpTVTEIQDNIRRALRAIDaKQFWINPDCGLKTRK--E 739
Cdd:cd00465 219 QLGVDVISFDMTV--NEPKEAIEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLG-PHYIINPDCGLGPDSdyK 293
|
330
....*....|..
gi 1254433488 740 PETIAALQDMIK 751
Cdd:cd00465 294 PEHLRAVVQLVD 305
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
433-755 |
4.99e-33 |
|
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: 129.85 E-value: 4.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 433 PTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERtDMveyFGQKLAGFQATKF 512
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DM---IGRFLEVLVDLET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESV--VANQVGLALRKE 590
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPDAYedLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 591 VEALERNGIKVIQVDEPALREGLPLKQArWQKYLDDAVYSFKLttasvQNDTQIHTHMCYsdfDDIIDTISALDADVISI 670
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFE-DLEIVDAALEEVSL-----KSGGDVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 671 ETSRS---HGEIISTFEEVTY-DKEIGLGVYDIHSPRVPTVTEIQDnIRRALRAID------AKQFWINPDCGLKTRKEP 740
Cdd:cd03310 228 DAAALpskYLEDLKKLLRIGVrTLILGLVVTDNEAKGRNAWKEIER-LEKLVRRLEepgevlDEILYLTPDCGLAFLPPQ 306
|
330
....*....|....*
gi 1254433488 741 ETIAALQDMIKATKE 755
Cdd:cd03310 307 EARRKLALLAEAARE 321
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
434-756 |
7.25e-22 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 97.68 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 434 TTTIGSFpQSPEVRKTRADWLKGniTDaEYNAFIEKETARWIKIQEDLDID-VLVHGEFERTDMVEYFGQKLAGFQAtkF 512
Cdd:PRK01207 6 TQEIGSF-RKPEYLSREFHKIEG--TD-KFYELAERATLETLDVFENAGLDnIGIGGEMFRWEMYEHPAERIKGIIF--Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEVE 592
Cdd:PRK01207 80 GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFARIINEELK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 593 ALER------NGIKV-IQVDEPAlreglplkQARWQKYLDDAVYSFKLTTASVqnDTQIHTHMCYS-DFDDIIDTISALD 664
Cdd:PRK01207 160 DIKSawdrksPGRKLeIQIDEPA--------TTTHPDEMDIVVDSINKSVYGI--DNEFSIHVCYSsDYRLLYDRIPELN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 665 ADVISIETS-------------RSHGEIISTFEEVT----YDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAI-DAKQF 726
Cdd:PRK01207 230 IDGYNLEYSnrdtlepgtsdekRPGFQDLKYFAEHNeslqRKKFIGLGVTDVHIDYVEPVKLIEDRIRYALKIIkDPELV 309
|
330 340 350
....*....|....*....|....*....|
gi 1254433488 727 WINPDCGLKTRKEPETIAALQDMIKATKEV 756
Cdd:PRK01207 310 RLNPDCGLRTRSREIGEQKLRNMVAAKNNI 339
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
430-734 |
9.53e-18 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 85.12 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 430 PLFPTTTIGSFPQ-----SPEvrKTRADW-LKGN-ITDAEYNAfiekeTARWIKIQEDLDIDVLVHGEFERTDMVEYFGQ 502
Cdd:PRK09121 1 TLLPTSTAGSLPKpswlaEPE--TLWSPWkLQGEeLIEGKQDA-----LRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 503 KLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIInwsfvrDDVPESVVANQ 582
Cdd:PRK09121 74 HLSGVDFEKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMI------DTLYDDHYKSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 583 VGLA------LRKEVEALERNGIKVIQVDEPALRegLPLKQAR-WQ-KYLDDAVYSFKLTTAsvqndtqihTHMCYS--- 651
Cdd:PRK09121 148 EKLAwefakiLNQEAKELEAAGVDIIQFDEPAFN--VFFDEVNdWGvAALERAIEGLKCETA---------VHICYGygi 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 652 ---------------DFDDIIDTISALDADVISIETSRSH--GEIIstfeEVTYDKEIGLGVYDIHSPRVPTVTEIQDNI 714
Cdd:PRK09121 217 kantdwkktlgsewrQYEEAFPKLQKSNIDIISLECHNSRvpMDLL----ELIRGKKVMVGAIDVASDTIETPEEVADTL 292
|
330 340
....*....|....*....|
gi 1254433488 715 RRALRAIDAKQFWINPDCGL 734
Cdd:PRK09121 293 RKALQFVDADKLYPCTNCGM 312
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
21-335 |
9.57e-15 |
|
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: 75.93 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 21 KRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFsfYDQVLDTSVTFGIIPKRFqhdggkvslntyfdi 100
Cdd:cd03310 15 TKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQL--GDDMIGRFLEVLVDLETG--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 101 argkndavasemTKWFNTNYHYIVPELADAEPKVLDNRALYYYEEAKKElGIEGKPVLVGPITYLKLGKGSDAKSF--EV 178
Cdd:cd03310 78 ------------TRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKE-ALKVKVVVTGPLTLALLAFLPNGEPDayED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 179 LLDKFIPAYVEILKELEAAGAKWVQIDEP----YLATSFDKKEIALFEKVYQAFQTAVPnLKIELQTYfeslDYYEEVVN 254
Cdd:cd03310 145 LAKSLAEFLREQVKELKNRGIVVVQIDEPslgaVGAGAFEDLEIVDAALEEVSLKSGGD-VEVHLCAP----LDYEALLE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 255 LPVAAIGIDFV---HDHGDSIKALKAHGFpEDKYLAAGVVD----GRNVWR--SDLDAKLELLtEIANYVADGKLIVQPS 325
Cdd:cd03310 220 LGVDVIGFDAAalpSKYLEDLKKLLRIGV-RTLILGLVVTDneakGRNAWKeiERLEKLVRRL-EEPGEVLDEILYLTPD 297
|
330
....*....|
gi 1254433488 326 NSLLHVPVTK 335
Cdd:cd03310 298 CGLAFLPPQE 307
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
10-335 |
5.55e-13 |
|
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: 70.61 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 10 GYPRLGEKREWKRALEkfWNGTISEKELLAEtkilrlhaLKKQQDKGIDLIPVgdfsFYDQVLDTSVTFGIIPkrfqhdg 89
Cdd:cd00465 6 GQTGIMEASETMAISE--EPGETSKAEWGIT--------LVEPEEIPLDVIPV----HEDDVLKVAQALGEWA------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 90 gkvslntyfdiargkndavasemtkWFNTNYHYIVPELADAEPKVLDNRALYYYEEAKKELGIEGKPVLVGPITYLK-LG 168
Cdd:cd00465 65 -------------------------FRYYSQAPSVPEIDEEEDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHhSM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 169 KGSDAKS--------FEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATS--------FDKKEIALFEKVYQAFqtAV 232
Cdd:cd00465 120 SMGDALMalyerpeaMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQInsflgpkmFKKFALPAYKKVAEYK--AA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 233 PNLKIELQTYFESLDYYEEVVNLPVAAIGIDFVhdHGDSIKALKAHGfpEDKYLAAGVVDGRNVWRSDLDAKL--ELLTE 310
Cdd:cd00465 198 GEVPIVHHSCYDAADLLEEMIQLGVDVISFDMT--VNEPKEAIEKVG--EKKTLVGGVDPGYLPATDEECIAKveELVER 273
|
330 340
....*....|....*....|....*
gi 1254433488 311 IanyvaDGKLIVQPSNSLLHVPVTK 335
Cdd:cd00465 274 L-----GPHYIINPDCGLGPDSDYK 293
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
11-324 |
2.04e-11 |
|
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: 66.10 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 11 YPRlgeKREWKRALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSFYDQVLDtsvtFGiipkrfQHDGG 90
Cdd:cd03311 8 FPR---PKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEY----FL------ERLDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 91 kvslntyFDiargKNDAVASEMTKwfntnyhYIVPELADAEPKVLDNRALYYYEEAKKelGIEGKPV---LVGPIT---Y 164
Cdd:cd03311 75 -------FE----FTGWVQSYGSR-------YYKPPGIVGDVSRRPPMTVEEGKIAQS--LTHPKPLkgiLTGPVTipsP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 165 LKLGKGSDAKSFEVLLDKFIPAYVEILKELEAAGAKWVQIDEPYLATSFDKKEIALFEKVYQAFQTAVPNLKIELQ---- 240
Cdd:cd03311 135 SFVRFRGYYPSREELAMDLALALREEIRDLYDAGCRYIQIDEPALAEGLPLEPDDLAADYLKWANEALADRPDDTQihth 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 241 --------TYFESLDY---YEEVVNLPVAAIGIDFVHDHGDSIKALKAhgFPEDKYLAAGVVDGRNVWRSDLDAKLELLT 309
Cdd:cd03311 215 icygnfrsTWAAEGGYepiAEYIFELDVDVFFLEYDNSRAGGLEPLKE--LPYDKKVGLGVVDVKSPEVESPEEVKDRIE 292
|
330
....*....|....*
gi 1254433488 310 EIANYVADGKLIVQP 324
Cdd:cd03311 293 EAAKYVPLEQLWVSP 307
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
22-295 |
7.72e-11 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 63.99 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 22 RALEKFWNGTISEKELLAETKILRLHALKKQQDKGIDLIPVGDFSfYDQVLDtsVTFGIIpkrfqhDGGKVSlntyfdia 101
Cdd:PRK08575 19 KVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFR-WDDIFD--PTISFI------SGVEKG-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 102 rgkndavasEMTKWFNTNYHYIVPELADAEPKVLDNRALYYYEEA---KKELGIEG--KPVLVGPITYLKLGKGSDAKSF 176
Cdd:PRK08575 82 ---------GLQRFYDNNFYYRQPVIKEKINLKEENPYLQWLESAreiKEEVSLESklKAVLPGPLTYAVLSDNEYYKNL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 177 EVLLDKFIPAYVEILKELEaAGAKWVQIDEPYLATSFDKKeiALFEKVYQAFQTAVPNLKIE--LQTYF--ESLDYYEEV 252
Cdd:PRK08575 153 IELMEDYASVVNSLIKELS-SVVDAVEIHEPSIFAKGIKR--DTLEKLPEVYKTMAKNVNIEkhLMTYFeiNNLKRLDIL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1254433488 253 VNLPVAAIGIDFVhdhgDSIKAL-KAHGFPEDKYLAAGVVDGRN 295
Cdd:PRK08575 230 FSLPVTYFGIDVI----ENLKKLgRVYTYLKGRKVYLGILNARN 269
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
191-324 |
6.92e-10 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 61.15 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 191 LKELEAAGAKWVQIDEPYLATSFDKKEIALfekvyQAFQTAVPNLKIELQTYFESLDY---YEEVVNLPVAAIGIDFVHD 267
Cdd:PRK04326 167 IKNLVEAGAKYIQIDEPALATHPEDVEIAV-----EALNRIVKGINAKLGLHVCYGDYsriAPYILEFPVDQFDLEFANG 241
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1254433488 268 HGDSIKALKAHGFpeDKYLAAGVVDGRNvwrsdldAKLELLTEIANYVADGKLIVQP 324
Cdd:PRK04326 242 NYKLLDLLKEYGF--DKELGLGVIDVHS-------ARVESVEEIKEAIKKGLEYVPP 289
|
|
| HemE |
COG0407 |
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
121-275 |
1.13e-03 |
|
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 41.75 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 121 HYIVPELADAE----PKVLDNRALYYYE---EAKKELGIEgKPVLV---GPIT---YLKLG----KG---SDAKSFEVLL 180
Cdd:COG0407 92 EHPIRDAEDVDalevPDPEDGRLPYVLEairLLKEELGDE-VPLIGfagGPFTlasYLVEGfeklKKlmyRDPELVHALL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 181 DKFIPAYVEILKELEAAGAKWVQIDEPyLATSFDKKeiaLFEK-VYQAFQTAVPNLK---IELQTYFE--SLDYYEEVVN 254
Cdd:COG0407 171 DKLTDAVIEYLKAQIEAGADAVQIFDS-WAGLLSPK---DFEEfVLPYLKRIVDALKergVPVIIHFCgdGTPLLEDMAE 246
|
170 180
....*....|....*....|.
gi 1254433488 255 LPVAAIGIDFVHDHGDSIKAL 275
Cdd:COG0407 247 TGADALSVDWRVDLAEAKERL 267
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
432-719 |
7.88e-03 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 39.33 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEDLDIDVLVHGEFERTDMVEYFGQKLAGfqATK 511
Cdd:PRK08575 3 IKKALVGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISG--VEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 512 FGWVQSYGSR-AVRPPLIYGDVAFTEEIT----------VKESVYAQSLTKRPVKGMLTAPVTIINWSFvrDDVPESVva 580
Cdd:PRK08575 81 GGLQRFYDNNfYYRQPVIKEKINLKEENPylqwlesareIKEEVSLESKLKAVLPGPLTYAVLSDNEYY--KNLIELM-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254433488 581 nqvgLALRKEVEALERN---GIKVIQVDEPALREGlPLKQARWQKylDDAVYsfKLTTASVQNDTQIHTHMCYSDFDDIi 657
Cdd:PRK08575 157 ----EDYASVVNSLIKElssVVDAVEIHEPSIFAK-GIKRDTLEK--LPEVY--KTMAKNVNIEKHLMTYFEINNLKRL- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1254433488 658 DTISALDADVISIETSRSHGEIISTFEEVTyDKEIGLGVYDIHSPRVPTVTEIQDNIRRALR 719
Cdd:PRK08575 227 DILFSLPVTYFGIDVIENLKKLGRVYTYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKR 287
|
|
| |
