|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
1-765 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1623.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 1 MASHIVGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPP 80
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 81 RYGWTGGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVS 160
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 161 YLLLSKPAKGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLV 240
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 241 ETYFADVPAEAYKTLTSLKGVTAYGFDLVRGTKTLDLIK-GDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGK 319
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 320 DNLVVSTSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKALAGNKDEAFFTANGQAHASRKSSPRVTNEGVQ 399
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 400 KAAAALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQE 479
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 480 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTVNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLT 559
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 560 GPVTILNWSFVRVDQPRSETCYQIALAIKDEVEDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGVQ 639
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 640 DTTQIHTHMCYSNFNDIIQSIINMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 719
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1229801197 720 AVLETNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQLASAK 765
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
6-760 |
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: 1288.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 6 VGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPPRYGWT 85
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 86 GGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVSYLLLS 165
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 166 KpakGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLVETYFA 245
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 246 DVPAeAYKTLTSLKgVTAYGFDLVRGTKTLDLIKGDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGKdnLVVS 325
Cdd:TIGR01371 238 SVGD-ALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 326 TSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKALAGNKDEAFFT--ANGQAHASRKSSPRVTNEGVQKAAA 403
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFAleANAAAIAARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 404 ALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDI 483
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 484 DVLVHGEPERNDMVEYFGEQLSGFAFTVNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVT 563
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 564 ILNWSFVRVDQPRSETCYQIALAIKDEVEDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGVQDTTQ 643
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 644 IHTHMCYSNFNDIIQSIINMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLE 723
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 1229801197 724 TNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQ 760
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
3-367 |
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: 601.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 3 SHIVGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPPRY 82
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 83 GWTGGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVSYL 162
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 163 LLSkpaKGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLVET 242
Cdd:cd03312 162 KLS---KAKGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 243 YFADVpAEAYKTLTSLkGVTAYGFDLVRGTKTLDLIKGDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGkDNL 322
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1229801197 323 VVSTSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKA 367
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
432-755 |
0e+00 |
|
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: 560.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 432 LPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTV 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 512 NGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQPRSETCYQIALAIKDEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 592 EDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGVQDTTQIHTHMCYSNFNDIIQSIINMDADVITIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKTRKYGEVNPALKNMV 751
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 1229801197 752 AAAK 755
Cdd:pfam01717 320 DAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-760 |
4.69e-150 |
|
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: 440.73 E-value: 4.69e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 432 LPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTV 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 512 NGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQPRSETCYQIALAIKDEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 592 EDLEKAGINVIQIDEAALREGLPlrkseqSFYLDWAVHSFRITNCGVQDtTQIHTHMCYSNFNDIIQSIINMDADVITIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKTRKYG----EVNPAL 747
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVDltreEAWAKL 312
|
330
....*....|...
gi 1229801197 748 KNMVAAAKLLRTQ 760
Cdd:COG0620 313 RNMVAFAREVRGE 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
1-765 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1623.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 1 MASHIVGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPP 80
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 81 RYGWTGGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVS 160
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 161 YLLLSKPAKGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLV 240
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 241 ETYFADVPAEAYKTLTSLKGVTAYGFDLVRGTKTLDLIK-GDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGK 319
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 320 DNLVVSTSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKALAGNKDEAFFTANGQAHASRKSSPRVTNEGVQ 399
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 400 KAAAALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQE 479
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 480 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTVNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLT 559
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 560 GPVTILNWSFVRVDQPRSETCYQIALAIKDEVEDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGVQ 639
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 640 DTTQIHTHMCYSNFNDIIQSIINMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 719
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1229801197 720 AVLETNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQLASAK 765
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-763 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1355.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 1 MASHIVGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPP 80
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 81 RYGWTGGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVS 160
Cdd:PRK05222 82 RFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 161 YLLLSKpakGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLV 240
Cdd:PRK05222 162 FLWLSK---SKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 241 ETYFADVpAEAYKTLTSLkGVTAYGFDLVRGTKTLDLIKGDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVgkD 320
Cdd:PRK05222 239 ATYFGSL-NDALDLLASL-PVDGLHLDLVRGPEQLAALLKYFPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV--D 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 321 NLVVSTSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKALAGNKD--EAFFTANGQAHASRKSSPRVTNEGV 398
Cdd:PRK05222 315 RLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGavAEALAANRAAIAARRTSPRVHNPAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 399 QKAAAALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQ 478
Cdd:PRK05222 395 RARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 479 EELDIDVLVHGEPERNDMVEYFGEQLSGFAFTVNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGML 558
Cdd:PRK05222 475 EELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGML 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 559 TGPVTILNWSFVRVDQPRSETCYQIALAIKDEVEDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGV 638
Cdd:PRK05222 555 TGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGV 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 639 QDTTQIHTHMCYSNFNDIIQSIINMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKM 718
Cdd:PRK05222 635 KDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFED-FGYPNEIGPGVYDIHSPRVPSVEEIEELLRKA 713
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1229801197 719 LAVLETNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQLAS 763
Cdd:PRK05222 714 LEVIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
6-760 |
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: 1288.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 6 VGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPPRYGWT 85
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 86 GGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVSYLLLS 165
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 166 KpakGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLVETYFA 245
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 246 DVPAeAYKTLTSLKgVTAYGFDLVRGTKTLDLIKGDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGKdnLVVS 325
Cdd:TIGR01371 238 SVGD-ALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 326 TSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKALAGNKDEAFFT--ANGQAHASRKSSPRVTNEGVQKAAA 403
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFAleANAAAIAARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 404 ALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDI 483
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 484 DVLVHGEPERNDMVEYFGEQLSGFAFTVNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVT 563
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 564 ILNWSFVRVDQPRSETCYQIALAIKDEVEDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGVQDTTQ 643
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 644 IHTHMCYSNFNDIIQSIINMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLE 723
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 1229801197 724 TNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQ 760
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
3-367 |
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: 601.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 3 SHIVGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPPRY 82
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 83 GWTGGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVSYL 162
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 163 LLSkpaKGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLVET 242
Cdd:cd03312 162 KLS---KAKGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 243 YFADVpAEAYKTLTSLkGVTAYGFDLVRGTKTLDLIKGDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGkDNL 322
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1229801197 323 VVSTSCSLLHTAVDLVNETKLDNEIKSWLAFAAQKIVEVNALAKA 367
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
432-755 |
0e+00 |
|
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: 560.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 432 LPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTV 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 512 NGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQPRSETCYQIALAIKDEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 592 EDLEKAGINVIQIDEAALREGLPLRKSEQSFYLDWAVHSFRITNCGVQDTTQIHTHMCYSNFNDIIQSIINMDADVITIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKTRKYGEVNPALKNMV 751
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 1229801197 752 AAAK 755
Cdd:pfam01717 320 DAAK 323
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
3-317 |
1.09e-172 |
|
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: 498.26 E-value: 1.09e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 3 SHIVGYPRMGPKRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGAVPPRY 82
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 83 GWTGGEIGFDTYFSMARGNASVPAMEMTKWFDTNYHFIVPELGPEVKFSYASHKAVDEYKEAKALGVDTVPVLVGPVSYL 162
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 163 LLSkpaKGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLVET 242
Cdd:pfam08267 161 KLS---KGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLAT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1229801197 243 YFADVpAEAYKTLTSLkGVTAYGFDLVRGTKTLDLIKGDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIV 317
Cdd:pfam08267 238 YFGSV-ADALELLASL-PVAGLGLDLVRGPENLAALKKGFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
433-756 |
1.65e-150 |
|
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: 442.44 E-value: 1.65e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 433 PTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTvn 512
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 513 GWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTA-RPMKGMLTGPVTILNWSFVR---VDQPRSETCYQIALAIK 588
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRfrgYYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 589 DEVEDLEKAGINVIQIDEAALREGLPLRK-SEQSFYLDWAVHSFRitncGVQDTTQIHTHMCYSNF----------NDII 657
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALA----DRPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 658 QSIINMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKT 737
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKE-LPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFAT 313
|
330
....*....|....*....
gi 1229801197 738 RKYGEVNPALKNMVAAAKL 756
Cdd:cd03311 314 RERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-760 |
4.69e-150 |
|
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: 440.73 E-value: 4.69e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 432 LPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTV 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 512 NGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQPRSETCYQIALAIKDEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 592 EDLEKAGINVIQIDEAALREGLPlrkseqSFYLDWAVHSFRITNCGVQDtTQIHTHMCYSNFNDIIQSIINMDADVITIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKTRKYG----EVNPAL 747
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVDltreEAWAKL 312
|
330
....*....|...
gi 1229801197 748 KNMVAAAKLLRTQ 760
Cdd:COG0620 313 RNMVAFAREVRGE 325
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
2-357 |
7.24e-89 |
|
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: 282.41 E-value: 7.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 2 ASHIVGYPRMgpkRELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDqvldttaMLGAVPPR 81
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 82 ygwtggeigFDTYfSMARgNASVpamemtKWFDTNYHfIVPELGPEVKFSyaSHKAVDEYKEAKAL-GVDTVPVLVGPVS 160
Cdd:COG0620 73 ---------LDGY-AFAR-NGWV------EWFDTNYH-YVPEITGDVSFS--GPMTVEEFRFAKSLtGKPVKPVLPGPVT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 161 YLLLSKPAKGVDKtfslLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSSAYAELESALSGLNVLV 240
Cdd:COG0620 133 LLLLSKVRDYKDR----EELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 241 ETYFADVpAEAYKTLTSLKgVTAYGFDLVRGT-KTLDLIKgDFPKGKHLFAGVVDGRNIWANDLAASVSTLEELAGIVGK 319
Cdd:COG0620 209 HTCYGGY-EDILEALAALP-VDGIHLEFVRSRaGLLEPLK-ELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPP 285
|
330 340 350
....*....|....*....|....*....|....*...
gi 1229801197 320 DNLVVSTSCSLLHTAVDLVNEtKLDNEIKSWLAFAAQK 357
Cdd:COG0620 286 ERLWVSPDCGLKHRPVDLTRE-EAWAKLRNMVAFAREV 322
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
428-761 |
4.43e-80 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 259.52 E-value: 4.43e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 428 NLPILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGF 507
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 508 AFtvNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTA-RPMKGMLTGPVTILNWSFVRVDQPRSETCYQIALA 586
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTYtRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 587 IKDEVEDLEKAGINVIQIDEAAlregLPLRKSEqsfyLDWAVHSFRITNCGVQdtTQIHTHMCYSNFNDIIQSIINMDAD 666
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPA----LATHPED----VEIAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEFPVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 667 VITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKTRKYGEVNPA 746
Cdd:PRK04326 233 QFDLEFANGNYKLLDLLKE-YGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQK 311
|
330
....*....|....*
gi 1229801197 747 LKNMVAAAKLLRTQL 761
Cdd:PRK04326 312 LVNMVKATREVREEL 326
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
433-756 |
1.65e-38 |
|
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: 145.65 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 433 PTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERnDMVEYFGEQLSGFAFtvn 512
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 513 GWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQP--RSETCYQIALAIKDE 590
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 591 VEDLEKAGINVIQIDEAALREGLPLRKSEQSfYLDWAvhsfrITNCGVQDTTQIHTHMCYsnfNDIIQSIINMDADVITI 670
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAA-----LEEVSLKSGGDVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 671 ENSRSD-------EKLLSVFREGVKYGAGIGPGVYDIHSPR--IPSTEEIADRINKMLAVLETnILWVNPDCGLKTRKYG 741
Cdd:cd03310 228 DAAALPskyledlKKLLRIGVRTLILGLVVTDNEAKGRNAWkeIERLEKLVRRLEEPGEVLDE-ILYLTPDCGLAFLPPQ 306
|
330
....*....|....*
gi 1229801197 742 EVNPALKNMVAAAKL 756
Cdd:cd03310 307 EARRKLALLAEAARE 321
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
431-758 |
9.51e-33 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 128.57 E-value: 9.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 431 ILPTTTIGSFPQTVELRRVRREYKANKIS-EEEYVKAIKEeinkVVKLQEELDIDVLVHGEPeRNDMVEYFGEQLSGF-A 508
Cdd:PRK00957 1 IMITTVVGSYPVVKGEPETLKDKIKGFFGlYDPYKPAIEE----AVADQVKAGIDIISDGQV-RGDMVEIFASNMPGFdG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 509 FTVNGWVQSygsrcVKPPIIYGDVSRPKpmtvfwSTAAQSMTARPMKGMLTGPVTILnwSFVRV-----DQPRSETCYQI 583
Cdd:PRK00957 76 KRVIGRVEP-----PAKPITLKDLKYAK------KVAKKKDPNKGVKGIITGPSTLA--YSLRVepfysDNKDEELIYDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 584 ALAIKDEVEDLEKAGINVIQIDEAALREGLPlrkseqsfYLDWAVHSFRITNCGVQDTTQIHThmCySNFNDIIQSIINM 663
Cdd:PRK00957 143 ARALRKEAEALEKAGVAMIQIDEPILSTGAY--------DLEVAKKAIDIITKGLNVPVAMHV--C-GDVSNIIDDLLKF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 664 DADVITIENSRSDEKLlSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNILWVNPDCGLKTRKYGEV 743
Cdd:PRK00957 212 NVDILDHEFASNKKNL-EILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMRMLPRDVA 290
|
330
....*....|....*
gi 1229801197 744 NPALKNMVAAAKLLR 758
Cdd:PRK00957 291 FEKLKNMVEAAREIR 305
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
433-755 |
1.66e-30 |
|
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: 122.22 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 433 PTTTIGSFPQTVELRRVRreykankISEEEYVKAIKEEINKVVkLQEELDIDVLVHGEpernDMVEYFGEQLsgfaftvN 512
Cdd:cd00465 1 PVQCEGQTGIMEASETMA-------ISEEPGETSKAEWGITLV-EPEEIPLDVIPVHE----DDVLKVAQAL-------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 513 GWVQSYGSRCVKPPIIYGDV-SRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVD---------QPRSETCYQ 582
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEdPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmalyerpEAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 583 IALAIKDEVEDLEKAGINVIQIDEAALREGLPLRKSEqsFYLDWAVHSFR-ITNCGVQDTTQIHTHMCYSNfNDIIQSII 661
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPK--MFKKFALPAYKkVAEYKAAGEVPIVHHSCYDA-ADLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 662 NMDADVITIENSRSDEKLLsvfREGVKYGAGIGPGVYDIHSPRipSTEEIADRINKMLAVLETNIlWVNPDCGLKTRKYG 741
Cdd:cd00465 219 QLGVDVISFDMTVNEPKEA---IEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLGPHY-IINPDCGLGPDSDY 292
|
330
....*....|....
gi 1229801197 742 EVnPALKNMVAAAK 755
Cdd:cd00465 293 KP-EHLRAVVQLVD 305
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
430-762 |
2.53e-22 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 98.99 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 430 PILPTTTIGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAF 509
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 510 TVNGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQPRSETCYQIALAIKD 589
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 590 EVEDLEKAGINVIQIDEAALreglplrkseqSFYL----DWAVHSFRITNCGVQDTTQIHthMCY-----SN-------- 652
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAF-----------NVFFdevnDWGVAALERAIEGLKCETAVH--ICYgygikANtdwkktlg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 653 ---------FNDIIQSIInmdaDVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSTEEIADRINKMLAV 721
Cdd:PRK09121 228 sewrqyeeaFPKLQKSNI----DIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVASDTIETPEEVADTLRKALQF 298
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1229801197 722 LETNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQLA 762
Cdd:PRK09121 299 VDADKLYPCTNCGMAPLSRDVARGKLNALSAGAEIVRRELA 339
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
429-761 |
4.07e-22 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 98.45 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 429 LPILPTTTIGSF--PQ--TVELRRVRREYKANKISEeeyvKAIKEEINkvVKLQEELDiDVLVHGEPERNDMVEYFGEQL 504
Cdd:PRK01207 1 MAALITQEIGSFrkPEylSREFHKIEGTDKFYELAE----RATLETLD--VFENAGLD-NIGIGGEMFRWEMYEHPAERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 505 SGFAFTvnGWVQSYGSRCVKPPIIYGDVSRPKPMTVFWSTAAQSMTARPMKGMLTGPVTILNWSFVRVDQPRSETCYQIA 584
Cdd:PRK01207 74 KGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 585 LAIKDEVEDLEKAGINV-------IQIDEAAlreglplrKSEQSFYLDWAVHSFRITNCGVQDttQIHTHMCYSN----F 653
Cdd:PRK01207 152 RIINEELKDIKSAWDRKspgrkleIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDN--EFSIHVCYSSdyrlL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 654 NDIIQSiINMD------ADVITIENSRSDE--------KLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 719
Cdd:PRK01207 222 YDRIPE-LNIDgynleySNRDTLEPGTSDEkrpgfqdlKYFAEHNESLQRKKFIGLGVTDVHIDYVEPVKLIEDRIRYAL 300
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1229801197 720 AVL-ETNILWVNPDCGLKTRKYGEVNPALKNMVAAAKLLRTQL 761
Cdd:PRK01207 301 KIIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
15-345 |
1.89e-11 |
|
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: 65.91 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 15 RELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFayYDQVLD-TTAMLGAVPPRygwtggeigfdt 93
Cdd:cd03310 12 DGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQL--GDDMIGrFLEVLVDLETG------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 94 yfsmargnasvpamemTKWFDTNYHFIVPELGPEVkFSYASHKAVDEYKEAKALGVDTVPVLVGPVSYLLLSKPAKGvdK 173
Cdd:cd03310 78 ----------------TRFFDNNFFYRPPEAKIEA-FLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNG--E 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 174 TFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKL-QAFSSAYAELESALSGLNVLVETYFADVPAEAY 252
Cdd:cd03310 139 PDAYEDLAKSLAEFLREQVKELKNRGIVVVQIDEPSLGAVGAGAFEdLEIVDAALEEVSLKSGGDVEVHLCAPLDYEALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 253 KTltslkGVTAYGFDLVRGTKTLDLIKGDFPK----GKHLFAGVVD----GRNIW--ANDLAASVSTLEELaGIVGKDNL 322
Cdd:cd03310 219 EL-----GVDVIGFDAAALPSKYLEDLKKLLRigvrTLILGLVVTDneakGRNAWkeIERLEKLVRRLEEP-GEVLDEIL 292
|
330 340
....*....|....*....|...
gi 1229801197 323 VVSTSCSLLHTAVDLVnETKLDN 345
Cdd:cd03310 293 YLTPDCGLAFLPPQEA-RRKLAL 314
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
2-345 |
7.11e-09 |
|
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: 58.01 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 2 ASHIVGYPRmgPKrELKFALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIPSNTFAYYDQVLDTTAMLGavppr 81
Cdd:cd03311 2 TTTVGSFPR--PK-ELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 82 ygwtggeiGFDTYfsmargnasvpamEMTKWFDTNYHFIVPELGPEvkfSYASHKAVDEYKEAKALgVDTVPV---LVGP 158
Cdd:cd03311 74 --------GFEFT-------------GWVQSYGSRYYKPPGIVGDV---SRRPPMTVEEGKIAQSL-THPKPLkgiLTGP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 159 VSYLLLS-KPAKGVDKTFSllSLLDKILPIYKEVVSDLKAAGATWIQFDEPTL--VMDLDSHKLQAfssAYAEL---ESA 232
Cdd:cd03311 129 VTIPSPSfVRFRGYYPSRE--ELAMDLALALREEIRDLYDAGCRYIQIDEPALaeGLPLEPDDLAA---DYLKWaneALA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 233 LSGLNVLV----------ETYFADVPAEayKTLTSLKGVTAYGFDL---VRGTKTLDLIKgDFPKGKHLFAGVVDGRNIW 299
Cdd:cd03311 204 DRPDDTQIhthicygnfrSTWAAEGGYE--PIAEYIFELDVDVFFLeydNSRAGGLEPLK-ELPYDKKVGLGVVDVKSPE 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1229801197 300 ANDLAASVSTLEELAGIVGKDNLVVSTSCSLLHTAVDLVnETKLDN 345
Cdd:cd03311 281 VESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATRERGNA-LTKLEN 325
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
5-297 |
1.05e-06 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 5 IVG-YPRmgPKRELKfALESFWDGKSSADDLKKVAADLRSSIWKQMADAGIKYIpsntfayydqvldTTAMlgavpprYG 83
Cdd:PRK08575 7 LVGsYPR--PVKLAK-VISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYT-------------TDGL-------FR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 84 WTggEIgFDTYFSMARGnasVPAMEMTKWFDTNYHF----IVPELGPEVKFSYA-SHKAVDEYKEAKALGVDTVPVLVGP 158
Cdd:PRK08575 64 WD--DI-FDPTISFISG---VEKGGLQRFYDNNFYYrqpvIKEKINLKEENPYLqWLESAREIKEEVSLESKLKAVLPGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 159 VSYLLLSkpakgvDKTFslLSLLDKILPIYKEVVSDLKAA---GATWIQFDEPTLVM-DLDSHKLQAFSSAYAELESALS 234
Cdd:PRK08575 138 LTYAVLS------DNEY--YKNLIELMEDYASVVNSLIKElssVVDAVEIHEPSIFAkGIKRDTLEKLPEVYKTMAKNVN 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229801197 235 GLNVLVeTYFADVPAEAYKTLTSLKgVTAYGFDLVRGTKTLDLIKGDFpKGKHLFAGVVDGRN 297
Cdd:PRK08575 210 IEKHLM-TYFEINNLKRLDILFSLP-VTYFGIDVIENLKKLGRVYTYL-KGRKVYLGILNARN 269
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
86-337 |
6.83e-05 |
|
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: 45.57 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 86 GGEIGFDTYFSMARGNASVP-AMEMTKWFDTNYHFIVPE-LGPEVKFSYAshKAVDEYKEAKALG-VDTVPVLVGPVSYL 162
Cdd:cd00465 38 PEEIPLDVIPVHEDDVLKVAqALGEWAFRYYSQAPSVPEiDEEEDPFREA--PALEHITAVRSLEeFPTAGAAGGPFTFT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 163 LLSK-----PAKGVDKTFSLLSLLDKILPIYKEVVSDLKAAGATWIQFDEPTLVMDLDSHKLQAFSS----AYAELESAL 233
Cdd:cd00465 116 HHSMsmgdaLMALYERPEAMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPKMFKKfalpAYKKVAEYK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 234 SGLNVLVETYFADVPAEAYKTLTSLkGVTAYGFDLVRG-TKTLdliKGDFPKGKHLFAGVVDGRNIWAN--DLAASVSTL 310
Cdd:cd00465 196 AAGEVPIVHHSCYDAADLLEEMIQL-GVDVISFDMTVNePKEA---IEKVGEKKTLVGGVDPGYLPATDeeCIAKVEELV 271
|
250 260
....*....|....*....|....*..
gi 1229801197 311 EELAGivgkdNLVVSTSCSLLHTAVDL 337
Cdd:cd00465 272 ERLGP-----HYIINPDCGLGPDSDYK 293
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
437-726 |
9.21e-05 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 45.11 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 437 IGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGfaFTVNGWVQ 516
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISG--VEKGGLQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 517 SYGSRCV-KPPIIYGDVSRPKPMT-VFWSTAAQSMTAR-----PMKGMLTGPVTILNWSFVRVDQPRSETCYQIALAIKD 589
Cdd:PRK08575 86 FYDNNFYyRQPVIKEKINLKEENPyLQWLESAREIKEEvslesKLKAVLPGPLTYAVLSDNEYYKNLIELMEDYASVVNS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 590 EVEDLeKAGINVIQIDEAALREG---LPLRKSEQSFYLDWAVhsfritncGVQDTTQIHTHMCYSNFnDIIQSIINMDAD 666
Cdd:PRK08575 166 LIKEL-SSVVDAVEIHEPSIFAKgikRDTLEKLPEVYKTMAK--------NVNIEKHLMTYFEINNL-KRLDILFSLPVT 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 667 VITIENSRSDEKLLSVFrEGVKyGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLETNI 726
Cdd:PRK08575 236 YFGIDVIENLKKLGRVY-TYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKRKGVSDI 293
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
187-330 |
6.53e-03 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 39.58 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 187 IYKEVvSDLKAAGATWIQFDEPTLVMDLDSHKL--QAFSSAYAELESALsGLNV------LVETYFADVPaeayktltsl 258
Cdd:PRK04326 163 INEEI-KNLVEAGAKYIQIDEPALATHPEDVEIavEALNRIVKGINAKL-GLHVcygdysRIAPYILEFP---------- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229801197 259 kgVTAYGFDLV-RGTKTLDLIKgDFPKGKHLFAGVVDGRNiwandlaASVSTLEELAG-------IVGKDNLVVSTSCSL 330
Cdd:PRK04326 231 --VDQFDLEFAnGNYKLLDLLK-EYGFDKELGLGVIDVHS-------ARVESVEEIKEaikkgleYVPPEKLYINPDCGL 300
|
|
| PRK06233 |
PRK06233 |
vitamin B12 independent methionine synthase; |
437-509 |
7.18e-03 |
|
vitamin B12 independent methionine synthase;
Pssm-ID: 180482 Cd Length: 372 Bit Score: 39.31 E-value: 7.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1229801197 437 IGSFPQTVELRRVRREYKANKISEEEYVKAIKEEINKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAF 509
Cdd:PRK06233 14 VGSFLRPERLKEAREQFAIGEISQDQLLKIQHAEIKRLVKEQVELGLKAVTDGEFNRSWWHLDFLWGLNGVGK 86
|
|
| |
