|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
53-817 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1650.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 53 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPP 132
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 133 RYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 212
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 213 YLLLSKPAKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 292
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 293 ETYFADVPVEAYKTLTSLKSVTGFGFDLVRGTKTLELIK-GGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGK 371
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 372 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQASRKSSPRVTNEAVQ 451
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 452 KAAVALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQE 531
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 532 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLT 611
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 612 GPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVE 691
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 692 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKML 771
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1375852693 772 AVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGSAQ 817
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
58-812 |
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: 1284.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 58 VGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRYGWN 137
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 138 GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLS 217
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 218 KpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVETYFA 297
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 298 DVPvEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGKdkLVVS 377
Cdd:TIGR01371 238 SVG-DALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 378 TSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQA--SRKSSPRVTNEAVQKAAV 455
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 456 ALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDI 535
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 536 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVT 615
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 616 ILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQ 695
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 696 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLE 775
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 1375852693 776 SNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTK 812
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
55-419 |
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: 595.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 55 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 134
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 135 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 214
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 215 LLSKPAKGvekSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 294
Cdd:cd03312 162 KLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 295 YFADVpVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGkDKL 374
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1375852693 375 VVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKA 419
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
484-807 |
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: 557.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 484 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 563
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 564 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 643
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 644 EDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIE 723
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 724 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPALSNMV 803
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 1375852693 804 AAAK 807
Cdd:pfam01717 320 DAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
484-810 |
1.77e-144 |
|
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: 428.02 E-value: 1.77e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 484 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 563
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 564 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 643
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 644 EDLEKAGITVIQIDEAALREGLPlrksehAFYLNWAVHSFRITNCGVEDtTQIHTHMCYSNFNDIIHSIIDMDADVITIE 723
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 724 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTR----KYAEVKPAL 799
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
330
....*....|.
gi 1375852693 800 SNMVAAAKHLR 810
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
53-817 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1650.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 53 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPP 132
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 133 RYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 212
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 213 YLLLSKPAKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 292
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 293 ETYFADVPVEAYKTLTSLKSVTGFGFDLVRGTKTLELIK-GGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGK 371
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 372 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQASRKSSPRVTNEAVQ 451
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 452 KAAVALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQE 531
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 532 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLT 611
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 612 GPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVE 691
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 692 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKML 771
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1375852693 772 AVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGSAQ 817
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASAK 766
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
52-815 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1352.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 52 AMASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVP 131
Cdd:PRK05222 1 MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 132 PRYGWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPV 211
Cdd:PRK05222 81 ERFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 212 SYLLLSKpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVL 291
Cdd:PRK05222 161 TFLWLSK---SKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 292 VETYFADVpVEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVgk 371
Cdd:PRK05222 238 LATYFGSL-NDALDLLASLP-VDGLHLDLVRGPEQLAALLKYFPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 372 DKLVVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQD--EAFFSANAAAQASRKSSPRVTNEA 449
Cdd:PRK05222 314 DRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGavAEALAANRAAIAARRTSPRVHNPA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 450 VQKAAVALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKI 529
Cdd:PRK05222 394 VRARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 530 QEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGM 609
Cdd:PRK05222 474 QEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 610 LTGPVTILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCG 689
Cdd:PRK05222 554 LTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 690 VEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEK 769
Cdd:PRK05222 634 VKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFED-FGYPNEIGPGVYDIHSPRVPSVEEIEELLRK 712
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1375852693 770 MLAVLESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKLGS 815
Cdd:PRK05222 713 ALEVIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
58-812 |
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: 1284.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 58 VGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRYGWN 137
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 138 GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLS 217
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 218 KpakGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVETYFA 297
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 298 DVPvEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGKdkLVVS 377
Cdd:TIGR01371 238 SVG-DALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 378 TSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKALAGQQDEAFFSANAAAQA--SRKSSPRVTNEAVQKAAV 455
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 456 ALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDI 535
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 536 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVT 615
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 616 ILNWSFVRNDQPRFETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQ 695
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 696 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLE 775
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 1375852693 776 SNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTK 812
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
55-419 |
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: 595.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 55 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 134
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 135 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 214
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 215 LLSKPAKGvekSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 294
Cdd:cd03312 162 KLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 295 YFADVpVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGkDKL 374
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1375852693 375 VVSTSCSLLHTAVDLVNEPKLDKEIKSWLAFAAQKVVEVNALAKA 419
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
484-807 |
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: 557.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 484 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 563
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 564 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 643
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 644 EDLEKAGITVIQIDEAALREGLPLRKSEHAFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFNDIIHSIIDMDADVITIE 723
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 724 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPALSNMV 803
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 1375852693 804 AAAK 807
Cdd:pfam01717 320 DAAK 323
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
55-369 |
4.21e-175 |
|
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: 505.96 E-value: 4.21e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 55 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDQVLDTTAMLGAVPPRY 134
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 135 GWNGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 214
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 215 LLSkpaKGVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLVET 294
Cdd:pfam08267 161 KLS---KGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLAT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375852693 295 YFADVpVEAYKTLTSLKsVTGFGFDLVRGTKTLELIKGGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIV 369
Cdd:pfam08267 238 YFGSV-ADALELLASLP-VAGLGLDLVRGPENLAALKKGFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
485-807 |
1.57e-147 |
|
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: 436.27 E-value: 1.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 485 PTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTan 564
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 565 GWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTK-RPMKGMLTGPVTILNWSFVRN---DQPRFETCYQIALAIK 640
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 641 DEVEDLEKAGITVIQIDEAALREGLPLRK-SEHAFYLNWAVHSFRitncGVEDTTQIHTHMCYSNF----------NDII 709
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALA----DRPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 710 HSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKT 789
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKE-LPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFAT 313
|
330
....*....|....*...
gi 1375852693 790 RKYAEVKPALSNMVAAAK 807
Cdd:cd03311 314 RERGNALTKLENMVKAAL 331
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
484-810 |
1.77e-144 |
|
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: 428.02 E-value: 1.77e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 484 LPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 563
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 564 NGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKDEV 643
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 644 EDLEKAGITVIQIDEAALREGLPlrksehAFYLNWAVHSFRITNCGVEDtTQIHTHMCYSNFNDIIHSIIDMDADVITIE 723
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 724 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTR----KYAEVKPAL 799
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
330
....*....|.
gi 1375852693 800 SNMVAAAKHLR 810
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
54-409 |
4.37e-85 |
|
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: 273.94 E-value: 4.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 54 ASHIVGYPRMgpkRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIPSNTFSCYDqvldttaMLGAVPPR 133
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 134 ygWNGgeigfdvyFSMARgNASVpamemtKWFDTNYHYiVPELGPEVNFSyaSHKAVNEYKEAKAL-GVDTVPVLVGPVS 212
Cdd:COG0620 73 --LDG--------YAFAR-NGWV------EWFDTNYHY-VPEITGDVSFS--GPMTVEEFRFAKSLtGKPVKPVLPGPVT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 213 YLLLSKpakgVEKSFSLLSLIDKILPVYQEVLAELKAAGASWIQFDEPKLVMDLGAHELQAFTHAYSALEASLSGLNVLV 292
Cdd:COG0620 133 LLLLSK----VRDYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 293 ETYFADVPvEAYKTLTSLKsVTGFGFDLVRGT-KTLELIKgGFPSGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGK 371
Cdd:COG0620 209 HTCYGGYE-DILEALAALP-VDGIHLEFVRSRaGLLEPLK-ELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPP 285
|
330 340 350
....*....|....*....|....*....|....*...
gi 1375852693 372 DKLVVSTSCSLLHTAVDLvNEPKLDKEIKSWLAFAAQK 409
Cdd:COG0620 286 ERLWVSPDCGLKHRPVDL-TREEAWAKLRNMVAFAREV 322
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
480-814 |
3.10e-80 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 261.07 E-value: 3.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 480 NLPILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGF 559
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 560 AFtaNGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMT-KRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALA 638
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 639 IKDEVEDLEKAGITVIQIDEAAlregLPLRKSEHAfylnWAVHSFRITNCGVEdtTQIHTHMCYSNFNDIIHSIIDMDAD 718
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPA----LATHPEDVE----IAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEFPVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 719 VITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLKTRKYAEVKPA 798
Cdd:PRK04326 233 QFDLEFANGNYKLLDLLKE-YGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQK 311
|
330
....*....|....*.
gi 1375852693 799 LSNMVAAAKHLRTKLG 814
Cdd:PRK04326 312 LVNMVKATREVREELD 327
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
485-807 |
4.44e-36 |
|
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: 139.10 E-value: 4.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 485 PTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERnDMVEYFGEQLSGFAFtan 564
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 565 GWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQP--RFETCYQIALAIKDE 642
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 643 VEDLEKAGITVIQIDEAALREGLPLRKSEHAfYLNWAVHSFRITNCGvedttQIHTHMCYsnfNDIIHSIIDMDADVITI 722
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAALEEVSLKSGG-----DVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 723 ENSRSD-------EKLLSVFREGVKYGAGIGPGVYDIHSPR--IPSEEEIADRIEKMLAVLESnILWVNPDCGLKTRKYA 793
Cdd:cd03310 228 DAAALPskyledlKKLLRIGVRTLILGLVVTDNEAKGRNAWkeIERLEKLVRRLEEPGEVLDE-ILYLTPDCGLAFLPPQ 306
|
330
....*....|....
gi 1375852693 794 EVKPALSNMVAAAK 807
Cdd:cd03310 307 EARRKLALLAEAAR 320
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
485-807 |
6.16e-31 |
|
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: 123.76 E-value: 6.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 485 PTTTIGSFPQTMDLRRvrreykaKKISEQNYVEAIKEEINKVVKiQEELDIDVLVHGEpernDMVEYFGEQLsgfaftaN 564
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPGETSKAEWGITLVE-PEEIPLDVIPVHE----DDVLKVAQAL-------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 565 GWVQSYGSRCVKPPIIYGDV-SRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRND---------QPRFETCYQ 634
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEdPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmalyerpEAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 635 IALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEhaFYLNWAVHSFR-ITNCGVEDTTQIHTHMCYSNfNDIIHSII 713
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPK--MFKKFALPAYKkVAEYKAAGEVPIVHHSCYDA-ADLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 714 DMDADVITIENSRSDEKLLsvfREGVKYGAGIGPGVYDIHSPRipSEEEIADRIEKMLAVLESNIlWVNPDCGLKTRKYA 793
Cdd:cd00465 219 QLGVDVISFDMTVNEPKEA---IEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLGPHY-IINPDCGLGPDSDY 292
|
330
....*....|....
gi 1375852693 794 EvKPALSNMVAAAK 807
Cdd:cd00465 293 K-PEHLRAVVQLVD 305
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
483-810 |
6.36e-31 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 123.56 E-value: 6.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 483 ILPTTTIGSFPQTmdlRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPeRNDMVEYFGEQLSGFAft 562
Cdd:PRK00957 1 IMITTVVGSYPVV---KGEPETLKDKIKGFFGLYDPYKPAIEEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGFD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 563 angwvqsyGSRCVkppiiyGDVSRP-KAMTV----FWSSMAQSMT-KRPMKGMLTGPVTILNWSFVRN---DQPRFETCY 633
Cdd:PRK00957 75 --------GKRVI------GRVEPPaKPITLkdlkYAKKVAKKKDpNKGVKGIITGPSTLAYSLRVEPfysDNKDEELIY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 634 QIALAIKDEVEDLEKAGITVIQIDEAALREGLP-LRKSEHAfyLNWAVHSFRITNCgvedttqihTHMCySNFNDIIHSI 712
Cdd:PRK00957 141 DLARALRKEAEALEKAGVAMIQIDEPILSTGAYdLEVAKKA--IDIITKGLNVPVA---------MHVC-GDVSNIIDDL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 713 IDMDADVITIENSRSDEKlLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNILWVNPDCGLK--TR 790
Cdd:PRK00957 209 LKFNVDILDHEFASNKKN-LEILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMRmlPR 287
|
330 340
....*....|....*....|
gi 1375852693 791 KYAEVKpaLSNMVAAAKHLR 810
Cdd:PRK00957 288 DVAFEK--LKNMVEAAREIR 305
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
481-813 |
1.50e-24 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 105.77 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 481 LPILPTTTIGSF--PQ--TMDLRRVRREYKAKKISEQNYVEAIKeeinkvVKIQEELDiDVLVHGEPERNDMVEYFGEQL 556
Cdd:PRK01207 1 MAALITQEIGSFrkPEylSREFHKIEGTDKFYELAERATLETLD------VFENAGLD-NIGIGGEMFRWEMYEHPAERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 557 SGFAFTanGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIA 636
Cdd:PRK01207 74 KGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 637 LAIKDEVEDLEKAGITV-------IQIDEAAlreglplrKSEHAFYLNWAVHSFRITNCGVEDttQIHTHMCYSNFNDII 709
Cdd:PRK01207 152 RIINEELKDIKSAWDRKspgrkleIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDN--EFSIHVCYSSDYRLL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 710 HSII-DMDADVITIENSRSDE----------------KLLSVFREGVKYGAGIGPGVYDIHSPRIPSEEEIADRIEKMLA 772
Cdd:PRK01207 222 YDRIpELNIDGYNLEYSNRDTlepgtsdekrpgfqdlKYFAEHNESLQRKKFIGLGVTDVHIDYVEPVKLIEDRIRYALK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1375852693 773 VL-ESNILWVNPDCGLKTRKYAEVKPALSNMVAAAKHLRTKL 813
Cdd:PRK01207 302 IIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
482-814 |
2.15e-20 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 93.21 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 482 PILPTTTIGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSGFAF 561
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 562 TANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSMAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRFETCYQIALAIKD 641
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 642 EVEDLEKAGITVIQIDEAALreglplrkseHAFY---LNWAVHSFRITNCGVEDTTQIhtHMCYS--------------- 703
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAF----------NVFFdevNDWGVAALERAIEGLKCETAV--HICYGygikantdwkktlgs 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 704 ---NFNDIIHSIIDMDADVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNI 778
Cdd:PRK09121 229 ewrQYEEAFPKLQKSNIDIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADK 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 1375852693 779 LWVNPDCGLK--TRKYAEVKpaLSNMVAAAKHLRTKLG 814
Cdd:PRK09121 304 LYPCTNCGMAplSRDVARGK--LNALSAGAEIVRRELA 339
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
57-349 |
8.42e-09 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 57.82 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 57 IVG-YPRmgPKRELKfALESFWDGKSSAEDLQKVAADLRSSIWKQMSDAGIKFIpsntfscydqvldTTAMlgavpprYG 135
Cdd:PRK08575 7 LVGsYPR--PVKLAK-VISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYT-------------TDGL-------FR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 136 WNggEIgFDVYFSMARGnasVPAMEMTKWFDTNYHYIVPELGPEVNFsyashKAVNEY----KEAKALGVDTVP------ 205
Cdd:PRK08575 64 WD--DI-FDPTISFISG---VEKGGLQRFYDNNFYYRQPVIKEKINL-----KEENPYlqwlESAREIKEEVSLesklka 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 206 VLVGPVSYLLLSKPakgvEKSFSLLSLIDKILPVYQEVLAELKaAGASWIQFDEPKLVM-DLGAHELQAFTHAYSALEAS 284
Cdd:PRK08575 133 VLPGPLTYAVLSDN----EYYKNLIELMEDYASVVNSLIKELS-SVVDAVEIHEPSIFAkGIKRDTLEKLPEVYKTMAKN 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375852693 285 LSGLNVLVeTYFADVPVEAYKTLTSLkSVTGFGFDLVRGTKTLELIKGGFpSGKYLFAGVVDGRN 349
Cdd:PRK08575 208 VNIEKHLM-TYFEINNLKRLDILFSL-PVTYFGIDVIENLKKLGRVYTYL-KGRKVYLGILNARN 269
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
489-778 |
1.98e-03 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 41.26 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 489 IGSFPQTMDLRRVRREYKAKKISEQNYVEAIKEEINKVVKIQEELDIDVLVHGEPERNDMVEYFGEQLSG------FAFT 562
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGvekgglQRFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 563 ANGWVqsYGSrcvkpPIIYGDVS-RPKAMTVFWSSMAQSMTKR-----PMKGMLTGPVTILNWSfvrnDQPRFETCYQIA 636
Cdd:PRK08575 88 DNNFY--YRQ-----PVIKEKINlKEENPYLQWLESAREIKEEvslesKLKAVLPGPLTYAVLS----DNEYYKNLIELM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 637 LAIKDEVEDLEKA---GITVIQIDEAALREglplrKSEHAFYLNWAVHSFRITNCGVEDTTQIHTHMCYSNFnDIIHSII 713
Cdd:PRK08575 157 EDYASVVNSLIKElssVVDAVEIHEPSIFA-----KGIKRDTLEKLPEVYKTMAKNVNIEKHLMTYFEINNL-KRLDILF 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375852693 714 DMDADVITIENSRSDEKLLSVFrEGVKyGAGIGPGVYDIHSPRIPSEEEIADRIEKMLAVLESNI 778
Cdd:PRK08575 231 SLPVTYFGIDVIENLKKLGRVY-TYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKRKGVSDI 293
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
239-382 |
7.13e-03 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 39.58 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375852693 239 VYQEVLaELKAAGASWIQFDEPKLVMDLGAHEL--QAFTHAYSALEASLsGLNV------LVETYFADVPveayktltsl 310
Cdd:PRK04326 163 INEEIK-NLVEAGAKYIQIDEPALATHPEDVEIavEALNRIVKGINAKL-GLHVcygdysRIAPYILEFP---------- 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375852693 311 ksVTGFGFDLV-RGTKTLELIKG-GFpsGKYLFAGVVDGRNIWANNLGSSLDTLKALEGIVGKDKLVVSTSCSL 382
Cdd:PRK04326 231 --VDQFDLEFAnGNYKLLDLLKEyGF--DKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGL 300
|
|
| |
