|
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: 1618.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 1 MASHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPS 80
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 81 RYGFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVS 160
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 161 YLLLSKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLV 240
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 241 ETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTIDLIK-SGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGK 319
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 320 DKLVVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESFFTANADALSSRRSSPRVTNESVQ 399
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 400 KAAAALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQE 479
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 480 DLDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLT 559
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 560 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQ 639
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 640 DSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKML 719
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 15228634 720 AVLEQNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQLGSAK 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: 1293.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 6 VGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRYGFT 85
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 86 SGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYLlls 165
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 166 KLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVETYFA 245
Cdd:TIGR01371 158 KLSKAVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 246 DIPAeAYKTLTSLKgVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGKdkLVVS 325
Cdd:TIGR01371 238 SVGD-ALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 326 TSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESFFT--ANADALSSRRSSPRVTNESVQKAAA 403
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFAleANAAAIAARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 404 ALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDI 483
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 484 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVT 563
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 564 ILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQDSTQ 643
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 644 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLE 723
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 15228634 724 QNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQ 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: 599.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 3 SHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRY 82
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 83 GFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYL 162
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 163 llsKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVET 242
Cdd:cd03312 162 ---KLSKAKGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 243 YFADIpAEAYKTLTSLkGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGkDKL 322
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15228634 323 VVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKA 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: 569.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 432 LPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 512 NGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 592 EDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKAMV 751
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 15228634 752 DAAK 755
Cdd:pfam01717 320 DAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-758 |
4.70e-146 |
|
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: 430.72 E-value: 4.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 432 LPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 512 NGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 592 EDLEKGGIGVIQIDEAALREGLPlrkaehSFYLDWAVHSFRITNCGVQDsTQIHTHMCYSNFNDIIHSIIDMDADVITIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYT----EVKPAL 747
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVDltreEAWAKL 312
|
330
....*....|.
gi 15228634 748 KAMVDAAKLIR 758
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| |
|
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: 1618.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 1 MASHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPS 80
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 81 RYGFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVS 160
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 161 YLLLSKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLV 240
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 241 ETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTIDLIK-SGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGK 319
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 320 DKLVVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESFFTANADALSSRRSSPRVTNESVQ 399
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 400 KAAAALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQE 479
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 480 DLDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLT 559
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 560 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQ 639
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 640 DSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKML 719
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 15228634 720 AVLEQNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQLGSAK 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: 1348.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 1 MASHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPS 80
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 81 RYGFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVS 160
Cdd:PRK05222 82 RFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 161 YLLLSKlakGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLV 240
Cdd:PRK05222 162 FLWLSK---SKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 241 ETYFADIpAEAYKTLTSLkGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVgkD 320
Cdd:PRK05222 239 ATYFGSL-NDALDLLASL-PVDGLHLDLVRGPEQLAALLKYFPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV--D 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 321 KLVVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESF--FTANADALSSRRSSPRVTNESV 398
Cdd:PRK05222 315 RLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAeaLAANRAAIAARRTSPRVHNPAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 399 QKAAAALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQ 478
Cdd:PRK05222 395 RARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 479 EDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGML 558
Cdd:PRK05222 475 EELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGML 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 559 TGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGV 638
Cdd:PRK05222 555 TGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGV 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 639 QDSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKM 718
Cdd:PRK05222 635 KDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFED-FGYPNEIGPGVYDIHSPRVPSVEEIEELLRKA 713
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 15228634 719 LAVLEQNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQLGS 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: 1293.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 6 VGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRYGFT 85
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 86 SGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYLlls 165
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFL--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 166 KLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVETYFA 245
Cdd:TIGR01371 158 KLSKAVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 246 DIPAeAYKTLTSLKgVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGKdkLVVS 325
Cdd:TIGR01371 238 SVGD-ALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 326 TSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKALAGQTNESFFT--ANADALSSRRSSPRVTNESVQKAAA 403
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFAleANAAAIAARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 404 ALKGSDHRRTTEVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDI 483
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 484 DVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVT 563
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 564 ILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQDSTQ 643
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 644 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLE 723
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 15228634 724 QNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQ 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: 599.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 3 SHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRY 82
Cdd:cd03312 2 THILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPERF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 83 GFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYL 162
Cdd:cd03312 82 GALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTFL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 163 llsKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVET 242
Cdd:cd03312 162 ---KLSKAKGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 243 YFADIpAEAYKTLTSLkGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGkDKL 322
Cdd:cd03312 239 YFGSL-GENLDLLASL-PVDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15228634 323 VVSTSCSLLHTAVDLINETKLDAEIKSWLAFAAQKVVEVDALAKA 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: 569.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 432 LPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 512 NGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 592 EDLEKGGIGVIQIDEAALREGLPLRKAEHSFYLDWAVHSFRITNCGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKAMV 751
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 15228634 752 DAAK 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 |
2.66e-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: 504.81 E-value: 2.66e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 3 SHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRY 82
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 83 GFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYL 162
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 163 llsKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVET 242
Cdd:pfam08267 161 ---KLSKGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLAT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15228634 243 YFADIpAEAYKTLTSLkGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVV 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 |
8.37e-148 |
|
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: 435.50 E-value: 8.37e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 433 PTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTan 512
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 513 GWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTK-RPMKGMLTGPVTILNWSFVRN---DQPRHETCYQIALAIK 588
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 589 DEVEDLEKGGIGVIQIDEAALREGLPLRK-AEHSFYLDWAVHSFRitncGVQDSTQIHTHMCYSNF----------NDII 657
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALA----DRPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 658 HSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKT 737
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKE-LPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFAT 313
|
330
....*....|....*....
gi 15228634 738 RKYTEVKPALKAMVDAAKL 756
Cdd:cd03311 314 RERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-758 |
4.70e-146 |
|
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: 430.72 E-value: 4.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 432 LPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAFTA 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 512 NGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 592 EDLEKGGIGVIQIDEAALREGLPlrkaehSFYLDWAVHSFRITNCGVQDsTQIHTHMCYSNFNDIIHSIIDMDADVITIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 672 NSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYT----EVKPAL 747
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVDltreEAWAKL 312
|
330
....*....|.
gi 15228634 748 KAMVDAAKLIR 758
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
2-357 |
5.33e-82 |
|
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: 264.31 E-value: 5.33e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 2 ASHIVGYPRMgpkRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDqvldttaMLGAVPSR 81
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 82 ygftsgeigLDVYfSMARgNASVpamemtKWFDTNYHYiVPELGPEVKFSyaSHKAVNEYKEAKAL-GVETVPVLVGPVS 160
Cdd:COG0620 73 ---------LDGY-AFAR-NGWV------EWFDTNYHY-VPEITGDVSFS--GPMTVEEFRFAKSLtGKPVKPVLPGPVT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 161 YLLLSKLAkgVDKsfDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLV 240
Cdd:COG0620 133 LLLLSKVR--DYK--DREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 241 ETYFADIpAEAYKTLTSLKgVTAFGFDLVRGT-KTIDLIKSgFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGK 319
Cdd:COG0620 209 HTCYGGY-EDILEALAALP-VDGIHLEFVRSRaGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPP 285
|
330 340 350
....*....|....*....|....*....|....*...
gi 15228634 320 DKLVVSTSCSLLHTAVDLiNETKLDAEIKSWLAFAAQK 357
Cdd:COG0620 286 ERLWVSPDCGLKHRPVDL-TREEAWAKLRNMVAFAREV 322
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
428-762 |
3.76e-79 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 257.21 E-value: 3.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 428 NLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGF 507
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 508 AFtaNGWVQSYGSRCVKPPVIYGDVSRPKPMTV-FWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALA 586
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVdEFEFAKSVTYTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 587 IKDEVEDLEKGGIGVIQIDEAAlregLPLRKAEHSfyldWAVHSFRITNCGVQdsTQIHTHMCYSNFNDIIHSIIDMDAD 666
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPA----LATHPEDVE----IAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEFPVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 667 VITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKTRKYTEVKPA 746
Cdd:PRK04326 233 QFDLEFANGNYKLLDLLKE-YGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQK 311
|
330
....*....|....*.
gi 15228634 747 LKAMVDAAKLIRSQLG 762
Cdd:PRK04326 312 LVNMVKATREVREELD 327
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
433-756 |
4.62e-37 |
|
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: 141.79 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 433 PTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERnDMVEYFGEQLSGFAFtan 512
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 513 GWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQP--RHETCYQIALAIKDE 590
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 591 VEDLEKGGIGVIQIDEAALREGLPLRKAEHSfYLDWAvhsfrITNCGVQDSTQIHTHMCYsnfNDIIHSIIDMDADVITI 670
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAA-----LEEVSLKSGGDVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 671 ENSRSD-------EKLLSVFREGVKYGAGIGPGVYDIHSPR--IPSTDEIADRINKMLAVLEQnILWVNPDCGLKTRKYT 741
Cdd:cd03310 228 DAAALPskyledlKKLLRIGVRTLILGLVVTDNEAKGRNAWkeIERLEKLVRRLEEPGEVLDE-ILYLTPDCGLAFLPPQ 306
|
330
....*....|....*
gi 15228634 742 EVKPALKAMVDAAKL 756
Cdd:cd03310 307 EARRKLALLAEAARE 321
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
431-758 |
7.42e-32 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 126.26 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 431 ILPTTTIGSFPQTVELRRVRREYKAKKISEEDyvkAIKEEIKKVVDIQEDLDIDVLVHGEPeRNDMVEYFGEQLSGFAft 510
Cdd:PRK00957 1 IMITTVVGSYPVVKGEPETLKDKIKGFFGLYD---PYKPAIEEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGFD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 511 angwvqsyGSRCVkppviyGDVSRP-KPMTV----FWSSTAQSMT-KRPMKGMLTGPVTILNWSFVRN---DQPRHETCY 581
Cdd:PRK00957 75 --------GKRVI------GRVEPPaKPITLkdlkYAKKVAKKKDpNKGVKGIITGPSTLAYSLRVEPfysDNKDEELIY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 582 QIALAIKDEVEDLEKGGIGVIQIDEAALREGLP----LRKAehsfyLDWAVHSFRITNCgvqdstqihTHMCySNFNDII 657
Cdd:PRK00957 141 DLARALRKEAEALEKAGVAMIQIDEPILSTGAYdlevAKKA-----IDIITKGLNVPVA---------MHVC-GDVSNII 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 658 HSIIDMDADVITIENSRSDEKLlSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQNILWVNPDCGLKT 737
Cdd:PRK00957 206 DDLLKFNVDILDHEFASNKKNL-EILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMRM 284
|
330 340
....*....|....*....|.
gi 15228634 738 RKYTEVKPALKAMVDAAKLIR 758
Cdd:PRK00957 285 LPRDVAFEKLKNMVEAAREIR 305
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
433-755 |
9.91e-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: 119.91 E-value: 9.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 433 PTTTIGSFPQTVELRRvrreykaKKISEEDYVKAIKEEIKKVVDiQEDLDIDVLVHGEpernDMVEYFGEQLsgfaftaN 512
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPGETSKAEWGITLVE-PEEIPLDVIPVHE----DDVLKVAQAL-------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 513 GWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSST-AQSMTKRPMKGMLTGPVTILNWSFVRND---------QPRHETCYQ 582
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEDPFREAPALEHITaVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmalyerpEAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 583 IALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKAEhsFYLDWAVHSFR-ITNCGVQDSTQIHTHMCYSNfNDIIHSII 661
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPK--MFKKFALPAYKkVAEYKAAGEVPIVHHSCYDA-ADLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 662 DMDADVITIENSRSDEKLLsvfREGVKYGAGIGPGVYDIHSPRipSTDEIADRINKMLAVLEQNIlWVNPDCGLKTRKYT 741
Cdd:cd00465 219 QLGVDVISFDMTVNEPKEA---IEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLGPHY-IINPDCGLGPDSDY 292
|
330
....*....|....
gi 15228634 742 EvKPALKAMVDAAK 755
Cdd:cd00465 293 K-PEHLRAVVQLVD 305
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
429-761 |
4.25e-24 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 104.23 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 429 LPILPTTTIGSF--PQ--TVELRRVRREYKAKKISEedyvKAIKEeikkVVDIQEDLDID-VLVHGEPERNDMVEYFGEQ 503
Cdd:PRK01207 1 MAALITQEIGSFrkPEylSREFHKIEGTDKFYELAE----RATLE----TLDVFENAGLDnIGIGGEMFRWEMYEHPAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 504 LSGFAFTanGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQI 583
Cdd:PRK01207 73 IKGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 584 ALAIKDEVEDLEK------GGIGV-IQIDEAAlreglplrKAEHSFYLDWAVHSFRITNCGVQDstQIHTHMCYSNFNDI 656
Cdd:PRK01207 151 ARIINEELKDIKSawdrksPGRKLeIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDN--EFSIHVCYSSDYRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 657 IHSII-DMDADVITIENSRSDE----------------KLLSVFREGVKYGAGIGPGVYDIHSPRIPSTDEIADRINKML 719
Cdd:PRK01207 221 LYDRIpELNIDGYNLEYSNRDTlepgtsdekrpgfqdlKYFAEHNESLQRKKFIGLGVTDVHIDYVEPVKLIEDRIRYAL 300
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15228634 720 AVL-EQNILWVNPDCGLKTRKYTEVKPALKAMVDAAKLIRSQL 761
Cdd:PRK01207 301 KIIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
430-762 |
4.95e-22 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 98.22 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 430 PILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAF 509
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 510 TANGWVQSYGSRCVKPPVIYGDVSRPKPMTVFWSSTAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKD 589
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 590 EVEDLEKGGIGVIQIDEAALreglplrkaehSFYL----DWAVHSFRITNCGVQDSTQIhtHMCYS-------------- 651
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAF-----------NVFFdevnDWGVAALERAIEGLKCETAV--HICYGygikantdwkktlg 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 652 ----NFNDIIHSIIDMDADVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSTDEIADRINKMLAVLEQN 725
Cdd:PRK09121 228 sewrQYEEAFPKLQKSNIDIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVASDTIETPEEVADTLRKALQFVDAD 302
|
330 340 350
....*....|....*....|....*....|....*....
gi 15228634 726 ILWVNPDCGLK--TRKYTEVKpaLKAMVDAAKLIRSQLG 762
Cdd:PRK09121 303 KLYPCTNCGMAplSRDVARGK--LNALSAGAEIVRRELA 339
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
110-330 |
2.05e-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: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 110 TKWFDTNYHYIVPELGPEVkFSYASHKAVNEYKEAKALGVETVPVLVGPVSYLLLSKLAKGVDKSF-DLLSLLPKILpvy 188
Cdd:cd03310 78 TRFFDNNFFYRPPEAKIEA-FLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPDAYeDLAKSLAEFL--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 189 KEVIAELKAAGASWIQLDEPLFVMDLEGHK--LQAFSGAYAELESTLSGlNVLVETYFADIPAEAYKTltslkGVTAFGF 266
Cdd:cd03310 154 REQVKELKNRGIVVVQIDEPSLGAVGAGAFedLEIVDAALEEVSLKSGG-DVEVHLCAPLDYEALLEL-----GVDVIGF 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228634 267 DLVRGTKTIDLIKSGFPQ----GKYLFAGVVD----GRNIWAN-DLAASLITLQSLEGVVGKDKLVVSTSCSL 330
Cdd:cd03310 228 DAAALPSKYLEDLKKLLRigvrTLILGLVVTDneakGRNAWKEiERLEKLVRRLEEPGEVLDEILYLTPDCGL 300
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
5-297 |
1.73e-08 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 57.05 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 5 IVG-YPRmgPKRELKfALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFsHYDQVLDTTamlgavpsrYG 83
Cdd:PRK08575 7 LVGsYPR--PVKLAK-VISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLF-RWDDIFDPT---------IS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 84 FTSG-EIGldvyfsmargnasvpamEMTKWFDTNYHY----IVPELGPEVKFSYA-SHKAVNEYKEAKALGVETVPVLVG 157
Cdd:PRK08575 74 FISGvEKG-----------------GLQRFYDNNFYYrqpvIKEKINLKEENPYLqWLESAREIKEEVSLESKLKAVLPG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 158 PVSYLLLSklakgvDKSF--DLLSLLPKILPVYKEVIAELKaAGASWIQLDEP-LFVMDLEGHKLQAFSGAYAELESTLS 234
Cdd:PRK08575 137 PLTYAVLS------DNEYykNLIELMEDYASVVNSLIKELS-SVVDAVEIHEPsIFAKGIKRDTLEKLPEVYKTMAKNVN 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228634 235 GLNVLVeTYFADIPAEAYKTLTSLKgVTAFGFDLVRGTKTIDLIKSGFPqGKYLFAGVVDGRN 297
Cdd:PRK08575 210 IEKHLM-TYFEINNLKRLDILFSLP-VTYFGIDVIENLKKLGRVYTYLK-GRKVYLGILNARN 269
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
437-717 |
6.82e-06 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 48.96 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 437 IGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSG------FAFT 510
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGvekgglQRFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 511 ANGWVqsygsrcVKPPVIYGDVSRPKPMT-VFWSSTAQSMTKR-----PMKGMLTGPVTILNWSfvrnDQPRHETCYQIA 584
Cdd:PRK08575 88 DNNFY-------YRQPVIKEKINLKEENPyLQWLESAREIKEEvslesKLKAVLPGPLTYAVLS----DNEYYKNLIELM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 585 LAIKDEVEDLEK---GGIGVIQIDEAALREGlPLRKAehsfYLDWAVHSFRITNCGVQDSTQIHTHMCYSNFnDIIHSII 661
Cdd:PRK08575 157 EDYASVVNSLIKelsSVVDAVEIHEPSIFAK-GIKRD----TLEKLPEVYKTMAKNVNIEKHLMTYFEINNL-KRLDILF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15228634 662 DMDADVITIENSRSDEKLLSVFrEGVKyGAGIGPGVYDIHSPRIPSTDEIADRINK 717
Cdd:PRK08575 231 SLPVTYFGIDVIENLKKLGRVY-TYLK-GRKVYLGILNARNTKMEKISTIRRIVNK 284
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
87-271 |
3.67e-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: 46.34 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 87 GEIGLDVYFSMARGNASVP-AMEMTKWFDTNYHYIVPE-LGPEVKFSYAshKAVNEYKEAKALG-VETVPVLVGPVSYLL 163
Cdd:cd00465 39 EEIPLDVIPVHEDDVLKVAqALGEWAFRYYSQAPSVPEiDEEEDPFREA--PALEHITAVRSLEeFPTAGAAGGPFTFTH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228634 164 LSK-----LAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFS----GAYAELESTLS 234
Cdd:cd00465 117 HSMsmgdaLMALYERPEAMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPKMFKkfalPAYKKVAEYKA 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 15228634 235 GLNVLVETYFADIPAEAYKTLTSLkGVTAFGFDLVRG 271
Cdd:cd00465 197 AGEVPIVHHSCYDAADLLEEMIQL-GVDVISFDMTVN 232
|
|
| PRK06233 |
PRK06233 |
vitamin B12 independent methionine synthase; |
437-509 |
2.42e-03 |
|
vitamin B12 independent methionine synthase;
Pssm-ID: 180482 Cd Length: 372 Bit Score: 40.85 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228634 437 IGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIKKVVDIQEDLDIDVLVHGEPERNDMVEYFGEQLSGFAF 509
Cdd:PRK06233 14 VGSFLRPERLKEAREQFAIGEISQDQLLKIQHAEIKRLVKEQVELGLKAVTDGEFNRSWWHLDFLWGLNGVGK 86
|
|
| |
