|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
49-812 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 49 MSSHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPS 128
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 129 RYGWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMT 208
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 209 YLLLSKPAKGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLI 288
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 289 ATYFADVPAEAYKTLMSLKCVTGFGFDLVRGLETLDLIK-MNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGK 367
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 368 EKVVVSTSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAKSFSGAKDEALFSSNSMRQASRRSSPRVTNAAVQ 447
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 448 QDVDAVKKSDHHRSTEVSVRLQAQQKKLNLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQE 527
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 528 ELGIDVLVHGEAERNDMVEFFGEQLSGFAFTSNGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLT 607
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 608 GPVTILNWSFVRNDQPRHETCFQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQ 687
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 688 DSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKML 767
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 145334531 768 AVLDSKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQLNKS 812
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASA 765
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
54-808 |
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: 1240.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 54 VGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPSRYGWE 133
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 134 SGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMTYLLLS 213
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 214 KpakGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIATYFA 293
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 294 DVPAeAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGKekVVVS 373
Cdd:TIGR01371 238 SVGD-ALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 374 TSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAKSFSGAKDEALFSSNSMRQA--SRRSSPRVTNAAVQQDVD 451
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 452 AVKKSDHHRSTEVSVRLQAQQKKLNLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGI 531
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 532 DVLVHGEAERNDMVEFFGEQLSGFAFTSNGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVT 611
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 612 ILNWSFVRNDQPRHETCFQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQDSTQ 691
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 692 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLD 771
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 145334531 772 SKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQ 808
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
50-414 |
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: 582.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 50 SSHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPSR 129
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 130 YGWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMTY 209
Cdd:cd03312 81 FGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 210 LLLSKPAKGvekSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIA 289
Cdd:cd03312 161 LKLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 290 TYFADVpAEAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGkEK 369
Cdd:cd03312 238 TYFGSL-GENLDLLASLP-VDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DR 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 145334531 370 VVVSTSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAK 414
Cdd:cd03312 315 LVVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLAR 359
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
480-803 |
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: 547.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 480 LPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTS 559
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 560 NGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQIALAIKDEV 639
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 640 EDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 720 NSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNYSEVKSALSNMV 799
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 145334531 800 AAAK 803
Cdd:pfam01717 320 DAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
480-806 |
1.97e-145 |
|
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: 430.33 E-value: 1.97e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 480 LPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTS 559
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 560 NGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQIALAIKDEV 639
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 640 EDLEKAGVTVIQIDEAALREGLPlrkseqKFYLDWAVHAFRITNSGVQDsTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 720 NSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNYS----EVKSAL 795
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVDltreEAWAKL 312
|
330
....*....|.
gi 145334531 796 SNMVAAAKLIR 806
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
49-812 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 1562.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 49 MSSHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPS 128
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 129 RYGWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMT 208
Cdd:PLN02475 81 RYGWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 209 YLLLSKPAKGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLI 288
Cdd:PLN02475 161 YLLLSKPAKGVDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 289 ATYFADVPAEAYKTLMSLKCVTGFGFDLVRGLETLDLIK-MNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGK 367
Cdd:PLN02475 241 ETYFADVPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLIKkAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 368 EKVVVSTSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAKSFSGAKDEALFSSNSMRQASRRSSPRVTNAAVQ 447
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRRSSPRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 448 QDVDAVKKSDHHRSTEVSVRLQAQQKKLNLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQE 527
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 528 ELGIDVLVHGEAERNDMVEFFGEQLSGFAFTSNGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLT 607
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 608 GPVTILNWSFVRNDQPRHETCFQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQ 687
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 688 DSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKML 767
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 145334531 768 AVLDSKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQLNKS 812
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLASA 765
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
48-811 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1329.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 48 AMSSHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVP 127
Cdd:PRK05222 1 MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 128 SRYGWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPM 207
Cdd:PRK05222 81 ERFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 208 TYLLLSKpakGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVL 287
Cdd:PRK05222 161 TFLWLSK---SKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 288 IATYFADVpAEAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVgk 367
Cdd:PRK05222 238 LATYFGSL-NDALDLLASLP-VDGLHLDLVRGPEQLAALLKYFPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 368 EKVVVSTSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAKSFSGAKD--EALFSSNSMRQASRRSSPRVTNAA 445
Cdd:PRK05222 314 DRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGavAEALAANRAAIAARRTSPRVHNPA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 446 VQQDVDAVKKSDHHRSTEVSVRLQAQQKKLNLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKL 525
Cdd:PRK05222 394 VRARLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 526 QEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTSNGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGM 605
Cdd:PRK05222 474 QEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGM 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 606 LTGPVTILNWSFVRNDQPRHETCFQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSG 685
Cdd:PRK05222 554 LTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSG 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 686 VQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINK 765
Cdd:PRK05222 634 VKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFED-FGYPNEIGPGVYDIHSPRVPSVEEIEELLRK 712
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 145334531 766 MLAVLDSKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQLNK 811
Cdd:PRK05222 713 ALEVIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
54-808 |
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: 1240.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 54 VGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPSRYGWE 133
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 134 SGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMTYLLLS 213
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 214 KpakGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIATYFA 293
Cdd:TIGR01371 161 K---AVEEPFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 294 DVPAeAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGKekVVVS 373
Cdd:TIGR01371 238 SVGD-ALEALVSLP-VKGIGLDFVHGKGTLELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 374 TSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAKSFSGAKDEALFSSNSMRQA--SRRSSPRVTNAAVQQDVD 451
Cdd:TIGR01371 314 TSCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAiaARKSSPRVNDAQVKARLA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 452 AVKKSDHHRSTEVSVRLQAQQKKLNLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGI 531
Cdd:TIGR01371 394 NLKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 532 DVLVHGEAERNDMVEFFGEQLSGFAFTSNGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVT 611
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 612 ILNWSFVRNDQPRHETCFQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQDSTQ 691
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 692 IHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLD 771
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740 750
....*....|....*....|....*....|....*..
gi 145334531 772 SKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQ 808
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
50-414 |
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: 582.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 50 SSHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPSR 129
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 130 YGWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMTY 209
Cdd:cd03312 81 FGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 210 LLLSKPAKGvekSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIA 289
Cdd:cd03312 161 LKLSKAKGG---GFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 290 TYFADVpAEAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGkEK 369
Cdd:cd03312 238 TYFGSL-GENLDLLASLP-VDGLHLDLVRGPENLEAVLKAGFADKVLSAGVVDGRNIWRADLAASLALLETLAAILG-DR 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 145334531 370 VVVSTSCSLLHTAVDLVNEMKLDKELKSWLAFAAQKVVEVNALAK 414
Cdd:cd03312 315 LVVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLAR 359
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
480-803 |
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: 547.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 480 LPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTS 559
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 560 NGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQIALAIKDEV 639
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 640 EDLEKAGVTVIQIDEAALREGLPLRKSEQKFYLDWAVHAFRITNSGVQDSTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 720 NSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNYSEVKSALSNMV 799
Cdd:pfam01717 241 ASRSDMELLEAFEE-WGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMV 319
|
....
gi 145334531 800 AAAK 803
Cdd:pfam01717 320 DAAK 323
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
51-365 |
6.98e-177 |
|
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: 510.58 E-value: 6.98e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 51 SHIVGYPRIGPKRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDQMLDTTAMLGAVPSRY 130
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 131 GWESGEIGFDVYFSMARGNASAHAMEMTKWFDTNYHYIVPELGPDVNFSYASHKAVVEFKEAKALGIDTVPVLIGPMTYL 210
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 211 LLSkpaKGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIAT 290
Cdd:pfam08267 161 KLS---KGKGGSFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLAT 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334531 291 YFADVpAEAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIV 365
Cdd:pfam08267 238 YFGSV-ADALELLASLP-VAGLGLDLVRGPENLAALKKGFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
481-804 |
1.16e-145 |
|
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: 431.27 E-value: 1.16e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 481 PTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTsn 560
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 561 GWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQ-RPMKGMLTGPVTILNWSFVRN---DQPRHETCFQIALAIK 636
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 637 DEVEDLEKAGVTVIQIDEAALREGLPLRK-SEQKFYLDWAVHAFRitnsGVQDSTQIHTHMCYSNF----------NDII 705
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPdDLAADYLKWANEALA----DRPDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 706 HSIIDMDADVITIENSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKT 785
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKE-LPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFAT 313
|
330
....*....|....*....
gi 145334531 786 RNYSEVKSALSNMVAAAKL 804
Cdd:cd03311 314 RERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
480-806 |
1.97e-145 |
|
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: 430.33 E-value: 1.97e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 480 LPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTS 559
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 560 NGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQIALAIKDEV 639
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 640 EDLEKAGVTVIQIDEAALREGLPlrkseqKFYLDWAVHAFRITNSGVQDsTQIHTHMCYSNFNDIIHSIIDMDADVITIE 719
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 720 NSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNYS----EVKSAL 795
Cdd:COG0620 234 FVRSRAGLLEPLKE-LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVDltreEAWAKL 312
|
330
....*....|.
gi 145334531 796 SNMVAAAKLIR 806
Cdd:COG0620 313 RNMVAFAREVR 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
51-405 |
2.07e-88 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 282.41 E-value: 2.07e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 51 SHIVGYPRIgpkRELKFALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIPSNTFSYYDqmldttaMLGAVPSRY 130
Cdd:COG0620 4 TTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPERL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 131 GwesgeiGFDvyfsMARgnasahaMEMTKWFDTNYHYiVPELGPDVNFSyaSHKAVVEFKEAKAL-GIDTVPVLIGPMTY 209
Cdd:COG0620 74 D------GYA----FAR-------NGWVEWFDTNYHY-VPEITGDVSFS--GPMTVEEFRFAKSLtGKPVKPVLPGPVTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 210 LLLSKPAKGVEKsfclLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSDAYSHMESSLAGLNVLIA 289
Cdd:COG0620 134 LLLSKVRDYKDR----EELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHLH 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 290 TYFADVpAEAYKTLMSLKcVTGFGFDLVRG-LETLDLIKmNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGKE 368
Cdd:COG0620 210 TCYGGY-EDILEALAALP-VDGIHLEFVRSrAGLLEPLK-ELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPE 286
|
330 340 350
....*....|....*....|....*....|....*..
gi 145334531 369 KVVVSTSCSLLHTAVDLVNEmKLDKELKSWLAFAAQK 405
Cdd:COG0620 287 RLWVSPDCGLKHRPVDLTRE-EAWAKLRNMVAFAREV 322
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
476-811 |
1.09e-79 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 259.52 E-value: 1.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 476 NLPALPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGF 555
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 556 AFtsNGWVQSYGSRCVKPPIIYGDITRPKAMTV----FWSSMAQKmtqRPMKGMLTGPVTILNWSFVRNDQPRHETCFQI 631
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVdefeFAKSVTYT---RPVKVPITGPYTIAEWSFNEYYKDKEELVFDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 632 ALAIKDEVEDLEKAGVTVIQIDEAAlregLPLRKSEqkfyLDWAVHAFRITNSGVQdsTQIHTHMCYSNFNDIIHSIIDM 711
Cdd:PRK04326 160 AKVINEEIKNLVEAGAKYIQIDEPA----LATHPED----VEIAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 712 DADVITIENSRSDEKLLSVFHEgVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNYSEV 791
Cdd:PRK04326 230 PVDQFDLEFANGNYKLLDLLKE-YGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIA 308
|
330 340
....*....|....*....|
gi 145334531 792 KSALSNMVAAAKLIRSQLNK 811
Cdd:PRK04326 309 YQKLVNMVKATREVREELDK 328
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
481-804 |
1.54e-38 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 146.03 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 481 PTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERnDMVEFFGEQLSGFAFtsn 560
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 561 GWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQP--RHETCFQIALAIKDE 638
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 639 VEDLEKAGVTVIQIDEAALREGLPLRKSEQKfYLDWAvhafrITNSGVQDSTQIHTHMCYsnfNDIIHSIIDMDADVITI 718
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAA-----LEEVSLKSGGDVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 719 ENSRSD-------EKLLSVFHEGVKYGAGIGPGVYDIHSPR--IPSTEEIAERINKMLAVLDsKVLWVNPDCGLKTRNYS 789
Cdd:cd03310 228 DAAALPskyledlKKLLRIGVRTLILGLVVTDNEAKGRNAWkeIERLEKLVRRLEEPGEVLD-EILYLTPDCGLAFLPPQ 306
|
330
....*....|....*
gi 145334531 790 EVKSALSNMVAAAKL 804
Cdd:cd03310 307 EARRKLALLAEAARE 321
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
479-806 |
1.20e-33 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 131.65 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 479 ALPTTTIGSFPQTTDLRRIRREFKAKKISEVD-YVQTIkeeyEKVIKLQEELGIDVLVHGEAeRNDMVEFFGEQLSGFAf 557
Cdd:PRK00957 1 IMITTVVGSYPVVKGEPETLKDKIKGFFGLYDpYKPAI----EEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGFD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 558 tsngwvqsyGSRCVkppiiyGDITRP-KAMTV----FWSSMAQKMTQRP-MKGMLTGPVTILNWSFVRN---DQPRHETC 628
Cdd:PRK00957 75 ---------GKRVI------GRVEPPaKPITLkdlkYAKKVAKKKDPNKgVKGIITGPSTLAYSLRVEPfysDNKDEELI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 629 FQIALAIKDEVEDLEKAGVTVIQIDEAALREGLPlrkseqkfYLDWAVHAFRITNSGVqdSTQIHTHMCySNFNDIIHSI 708
Cdd:PRK00957 140 YDLARALRKEAEALEKAGVAMIQIDEPILSTGAY--------DLEVAKKAIDIITKGL--NVPVAMHVC-GDVSNIIDDL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 709 IDMDADVITIENSRSDEKLlSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNPDCGLKTRNY 788
Cdd:PRK00957 209 LKFNVDILDHEFASNKKNL-EILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMRMLPR 287
|
330
....*....|....*...
gi 145334531 789 SEVKSALSNMVAAAKLIR 806
Cdd:PRK00957 288 DVAFEKLKNMVEAAREIR 305
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
481-803 |
5.13e-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: 121.07 E-value: 5.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 481 PTTTIGSFPQTTDLRRirrefkaKKISEVDYvQTIKEEYEKVIKLQEELGIDVLVHGEaernDMVEFFGEQLsgfaftsN 560
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPG-ETSKAEWGITLVEPEEIPLDVIPVHE----DDVLKVAQAL-------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 561 GWVQSYGSRCVKPPIIYGD-ITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRND---------QPRHETCFQ 630
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEeDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmalyerpEAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 631 IALAIKDEVEDLEKAGVTVIQIDEAALREGLPlrKSEQKFYLDWAVHAFR-ITNSGVQDSTQIHTHMCYSNfNDIIHSII 709
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINS--FLGPKMFKKFALPAYKkVAEYKAAGEVPIVHHSCYDA-ADLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 710 DMDADVITIENSRSD-EKLLSVFHEGVKYGAGIGPGvydiHSPRipSTEEIAERINKMLAVLDSKVlWVNPDCGLKTRNY 788
Cdd:cd00465 219 QLGVDVISFDMTVNEpKEAIEKVGEKKTLVGGVDPG----YLPA--TDEECIAKVEELVERLGPHY-IINPDCGLGPDSD 291
|
330
....*....|....*
gi 145334531 789 SEVKSaLSNMVAAAK 803
Cdd:cd00465 292 YKPEH-LRAVVQLVD 305
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
477-809 |
5.83e-27 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 113.09 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 477 LPALPTTTIGSF--PQ--TTDLRRIRREFKAKKISEVDYVQTIKeeyekvikLQEELGID-VLVHGEAERNDMVEFFGEQ 551
Cdd:PRK01207 1 MAALITQEIGSFrkPEylSREFHKIEGTDKFYELAERATLETLD--------VFENAGLDnIGIGGEMFRWEMYEHPAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 552 LSGFAFTsnGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQI 631
Cdd:PRK01207 73 IKGIIFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 632 ALAIKDEVEDLEKAGVTV-------IQIDEAAlreglplrKSEQKFYLDWAVHAFRITNSGVQDstQIHTHMCYSNFNDI 704
Cdd:PRK01207 151 ARIINEELKDIKSAWDRKspgrkleIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDN--EFSIHVCYSSDYRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 705 IHSII-DMDADVITIENSRSDE----------------KLLSVFHEGVKYGAGIGPGVYDIHSPRIPSTEEIAERINKML 767
Cdd:PRK01207 221 LYDRIpELNIDGYNLEYSNRDTlepgtsdekrpgfqdlKYFAEHNESLQRKKFIGLGVTDVHIDYVEPVKLIEDRIRYAL 300
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 145334531 768 AVL-DSKVLWVNPDCGLKTRNYSEVKSALSNMVAAAKLIRSQL 809
Cdd:PRK01207 301 KIIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
480-809 |
2.27e-21 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 96.29 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 480 LPTTTIGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSGFAFTS 559
Cdd:PRK09121 3 LPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDFEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 560 NGWVQSYGSRCVKPPIIYGDITRPKAMTVFWSSMAQKMTQRPMKGMLTGPVTILNWSFVRNDQPRHETCFQIALAIKDEV 639
Cdd:PRK09121 83 RETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 640 EDLEKAGVTVIQIDEAALReglpLRKSEQKfylDWAVHAFRITNSGVQDSTQIhtHMCYS------------------NF 701
Cdd:PRK09121 163 KELEAAGVDIIQFDEPAFN----VFFDEVN---DWGVAALERAIEGLKCETAV--HICYGygikantdwkktlgsewrQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 702 NDIIHSIIDMDADVITIE--NSRSDEKLLSVFHegvkyGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVLDSKVLWVNP 779
Cdd:PRK09121 234 EEAFPKLQKSNIDIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADKLYPCT 308
|
330 340 350
....*....|....*....|....*....|...
gi 145334531 780 DCGLK--TRNYSEVK-SALSnmvAAAKLIRSQL 809
Cdd:PRK09121 309 NCGMAplSRDVARGKlNALS---AGAEIVRREL 338
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
145-378 |
3.18e-10 |
|
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: 62.44 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 145 MARGNASAHAMEMTKW--FDTNYHY------IVPELGPDVnfsyashKAVVEFKEAKALGIDTVPVLIGPMTYLLLSKPA 216
Cdd:cd03310 63 MIGRFLEVLVDLETGTrfFDNNFFYrppeakIEAFLPLEL-------DYLEEVAEAYKEALKVKVVVTGPLTLALLAFLP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 217 KGVEKSfcLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDL-----DTSQLQAFSDAYSHmessLAGLNVLIATY 291
Cdd:cd03310 136 NGEPDA--YEDLAKSLAEFLREQVKELKNRGIVVVQIDEPSLGAVGagafeDLEIVDAALEEVSL----KSGGDVEVHLC 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 292 FADVpaeaYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPR----GKLLFAGVVD----GRNIWANdlsasLKTLQTLED 363
Cdd:cd03310 210 APLD----YEALLELG-VDVIGFDAAALPSKYLEDLKKLLRigvrTLILGLVVTDneakGRNAWKE-----IERLEKLVR 279
|
250 260
....*....|....*....|.
gi 145334531 364 IVGKEKVV------VSTSCSL 378
Cdd:cd03310 280 RLEEPGEVldeilyLTPDCGL 300
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
53-367 |
2.69e-07 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 53.20 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 53 IVG-YPRigPKRELKfALESFWDGKTNVDDLQNVAANLRKSIWKHMAHAGIKYIpsntfsyydqmldTTAMlgavpsrYG 131
Cdd:PRK08575 7 LVGsYPR--PVKLAK-VISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYT-------------TDGL-------FR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 132 WEsgEIgFDVYFSMARGnasAHAMEMTKWFDTNYHY----IVPELGPDVNFSYA-SHKAVVEFKEAKALGIDTVPVLIGP 206
Cdd:PRK08575 64 WD--DI-FDPTISFISG---VEKGGLQRFYDNNFYYrqpvIKEKINLKEENPYLqWLESAREIKEEVSLESKLKAVLPGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 207 MTYLLLSKPakgvEKSFCLLSLIDKILPVYKEVLADLKSaGARWIQFDEP-ILVMDLDTSQLQAFSDAYSHMESSLAGLN 285
Cdd:PRK08575 138 LTYAVLSDN----EYYKNLIELMEDYASVVNSLIKELSS-VVDAVEIHEPsIFAKGIKRDTLEKLPEVYKTMAKNVNIEK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 286 VLIaTYFADVPAEAYKTLMSLKcVTGFGFDLVRGLETLDLIKMNFPrGKLLFAGVVDGRNiwandlsASLKTLQTLEDIV 365
Cdd:PRK08575 213 HLM-TYFEINNLKRLDILFSLP-VTYFGIDVIENLKKLGRVYTYLK-GRKVYLGILNARN-------TKMEKISTIRRIV 282
|
..
gi 145334531 366 GK 367
Cdd:PRK08575 283 NK 284
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
133-385 |
5.91e-06 |
|
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: 49.03 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 133 ESGEIGFDVYFSMA-RGNASAHAMEMTKWFDTNYHYIVPElgPDVNFSYAS-HKAVVEFKEAKALG-IDTVPVLIGPMTY 209
Cdd:cd00465 37 EPEEIPLDVIPVHEdDVLKVAQALGEWAFRYYSQAPSVPE--IDEEEDPFReAPALEHITAVRSLEeFPTAGAAGGPFTF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 210 LLLSK-----PAKGVEKSFCLLSLIDKILPVYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSD----AYSHMESS 280
Cdd:cd00465 115 THHSMsmgdaLMALYERPEAMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGPKMFKKfalpAYKKVAEY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 281 LAGLNVLIATYFADVPAEAYKTLMSLKcVTGFGFDLVRGlETLDLIKmNFPRGKLLFAGVVDGRnIWANDLSASLKTLQT 360
Cdd:cd00465 195 KAAGEVPIVHHSCYDAADLLEEMIQLG-VDVISFDMTVN-EPKEAIE-KVGEKKTLVGGVDPGY-LPATDEECIAKVEEL 270
|
250 260
....*....|....*....|....*
gi 145334531 361 LEDIVGkeKVVVSTSCSLLHTAVDL 385
Cdd:cd00465 271 VERLGP--HYIINPDCGLGPDSDYK 293
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
235-376 |
1.93e-05 |
|
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: 47.61 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 235 VYKEVLADLKSAGARWIQFDEPILVMDLDTSQLQAFSD-AYSHMES-SLAGLNVLIAT----------YFADVPAE-AYK 301
Cdd:cd03311 156 ALREEIRDLYDAGCRYIQIDEPALAEGLPLEPDDLAADyLKWANEAlADRPDDTQIHThicygnfrstWAAEGGYEpIAE 235
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 302 TLMSLKCVtgfGFDL---VRGLETLDLIKmNFPRGKLLFAGVVDgrniwandlSASlKTLQTLEDI----------VGKE 368
Cdd:cd03311 236 YIFELDVD---VFFLeydNSRAGGLEPLK-ELPYDKKVGLGVVD---------VKS-PEVESPEEVkdrieeaakyVPLE 301
|
....*...
gi 145334531 369 KVVVSTSC 376
Cdd:cd03311 302 QLWVSPDC 309
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| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
485-779 |
1.36e-04 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 485 IGSFPQTTDLRRIRREFKAKKISEVDYVQTIKEEYEKVIKLQEELGIDVLVHGEAERNDMVEFFGEQLSG------FAFT 558
Cdd:PRK08575 8 VGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGvekgglQRFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 559 SNGWVqsYGSrcvkpPIIYGDIT-RPKAMTVFWSSMAQKMTQR-----PMKGMLTGPVTILNWSFVRNDQPRHETCFQIA 632
Cdd:PRK08575 88 DNNFY--YRQ-----PVIKEKINlKEENPYLQWLESAREIKEEvslesKLKAVLPGPLTYAVLSDNEYYKNLIELMEDYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 633 LAIKDEVEDLeKAGVTVIQIDEAALREglplrKSEQKFYLDWAVHAFRITNSGVQDSTQIHTHMCYSNFnDIIHSIIDMD 712
Cdd:PRK08575 161 SVVNSLIKEL-SSVVDAVEIHEPSIFA-----KGIKRDTLEKLPEVYKTMAKNVNIEKHLMTYFEINNL-KRLDILFSLP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334531 713 ADVITIENSRSDEKLLSVFhEGVKyGAGIGPGVYDIHSPRIPSTEEIAERINKMLAVlDSKVLWVNP 779
Cdd:PRK08575 234 VTYFGIDVIENLKKLGRVY-TYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKRK-GVSDIIVGN 297
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
235-378 |
3.98e-03 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 40.35 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334531 235 VYKEVLaDLKSAGARWIQFDEPILVMDLDTSQL--QAFSDAYSHMESSLaGLNV------LIATYFADVPaeayktlmsl 306
Cdd:PRK04326 163 INEEIK-NLVEAGAKYIQIDEPALATHPEDVEIavEALNRIVKGINAKL-GLHVcygdysRIAPYILEFP---------- 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145334531 307 kcVTGFGFDLV-RGLETLDLIKmNFPRGKLLFAGVVDGRNIWANDLSASLKTLQTLEDIVGKEKVVVSTSCSL 378
Cdd:PRK04326 231 --VDQFDLEFAnGNYKLLDLLK-EYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGL 300
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