|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
4-762 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1327.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 4 AISSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPK 83
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 84 RFQHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPEL-ADADPKVLDNRALYYYEEAKkELGIEGKPVLVGPV 162
Cdd:PRK05222 82 RFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFdPDTQFKLTSNKLLDEFEEAK-ALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 163 TYLKLGK-GNDAENFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQT 241
Cdd:PRK05222 161 TFLWLSKsKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 242 YFESL-DYYEEVVNLPVAAIGIDFVHDHGDsLEALKAHgFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVtdGKL 320
Cdd:PRK05222 241 YFGSLnDALDLLASLPVDGLHLDLVRGPEQ-LAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV--DRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 321 IVQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKALTDGAESVTAELEDARAAVTALNESSHRNNLEVQE 400
Cdd:PRK05222 317 WVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVHNPAVRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 401 AIANLENVRVDRELPFAERIKLQHAWLNLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEE 480
Cdd:PRK05222 397 RLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 481 LDIDVLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTA 560
Cdd:PRK05222 477 LGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 561 PVTIINWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWEKYLNDAVYSFKLTTASVQN 640
Cdd:PRK05222 557 PVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGVKD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 641 DTQIHTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRA 720
Cdd:PRK05222 637 ETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALEV 716
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 489829542 721 IDAKQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAEYQV 762
Cdd:PRK05222 717 IPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
9-759 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273583 [Multi-domain] Cd Length: 750 Bit Score: 1118.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 9 LGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRFQHD 88
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 89 GGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPELADADPKVLD-NRALYYYEEAKkELGIEGKPVLVGPVTYLKL 167
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTsNKPLEEYLEAK-ELGIETKPVLLGPITFLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 168 GKGNDaENFEAL--LDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQTYFES 245
Cdd:TIGR01371 160 SKAVE-EPFEPLslLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 246 L-DYYEEVVNLPVAAIGIDFVHDHGDslEALKAHGFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVtdGKLIVQP 324
Cdd:TIGR01371 239 VgDALEALVSLPVKGIGLDFVHGKGT--LELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHV--GKLVVST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 325 SNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKALTDGAESVTAELEDARAAVTALNESSHRNNLEVQEAIAN 404
Cdd:TIGR01371 315 SCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIAARKSSPRVNDAQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 405 LENVRVDRELPFAERIKLQHAWLNLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDID 484
Cdd:TIGR01371 395 LKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 485 VLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTI 564
Cdd:TIGR01371 475 VLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 565 INWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWEKYLNDAVYSFKLTTASVQNDTQI 644
Cdd:TIGR01371 555 LNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 645 HTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVT-YDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDA 723
Cdd:TIGR01371 635 HTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFgYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPA 714
|
730 740 750
....*....|....*....|....*....|....*.
gi 489829542 724 KQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAE 759
Cdd:TIGR01371 715 ERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
5-365 |
0e+00 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 553.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 5 ISSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKR 84
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 85 FQHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPEL-ADADPKVLDNRALYYYEEAkKELGIEGKPVLVGPVT 163
Cdd:cd03312 81 FGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELsPDTEFKLASNKLLDEYLEA-KALGINTKPVLLGPVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 164 YLKLGKGNDAE-NFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQTY 242
Cdd:cd03312 160 FLKLSKAKGGGfDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLATY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 243 FESL-DYYEEVVNLPVAAIGIDFVHDhGDSLEALKAHGFPeDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVTDgKLI 321
Cdd:cd03312 240 FGSLgENLDLLASLPVDGLHLDLVRG-PENLEAVLKAGFA-DKVLSAGVVDGRNIWRADLAASLALLETLAAILGD-RLV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489829542 322 VQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKA 365
Cdd:cd03312 317 VSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
6-315 |
5.79e-171 |
|
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: 493.64 E-value: 5.79e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 6 SSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRF 85
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 86 QHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPELADAD-PKVLDNRALYYYEEAkKELGIEGKPVLVGPVTY 164
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTeFKLNSNKLLDEYKEA-KALGIETKPVLLGPVTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 165 LKLGKGNDAE-NFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQTYF 243
Cdd:pfam08267 160 LKLSKGKGGSfDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLATYF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489829542 244 ESL-DYYEEVVNLPVAAIGIDFVHdHGDSLEALKAhGFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYV 315
Cdd:pfam08267 240 GSVaDALELLASLPVAGLGLDLVR-GPENLAALKK-GFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-759 |
3.00e-137 |
|
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: 407.99 E-value: 3.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 592 EALERNGIKVIQVDEPALREGLPlkqarwEKYLNDAVYSFKLTTASVQnDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVP-DTKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTR----KEPETIAALQ 747
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKLR 313
|
330
....*....|..
gi 489829542 748 DMIKATKEVRAE 759
Cdd:COG0620 314 NMVAFAREVRGE 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
4-762 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1327.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 4 AISSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPK 83
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 84 RFQHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPEL-ADADPKVLDNRALYYYEEAKkELGIEGKPVLVGPV 162
Cdd:PRK05222 82 RFGNLGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFdPDTQFKLTSNKLLDEFEEAK-ALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 163 TYLKLGK-GNDAENFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQT 241
Cdd:PRK05222 161 TFLWLSKsKGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 242 YFESL-DYYEEVVNLPVAAIGIDFVHDHGDsLEALKAHgFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVtdGKL 320
Cdd:PRK05222 241 YFGSLnDALDLLASLPVDGLHLDLVRGPEQ-LAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKV--DRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 321 IVQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKALTDGAESVTAELEDARAAVTALNESSHRNNLEVQE 400
Cdd:PRK05222 317 WVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVHNPAVRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 401 AIANLENVRVDRELPFAERIKLQHAWLNLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEE 480
Cdd:PRK05222 397 RLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 481 LDIDVLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTA 560
Cdd:PRK05222 477 LGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 561 PVTIINWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWEKYLNDAVYSFKLTTASVQN 640
Cdd:PRK05222 557 PVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGVKD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 641 DTQIHTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRA 720
Cdd:PRK05222 637 ETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALEV 716
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 489829542 721 IDAKQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAEYQV 762
Cdd:PRK05222 717 IPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELAA 758
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
9-759 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes the cobalamin-independent methionine synthase. A family of uncharacterized archaeal proteins is homologous to the C-terminal region of this family. That family is excluded from this model but, along with this family, belongs to pfam01717. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273583 [Multi-domain] Cd Length: 750 Bit Score: 1118.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 9 LGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRFQHD 88
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 89 GGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPELADADPKVLD-NRALYYYEEAKkELGIEGKPVLVGPVTYLKL 167
Cdd:TIGR01371 81 GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEFKLTsNKPLEEYLEAK-ELGIETKPVLLGPITFLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 168 GKGNDaENFEAL--LDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQTYFES 245
Cdd:TIGR01371 160 SKAVE-EPFEPLslLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 246 L-DYYEEVVNLPVAAIGIDFVHDHGDslEALKAHGFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVtdGKLIVQP 324
Cdd:TIGR01371 239 VgDALEALVSLPVKGIGLDFVHGKGT--LELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHV--GKLVVST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 325 SNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKALTDGAESVTAELEDARAAVTALNESSHRNNLEVQEAIAN 404
Cdd:TIGR01371 315 SCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIAARKSSPRVNDAQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 405 LENVRVDRELPFAERIKLQHAWLNLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDID 484
Cdd:TIGR01371 395 LKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLD 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 485 VLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTI 564
Cdd:TIGR01371 475 VLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 565 INWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWEKYLNDAVYSFKLTTASVQNDTQI 644
Cdd:TIGR01371 555 LNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 645 HTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEEVT-YDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDA 723
Cdd:TIGR01371 635 HTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFgYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPA 714
|
730 740 750
....*....|....*....|....*....|....*.
gi 489829542 724 KQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAE 759
Cdd:TIGR01371 715 ERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
6-761 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 871.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 6 SSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRF 85
Cdd:PLN02475 3 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPPRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 86 QHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPELA-DADPKVLDNRALYYYEEAKkELGIEGKPVLVGPVTY 164
Cdd:PLN02475 83 GWTGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGpEVKFSYASHKAVNEYKEAK-ALGVDTVPVLVGPVSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 165 LKLGKG----NDAENFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQ 240
Cdd:PLN02475 162 LLLSKPakgvDKSFDLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNVLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 241 TYFESL--DYYEEVVNLP-VAAIGIDFVHDHgDSLEALKAHGFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVTD 317
Cdd:PLN02475 242 TYFADVpaEAYKTLTSLKgVTAFGFDLVRGT-KTLDLIKKAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGIVGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 318 GKLIVQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKALTDGAEsvtAELEDARAAVTALNESSHR-NNL 396
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKD---EAFFSANAAAQASRRSSPRvTNE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 397 EVQEAIANLENVRVDRELPFAERIKLQHAWLNLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIK 476
Cdd:PLN02475 398 AVQKAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 477 IQEELDIDVLVHGEFERTDMVEYFGQKLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKG 556
Cdd:PLN02475 478 LQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKG 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 557 MLTAPVTIINWSFVRDDVPESVVANQVGLALRKEVEALERNGIKVIQVDEPALREGLPLKQARWEKYLNDAVYSFKLTTA 636
Cdd:PLN02475 558 MLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNC 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 637 SVQNDTQIHTHMCYSDFDDIIDTISALDADVISIETSRSHGEIISTFEE-VTYDKEIGLGVYDIHSPRVPTVTEIQDNIR 715
Cdd:PLN02475 638 GVQDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREgVKYGAGIGPGVYDIHSPRIPSTEEIADRIN 717
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 489829542 716 RALRAIDAKQFWINPDCGLKTRKEPETIAALQDMIKATKEVRAEYQ 761
Cdd:PLN02475 718 KMLAVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQLA 763
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
5-365 |
0e+00 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the N-terminal barrel, and a few single-barrel sequences most similar to the N-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239428 [Multi-domain] Cd Length: 360 Bit Score: 553.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 5 ISSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKR 84
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 85 FQHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPEL-ADADPKVLDNRALYYYEEAkKELGIEGKPVLVGPVT 163
Cdd:cd03312 81 FGALGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELsPDTEFKLASNKLLDEYLEA-KALGINTKPVLLGPVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 164 YLKLGKGNDAE-NFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQTY 242
Cdd:cd03312 160 FLKLSKAKGGGfDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLATY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 243 FESL-DYYEEVVNLPVAAIGIDFVHDhGDSLEALKAHGFPeDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVTDgKLI 321
Cdd:cd03312 240 FGSLgENLDLLASLPVDGLHLDLVRG-PENLEAVLKAGFA-DKVLSAGVVDGRNIWRADLAASLALLETLAAILGD-RLV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489829542 322 VQPSNSLLHVPVTKLSEPDLDEVILGGLSFADQKLDEIAILTKA 365
Cdd:cd03312 317 VSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
6-315 |
5.79e-171 |
|
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: 493.64 E-value: 5.79e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 6 SSNLGYPRLGEKREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDTSVTFGIIPKRF 85
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 86 QHDGGKVSLNTYFDIARGKSDAVASEMTKWFNTNYHYIVPELADAD-PKVLDNRALYYYEEAkKELGIEGKPVLVGPVTY 164
Cdd:pfam08267 81 GNDGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDTeFKLNSNKLLDEYKEA-KALGIETKPVLLGPVTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 165 LKLGKGNDAE-NFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQTYF 243
Cdd:pfam08267 160 LKLSKGKGGSfDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLATYF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489829542 244 ESL-DYYEEVVNLPVAAIGIDFVHdHGDSLEALKAhGFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYV 315
Cdd:pfam08267 240 GSVaDALELLASLPVAGLGLDLVR-GPENLAALKK-GFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
432-754 |
1.70e-170 |
|
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: 493.10 E-value: 1.70e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 592 EALERNGIKVIQVDEPALREGLPLKQARWEKYLNDAVYSFKLTTASVQNDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTRKEPETIAALQDMIK 751
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMVD 320
|
...
gi 489829542 752 ATK 754
Cdd:pfam01717 321 AAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
432-759 |
3.00e-137 |
|
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: 407.99 E-value: 3.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERTDMVEYFGQKLAGFQATK 511
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 512 FGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEV 591
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 592 EALERNGIKVIQVDEPALREGLPlkqarwEKYLNDAVYSFKLTTASVQnDTQIHTHMCYSDFDDIIDTISALDADVISIE 671
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVP-DTKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 672 TSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTR----KEPETIAALQ 747
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKLR 313
|
330
....*....|..
gi 489829542 748 DMIKATKEVRAE 759
Cdd:COG0620 314 NMVAFAREVRGE 325
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
433-755 |
6.83e-128 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers the C-terminal barrel, and a few single-barrel sequences most similar to the C-terminal barrel. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Sidechains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239427 [Multi-domain] Cd Length: 332 Bit Score: 384.27 E-value: 6.83e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 433 PTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERTDMVEYFGQKLAGFQATkf 512
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTK-RPVKGMLTAPVTIINWSFVRD---DVPESVVANQVGLALR 588
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 589 KEVEALERNGIKVIQVDEPALREGLPL-KQARWEKYLNDAVYSFKLTtasvQNDTQIHTHMCYSDF----------DDII 657
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLePDDLAADYLKWANEALADR----PDDTQIHTHICYGNFrstwaaeggyEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 658 DTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLKTR 737
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATR 314
|
330
....*....|....*...
gi 489829542 738 KEPETIAALQDMIKATKE 755
Cdd:cd03311 315 ERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
6-358 |
4.50e-89 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 283.18 E-value: 4.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 6 SSNLGYPRLgekREWKRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSFYDQVLDtsvtfgiIPKRF 85
Cdd:COG0620 4 TTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGY-------FPERL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 86 qhDGgkvslntyFDIARGKSDavasemtKWFNTNYHYiVPELAD----ADPKVLDnralyYYEEAKKELGIEGKPVLVGP 161
Cdd:COG0620 74 --DG--------YAFARNGWV-------EWFDTNYHY-VPEITGdvsfSGPMTVE-----EFRFAKSLTGKPVKPVLPGP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 162 VTYLKLGKGNDAENFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQT 241
Cdd:COG0620 131 VTLLLLSKVRDYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHLHT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 242 YFESLDY-YEEVVNLPVAAIGIDFVHDHGDSLEALKAhgFPEDKYLAAGVIDGRNVWRSDLDAKLSLLTEIADYVTDGKL 320
Cdd:COG0620 211 CYGGYEDiLEALAALPVDGIHLEFVRSRAGLLEPLKE--LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERL 288
|
330 340 350
....*....|....*....|....*....|....*...
gi 489829542 321 IVQPSNSLLHVPVTkLSEPDLDEVILGGLSFADQKLDE 358
Cdd:COG0620 289 WVSPDCGLKHRPVD-LTREEAWAKLRNMVAFAREVRGE 325
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
424-760 |
1.02e-69 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 232.18 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 424 HAWLNLPLFPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERTDMVEYFGQK 503
Cdd:PRK04326 1 MDHDKLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 504 LAGFqatKF-GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLT-KRPVKGMLTAPVTIINWSF--VRDDVPESVV 579
Cdd:PRK04326 81 IEGF---KFyGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFneYYKDKEELVF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 580 AnqvgLA--LRKEVEALERNGIKVIQVDEPAL---REGLPLkqarwekylndAVYSFKLTTASVqnDTQIHTHMCYSDFD 654
Cdd:PRK04326 158 D----LAkvINEEIKNLVEAGAKYIQIDEPALathPEDVEI-----------AVEALNRIVKGI--NAKLGLHVCYGDYS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 655 DIIDTISALDADVISIETSRSHGEIISTFEEVTYDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGL 734
Cdd:PRK04326 221 RIAPYILEFPVDQFDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGL 300
|
330 340
....*....|....*....|....*.
gi 489829542 735 KTRKEPETIAALQDMIKATKEVRAEY 760
Cdd:PRK04326 301 KLLPREIAYQKLVNMVKATREVREEL 326
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
431-757 |
2.65e-37 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 142.05 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 431 LFPTTTIGSFPQSPEVRKTRADWLKGNI-TDAEYNAFIEKEtarwIKIQEELDIDVLVHGEFeRTDMVEYFGQKLAGFQA 509
Cdd:PRK00957 1 IMITTVVGSYPVVKGEPETLKDKIKGFFgLYDPYKPAIEEA----VADQVKAGIDIISDGQV-RGDMVEIFASNMPGFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 510 tkfgwvQSYGSRaVRPPliygdvafTEEITVKESVYAQSLTK-----RPVKGMLTAPVTIINWS----FVRDDVPESVVA 580
Cdd:PRK00957 76 ------KRVIGR-VEPP--------AKPITLKDLKYAKKVAKkkdpnKGVKGIITGPSTLAYSLrvepFYSDNKDEELIY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 581 NqVGLALRKEVEALERNGIKVIQVDEPALREGLP-LKQARweKYLNDAVYSFKLTTAsvqndtqihTHMCySDFDDIIDT 659
Cdd:PRK00957 141 D-LARALRKEAEALEKAGVAMIQIDEPILSTGAYdLEVAK--KAIDIITKGLNVPVA---------MHVC-GDVSNIIDD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 660 ISALDADVISIETSrSHGEIISTFEEVTY-DKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAIDAKQFWINPDCGLktRK 738
Cdd:PRK00957 208 LLKFNVDILDHEFA-SNKKNLEILEEKDLiGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGM--RM 284
|
330 340
....*....|....*....|.
gi 489829542 739 EPETIA--ALQDMIKATKEVR 757
Cdd:PRK00957 285 LPRDVAfeKLKNMVEAAREIR 305
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
433-751 |
2.49e-36 |
|
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc.
Pssm-ID: 238261 [Multi-domain] Cd Length: 306 Bit Score: 139.17 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 433 PTTTIGSFPQSPEVRKTRadwlkgnITDAEYNAFIEKETARWIKiQEELDIDVLVHGEFERTDMVEYFGqklagfqatkf 512
Cdd:cd00465 1 PVQCEGQTGIMEASETMA-------ISEEPGETSKAEWGITLVE-PEEIPLDVIPVHEDDVLKVAQALG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESV-YAQSLTKRPVKGMLTAPVTIINWSFVRDDV---------PESVVANQ 582
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEDPFREAPALEHItAVRSLEEFPTAGAAGGPFTFTHHSMSMGDAlmalyerpeAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 583 VGLALRKEVEALERNGIKVIQVDEPALREGLP--LKQARWEKYLNdavYSFKLTTASVQNDTQIHTHMCYSDFDDiIDTI 660
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSflGPKMFKKFALP---AYKKVAEYKAAGEVPIVHHSCYDAADL-LEEM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 661 SALDADVISIETSRshGEIISTFEEVTYDKEIGLGVYDIHSPRvpTVTEIQDNIRRALRAIDaKQFWINPDCGLKTRK-- 738
Cdd:cd00465 218 IQLGVDVISFDMTV--NEPKEAIEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLG-PHYIINPDCGLGPDSdy 292
|
330
....*....|...
gi 489829542 739 EPETIAALQDMIK 751
Cdd:cd00465 293 KPEHLRAVVQLVD 305
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
433-755 |
4.15e-32 |
|
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: 127.16 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 433 PTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERtDMveyFGQKLAGFQATKF 512
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DM---IGRFLEVLVDLET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESV--VANQVGLALRKE 590
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPDAYedLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 591 VEALERNGIKVIQVDEPALREGLPLKQArWEKYLNDAVYSFKLttasvQNDTQIHTHMCYsdfDDIIDTISALDADVISI 670
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFE-DLEIVDAALEEVSL-----KSGGDVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 671 ETSRS---HGEIISTFEEVTY-DKEIGLGVYDIHSPRVPTVTEIQDnIRRALRAID------AKQFWINPDCGLKTRKEP 740
Cdd:cd03310 228 DAAALpskYLEDLKKLLRIGVrTLILGLVVTDNEAKGRNAWKEIER-LEKLVRRLEepgevlDEILYLTPDCGLAFLPPQ 306
|
330
....*....|....*
gi 489829542 741 ETIAALQDMIKATKE 755
Cdd:cd03310 307 EARRKLALLAEAARE 321
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
434-759 |
1.46e-21 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 96.91 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 434 TTTIGSFpQSPEVRKTRADWLKGniTDaEYNAFIEKETARWIKIQEELDID-VLVHGEFERTDMVEYFGQKLAGFQAtkF 512
Cdd:PRK01207 6 TQEIGSF-RKPEYLSREFHKIEG--TD-KFYELAERATLETLDVFENAGLDnIGIGGEMFRWEMYEHPAERIKGIIF--Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 513 GWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIINWSFVRDDVPESVVANQVGLALRKEVE 592
Cdd:PRK01207 80 GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFARIINEELK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 593 ALER------NGIKV-IQVDEPALREGlPLKQARWEKYLNDAVYSFklttasvqnDTQIHTHMCYS-DFDDIIDTISALD 664
Cdd:PRK01207 160 DIKSawdrksPGRKLeIQIDEPATTTH-PDEMDIVVDSINKSVYGI---------DNEFSIHVCYSsDYRLLYDRIPELN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 665 ADVISIETS-------------RSHGEIISTFEEVT----YDKEIGLGVYDIHSPRVPTVTEIQDNIRRALRAI-DAKQF 726
Cdd:PRK01207 230 IDGYNLEYSnrdtlepgtsdekRPGFQDLKYFAEHNeslqRKKFIGLGVTDVHIDYVEPVKLIEDRIRYALKIIkDPELV 309
|
330 340 350
....*....|....*....|....*....|...
gi 489829542 727 WINPDCGLKTRKEPETIAALQDMIKATKEVRAE 759
Cdd:PRK01207 310 RLNPDCGLRTRSREIGEQKLRNMVAAKNNILKE 342
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
21-335 |
1.96e-17 |
|
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: 84.02 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 21 KRALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFsfYDQVLDTSVTFGIIPKRFqhdggkvslntyfdi 100
Cdd:cd03310 15 TKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQL--GDDMIGRFLEVLVDLETG--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 101 argksdavasemTKWFNTNYHYIVPEladADPKVLDNRALYYYEEAK--KELGIEGKPVLVGPVTYLKLGKGNDAENF-- 176
Cdd:cd03310 78 ------------TRFFDNNFFYRPPE---AKIEAFLPLELDYLEEVAeaYKEALKVKVVVTGPLTLALLAFLPNGEPDay 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 177 EALLDKFIPAYVEILKELERAGAKWVQIDEP----YLATSFDKSEIKLFEKVYQAFQTAVPnLKIELQTYfeslDYYEEV 252
Cdd:cd03310 143 EDLAKSLAEFLREQVKELKNRGIVVVQIDEPslgaVGAGAFEDLEIVDAALEEVSLKSGGD-VEVHLCAP----LDYEAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 253 VNLPVAAIGIDFVHDHGDSLEALKA---HGFpEDKYLAAGVID----GRNVWR--SDLDAKLSLLtEIADYVTDGKLIVQ 323
Cdd:cd03310 218 LELGVDVIGFDAAALPSKYLEDLKKllrIGV-RTLILGLVVTDneakGRNAWKeiERLEKLVRRL-EEPGEVLDEILYLT 295
|
330
....*....|..
gi 489829542 324 PSNSLLHVPVTK 335
Cdd:cd03310 296 PDCGLAFLPPQE 307
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
430-734 |
6.77e-17 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 82.81 E-value: 6.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 430 PLFPTTTIGSFPQ-----SPEvrKTRADW-LKGN-ITDAEYNAfiekeTARWIKIQEELDIDVLVHGEFERTDMVEYFGQ 502
Cdd:PRK09121 1 TLLPTSTAGSLPKpswlaEPE--TLWSPWkLQGEeLIEGKQDA-----LRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 503 KLAGFQATKFGWVQSYGSRAVRPPLIYGDVAFTEEITVKESVYAQSLTKRPVKGMLTAPVTIInwsfvrDDVPESVVANQ 582
Cdd:PRK09121 74 HLSGVDFEKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMI------DTLYDDHYKSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 583 VGLA------LRKEVEALERNGIKVIQVDEPALRegLPLKQAR-WE-KYLNDAVYSFKLTTAsvqndtqihTHMCYS--- 651
Cdd:PRK09121 148 EKLAwefakiLNQEAKELEAAGVDIIQFDEPAFN--VFFDEVNdWGvAALERAIEGLKCETA---------VHICYGygi 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 652 ---------------DFDDIIDTISALDADVISIETSRSH--GEIIstfeEVTYDKEIGLGVYDIHSPRVPTVTEIQDNI 714
Cdd:PRK09121 217 kantdwkktlgsewrQYEEAFPKLQKSNIDIISLECHNSRvpMDLL----ELIRGKKVMVGAIDVASDTIETPEEVADTL 292
|
330 340
....*....|....*....|
gi 489829542 715 RRALRAIDAKQFWINPDCGL 734
Cdd:PRK09121 293 RKALQFVDADKLYPCTNCGM 312
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
10-335 |
1.97e-14 |
|
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: 74.84 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 10 GYPRLGEKREWKRALEKFWngaiseeellAETKALRLHALKKQQEKGIDLIPVgdfsFYDQVLDTSVTFGIIPkrfqhdg 89
Cdd:cd00465 6 GQTGIMEASETMAISEEPG----------ETSKAEWGITLVEPEEIPLDVIPV----HEDDVLKVAQALGEWA------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 90 gkvslntyfdiargksdavasemtkWFNTNYHYIVPELADADPKVLDNRALYYYEEAKKELGIEGKPVLVGPVTYLKLGK 169
Cdd:cd00465 65 -------------------------FRYYSQAPSVPEIDEEEDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSM 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 170 GNDA---------ENFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATS--------FDKSEIKLFEKVYQAFqtAV 232
Cdd:cd00465 120 SMGDalmalyerpEAMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQInsflgpkmFKKFALPAYKKVAEYK--AA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 233 PNLKIELQTYFESLDYYEEVVNLPVAAIGIDFVhdHGDSLEALKAHGfpEDKYLAAGVIDGRNVWRSDLDAKLSllTEIA 312
Cdd:cd00465 198 GEVPIVHHSCYDAADLLEEMIQLGVDVISFDMT--VNEPKEAIEKVG--EKKTLVGGVDPGYLPATDEECIAKV--EELV 271
|
330 340
....*....|....*....|...
gi 489829542 313 DYVtDGKLIVQPSNSLLHVPVTK 335
Cdd:cd00465 272 ERL-GPHYIINPDCGLGPDSDYK 293
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
11-324 |
1.95e-13 |
|
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: 72.26 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 11 YPRlgeKREWKRALEKFWNGAISEEELL-AETKALRlHALKKQQEKGIDLIPVGDFSFYDQVLDtsvtFGiipkrfQHDG 89
Cdd:cd03311 8 FPR---PKELREARAKFKKGEISAEELReAEDDAIA-DAVKDQEEAGLDVVTDGEFRRSDMVEY----FL------ERLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 90 GkvslntyFDiargKSDAVASEMTKwfntnyhYIVPELADADPKVLDNRALYYYEEAKKelGIEGKPV---LVGPVT--- 163
Cdd:cd03311 74 G-------FE----FTGWVQSYGSR-------YYKPPGIVGDVSRRPPMTVEEGKIAQS--LTHPKPLkgiLTGPVTips 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 164 YLKLGKGNDAENFEALLDKFIPAYVEILKELERAGAKWVQIDEPYLATSFDKSEIKLFEKVYQAFQTAVPNLKIELQ--- 240
Cdd:cd03311 134 PSFVRFRGYYPSREELAMDLALALREEIRDLYDAGCRYIQIDEPALAEGLPLEPDDLAADYLKWANEALADRPDDTQiht 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 241 ---------TYFESLDY---YEEVVNLPVAAIGIDFVHDHGDSLEALKAhgFPEDKYLAAGVIDGRNVWRSDLDAKLSLL 308
Cdd:cd03311 214 hicygnfrsTWAAEGGYepiAEYIFELDVDVFFLEYDNSRAGGLEPLKE--LPYDKKVGLGVVDVKSPEVESPEEVKDRI 291
|
330
....*....|....*.
gi 489829542 309 TEIADYVTDGKLIVQP 324
Cdd:cd03311 292 EEAAKYVPLEQLWVSP 307
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
22-295 |
4.83e-12 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 22 RALEKFWNGAISEEELLAETKALRLHALKKQQEKGIDLIPVGDFSfYDQVLDtsVTFGIIpkrfqhDGGKVSlntyfdia 101
Cdd:PRK08575 19 KVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFR-WDDIFD--PTISFI------SGVEKG-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 102 rgksdavasEMTKWFNTNYHYIVPELADADPKVLDNRALYYYEEA---KKELGIEG--KPVLVGPVTYLKLGKGNDAENF 176
Cdd:PRK08575 82 ---------GLQRFYDNNFYYRQPVIKEKINLKEENPYLQWLESAreiKEEVSLESklKAVLPGPLTYAVLSDNEYYKNL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 177 EALLDKFIPAYVEILKELErAGAKWVQIDEPylatSFDKSEIK--LFEKVYQAFQTAVPNLKIE--LQTYF--ESLDYYE 250
Cdd:PRK08575 153 IELMEDYASVVNSLIKELS-SVVDAVEIHEP----SIFAKGIKrdTLEKLPEVYKTMAKNVNIEkhLMTYFeiNNLKRLD 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489829542 251 EVVNLPVAAIGIDFVhdhgdslEALKAHG----FPEDKYLAAGVIDGRN 295
Cdd:PRK08575 228 ILFSLPVTYFGIDVI-------ENLKKLGrvytYLKGRKVYLGILNARN 269
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
191-292 |
8.06e-10 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 61.15 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 191 LKELERAGAKWVQIDEPYLATSFDKSEIklfekVYQAFQTAVPNLKIELQTYFESLDY---YEEVVNLPVAAIGIDFVHD 267
Cdd:PRK04326 167 IKNLVEAGAKYIQIDEPALATHPEDVEI-----AVEALNRIVKGINAKLGLHVCYGDYsriAPYILEFPVDQFDLEFANG 241
|
90 100
....*....|....*....|....*
gi 489829542 268 HGDSLEALKAHGFpeDKYLAAGVID 292
Cdd:PRK04326 242 NYKLLDLLKEYGF--DKELGLGVID 264
|
|
| HemE |
COG0407 |
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
121-275 |
9.77e-06 |
|
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440176 [Multi-domain] Cd Length: 336 Bit Score: 48.29 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 121 HYIVPELADAD----PKVLDNRALYYYE---EAKKELGIEgKPVLV---GPVT---YLKLGKGN-------DAENFEALL 180
Cdd:COG0407 92 EHPIRDAEDVDalevPDPEDGRLPYVLEairLLKEELGDE-VPLIGfagGPFTlasYLVEGFEKlkklmyrDPELVHALL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 181 DKFIPAYVEILKELERAGAKWVQIDEPyLATS-----FDKSEIKLFEKVYQAFQTA-VPNLkielqTYFE--SLDYYEEV 252
Cdd:COG0407 171 DKLTDAVIEYLKAQIEAGADAVQIFDS-WAGLlspkdFEEFVLPYLKRIVDALKERgVPVI-----IHFCgdGTPLLEDM 244
|
170 180
....*....|....*....|...
gi 489829542 253 VNLPVAAIGIDFVHDHGDSLEAL 275
Cdd:COG0407 245 AETGADALSVDWRVDLAEAKERL 267
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
432-719 |
5.51e-03 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 432 FPTTTIGSFPQSPEVRKTRADWLKGNITDAEYNAFIEKETARWIKIQEELDIDVLVHGEFERTDMVEYFGQKLAGfqATK 511
Cdd:PRK08575 3 IKKALVGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISG--VEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 512 FGWVQSYGSR-AVRPPLIYGDVAFTEEIT----------VKESVYAQSLTKRPVKGMLTAPVTIINWSFvrDDVPESVva 580
Cdd:PRK08575 81 GGLQRFYDNNfYYRQPVIKEKINLKEENPylqwlesareIKEEVSLESKLKAVLPGPLTYAVLSDNEYY--KNLIELM-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489829542 581 nqvgLALRKEVEALERN---GIKVIQVDEPALREGlPLKQARWEKylNDAVYsfKLTTASVQNDTQIHTHMCYSDFDDIi 657
Cdd:PRK08575 157 ----EDYASVVNSLIKElssVVDAVEIHEPSIFAK-GIKRDTLEK--LPEVY--KTMAKNVNIEKHLMTYFEINNLKRL- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489829542 658 DTISALDADVISIETSRSHGEIISTFEEVTyDKEIGLGVYDIHSPRVPTVTEIQDNIRRALR 719
Cdd:PRK08575 227 DILFSLPVTYFGIDVIENLKKLGRVYTYLK-GRKVYLGILNARNTKMEKISTIRRIVNKVKR 287
|
|
| |
