|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-754 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1272.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 1 MTTTIIGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPK 80
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 81 RYQDLNLS-PLDTYFAQARGYQGEAgdvkALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLI 159
Cdd:PRK05222 82 RFGNLGGSvDLDTYFAMARGGKDVA----ALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 160 GPYTLLKLSRFI--DVVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKIL 237
Cdd:PRK05222 158 GPVTFLWLSKSKgeGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 238 VQTYFGDLTDSFDRIQKLPFDGFGLDFVEGYANLDLLKQHgFPAHATLFAGIVNGKNIWRTHYADALATIKQLATITDKL 317
Cdd:PRK05222 238 LATYFGSLNDALDLLASLPVDGLHLDLVRGPEQLAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKVDRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 318 VLSTSTSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAIF--HTGADHAAYQANVALFSKPRYQE---NKALNA 392
Cdd:PRK05222 317 WVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALngGRGAVAEALAANRAAIAARRTSPrvhNPAVRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 393 KIAALTPEDYKRTPARKTRLAIQAKEFKLPLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEE 472
Cdd:PRK05222 397 RLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 473 IGLDVLVHGEFERNDMVEYFGENFGGFRFTDNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTG 552
Cdd:PRK05222 477 LGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 553 PVTIYNWSFPREDLSQKTSVEQIALALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAFRLVASKVK 632
Cdd:PRK05222 557 PVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDW-DAYLDWAVEAFRLATSGVK 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 633 PETQIHTHMCYSQFGDIIKAIDDLDADVISFEAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILK 712
Cdd:PRK05222 636 DETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALE 715
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 491943685 713 RLPADHVWINPDCGLKTRDVPETKASLINMVAAAKQVRKELT 754
Cdd:PRK05222 716 VIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELA 757
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
6-752 |
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: 1058.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 6 IGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPKRYQDL 85
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 86 NLSP-LDTYFAQARGYqgeaGDVKALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLIGPYTL 164
Cdd:TIGR01371 81 GGDLdLDTYFAMARGN----KDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 165 LKLSRFID--VVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKILVQTYF 242
Cdd:TIGR01371 157 LKLSKAVEepFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 243 GDLTDSFDRIQKLPFDGFGLDFVEGYANLDLlKQHGFPAHATLFAGIVNGKNIWRTHYADALATIKQLATITDKLVLSTS 322
Cdd:TIGR01371 237 DSVGDALEALVSLPVKGIGLDFVHGKGTLEL-VKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 323 TSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAIFHTGAD------HAAYQANVALFSKPRyQENKALNAKIAA 396
Cdd:TIGR01371 316 CSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDavafalEANAAAIAARKSSPR-VNDAQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 397 LTPEDYKRTPARKTRLAIQAKEFKLPLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNhKEEI-EWLKFQEEIGL 475
Cdd:TIGR01371 395 LKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFI-KEEIkKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 476 DVLVHGEFERNDMVEYFGENFGGFRFTDNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVT 555
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 556 IYNWSFPREDLSQKTSVEQIALALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAFRLVASKVKPET 635
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDW-PEYLDWAVEAFRLATSGVKDET 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 636 QIHTHMCYSQFGDIIKAIDDLDADVISFEAARSDFSLLDILKAT-HFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRL 714
Cdd:TIGR01371 633 QIHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGfGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVL 712
|
730 740 750
....*....|....*....|....*....|....*...
gi 491943685 715 PADHVWINPDCGLKTRDVPETKASLINMVAAAKQVRKE 752
Cdd:TIGR01371 713 PAERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
2-362 |
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: 528.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 2 TTTIIGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPKR 81
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 82 YQDLN-LSPLDTYFAQARGYQgeagDVKALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLIG 160
Cdd:cd03312 81 FGALGgLVDLDTYFAMARGNQ----DVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 161 PYTLLKLSRFID--VVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKILV 238
Cdd:cd03312 157 PVTFLKLSKAKGggFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 239 QTYFGDLTDSFDRIQKLPFDGFGLDFVEGYANLDLLKQHGFpAHATLFAGIVNGKNIWRTHYADALATIKQLATIT-DKL 317
Cdd:cd03312 237 ATYFGSLGENLDLLASLPVDGLHLDLVRGPENLEAVLKAGF-ADKVLSAGVVDGRNIWRADLAASLALLETLAAILgDRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 491943685 318 VLSTSTSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAI 362
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
424-747 |
1.40e-165 |
|
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: 480.39 E-value: 1.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 424 LPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFnHKEEIE-WLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFT 502
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELR-IRGEIEdAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 503 DNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALALEDE 582
Cdd:pfam01717 80 KNGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 583 VLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAFRLVASKVKPETQIHTHMCYSQFGDIIKAIDDLDADVIS 662
Cdd:pfam01717 160 VADLEAAGIAVIQIDEPALREGLPLKKLDW-AAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 663 FEAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWINPDCGLKTRDVPETKASLINM 742
Cdd:pfam01717 239 IEASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNM 318
|
....*
gi 491943685 743 VAAAK 747
Cdd:pfam01717 319 VDAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
424-752 |
8.44e-146 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 429.95 E-value: 8.44e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 424 LPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFTD 503
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 504 NGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALALEDEV 583
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 584 LDLEKHGIKIIQIDEPALRENLPlrkkdwyPKYLDWAVPAFRLVASKVkPETQIHTHMCYSQFGDIIKAIDDLDADVISF 663
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP-------DEYLDWAVEAYNRAAAGV-PDTKIHLHTCYGGYEDILEALAALPVDGIHL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 664 EAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWINPDCGLKTRDV----PETKASL 739
Cdd:COG0620 233 EFVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVdltrEEAWAKL 312
|
330
....*....|...
gi 491943685 740 INMVAAAKQVRKE 752
Cdd:COG0620 313 RNMVAFAREVRGE 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
1-754 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1272.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 1 MTTTIIGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPK 80
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 81 RYQDLNLS-PLDTYFAQARGYQGEAgdvkALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLI 159
Cdd:PRK05222 82 RFGNLGGSvDLDTYFAMARGGKDVA----ALEMTKWFNTNYHYIVPEFDPDTQFKLTSNKLLDEFEEAKALGINTKPVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 160 GPYTLLKLSRFI--DVVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKIL 237
Cdd:PRK05222 158 GPVTFLWLSKSKgeGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 238 VQTYFGDLTDSFDRIQKLPFDGFGLDFVEGYANLDLLKQHgFPAHATLFAGIVNGKNIWRTHYADALATIKQLATITDKL 317
Cdd:PRK05222 238 LATYFGSLNDALDLLASLPVDGLHLDLVRGPEQLAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKVDRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 318 VLSTSTSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAIF--HTGADHAAYQANVALFSKPRYQE---NKALNA 392
Cdd:PRK05222 317 WVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALngGRGAVAEALAANRAAIAARRTSPrvhNPAVRA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 393 KIAALTPEDYKRTPARKTRLAIQAKEFKLPLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEE 472
Cdd:PRK05222 397 RLAALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 473 IGLDVLVHGEFERNDMVEYFGENFGGFRFTDNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTG 552
Cdd:PRK05222 477 LGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 553 PVTIYNWSFPREDLSQKTSVEQIALALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAFRLVASKVK 632
Cdd:PRK05222 557 PVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDW-DAYLDWAVEAFRLATSGVK 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 633 PETQIHTHMCYSQFGDIIKAIDDLDADVISFEAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILK 712
Cdd:PRK05222 636 DETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALE 715
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 491943685 713 RLPADHVWINPDCGLKTRDVPETKASLINMVAAAKQVRKELT 754
Cdd:PRK05222 716 VIPAERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAELA 757
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
6-752 |
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: 1058.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 6 IGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPKRYQDL 85
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 86 NLSP-LDTYFAQARGYqgeaGDVKALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLIGPYTL 164
Cdd:TIGR01371 81 GGDLdLDTYFAMARGN----KDVPALEMTKWFNTNYHYIVPELSPTTEFKLTSNKPLEEYLEAKELGIETKPVLLGPITF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 165 LKLSRFID--VVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKILVQTYF 242
Cdd:TIGR01371 157 LKLSKAVEepFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 243 GDLTDSFDRIQKLPFDGFGLDFVEGYANLDLlKQHGFPAHATLFAGIVNGKNIWRTHYADALATIKQLATITDKLVLSTS 322
Cdd:TIGR01371 237 DSVGDALEALVSLPVKGIGLDFVHGKGTLEL-VKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 323 TSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAIFHTGAD------HAAYQANVALFSKPRyQENKALNAKIAA 396
Cdd:TIGR01371 316 CSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDavafalEANAAAIAARKSSPR-VNDAQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 397 LTPEDYKRTPARKTRLAIQAKEFKLPLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNhKEEI-EWLKFQEEIGL 475
Cdd:TIGR01371 395 LKEDDFRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFI-KEEIkKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 476 DVLVHGEFERNDMVEYFGENFGGFRFTDNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVT 555
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 556 IYNWSFPREDLSQKTSVEQIALALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAFRLVASKVKPET 635
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDW-PEYLDWAVEAFRLATSGVKDET 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 636 QIHTHMCYSQFGDIIKAIDDLDADVISFEAARSDFSLLDILKAT-HFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRL 714
Cdd:TIGR01371 633 QIHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGfGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVL 712
|
730 740 750
....*....|....*....|....*....|....*...
gi 491943685 715 PADHVWINPDCGLKTRDVPETKASLINMVAAAKQVRKE 752
Cdd:TIGR01371 713 PAERLWVNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
1-753 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 848.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 1 MTTTIIGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPK 80
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 81 RYQDLN-LSPLDTYFAQARGYQGeagdVKALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLI 159
Cdd:PLN02475 81 RYGWTGgEIGFDVYFSMARGNAS----VPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVDTVPVLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 160 GPYTLLKLSRFIDVVPDDF-----VADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAA 234
Cdd:PLN02475 157 GPVSYLLLSKPAKGVDKSFdllslLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 235 KILVQTYFGDL-TDSFDRIQKLP-FDGFGLDFVEGYANLDLLKQHGFPAHATLFAGIVNGKNIWRTHYADALATIKQLAT 312
Cdd:PLN02475 237 NVLVETYFADVpAEAYKTLTSLKgVTAFGFDLVRGTKTLDLIKKAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 313 I--TDKLVLSTSTSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAIFHTGADHAAYQANVALF----SKPRYQe 386
Cdd:PLN02475 317 IvgKDKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQasrrSSPRVT- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 387 NKALNAKIAALTPEDYKRTPARKTRLAIQAKEFKLPLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEY-TAFnhKEEIE 465
Cdd:PLN02475 396 NEAVQKAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYvKAI--KEEIA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 466 W-LKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFTDNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDH 544
Cdd:PLN02475 474 KvVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 545 LVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAF 624
Cdd:PLN02475 554 PMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEH-AFYLDWAVHSF 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 625 RLVASKVKPETQIHTHMCYSQFGDIIKAIDDLDADVISFEAARSDFSLLDILK-ATHFQTHVGPGVYDIHSPRIPSKDEI 703
Cdd:PLN02475 633 RITNCGVQDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFReGVKYGAGIGPGVYDIHSPRIPSTEEI 712
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 491943685 704 VHIIHEILKRLPADHVWINPDCGLKTRDVPETKASLINMVAAAKQVRKEL 753
Cdd:PLN02475 713 ADRINKMLAVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQL 762
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
2-362 |
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: 528.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 2 TTTIIGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPKR 81
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 82 YQDLN-LSPLDTYFAQARGYQgeagDVKALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLIG 160
Cdd:cd03312 81 FGALGgLVDLDTYFAMARGNQ----DVPALEMTKWFDTNYHYIVPELSPDTEFKLASNKLLDEYLEAKALGINTKPVLLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 161 PYTLLKLSRFID--VVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKILV 238
Cdd:cd03312 157 PVTFLKLSKAKGggFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 239 QTYFGDLTDSFDRIQKLPFDGFGLDFVEGYANLDLLKQHGFpAHATLFAGIVNGKNIWRTHYADALATIKQLATIT-DKL 317
Cdd:cd03312 237 ATYFGSLGENLDLLASLPVDGLHLDLVRGPENLEAVLKAGF-ADKVLSAGVVDGRNIWRADLAASLALLETLAAILgDRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 491943685 318 VLSTSTSLLHVPYTLRNETHLKPEEKQYLAFAEEKLNELHELDAI 362
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
424-747 |
1.40e-165 |
|
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: 480.39 E-value: 1.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 424 LPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFnHKEEIE-WLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFT 502
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELR-IRGEIEdAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 503 DNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALALEDE 582
Cdd:pfam01717 80 KNGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 583 VLDLEKHGIKIIQIDEPALRENLPLRKKDWyPKYLDWAVPAFRLVASKVKPETQIHTHMCYSQFGDIIKAIDDLDADVIS 662
Cdd:pfam01717 160 VADLEAAGIAVIQIDEPALREGLPLKKLDW-AAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 663 FEAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWINPDCGLKTRDVPETKASLINM 742
Cdd:pfam01717 239 IEASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNM 318
|
....*
gi 491943685 743 VAAAK 747
Cdd:pfam01717 319 VDAAK 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
424-752 |
8.44e-146 |
|
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; Methionine synthase II (cobalamin-independent) is part of the Pathway/BioSystem: Methionine biosynthesis
Pssm-ID: 440385 [Multi-domain] Cd Length: 325 Bit Score: 429.95 E-value: 8.44e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 424 LPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFTD 503
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 504 NGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALALEDEV 583
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 584 LDLEKHGIKIIQIDEPALRENLPlrkkdwyPKYLDWAVPAFRLVASKVkPETQIHTHMCYSQFGDIIKAIDDLDADVISF 663
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP-------DEYLDWAVEAYNRAAAGV-PDTKIHLHTCYGGYEDILEALAALPVDGIHL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 664 EAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWINPDCGLKTRDV----PETKASL 739
Cdd:COG0620 233 EFVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRPVdltrEEAWAKL 312
|
330
....*....|...
gi 491943685 740 INMVAAAKQVRKE 752
Cdd:COG0620 313 RNMVAFAREVRGE 325
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
3-314 |
1.22e-144 |
|
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: 426.23 E-value: 1.22e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 3 TTIIGYPRIGEHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTLDVANLLNIVPKRY 82
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 83 QDLN-LSPLDTYFAQARGYQgeagDVKALAMKKWFNTNYHYLVPEFDHDTKIQVTDWQLFVQFEEAKALGINGRPTLIGP 161
Cdd:pfam08267 81 GNDGgLDDLDTYFAMARGNK----DVPALEMTKWFNTNYHYIVPELDKDTEFKLNSNKLLDEYKEAKALGIETKPVLLGP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 162 YTLLKLSRFID--VVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKILVQ 239
Cdd:pfam08267 157 VTFLKLSKGKGgsFDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491943685 240 TYFGDLTDSFDRIQKLPFDGFGLDFVEGYANLDLLKQhGFPAHATLFAGIVNGKNIWRTHYADALATIKQLATIT 314
Cdd:pfam08267 237 TYFGSVADALELLASLPVAGLGLDLVRGPENLAALKK-GFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
425-747 |
6.37e-131 |
|
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: 391.98 E-value: 6.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 425 PTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFTdn 504
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 505 GWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDH-LVKGMLTGPVTIYNWSFPREDLSQKTSVE---QIALALE 580
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHPkPLKGILTGPVTIPSPSFVRFRGYYPSREElamDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 581 DEVLDLEKHGIKIIQIDEPALRENLPLRKKDWYPKYLDWAVPAFRlvasKVKPETQIHTHMCYSQFG----------DII 650
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPDDLAADYLKWANEALA----DRPDDTQIHTHICYGNFRstwaaeggyePIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 651 KAIDDLDADVISFEAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWINPDCGLKTR 730
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATR 314
|
330
....*....|....*..
gi 491943685 731 DVPETKASLINMVAAAK 747
Cdd:cd03311 315 ERGNALTKLENMVKAAL 331
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
420-757 |
6.93e-83 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 266.84 E-value: 6.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 420 KLPLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGF 499
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 500 RFtdNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQT-DHLVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALA 578
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 579 LEDEVLDLEKHGIKIIQIDEPALREnlplrkkdwYPKYLDWAVPAFRLVASKVkpETQIHTHMCYSQFGDIIKAIDDLDA 658
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPALAT---------HPEDVEIAVEALNRIVKGI--NAKLGLHVCYGDYSRIAPYILEFPV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 659 DVISFEAARSDFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWINPDCGLKTRDVPETKAS 738
Cdd:PRK04326 232 DQFDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQK 311
|
330
....*....|....*....
gi 491943685 739 LINMVAAAKQVRKELTHEN 757
Cdd:PRK04326 312 LVNMVKATREVREELDKGG 330
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
2-355 |
4.92e-81 |
|
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: 262.00 E-value: 4.92e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 2 TTTIIGYPRIgehRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDntldvanLLNIVPKR 81
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 82 yqdlnlspLDTYfAQARgyqgeAGDVKalamkkWFNTNYHYlVPEFDHDTKIqvtDWQLFV-QFEEAKAL-GINGRPTLI 159
Cdd:COG0620 73 --------LDGY-AFAR-----NGWVE------WFDTNYHY-VPEITGDVSF---SGPMTVeEFRFAKSLtGKPVKPVLP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 160 GPYTLLKLSR---FIDvvPDDFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILTQKKAAKI 236
Cdd:COG0620 129 GPVTLLLLSKvrdYKD--REELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 237 LVQTYFGDLTDSFDRIQKLPFDGFGLDFV-EGYANLDLLKQhgFPAHATLFAGIVNGKNIWRTHYADALATIKQLATI-- 313
Cdd:COG0620 207 HLHTCYGGYEDILEALAALPVDGIHLEFVrSRAGLLEPLKE--LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYvp 284
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 491943685 314 TDKLVLSTSTSLLHVPYTLRNEtHLKPEEKQYLAFAEEKLNE 355
Cdd:COG0620 285 PERLWVSPDCGLKHRPVDLTRE-EAWAKLRNMVAFAREVRGE 325
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
423-750 |
5.30e-36 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 138.20 E-value: 5.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 423 LLPTTTIGSFPqtaeVRRNRAKFRRHEITE-----DEYtafnhKEEIEW-LKFQEEIGLDVLVHGEFeRNDMVEYFGENF 496
Cdd:PRK00957 1 IMITTVVGSYP----VVKGEPETLKDKIKGffglyDPY-----KPAIEEaVADQVKAGIDIISDGQV-RGDMVEIFASNM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 497 GGFrftDNGWVQSYgtrgVKPPiiwgdvvrTKPITVAETVFAQSQTDHL-----VKGMLTGPVTI--------YNWSFPR 563
Cdd:PRK00957 71 PGF---DGKRVIGR----VEPP--------AKPITLKDLKYAKKVAKKKdpnkgVKGIITGPSTLayslrvepFYSDNKD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 564 EDLsqktsVEQIALALEDEVLDLEKHGIKIIQIDEPALRENLPlrkkDwypkyLDWAVPAFRLVASKVKPETQIHThmCy 643
Cdd:PRK00957 136 EEL-----IYDLARALRKEAEALEKAGVAMIQIDEPILSTGAY----D-----LEVAKKAIDIITKGLNVPVAMHV--C- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 644 sqfGDIIKAIDDL---DADVISFEAARSDFSLlDILKATHFQTH-VGPGVYDIHSPRIPSKDEIVHIIHEILKRLPADHV 719
Cdd:PRK00957 199 ---GDVSNIIDDLlkfNVDILDHEFASNKKNL-EILEEKDLIGKkIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENI 274
|
330 340 350
....*....|....*....|....*....|.
gi 491943685 720 WINPDCGLKTRDVPETKASLINMVAAAKQVR 750
Cdd:PRK00957 275 LIDPDCGMRMLPRDVAFEKLKNMVEAAREIR 305
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
425-747 |
4.98e-34 |
|
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: 132.94 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 425 PTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERnDMVEYFGENFGGFRFtdn 504
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 505 GWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSF-------PREDLsqktsVEQIAL 577
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFlpngepdAYEDL-----AKSLAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 578 ALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKDwyPKYLDWAvpafrLVASKVKPETQIHTHMCYsqfGDIIKAIDDLD 657
Cdd:cd03310 152 FLREQVKELKNRGIVVVQIDEPSLGAVGAGAFED--LEIVDAA-----LEEVSLKSGGDVEVHLCA---PLDYEALLELG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 658 ADVISFEAARSDFSLLDILKA--THFQTHVGPGVYDI------HSPRIpSKDEIVHIIHEILKRLP--ADHVWINPDCGL 727
Cdd:cd03310 222 VDVIGFDAAALPSKYLEDLKKllRIGVRTLILGLVVTdneakgRNAWK-EIERLEKLVRRLEEPGEvlDEILYLTPDCGL 300
|
330 340
....*....|....*....|
gi 491943685 728 KTRDVPETKASLINMVAAAK 747
Cdd:cd03310 301 AFLPPQEARRKLALLAEAAR 320
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
425-747 |
5.68e-34 |
|
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: 132.24 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 425 PTTTIGSFPQTAEVRRNRakfrrheITEDEYTAFNHKEEIEWLKfQEEIGLDVLVHGEFERNDMVEYFGenfggfrftdn 504
Cdd:cd00465 1 PVQCEGQTGIMEASETMA-------ISEEPGETSKAEWGITLVE-PEEIPLDVIPVHEDDVLKVAQALG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 505 GWVQSYGTRGVKPPIIWGDVV-RTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSFPREDLSQKTS---------VEQ 574
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEDpFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDALMALYerpeamhelIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 575 IALALEDEVLDLEKHGIKIIQIDEPALRENLPLRKKdwyPKYLDWAVPAFRLVAS-KVKPETQIHTHMCYSQFgDIIKAI 653
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGP---KMFKKFALPAYKKVAEyKAAGEVPIVHHSCYDAA-DLLEEM 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 654 DDLDADVISFeaarsDFSLLDILKAthFQTH-----VGPGVYDIHSPRipSKDEIVHIIHEILKRLpADHVWINPDCGLK 728
Cdd:cd00465 218 IQLGVDVISF-----DMTVNEPKEA--IEKVgekktLVGGVDPGYLPA--TDEECIAKVEELVERL-GPHYIINPDCGLG 287
|
330
....*....|....*....
gi 491943685 729 TRDVPEtKASLINMVAAAK 747
Cdd:cd00465 288 PDSDYK-PEHLRAVVQLVD 305
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
422-754 |
3.22e-25 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 107.46 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 422 PLLPTTTIGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRF 501
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 502 TDNGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSFPREDLSQKTSVEQIALALED 581
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 582 EVLDLEKHGIKIIQIDEPALreNLplrkkdWYPKYLDWAVPAFRLVASKVKPETQIhtHMCYS----------------- 644
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAF--NV------FFDEVNDWGVAALERAIEGLKCETAV--HICYGygikantdwkktlgsew 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 645 -QFGDIIKAIDDLDADVISFEA--ARSDFSLLDILKATHFQThvgpGVYDIHSPRIPSKDEIVHIIHEILKRLPADHVWI 721
Cdd:PRK09121 231 rQYEEAFPKLQKSNIDIISLEChnSRVPMDLLELIRGKKVMV----GAIDVASDTIETPEEVADTLRKALQFVDADKLYP 306
|
330 340 350
....*....|....*....|....*....|....*
gi 491943685 722 NPDCGLK--TRDVPETKasLINMVAAAKQVRKELT 754
Cdd:PRK09121 307 CTNCGMAplSRDVARGK--LNALSAGAEIVRRELA 339
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
421-753 |
1.25e-22 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 99.99 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 421 LPLLPTTTIGSFPQTAEVRRnraKFRRHEITeDEYTAFNHKEEIEWLKFQEEIGLD-VLVHGEFERNDMVEYFGENFGGF 499
Cdd:PRK01207 1 MAALITQEIGSFRKPEYLSR---EFHKIEGT-DKFYELAERATLETLDVFENAGLDnIGIGGEMFRWEMYEHPAERIKGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 500 RFTdnGWVQSYGTRGVKPPIIWGDVVRTKPITVAETVFAQSQTDHLVKGMLTGPVTIYNWSF-----PREDLSQktsveQ 574
Cdd:PRK01207 77 IFY--GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFndfyrDRYDLAM-----E 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 575 IALALEDEVLDLEK------HGIKI-IQIDEPALREnlplrkkdwYPKYLDWAVPAFRLVASKVKPETQIHthMCYSQ-F 646
Cdd:PRK01207 150 FARIINEELKDIKSawdrksPGRKLeIQIDEPATTT---------HPDEMDIVVDSINKSVYGIDNEFSIH--VCYSSdY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 647 GDIIKAIDDLDADVISFEAARSDFSLLDI--------LKATHFQTH---------VGPGVYDIHSPRIPSKDEIVHIIHE 709
Cdd:PRK01207 219 RLLYDRIPELNIDGYNLEYSNRDTLEPGTsdekrpgfQDLKYFAEHneslqrkkfIGLGVTDVHIDYVEPVKLIEDRIRY 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 491943685 710 ILKRLP-ADHVWINPDCGLKTRDVPETKASLINMVAAAKQVRKEL 753
Cdd:PRK01207 299 ALKIIKdPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
3-279 |
1.10e-10 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 63.84 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 3 TTIIG-YPRIGEHRElkfATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFSFFDNTldvanllnivpkr 81
Cdd:PRK04326 11 TTVVGsYPKPKWLRE---AIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMV------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 82 yqdlnlspldTYFAQ-ARGYQgEAGDVKAlamkkwFNTNYH---YLVPEFDHDTKIQVTDWQlfvqFEEAKALGINGRPT 157
Cdd:PRK04326 75 ----------EYFAErIEGFK-FYGPVRV------WGNNYFrkpSVVGKIEYKEPMLVDEFE----FAKSVTYTRPVKVP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 158 LIGPYTLLKLSrFIDVVPD--DFVADLISAYTTIIDRLHDAGADWVQLDEPALVYDQTDADLAL--FERLYTPIltqkkA 233
Cdd:PRK04326 134 ITGPYTIAEWS-FNEYYKDkeELVFDLAKVINEEIKNLVEAGAKYIQIDEPALATHPEDVEIAVeaLNRIVKGI-----N 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 491943685 234 AKILVQTYFGDLTDSFDRIQKLPFDGFGLDFVEG-YANLDLLKQHGF 279
Cdd:PRK04326 208 AKLGLHVCYGDYSRIAPYILEFPVDQFDLEFANGnYKLLDLLKEYGF 254
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
108-292 |
8.08e-07 |
|
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: 51.73 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 108 KALAMKKWFNTNYHYLVPEfdHDTKIQVTDWqlFVQFEEAKALGINGR----PTLIGPYTLLKLSR----FIDVVPD--- 176
Cdd:cd00465 58 QALGEWAFRYYSQAPSVPE--IDEEEDPFRE--APALEHITAVRSLEEfptaGAAGGPFTFTHHSMsmgdALMALYErpe 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 177 ------DFVADLISAYttiIDRLHDAGADWVQLDEPALVYDQTDADLALFERLYTPILtqKKAAKI-------LVQTYFG 243
Cdd:cd00465 134 amheliEYLTEFILEY---AKTLIEAGAKALQIHEPAFSQINSFLGPKMFKKFALPAY--KKVAEYkaagevpIVHHSCY 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491943685 244 DLTDSFDRIQKLPFDGFGLDFVEGyANLDLLKQHGfpAHATLFAGIVNG 292
Cdd:cd00465 209 DAADLLEEMIQLGVDVISFDMTVN-EPKEAIEKVG--EKKTLVGGVDPG 254
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
1-317 |
2.84e-05 |
|
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: 47.04 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 1 MTTTIIGYPRigeHRELKFATQKYFKHQITAQDLQEKAKALRKAHWETIQAAGIDQIPTGDFsfFDNTLD-VANLLNIVP 79
Cdd:cd03310 1 LATGIGSYPL---PDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQL--GDDMIGrFLEVLVDLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 80 KRYQdlnlspldtyfaqargyqgeagdvkalamkkWFNTNYHYLVPEFDhDTKIQVTDWQLFVQFEEAKALGINGRPTLI 159
Cdd:cd03310 76 TGTR-------------------------------FFDNNFFYRPPEAK-IEAFLPLELDYLEEVAEAYKEALKVKVVVT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 160 GPYTLLKLSRFIDVVPD---DFVADLISAYTTIIDRLHDAGADWVQLDEPALVYD--QTDADLALFERLytpILTQKKAA 234
Cdd:cd03310 124 GPLTLALLAFLPNGEPDayeDLAKSLAEFLREQVKELKNRGIVVVQIDEPSLGAVgaGAFEDLEIVDAA---LEEVSLKS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 235 KILVQ------TYFGDLTDsfdriqkLPFDGFGLDFVE----GYANLDLLKQHGFpahATLFAGIVNGKNIWRTHyaDAL 304
Cdd:cd03310 201 GGDVEvhlcapLDYEALLE-------LGVDVIGFDAAAlpskYLEDLKKLLRIGV---RTLILGLVVTDNEAKGR--NAW 268
|
330
....*....|...
gi 491943685 305 ATIKQLATITDKL 317
Cdd:cd03310 269 KEIERLEKLVRRL 281
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
111-294 |
4.64e-05 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 46.27 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 111 AMKKWFNTNYHYLVPEFDHDTKIQVTDwqLFVQ-FEEAKAL------GINGRPTLIGPYTLLKLS--RFIDVVpddfvAD 181
Cdd:PRK08575 82 GLQRFYDNNFYYRQPVIKEKINLKEEN--PYLQwLESAREIkeevslESKLKAVLPGPLTYAVLSdnEYYKNL-----IE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 182 LISAYTTIIDRLH---DAGADWVQLDEPALVydQTDADLALFERL---YTPILTQKKAAKILVqTYFGdlTDSFDRIQKL 255
Cdd:PRK08575 155 LMEDYASVVNSLIkelSSVVDAVEIHEPSIF--AKGIKRDTLEKLpevYKTMAKNVNIEKHLM-TYFE--INNLKRLDIL 229
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491943685 256 ---PFDGFGLDFVEGYANLDLLkqHGFPAHATLFAGIVNGKN 294
Cdd:PRK08575 230 fslPVTYFGIDVIENLKKLGRV--YTYLKGRKVYLGILNARN 269
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
157-208 |
7.96e-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: 45.68 E-value: 7.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491943685 157 TLIGPYTLLKLS----RFIDVVPDDFVADLISAYTTIIDRLHDAGADWVQLDEPAL 208
Cdd:cd03311 124 ILTGPVTIPSPSfvrfRGYYPSREELAMDLALALREEIRDLYDAGCRYIQIDEPAL 179
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
532-754 |
8.99e-04 |
|
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: 42.13 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 532 VAETVFAQSQtDHLVKGMLTGPVT------IYNWSFPREDLsqktsVEQIaLALEDEVLD-LEKHGIKIIQIDEPALREN 604
Cdd:cd03312 137 LDEYLEAKAL-GINTKPVLLGPVTflklskAKGGGFDRLSL-----LDKL-LPVYKELLKkLAAAGAEWVQIDEPALVLD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 605 LPlrkkdwyPKYLDWAVPAFRlVASKVKPETQIHTHMCYSQFGDIIKAIDDLDADVISFEAARSDFSLLDILKATHFQTH 684
Cdd:cd03312 210 LP-------EEWLAAFKRAYE-ELAKAAPGLKLLLATYFGSLGENLDLLASLPVDGLHLDLVRGPENLEAVLKAGFADKV 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491943685 685 VGPGVYDIHSPRIPSKDEIVHIIHEILKRLpADHVWINPDCGLktRDVP-----ETKAS--LINMVAAAKQVRKELT 754
Cdd:cd03312 282 LSAGVVDGRNIWRADLAASLALLETLAAIL-GDRLVVSPSCSL--LHVPvdlenETKLDpeLKSWLAFAKQKLEELA 355
|
|
| PRK06233 |
PRK06233 |
vitamin B12 independent methionine synthase; |
429-726 |
1.76e-03 |
|
vitamin B12 independent methionine synthase;
Pssm-ID: 180482 Cd Length: 372 Bit Score: 41.24 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 429 IGSFPQTAEVRRNRAKFRRHEITEDEYTAFNHKEEIEWLKFQEEIGLDVLVHGEFERNDMVEYFGENFGGFRFTDngWVQ 508
Cdd:PRK06233 14 VGSFLRPERLKEAREQFAIGEISQDQLLKIQHAEIKRLVKEQVELGLKAVTDGEFNRSWWHLDFLWGLNGVGKYE--YED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 509 SYGTRGVKppiiwgdvVRTKPITVAETV-------------FAQSQT--DHLVKGMLTGPVTI------YNWSFPREdlS 567
Cdd:PRK06233 92 SYKFHGAK--------TRTDNAELAGKVafnpdhpffaafkYLKSIVpeGVLPKQTIPSPSLLfrdnrsDNWPKFYD--S 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 568 QKTSVEQIALALEDEVLDLEKHGIKIIQIDEPA---LRENLPLRKKD--WYPKYLDWAVPAFRLV--ASKVKPET-QIHT 639
Cdd:PRK06233 162 WDDYLDDLAQAYHDTIQHFYDLGARYIQLDDTTwayLISKLNDTENDpkEHQKYVKLAEDAVYVInkALADLPEDlTVTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 640 HMCYSQFG----------DIIKAIDDLDAD--VISFEAARS-DFSLLDILKATHFQTHVGPGVYDIHSPRIPSKDEIVHI 706
Cdd:PRK06233 242 HICRGNFKstylfsggyePVAKYLGQLNYDgfFLEYDNDRSgSFEPLKQIWNNRDNVRIVLGLITSKFPELEDEDEIIAR 321
|
330 340
....*....|....*....|
gi 491943685 707 IHEILKRLPADHVWINPDCG 726
Cdd:PRK06233 322 IDEATEYVPLSNLALSTQCG 341
|
|
| HemE |
COG0407 |
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ... |
177-263 |
2.52e-03 |
|
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: 40.59 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491943685 177 DFVADLISAYttiIDRLHDAGADWVQLDEPAlvydqtdADL---ALFERLYTP----ILTQKKAAKILVQTYF-GDLTDS 248
Cdd:COG0407 171 DKLTDAVIEY---LKAQIEAGADAVQIFDSW-------AGLlspKDFEEFVLPylkrIVDALKERGVPVIIHFcGDGTPL 240
|
90
....*....|....*
gi 491943685 249 FDRIQKLPFDGFGLD 263
Cdd:COG0407 241 LEDMAETGADALSVD 255
|
|
| |
