|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
12-754 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1243.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 12 LTSSNLGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPE 91
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 92 RFNYRPtGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELE-NAAPVLTENKPLLAYREAKQeLGIDGKPVLIGP 170
Cdd:PRK05222 82 RFGNLG-GSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDpDTQFKLTSNKLLDEFEEAKA-LGINTKPVLLGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 171 YSFVVLSK----GYDRKDLasiIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNI 246
Cdd:PRK05222 160 VTFLWLSKskgeGFDRLDL---LDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 247 MLQTYFGSL-DHYERLTELPVQGLGLDFVYDDgENLQHISRHgFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQin 325
Cdd:PRK05222 237 LLATYFGSLnDALDLLASLPVDGLHLDLVRGP-EQLAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAK-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 326 AEQLIVQPSCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAALGKHDPSALAKLEQSAEAVARFNSSAAR--- 402
Cdd:PRK05222 313 VDRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVhnp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 403 -VQTAadLANLLAkEPLSRSVPFAERRIIQQNRLKLPPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKE 481
Cdd:PRK05222 393 aVRAR--LAALTE-ADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIAR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 482 WIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKP 561
Cdd:PRK05222 470 AIRLQEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKP 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 562 VKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLV 641
Cdd:PRK05222 550 VKGMLTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRL 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 642 TTATVEPATQIHTHMCYSEFQDMIQSISDMDADVISIETSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSM 721
Cdd:PRK05222 630 ATSGVKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEEL 709
|
730 740 750
....*....|....*....|....*....|...
gi 515997995 722 IQRALRVLPADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:PRK05222 710 LRKALEVIPAERLWVNPDCGLKTRGWEETIAAL 742
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
17-754 |
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: 1118.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 17 LGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPERFNYR 96
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 97 pTGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELENAAP-VLTENKPLLAYREAKqELGIDGKPVLIGPYSFVV 175
Cdd:TIGR01371 81 -GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEfKLTSNKPLEEYLEAK-ELGIETKPVLLGPITFLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 176 LSKGYDR-KDLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNIMLQTYFGS 254
Cdd:TIGR01371 159 LSKAVEEpFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 255 L-DHYERLTELPVQGLGLDFVYDdGENLQHISrHGFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQINAeqLIVQP 333
Cdd:TIGR01371 239 VgDALEALVSLPVKGIGLDFVHG-KGTLELVK-AGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 334 SCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAALGKHDPSALAKLEQSAEAVARFNSSAARV--QTAADLAN 411
Cdd:TIGR01371 315 SCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIAARKSSPRVNdaQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 412 LLAKEpLSRSVPFAERRIIQQNRLKLPPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGI 491
Cdd:TIGR01371 395 LKEDD-FRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 492 DVLVHGEFERTDMVEFFGEKLKGFAFTQNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVT 571
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 572 ILNWSFERNDIPRRQVALQLALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLVTTATVEPATQ 651
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 652 IHTHMCYSEFQDMIQSISDMDADVISIETSRSHGELIVSFEDQV-YDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLP 730
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFgYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740
....*....|....*....|....
gi 515997995 731 ADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASL 737
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
13-374 |
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: 529.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 13 TSSNLGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPER 92
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 93 FNYRPtGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELE-NAAPVLTENKPLLAYREAKqELGIDGKPVLIGPY 171
Cdd:cd03312 81 FGALG-GLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSpDTEFKLASNKLLDEYLEAK-ALGINTKPVLLGPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 172 SFVVLSKGYDRK-DLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNIMLQT 250
Cdd:cd03312 159 TFLKLSKAKGGGfDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 251 YFGSL-DHYERLTELPVQGLGLDFVYdDGENLQHISRHGFPkGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQInAEQL 329
Cdd:cd03312 239 YFGSLgENLDLLASLPVDGLHLDLVR-GPENLEAVLKAGFA-DKVLSAGVVDGRNIWRADLAASLALLETLAAIL-GDRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 515997995 330 IVQPSCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAA 374
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
440-754 |
9.66e-171 |
|
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: 493.87 E-value: 9.66e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQ 519
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 520 NGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEV 599
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 600 EALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLVTTATVEPATQIHTHMCYSEFQDMIQSISDMDADVISIE 679
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515997995 680 TSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAAL 315
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
440-754 |
9.80e-136 |
|
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: 404.14 E-value: 9.80e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQ 519
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 520 NGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEV 599
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 600 EALEQAGISMIQVDEPAIREGLPlkkeqqQAYLDWAVQAFLVTTATVePATQIHTHMCYSEFQDMIQSISDMDADVISIE 679
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGV-PDTKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515997995 680 TSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDCGLKTR----TKEESVAAL 754
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
12-754 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1243.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 12 LTSSNLGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPE 91
Cdd:PRK05222 2 IKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 92 RFNYRPtGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELE-NAAPVLTENKPLLAYREAKQeLGIDGKPVLIGP 170
Cdd:PRK05222 82 RFGNLG-GSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDpDTQFKLTSNKLLDEFEEAKA-LGINTKPVLLGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 171 YSFVVLSK----GYDRKDLasiIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNI 246
Cdd:PRK05222 160 VTFLWLSKskgeGFDRLDL---LDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 247 MLQTYFGSL-DHYERLTELPVQGLGLDFVYDDgENLQHISRHgFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQin 325
Cdd:PRK05222 237 LLATYFGSLnDALDLLASLPVDGLHLDLVRGP-EQLAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAK-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 326 AEQLIVQPSCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAALGKHDPSALAKLEQSAEAVARFNSSAAR--- 402
Cdd:PRK05222 313 VDRLWVAPSCSLLHVPVDLDAETKLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAANRAAIAARRTSPRVhnp 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 403 -VQTAadLANLLAkEPLSRSVPFAERRIIQQNRLKLPPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKE 481
Cdd:PRK05222 393 aVRAR--LAALTE-ADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIAR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 482 WIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKP 561
Cdd:PRK05222 470 AIRLQEELGLDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKP 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 562 VKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLV 641
Cdd:PRK05222 550 VKGMLTGPVTILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRL 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 642 TTATVEPATQIHTHMCYSEFQDMIQSISDMDADVISIETSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSM 721
Cdd:PRK05222 630 ATSGVKDETQIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEEL 709
|
730 740 750
....*....|....*....|....*....|...
gi 515997995 722 IQRALRVLPADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:PRK05222 710 LRKALEVIPAERLWVNPDCGLKTRGWEETIAAL 742
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
17-754 |
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: 1118.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 17 LGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPERFNYR 96
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 97 pTGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELENAAP-VLTENKPLLAYREAKqELGIDGKPVLIGPYSFVV 175
Cdd:TIGR01371 81 -GGDLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEfKLTSNKPLEEYLEAK-ELGIETKPVLLGPITFLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 176 LSKGYDR-KDLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNIMLQTYFGS 254
Cdd:TIGR01371 159 LSKAVEEpFEPLSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 255 L-DHYERLTELPVQGLGLDFVYDdGENLQHISrHGFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQINAeqLIVQP 333
Cdd:TIGR01371 239 VgDALEALVSLPVKGIGLDFVHG-KGTLELVK-AGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGK--LVVST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 334 SCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAALGKHDPSALAKLEQSAEAVARFNSSAARV--QTAADLAN 411
Cdd:TIGR01371 315 SCSLLHVPVDLELETKLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIAARKSSPRVNdaQVKARLAN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 412 LLAKEpLSRSVPFAERRIIQQNRLKLPPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGI 491
Cdd:TIGR01371 395 LKEDD-FRRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 492 DVLVHGEFERTDMVEFFGEKLKGFAFTQNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVT 571
Cdd:TIGR01371 474 DVLVHGEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVT 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 572 ILNWSFERNDIPRRQVALQLALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLVTTATVEPATQ 651
Cdd:TIGR01371 554 ILNWSFVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQ 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 652 IHTHMCYSEFQDMIQSISDMDADVISIETSRSHGELIVSFEDQV-YDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLP 730
Cdd:TIGR01371 634 IHTHMCYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGFgYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLP 713
|
730 740
....*....|....*....|....
gi 515997995 731 ADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:TIGR01371 714 AERLWVNPDCGLKTRNWEEVIASL 737
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
12-754 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 861.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 12 LTSSNLGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPE 91
Cdd:PLN02475 1 MASHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 92 RFNYRpTGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPEL-ENAAPVLTENKPLLAYREAKqELGIDGKPVLIGP 170
Cdd:PLN02475 81 RYGWT-GGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELgPEVKFSYASHKAVNEYKEAK-ALGVDTVPVLVGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 171 YSFVVLSKGYDRKD----LASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNI 246
Cdd:PLN02475 159 VSYLLLSKPAKGVDksfdLLSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDLESHKLQAFKTAYAELESTLSGLNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 247 MLQTYFGSL--DHYERLTELP-VQGLGLDFVYDDgENLQHISRHGFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQ 323
Cdd:PLN02475 239 LVETYFADVpaEAYKTLTSLKgVTAFGFDLVRGT-KTLDLIKKAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 324 INAEQLIVQPSCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAALGKHDPSALAKLEQSAEAVARfnsSAARV 403
Cdd:PLN02475 318 VGKDKLVVSTSCSLLHTAVDLVNETKLDKELKSWLAFAAQKVVEVVALAKALAGQKDEAFFSANAAAQASRR---SSPRV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 404 QTAA--DLANLLAKEPLSRSVPFAERRIIQQNRLKLPPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKE 481
Cdd:PLN02475 395 TNEAvqKAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 482 WIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKP 561
Cdd:PLN02475 475 VVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 562 VKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLV 641
Cdd:PLN02475 555 MKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 642 TTATVEPATQIHTHMCYSEFQDMIQSISDMDADVISIETSRSHGELIVSFEDQV-YDKGIGLGVYDIHSPRIPDESEMLS 720
Cdd:PLN02475 635 TNCGVQDTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVkYGAGIGPGVYDIHSPRIPSTEEIAD 714
|
730 740 750
....*....|....*....|....*....|....
gi 515997995 721 MIQRALRVLPADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:PLN02475 715 RINKMLAVLESNILWVNPDCGLKTRKYPEVKPAL 748
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
13-374 |
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: 529.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 13 TSSNLGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPER 92
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 93 FNYRPtGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELE-NAAPVLTENKPLLAYREAKqELGIDGKPVLIGPY 171
Cdd:cd03312 81 FGALG-GLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSpDTEFKLASNKLLDEYLEAK-ALGINTKPVLLGPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 172 SFVVLSKGYDRK-DLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNIMLQT 250
Cdd:cd03312 159 TFLKLSKAKGGGfDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 251 YFGSL-DHYERLTELPVQGLGLDFVYdDGENLQHISRHGFPkGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQInAEQL 329
Cdd:cd03312 239 YFGSLgENLDLLASLPVDGLHLDLVR-GPENLEAVLKAGFA-DKVLSAGVVDGRNIWRADLAASLALLETLAAIL-GDRL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 515997995 330 IVQPSCSLLHVPVSLEAEHKLDRELVHALAFADEKLDEIAVLTAA 374
Cdd:cd03312 316 VVSPSCSLLHVPVDLENETKLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
440-754 |
9.66e-171 |
|
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: 493.87 E-value: 9.66e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQ 519
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 520 NGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEV 599
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 600 EALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLVTTATVEPATQIHTHMCYSEFQDMIQSISDMDADVISIE 679
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515997995 680 TSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAAL 315
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
14-324 |
1.12e-159 |
|
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: 465.13 E-value: 1.12e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 14 SSNLGYPRIGGNREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDTSVMFGLVPERF 93
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 94 NYRPtGPVPLSVYFGMARGQKGATASEMTKWMNTNYHYIVPELENA-APVLTENKPLLAYREAKqELGIDGKPVLIGPYS 172
Cdd:pfam08267 81 GNDG-GLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDKDtEFKLNSNKLLDEYKEAK-ALGIETKPVLLGPVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 173 FVVLSKGYDRK-DLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNIMLQTY 251
Cdd:pfam08267 159 FLKLSKGKGGSfDRLELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLATY 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515997995 252 FGSL-DHYERLTELPVQGLGLDFVYdDGENLQHIsRHGFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQI 324
Cdd:pfam08267 239 FGSVaDALELLASLPVAGLGLDLVR-GPENLAAL-KKGFPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
440-754 |
9.80e-136 |
|
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: 404.14 E-value: 9.80e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQ 519
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 520 NGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAEV 599
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 600 EALEQAGISMIQVDEPAIREGLPlkkeqqQAYLDWAVQAFLVTTATVePATQIHTHMCYSEFQDMIQSISDMDADVISIE 679
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGV-PDTKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515997995 680 TSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDCGLKTR----TKEESVAAL 754
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKL 312
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
441-754 |
1.55e-122 |
|
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: 370.40 E-value: 1.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 441 PTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGFAFTQn 520
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 521 gWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLT-SKPVKGMLTGPVTILNWSFERN---DIPRRQVALQLALALR 596
Cdd:cd03311 80 -WVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLThPKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 597 AEVEALEQAGISMIQVDEPAIREGLPLKKEQ-QQAYLDWAVQAFlvttATVEPATQIHTHMCYSEFQ----------DMI 665
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLEPDDlAADYLKWANEAL----ADRPDDTQIHTHICYGNFRstwaaeggyePIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 666 QSISDMDADVISIETSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDCGLKTR 745
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATR 314
|
....*....
gi 515997995 746 TKEESVAAL 754
Cdd:cd03311 315 ERGNALTKL 323
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
13-367 |
9.23e-97 |
|
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: 303.21 E-value: 9.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 13 TSSNLGYPRIggnREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDhvldtsvMFGLVPER 92
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 93 FNyrptgpvplsvyfGMARGQKGataseMTKWMNTNYHYiVPELEnaAPV-LTENKPLLAYREAKQELGIDGKPVLIGPY 171
Cdd:COG0620 73 LD-------------GYAFARNG-----WVEWFDTNYHY-VPEIT--GDVsFSGPMTVEEFRFAKSLTGKPVKPVLPGPV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 172 SFVVLSKGYDRKDLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNIMLQTY 251
Cdd:COG0620 132 TLLLLSKVRDYKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRAAAGVPDTKIHLHTC 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 252 FGSL-DHYERLTELPVQGLGLDFVYDDGENLQHISRhgFPKGKTLGAGVIDGRNIWRSDLNAMAALLGQLAEQINAEQLI 330
Cdd:COG0620 212 YGGYeDILEALAALPVDGIHLEFVRSRAGLLEPLKE--LPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLW 289
|
330 340 350
....*....|....*....|....*....|....*..
gi 515997995 331 VQPSCSLLHVPVSLEAEHkLDRELVHALAFADEKLDE 367
Cdd:COG0620 290 VSPDCGLKHRPVDLTREE-AWAKLRNMVAFAREVRGE 325
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
436-754 |
8.35e-69 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 229.86 E-value: 8.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 436 KLPPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEKLKGF 515
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 516 AFtqNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLT-SKPVKGMLTGPVTILNWSFERNDIPRRQVALQLALA 594
Cdd:PRK04326 85 KF--YGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 595 LRAEVEALEQAGISMIQVDEPAiregLPLKKEQqqayLDWAVQAFLVTTATVEpaTQIHTHMCYSEFQDMIQSISDMDAD 674
Cdd:PRK04326 163 INEEIKNLVEAGAKYIQIDEPA----LATHPED----VEIAVEALNRIVKGIN--AKLGLHVCYGDYSRIAPYILEFPVD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 675 VISIETSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDCGLKTRTKEESVAAL 754
Cdd:PRK04326 233 QFDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQKL 312
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
441-754 |
1.50e-35 |
|
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: 136.86 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 441 PTTTIGSFPQTAEVRKARLhyrkgewSAEQYRTFIQQQIKEWIDiQEDIGIDVLVHGEFERTDMVEFFGeklkgfaftqn 520
Cdd:cd00465 1 PVQCEGQTGIMEASETMAI-------SEEPGETSKAEWGITLVE-PEEIPLDVIPVHEDDVLKVAQALG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 521 GWVQSYGSRCVKPPIIYGDV-SFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDI---------PRRQVALQ 590
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEdPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDAlmalyerpeAMHELIEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 591 LALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEqqQAYLDWAVQAF-LVTTATVEPATQIHTHMCYSEFqDMIQSIS 669
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGP--KMFKKFALPAYkKVAEYKAAGEVPIVHHSCYDAA-DLLEEMI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 670 DMDADVISIETSRshGELIVSFEDQVYDKGIGLGVYDIHSPrIPDEsEMLSMIQRALRVLpADLFWVNPDCGLKTR--TK 747
Cdd:cd00465 219 QLGVDVISFDMTV--NEPKEAIEKVGEKKTLVGGVDPGYLP-ATDE-ECIAKVEELVERL-GPHYIINPDCGLGPDsdYK 293
|
....*..
gi 515997995 748 EESVAAL 754
Cdd:cd00465 294 PEHLRAV 300
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
441-754 |
2.52e-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: 127.93 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 441 PTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERtDMVEFFGEKLKGFAFtqn 520
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVDLET--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 521 GWVQSYGSRCVKPPIIYGDVSF-DQPMTVEEAAFAQSLTsKPVKGMLTGPVTILNWSFERNDIP--RRQVALQLALALRA 597
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLpLELDYLEEVAEAYKEA-LKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 598 EVEALEQAGISMIQVDEPAIREGLPLKKEQQQaYLDWAVQAFLVTtatvePATQIHTHMCYSEFqdmIQSISDMDADVIS 677
Cdd:cd03310 156 QVKELKNRGIVVVQIDEPSLGAVGAGAFEDLE-IVDAALEEVSLK-----SGGDVEVHLCAPLD---YEALLELGVDVIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 678 IETSRS---HGELIVSFED-QVYDKGIGLGVYDI----HSPRipDESEMLSMIQRALRVLPADLF---WVNPDCGLKTRT 746
Cdd:cd03310 227 FDAAALpskYLEDLKKLLRiGVRTLILGLVVTDNeakgRNAW--KEIERLEKLVRRLEEPGEVLDeilYLTPDCGLAFLP 304
|
....*...
gi 515997995 747 KEESVAAL 754
Cdd:cd03310 305 PQEARRKL 312
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
440-748 |
2.11e-26 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 110.08 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFPQTAEVRKARLHYRKGEWSA-EQYRTFIQQQIKEwidiQEDIGIDVLVHGEFeRTDMVEFFGEKLKGFAft 518
Cdd:PRK00957 2 MITTVVGSYPVVKGEPETLKDKIKGFFGLyDPYKPAIEEAVAD----QVKAGIDIISDGQV-RGDMVEIFASNMPGFD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 519 qngwvqsyGSRCVkppiiyGDVSF-DQPMTVEEAAFAQSLT-----SKPVKGMLTGPVTILNWS----FERN-------- 580
Cdd:PRK00957 75 --------GKRVI------GRVEPpAKPITLKDLKYAKKVAkkkdpNKGVKGIITGPSTLAYSLrvepFYSDnkdeeliy 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 581 DIPRRQVAlqlalalraEVEALEQAGISMIQVDEPAIREGLplkkeqqqAYLDWAVQAFLVTTATVEPATQIHThmCySE 660
Cdd:PRK00957 141 DLARALRK---------EAEALEKAGVAMIQIDEPILSTGA--------YDLEVAKKAIDIITKGLNVPVAMHV--C-GD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 661 FQDMIQSISDMDADVISIETSRSHGELIVSFEDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLFWVNPDC 740
Cdd:PRK00957 201 VSNIIDDLLKFNVDILDHEFASNKKNLEILEEKDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDC 280
|
....*...
gi 515997995 741 GLKTRTKE 748
Cdd:PRK00957 281 GMRMLPRD 288
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
440-742 |
3.89e-21 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 95.52 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFPQT---AEVRKArlhyrkgeWS-----AEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERTDMVEFFGEK 511
Cdd:PRK09121 3 LPTSTAGSLPKPswlAEPETL--------WSpwklqGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 512 LKGFAFTQNGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDIPRRQVALQL 591
Cdd:PRK09121 75 LSGVDFEKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 592 ALALRAEVEALEQAGISMIQVDEPAIREGLPLKKEQQQAYLDWAVQAFLVTTAtvepatqihTHMCY------------- 658
Cdd:PRK09121 155 AKILNQEAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETA---------VHICYgygikantdwkkt 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 659 --SEFQDMIQSISDMDA---DVISIETSRSH--GELIvsfeDQVYDKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLPA 731
Cdd:PRK09121 226 lgSEWRQYEEAFPKLQKsniDIISLECHNSRvpMDLL----ELIRGKKVMVGAIDVASDTIETPEEVADTLRKALQFVDA 301
|
330
....*....|.
gi 515997995 732 DLFWVNPDCGL 742
Cdd:PRK09121 302 DKLYPCTNCGM 312
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
440-748 |
9.16e-20 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 91.52 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 440 LPTTTIGSFpQTAEVRKARLHYRKGewsAEQYRTFIQQQIKEWIDIQEDIGID-VLVHGEFERTDMVEFFGEKLKGFAFT 518
Cdd:PRK01207 4 LITQEIGSF-RKPEYLSREFHKIEG---TDKFYELAERATLETLDVFENAGLDnIGIGGEMFRWEMYEHPAERIKGIIFY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 519 qnGWVQSYGSRCVKPPIIYGDVSFDQPMTVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDIPRRQVALQLALALRAE 598
Cdd:PRK01207 80 --GMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFARIINEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 599 VEALEQA------GISM-IQVDEPAireglplkKEQQQAYLDWAVQAFLVTTATVEpaTQIHTHMCYS-EFQDMIQSISD 670
Cdd:PRK01207 158 LKDIKSAwdrkspGRKLeIQIDEPA--------TTTHPDEMDIVVDSINKSVYGID--NEFSIHVCYSsDYRLLYDRIPE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 671 MDADVISIETS-RSHGELIVS------FEDQVY----------DKGIGLGVYDIHSPRIPDESEMLSMIQRALRVLP-AD 732
Cdd:PRK01207 228 LNIDGYNLEYSnRDTLEPGTSdekrpgFQDLKYfaehneslqrKKFIGLGVTDVHIDYVEPVKLIEDRIRYALKIIKdPE 307
|
330
....*....|....*.
gi 515997995 733 LFWVNPDCGLKTRTKE 748
Cdd:PRK01207 308 LVRLNPDCGLRTRSRE 323
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
29-350 |
3.32e-18 |
|
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: 86.33 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 29 KKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFsyYDHVLDTSVMFGLVPERFnyrptgpvplsvyfg 108
Cdd:cd03310 15 TKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQL--GDDMIGRFLEVLVDLETG--------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 109 margqkgatasemTKWMNTNYHYIVPELENAAPVLTENKPLLAYREAKQElGIDGKPVLIGPYSFVVLSKGYDRKDLASi 188
Cdd:cd03310 78 -------------TRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKE-ALKVKVVVTGPLTLALLAFLPNGEPDAY- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 189 iRTFLPLYARVLSELAAE----GVQWVQIDEPVLTT--SFPVEDLDIIQEVYEALT-QAAPSLNIMLQTYfgslDHYERL 261
Cdd:cd03310 143 -EDLAKSLAEFLREQVKElknrGIVVVQIDEPSLGAvgAGAFEDLEIVDAALEEVSlKSGGDVEVHLCAP----LDYEAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 262 TELPVQGLGLDFVYDDGENLQHIS---RHGFpKGKTLGAGVID----GRNIWR--SDLNAMAALLGQLAEqINAEQLIVQ 332
Cdd:cd03310 218 LELGVDVIGFDAAALPSKYLEDLKkllRIGV-RTLILGLVVTDneakGRNAWKeiERLEKLVRRLEEPGE-VLDEILYLT 295
|
330
....*....|....*...
gi 515997995 333 PSCSLLHVPVSlEAEHKL 350
Cdd:cd03310 296 PDCGLAFLPPQ-EARRKL 312
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
115-348 |
7.22e-16 |
|
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: 79.08 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 115 GATASEMTKW--MNTNYHYIVPELENAAPVLTENKPLLAYREAKQELGIDGKPVLIGPYSFVVLSKG--------YDR-K 183
Cdd:cd00465 54 LKVAQALGEWafRYYSQAPSVPEIDEEEDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSmgdalmalYERpE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 184 DLASIIRTFLPLYARVLSELAAEGVQWVQIDEPVLTTSFPVED--------LDIIQEVYEAltQAAPSLNIMLQTYFGSL 255
Cdd:cd00465 134 AMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGpkmfkkfaLPAYKKVAEY--KAAGEVPIVHHSCYDAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 256 DHYERLTELPVQGLGLDFVYddGENLQHISRHGfpKGKTLGAGVIDGRNIWRS--DLNAMAALLGQLAEQInaeqlIVQP 333
Cdd:cd00465 212 DLLEEMIQLGVDVISFDMTV--NEPKEAIEKVG--EKKTLVGGVDPGYLPATDeeCIAKVEELVERLGPHY-----IINP 282
|
250
....*....|....*
gi 515997995 334 SCSLLHVPVSlEAEH 348
Cdd:cd00465 283 DCGLGPDSDY-KPEH 296
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
30-304 |
2.84e-10 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 62.45 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 30 KALERFWQGSINESELHSE----MKRLrlehLSKQRDKGIDRIPVGDFSYyDHVLDTSVMFglvperfnyrptgpvplsv 105
Cdd:PRK08575 19 KVISWYNSGKISKEKLEKAinenTKRF----FELAKDVGIDYTTDGLFRW-DDIFDPTISF------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 106 yfgmargQKGATASEMTKWMNTNYHYIVPELENAAPVLTENkPLLAY----REAKQELGIDG--KPVLIGPYSFVVLSKG 179
Cdd:PRK08575 75 -------ISGVEKGGLQRFYDNNFYYRQPVIKEKINLKEEN-PYLQWlesaREIKEEVSLESklKAVLPGPLTYAVLSDN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 180 YDRKDLASIIRTflplYARVLSELAAE---GVQWVQIDEPVLTTSFPVED-LDIIQEVYEALTQAApSLNIMLQTYF--G 253
Cdd:PRK08575 147 EYYKNLIELMED----YASVVNSLIKElssVVDAVEIHEPSIFAKGIKRDtLEKLPEVYKTMAKNV-NIEKHLMTYFeiN 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 515997995 254 SLDHYERLTELPVQGLGLDFVyddgENLQHISR-HGFPKGKTLGAGVIDGRN 304
Cdd:PRK08575 222 NLKRLDILFSLPVTYFGIDVI----ENLKKLGRvYTYLKGRKVYLGILNARN 269
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
19-335 |
3.66e-10 |
|
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: 62.24 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 19 YPRIggnREWKKALERFWQGSINESELHSEMKRLRLEHLSKQRDKGIDRIPVGDFSYYDHVLDtsvmFGlvpERFN-YRP 97
Cdd:cd03311 8 FPRP---KELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEY----FL---ERLDgFEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 98 TGPVPlsvyfgmargqkgatasemtKWMNTNY--HYIVPELENAAPVLTENKPLL----AYREAKQelGIDGkPVLIGPY 171
Cdd:cd03311 78 TGWVQ--------------------SYGSRYYkpPGIVGDVSRRPPMTVEEGKIAqsltHPKPLKG--ILTG-PVTIPSP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 172 SFVVLSKGYDRK-----DLASIIRtflplyaRVLSELAAEGVQWVQIDEPVLTTSFPVEDLDIIQEVYEALTQAAPSLNI 246
Cdd:cd03311 135 SFVRFRGYYPSReelamDLALALR-------EEIRDLYDAGCRYIQIDEPALAEGLPLEPDDLAADYLKWANEALADRPD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 247 MLQT-------YFGSLDH--------YERLTELPVQGLGLDFVYDDGENLQHISRhgFPKGKTLGAGVIDGRNIWRSDLN 311
Cdd:cd03311 208 DTQIhthicygNFRSTWAaeggyepiAEYIFELDVDVFFLEYDNSRAGGLEPLKE--LPYDKKVGLGVVDVKSPEVESPE 285
|
330 340
....*....|....*....|....
gi 515997995 312 AMAALLGQLAEQINAEQLIVQPSC 335
Cdd:cd03311 286 EVKDRIEEAAKYVPLEQLWVSPDC 309
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
163-337 |
1.75e-08 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 56.91 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 163 GKPV---LIGPYSFVVLS--KGYDRK-----DLASIIRtflplyaRVLSELAAEGVQWVQIDEPVLTTSfPvEDLDIiqe 232
Cdd:PRK04326 127 TRPVkvpITGPYTIAEWSfnEYYKDKeelvfDLAKVIN-------EEIKNLVEAGAKYIQIDEPALATH-P-EDVEI--- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 233 VYEALTQAAPSLN--IMLQTYFGSldhYERL----TELPVQGLGLDFVYDDGENLQHISRHGFpkGKTLGAGVIDGRNIW 306
Cdd:PRK04326 195 AVEALNRIVKGINakLGLHVCYGD---YSRIapyiLEFPVDQFDLEFANGNYKLLDLLKEYGF--DKELGLGVIDVHSAR 269
|
170 180 190
....*....|....*....|....*....|.
gi 515997995 307 RSDLNAMAALLGQLAEQINAEQLIVQPSCSL 337
Cdd:PRK04326 270 VESVEEIKEAIKKGLEYVPPEKLYINPDCGL 300
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
197-366 |
2.56e-05 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 46.91 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 197 ARVLSE----LAAEGVQWVQIDEPVLTTSfpVEDLDIIQEVYEALTQAapsLNIMLQTYF-GSLDH-YERLTELPVQGLG 270
Cdd:PRK00957 143 ARALRKeaeaLEKAGVAMIQIDEPILSTG--AYDLEVAKKAIDIITKG---LNVPVAMHVcGDVSNiIDDLLKFNVDILD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 271 LDFVYDDgENLQHISRHGFpKGKTLGAGVIDgrniwrSDLNA------MAALLGQLAEQINAEQLIVQPSCSLlhvpvsl 344
Cdd:PRK00957 218 HEFASNK-KNLEILEEKDL-IGKKIGFGCVD------TKSKSvesvdeIKALIEEGIEILGAENILIDPDCGM------- 282
|
170 180
....*....|....*....|..
gi 515997995 345 eaeHKLDRELvhalafADEKLD 366
Cdd:PRK00957 283 ---RMLPRDV------AFEKLK 295
|
|
| PRK06520 |
PRK06520 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; |
438-582 |
1.44e-04 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase;
Pssm-ID: 180601 Cd Length: 368 Bit Score: 44.71 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 438 PPLPTTTIGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERT----------DMVEF 507
Cdd:PRK06520 6 APFRADVVGSFLRPAAIKQARQQFAAGEIDAAALRKIEDMEIRKVVEKQRACGLKVVTDGEFRRAwwhfdffdglQGVER 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515997995 508 FgEKLKGFAFtqNGwVQSYGsRCVKppiIYGDVSF--DQPMtVEEAAFAQSLTSKPVKGMLTGPVTILNWSFERNDI 582
Cdd:PRK06520 86 Y-EAEQGIQF--NG-VQTKA-RGVR---VTGKLDFpdDHPM-LEDFRFLKSISGDATPKMTIPSPSVLHFRGGRKAI 153
|
|
| PRK06233 |
PRK06233 |
vitamin B12 independent methionine synthase; |
445-502 |
8.55e-04 |
|
vitamin B12 independent methionine synthase;
Pssm-ID: 180482 Cd Length: 372 Bit Score: 42.39 E-value: 8.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515997995 445 IGSFPQTAEVRKARLHYRKGEWSAEQYRTFIQQQIKEWIDIQEDIGIDVLVHGEFERT 502
Cdd:PRK06233 14 VGSFLRPERLKEAREQFAIGEISQDQLLKIQHAEIKRLVKEQVELGLKAVTDGEFNRS 71
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
548-742 |
4.13e-03 |
|
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: 40.21 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 548 VEEAAFAQSL--TSKPVkgmLTGPVTIL------NWSFERNDIPRRQVALQLalalraEV-EALEQAGISMIQVDEPAIr 618
Cdd:cd03312 137 LDEYLEAKALgiNTKPV---LLGPVTFLklskakGGGFDRLSLLDKLLPVYK------ELlKKLAAAGAEWVQIDEPAL- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515997995 619 eGLPLKKEQQQAYLDwaVQAFLvttATVEPATQIHTHMCYSEFQDMIQSISDMDADVISIETSRSHG--ELIVS--FEDQ 694
Cdd:cd03312 207 -VLDLPEEWLAAFKR--AYEEL---AKAAPGLKLLLATYFGSLGENLDLLASLPVDGLHLDLVRGPEnlEAVLKagFADK 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515997995 695 VydkgIGLGVYDIHSPRIPDESEMLSMIQRALRVLPADLfWVNPDCGL 742
Cdd:cd03312 281 V----LSAGVVDGRNIWRADLAASLALLETLAAILGDRL-VVSPSCSL 323
|
|
| |
