|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
3-742 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1235.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 3 TIKTSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIP 82
Cdd:PRK05222 1 MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 83 ERFQ--GRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWD-NVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPI 159
Cdd:PRK05222 81 ERFGnlGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDpDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 160 TFVKLSK--GGHQTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQT 237
Cdd:PRK05222 161 TFLWLSKskGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 238 YFE--RAHLKFLSSLPVGGLGLDFVHDNGyNLKQIEAGdFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHTNELVI 315
Cdd:PRK05222 241 YFGslNDALDLLASLPVDGLHLDLVRGPE-QLAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKVDRLWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 316 QPSSSLLHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRLFNQNDSVKYDKLKA---------RYERFQNQSFKNLD 385
Cdd:PRK05222 319 APSCSLLHVPVDLDAETkLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAAnraaiaarrTSPRVHNPAVRARL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 386 YDFESVRTSRQSPFAQRIEQQQKRLNLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIG 465
Cdd:PRK05222 399 AALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEELG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 466 LDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPV 545
Cdd:PRK05222 479 LDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTGPV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 546 TILNWSFERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDET 625
Cdd:PRK05222 559 TILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGVKDET 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 626 QIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQID 705
Cdd:PRK05222 639 QIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALEVIP 718
|
730 740 750
....*....|....*....|....*....|....*..
gi 612673931 706 RSLFWVNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE 742
Cdd:PRK05222 719 AERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAE 755
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
9-742 |
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: 1234.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 9 LGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGR 88
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 89 T--IDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWDNVEP-KVSRNVLLDRFKYAQSLNVNAHPVIVGPITFVKLS 165
Cdd:TIGR01371 81 GgdLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEfKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 166 KGGHQTFE--EKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYFE--R 241
Cdd:TIGR01371 161 KAVEEPFEplSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDsvG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 242 AHLKFLSSLPVGGLGLDFVHDNGYnlKQIEAGDFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHTNELVIQPSSSL 321
Cdd:TIGR01371 241 DALEALVSLPVKGIGLDFVHGKGT--LELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTSCSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 322 LHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRLFNQNDSVKYDKLKARYERF---QNQSFKNLDYDFESVRTS--- 394
Cdd:TIGR01371 319 LHVPVDLELETkLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIaarKSSPRVNDAQVKARLANLked 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 395 ---RQSPFAQRIEQQQKRLNLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVH 471
Cdd:TIGR01371 399 dfrRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLDVLVH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 472 GEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWS 551
Cdd:TIGR01371 479 GEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTILNWS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 552 FERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDETQIHTHM 631
Cdd:TIGR01371 559 FVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQIHTHM 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 632 CYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDFEDI-NYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFW 710
Cdd:TIGR01371 639 CYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGfGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPAERLW 718
|
730 740 750
....*....|....*....|....*....|..
gi 612673931 711 VNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE 742
Cdd:TIGR01371 719 VNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
415-737 |
2.18e-164 |
|
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: 476.54 E-value: 2.18e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTK 494
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 495 FGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIALAINEEV 574
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 575 LALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDETQIHTHMCYSQFGQIIHAIHDLDADVISIE 654
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 655 TSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTRKEEEVKDALTVLVN 734
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMVD 320
|
...
gi 612673931 735 AVK 737
Cdd:pfam01717 321 AAK 323
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
5-357 |
1.64e-163 |
|
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: 475.87 E-value: 1.64e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 5 KTSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPER 84
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 85 FQ--GRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWD-NVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPITF 161
Cdd:cd03312 81 FGalGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSpDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 162 VKLSK--GGHQTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYF 239
Cdd:cd03312 161 LKLSKakGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLATYF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 240 E--RAHLKFLSSLPVGGLGLDFVHdNGYNLKQIEAGDFdKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHTNE-LVIQ 316
Cdd:cd03312 241 GslGENLDLLASLPVDGLHLDLVR-GPENLEAVLKAGF-ADKVLSAGVVDGRNIWRADLAASLALLETLAAILGDrLVVS 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 612673931 317 PSSSLLHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRL 357
Cdd:cd03312 319 PSCSLLHVPVDLENETkLDPELKSWLAFAKQKLEELALLARA 360
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
415-742 |
5.38e-140 |
|
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: 414.15 E-value: 5.38e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTK 494
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 495 FGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIALAINEEV 574
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 575 LALEAAGIKVIQVDEPALREGLPlrseyhEQYLKDAVLSFKLATSSVRDeTQIHTHMCYSQFGQIIHAIHDLDADVISIE 654
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 655 TSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTR----KEEEVKDALT 730
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKLR 313
|
330
....*....|..
gi 612673931 731 VLVNAVKAKRQE 742
Cdd:COG0620 314 NMVAFAREVRGE 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
3-742 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 1235.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 3 TIKTSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIP 82
Cdd:PRK05222 1 MIKTHILGFPRIGPRRELKKALESYWAGKISEEELLATARELRARHWQRQKEAGLDLIPVGDFSYYDHVLDTAVLLGAIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 83 ERFQ--GRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWD-NVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPI 159
Cdd:PRK05222 81 ERFGnlGGSVDLDTYFAMARGGKDVAALEMTKWFNTNYHYIVPEFDpDTQFKLTSNKLLDEFEEAKALGINTKPVLLGPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 160 TFVKLSK--GGHQTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQT 237
Cdd:PRK05222 161 TFLWLSKskGEGFDRLDLLDDLLPVYAELLAELAAAGAEWVQIDEPALVLDLPQEWLEAFKRAYEALAAAKPRPKLLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 238 YFE--RAHLKFLSSLPVGGLGLDFVHDNGyNLKQIEAGdFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHTNELVI 315
Cdd:PRK05222 241 YFGslNDALDLLASLPVDGLHLDLVRGPE-QLAALLKY-FPADKVLSAGVIDGRNIWRADLEAALALLEPLAAKVDRLWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 316 QPSSSLLHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRLFNQNDSVKYDKLKA---------RYERFQNQSFKNLD 385
Cdd:PRK05222 319 APSCSLLHVPVDLDAETkLDPELKSWLAFAKQKLEELALLARALNGGRGAVAEALAAnraaiaarrTSPRVHNPAVRARL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 386 YDFESVRTSRQSPFAQRIEQQQKRLNLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIG 465
Cdd:PRK05222 399 AALTEADFQRQSPYAERAAAQRARLNLPLLPTTTIGSFPQTTEIRKARAAFKKGELSEEEYEAFIREEIARAIRLQEELG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 466 LDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPV 545
Cdd:PRK05222 479 LDVLVHGEFERNDMVEYFGEQLDGFAFTQNGWVQSYGSRCVKPPIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTGPV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 546 TILNWSFERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDET 625
Cdd:PRK05222 559 TILNWSFVRDDQPREETARQIALAIRDEVLDLEAAGIKIIQIDEPALREGLPLRRSDWDAYLDWAVEAFRLATSGVKDET 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 626 QIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQID 705
Cdd:PRK05222 639 QIHTHMCYSEFNDIIDAIAALDADVISIETSRSDMELLDAFEDFGYPNEIGPGVYDIHSPRVPSVEEIEELLRKALEVIP 718
|
730 740 750
....*....|....*....|....*....|....*..
gi 612673931 706 RSLFWVNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE 742
Cdd:PRK05222 719 AERLWVNPDCGLKTRGWEETIAALKNMVAAAKELRAE 755
|
|
| met_syn_B12ind |
TIGR01371 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; This model describes ... |
9-742 |
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: 1234.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 9 LGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPERFQGR 88
Cdd:TIGR01371 1 LGFPRIGPKRELKKALESYWAGKITKEELLKVAKDLRKKNWKLQKEAGVDFIPSNDFSLYDHVLDTAVMLGAIPERFGNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 89 T--IDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWDNVEP-KVSRNVLLDRFKYAQSLNVNAHPVIVGPITFVKLS 165
Cdd:TIGR01371 81 GgdLDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELSPTTEfKLTSNKPLEEYLEAKELGIETKPVLLGPITFLKLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 166 KGGHQTFE--EKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYFE--R 241
Cdd:TIGR01371 161 KAVEEPFEplSLLEKLLPVYKEVLKKLAEAGATWVQIDEPALVTDLSKEDLAAFKEAYTELSEALSGLKLLLQTYFDsvG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 242 AHLKFLSSLPVGGLGLDFVHDNGYnlKQIEAGDFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHTNELVIQPSSSL 321
Cdd:TIGR01371 241 DALEALVSLPVKGIGLDFVHGKGT--LELVKAGFPEDKVLSAGVIDGRNIWRNDLEASLSLLKKLLAHVGKLVVSTSCSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 322 LHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRLFNQNDSVKYDKLKARYERF---QNQSFKNLDYDFESVRTS--- 394
Cdd:TIGR01371 319 LHVPVDLELETkLDPELKSWLAFAKEKLEELKALKRALNGNDDAVAFALEANAAAIaarKSSPRVNDAQVKARLANLked 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 395 ---RQSPFAQRIEQQQKRLNLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVH 471
Cdd:TIGR01371 399 dfrRRSPFKERLPLQQKRLNLPLLPTTTIGSFPQTPEVRKARAAYRKGEISEEEYEKFIKEEIKKVIKIQEELGLDVLVH 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 472 GEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWS 551
Cdd:TIGR01371 479 GEFERNDMVEYFGEKLAGFAFTQNGWVQSYGSRCVRPPIIYGDVSRPKPMTVKWSVYAQSLTSKPVKGMLTGPVTILNWS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 552 FERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDETQIHTHM 631
Cdd:TIGR01371 559 FVRDDIPRKEIAYQIALAIRDEVLDLEEAGIKIIQIDEPALREGLPLRKSDWPEYLDWAVEAFRLATSGVKDETQIHTHM 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 632 CYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDFEDI-NYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFW 710
Cdd:TIGR01371 639 CYSEFNEIIESIADLDADVISIEASRSDMELLSAFKNGfGYPNGIGPGVYDIHSPRVPSVEEMADLIEKALQVLPAERLW 718
|
730 740 750
....*....|....*....|....*....|..
gi 612673931 711 VNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE 742
Cdd:TIGR01371 719 VNPDCGLKTRNWEEVIASLKNMVEAAKEAREQ 750
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
6-742 |
0e+00 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 790.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 6 TSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPERF 85
Cdd:PLN02475 3 SHIVGYPRMGPKRELKFALESFWDGKSSAEDLQKVAADLRSSIWKQMSAAGIKYIPSNTFSYYDQVLDTTAMLGAVPPRY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 86 Q--GRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWD-NVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPITFV 162
Cdd:PLN02475 83 GwtGGEIGFDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGpEVKFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 163 KLSK---GGHQTFE--EKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTD-DSESYENITrEAYDYFEKAGVAKKLVIQ 236
Cdd:PLN02475 163 LLSKpakGVDKSFDllSLLDKILPVYKEVIAELKAAGASWIQFDEPALVMDlESHKLQAFK-TAYAELESTLSGLNVLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 237 TYFE---RAHLKFLSSLP-VGGLGLDFVHDNGyNLKQIEAGDFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLA--HT 310
Cdd:PLN02475 242 TYFAdvpAEAYKTLTSLKgVTAFGFDLVRGTK-TLDLIKKAGFPSGKYLFAGVVDGRNIWANDLAASLATLQALEGivGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 311 NELVIQPSSSLLHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRLF-NQNDSVKYDKLKARYE------RFQNQSFK 382
Cdd:PLN02475 321 DKLVVSTSCSLLHTAVDLVNETkLDKELKSWLAFAAQKVVEVVALAKALaGQKDEAFFSANAAAQAsrrsspRVTNEAVQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 383 NLDYDFESVRTSRQSPFAQRIEQQQKRLNLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQE 462
Cdd:PLN02475 401 KAAAALKGSDHRRATPVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 463 DIGLDVLVHGEFERNDMVEFFGEKLQGFLVTKFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLT 542
Cdd:PLN02475 481 ELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLT 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 543 GPVTILNWSFERVDLPRKVVQDQIALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVR 622
Cdd:PLN02475 561 GPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKAGITVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 623 DETQIHTHMCYSQFGQIIHAIHDLDADVISIETSRSHGDLIKDF-EDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSL 701
Cdd:PLN02475 641 DTTQIHTHMCYSNFNDIIHSIIDMDADVITIENSRSDEKLLSVFrEGVKYGAGIGPGVYDIHSPRIPSTEEIADRINKML 720
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 612673931 702 QQIDRSLFWVNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE 742
Cdd:PLN02475 721 AVLESNILWVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQ 761
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
415-737 |
2.18e-164 |
|
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: 476.54 E-value: 2.18e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTK 494
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 495 FGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIALAINEEV 574
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 575 LALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSSVRDETQIHTHMCYSQFGQIIHAIHDLDADVISIE 654
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALREGLPLKKLDWAAYLDWAVAAFRLDTCGAADDTQIHTHMCYSDFNDILSAIAALDADVITIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 655 TSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTRKEEEVKDALTVLVN 734
Cdd:pfam01717 241 ASRSDMELLEAFEEWGYGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPDCGLKTRGWEEARAALRNMVD 320
|
...
gi 612673931 735 AVK 737
Cdd:pfam01717 321 AAK 323
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
5-357 |
1.64e-163 |
|
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: 475.87 E-value: 1.64e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 5 KTSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPER 84
Cdd:cd03312 1 KTHILGFPRIGANRELKKALESYWKGKISEEELLATAKELRLRHWKLQKEAGIDLIPVGDFSLYDHVLDTSVLLGAIPER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 85 FQ--GRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWD-NVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPITF 161
Cdd:cd03312 81 FGalGGLVDLDTYFAMARGNQDVPALEMTKWFDTNYHYIVPELSpDTEFKLASNKLLDEYLEAKALGINTKPVLLGPVTF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 162 VKLSK--GGHQTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYF 239
Cdd:cd03312 161 LKLSKakGGGFDRLSLLDKLLPVYKELLKKLAAAGAEWVQIDEPALVLDLPEEWLAAFKRAYEELAKAAPGLKLLLATYF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 240 E--RAHLKFLSSLPVGGLGLDFVHdNGYNLKQIEAGDFdKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHTNE-LVIQ 316
Cdd:cd03312 241 GslGENLDLLASLPVDGLHLDLVR-GPENLEAVLKAGF-ADKVLSAGVVDGRNIWRADLAASLALLETLAAILGDrLVVS 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 612673931 317 PSSSLLHVPVSLDDET-LDSSVGEGLSFATEKLDELDALRRL 357
Cdd:cd03312 319 PSCSLLHVPVDLENETkLDPELKSWLAFAKQKLEELALLARA 360
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
6-310 |
4.06e-148 |
|
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: 434.70 E-value: 4.06e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 6 TSNLGFPRLGRKREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDHILDTSLLFNIIPERF 85
Cdd:pfam08267 1 TSILGFPRIGENRELKKALESYWKGKISEEELLKTAKELRLRHWKKQKEAGIDLIPVGDFSYYDHVLDTAVLLGAIPERF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 86 Q--GRTIDDDLLFDIARGNKDHVASALIKWFNTNYHYIVPEWD-NVEPKVSRNVLLDRFKYAQSLNVNAHPVIVGPITFV 162
Cdd:pfam08267 81 GndGGLDDLDTYFAMARGNKDVPALEMTKWFNTNYHYIVPELDkDTEFKLNSNKLLDEYKEAKALGIETKPVLLGPVTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 163 KLSKGGHQTFE--EKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFEKAGVAKKLVIQTYFE 240
Cdd:pfam08267 161 KLSKGKGGSFDrlELLPKLLPVYKELLKELAAAGAEWVQIDEPALVLDLPPEWLAAFKEAYQELASAKPGPKLLLATYFG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612673931 241 --RAHLKFLSSLPVGGLGLDFVHdNGYNLKQIEAGdFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAHT 310
Cdd:pfam08267 241 svADALELLASLPVAGLGLDLVR-GPENLAALKKG-FPADKVLSAGVIDGRNIWRADLEAALELLETLAQKL 310
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
415-742 |
5.38e-140 |
|
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: 414.15 E-value: 5.38e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTK 494
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 495 FGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIALAINEEV 574
Cdd:COG0620 81 NGWVEWFDTNYHYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 575 LALEAAGIKVIQVDEPALREGLPlrseyhEQYLKDAVLSFKLATSSVRDeTQIHTHMCYSQFGQIIHAIHDLDADVISIE 654
Cdd:COG0620 161 KALEAAGARWIQIDEPALAEDLP------DEYLDWAVEAYNRAAAGVPD-TKIHLHTCYGGYEDILEALAALPVDGIHLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 655 TSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTR----KEEEVKDALT 730
Cdd:COG0620 234 FVRSRAGLLEPLKELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHRpvdlTREEAWAKLR 313
|
330
....*....|..
gi 612673931 731 VLVNAVKAKRQE 742
Cdd:COG0620 314 NMVAFAREVRGE 325
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
416-740 |
2.64e-124 |
|
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: 374.26 E-value: 2.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 416 PTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGFLVTkf 495
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 496 GWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTD-KPVKGMLTGPVTILNWSF---ERVDLPRKVVQDQIALAIN 571
Cdd:cd03311 79 GWVQSYGSRYYKPPGIVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFvrfRGYYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 572 EEVLALEAAGIKVIQVDEPALREGLPL-RSEYHEQYLKDAVLSFKLAtssvRDETQIHTHMCYSQFGQ----------II 640
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPLePDDLAADYLKWANEALADR----PDDTQIHTHICYGNFRStwaaeggyepIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 641 HAIHDLDADVISIETSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTR 720
Cdd:cd03311 235 EYIFELDVDVFFLEYDNSRAGGLEPLKELPYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCGFATR 314
|
330 340
....*....|....*....|
gi 612673931 721 KEEEvkdALTVLVNAVKAKR 740
Cdd:cd03311 315 ERGN---ALTKLENMVKAAL 331
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
411-742 |
8.32e-72 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 237.18 E-value: 8.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 411 NLPDLPTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGF 490
Cdd:PRK04326 5 KLPFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 491 lvtKF-GWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLT-DKPVKGMLTGPVTILNWSF-ERVDLPRKVVQDqIA 567
Cdd:PRK04326 85 ---KFyGPVRVWGNNYFRKPSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFnEYYKDKEELVFD-LA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 568 LAINEEVLALEAAGIKVIQVDEPALreglPLRSEYHEQylkdAVLSFKLATSSVrdETQIHTHMCYSQFGQIIHAIHDLD 647
Cdd:PRK04326 161 KVINEEIKNLVEAGAKYIQIDEPAL----ATHPEDVEI----AVEALNRIVKGI--NAKLGLHVCYGDYSRIAPYILEFP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 648 ADVISIETSRSHGDLIKDFEDINYDLGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLKTRKEEEVKD 727
Cdd:PRK04326 231 VDQFDLEFANGNYKLLDLLKEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPREIAYQ 310
|
330
....*....|....*
gi 612673931 728 ALTVLVNAVKAKRQE 742
Cdd:PRK04326 311 KLVNMVKATREVREE 325
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
5-350 |
4.49e-70 |
|
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: 232.34 E-value: 4.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 5 KTSNLGFPRLgrkREWKKAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSLYDhildtslLFNIIPER 84
Cdd:COG0620 3 TTTVGSFPRP---RELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYD-------MVGYFPER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 85 FQGrtidddllFDIARgnkdhvaSALIKWFNTNYHYiVPEwdnVEPKVSR--NVLLDRFKYAQSL-NVNAHPVIVGPITF 161
Cdd:COG0620 73 LDG--------YAFAR-------NGWVEWFDTNYHY-VPE---ITGDVSFsgPMTVEEFRFAKSLtGKPVKPVLPGPVTL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 162 VKLSKGGH-QTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESYENITREAYDYFeKAGVAK-KLVIQTYF 239
Cdd:COG0620 134 LLLSKVRDyKDREELLDDLAPAYREELKALEAAGARWIQIDEPALAEDLPDEYLDWAVEAYNRA-AAGVPDtKIHLHTCY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 240 E--RAHLKFLSSLPVGGLGLDFVHDNGYNLKQIEagDFDKSKTLYAGIIDGRNVWASDIEAKKALIDKLLAH--TNELVI 315
Cdd:COG0620 213 GgyEDILEALAALPVDGIHLEFVRSRAGLLEPLK--ELPYDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYvpPERLWV 290
|
330 340 350
....*....|....*....|....*....|....*
gi 612673931 316 QPSSSLLHVPVSLDDETLDSSVGEGLSFATEKLDE 350
Cdd:COG0620 291 SPDCGLKHRPVDLTREEAWAKLRNMVAFAREVRGE 325
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
416-740 |
8.29e-38 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 143.72 E-value: 8.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 416 PTTTIGSFPQSREVRKYRADWKNKRITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERnDMVEFFGEKLQGflvTKF 495
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSILEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQLGD-DMIGRFLEVLVD---LET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 496 GWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLP--RKVVQDQIALAINEE 573
Cdd:cd03310 77 GTRFFDNNFFYRPPEAKIEAFLPLELDYLEEVAEAYKEALKVKVVVTGPLTLALLAFLPNGEPdaYEDLAKSLAEFLREQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 574 VLALEAAGIKVIQVDEPALREGLPLRSEYHEQylkdavLSFKLATSSVRDETQIHTHMCYsqfGQIIHAIHDLDADVISI 653
Cdd:cd03310 157 VKELKNRGIVVVQIDEPSLGAVGAGAFEDLEI------VDAALEEVSLKSGGDVEVHLCA---PLDYEALLELGVDVIGF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 654 ETSRS---HGDLIKDFEDINY-DLGIGLGVYDI----HSPR--IPTKEEITTAINRSLQQIDRSLfWVNPDCGLKTRKEE 723
Cdd:cd03310 228 DAAALpskYLEDLKKLLRIGVrTLILGLVVTDNeakgRNAWkeIERLEKLVRRLEEPGEVLDEIL-YLTPDCGLAFLPPQ 306
|
330
....*....|....*..
gi 612673931 724 EvkdALTVLVNAVKAKR 740
Cdd:cd03310 307 E---ARRKLALLAEAAR 320
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
416-721 |
3.97e-36 |
|
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc.
Pssm-ID: 238261 [Multi-domain] Cd Length: 306 Bit Score: 138.40 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 416 PTTTIGSFPQSREVRKyradwknKRITDEAYETFLKNEIARWIKiQEDIGLDVLVHGEFERNDMVEFFGeklqgflvtkf 495
Cdd:cd00465 1 PVQCEGQTGIMEASET-------MAISEEPGETSKAEWGITLVE-PEEIPLDVIPVHEDDVLKVAQALG----------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 496 GWVQSYGSRAVKPPIIYGDVKW-TAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVD----LPRKVVQ-----DQ 565
Cdd:cd00465 62 EWAFRYYSQAPSVPEIDEEEDPfREAPALEHITAVRSLEEFPTAGAAGGPFTFTHHSMSMGDalmaLYERPEAmheliEY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 566 IALAINEEVLALEAAGIKVIQVDEPALREGLPLRSEyhEQYLKDAVLSF-KLATSSVRDETQIHTHMCYSQFgQIIHAIH 644
Cdd:cd00465 142 LTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLGP--KMFKKFALPAYkKVAEYKAAGEVPIVHHSCYDAA-DLLEEMI 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612673931 645 DLDADVISIETSRshGDLIKDFEDINYDLGIGLGVYDIHSPRipTKEEITTAINRSLQQIDRsLFWVNPDCGLKTRK 721
Cdd:cd00465 219 QLGVDVISFDMTV--NEPKEAIEKVGEKKTLVGGVDPGYLPA--TDEECIAKVEELVERLGP-HYIINPDCGLGPDS 290
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
415-737 |
5.52e-26 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 108.92 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPqsreVRKYRADWKNKRITDE--AYETFlKNEIARWIKIQEDIGLDVLVHGEFeRNDMVEFFGEKLQGFlv 492
Cdd:PRK00957 2 MITTVVGSYP----VVKGEPETLKDKIKGFfgLYDPY-KPAIEEAVADQVKAGIDIISDGQV-RGDMVEIFASNMPGF-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 493 tkfgwvqsYGSRAVkppiiyGDVKWTA-PLTVDETVYAQSLT-----DKPVKGMLTGPVTILNWSfeRVDLPRK------ 560
Cdd:PRK00957 74 --------DGKRVI------GRVEPPAkPITLKDLKYAKKVAkkkdpNKGVKGIITGPSTLAYSL--RVEPFYSdnkdee 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 561 VVQDqIALAINEEVLALEAAGIKVIQVDEPALREGLPlrseyheqYLKDAVLSFKLATSSVRDETQIHThmCySQFGQII 640
Cdd:PRK00957 138 LIYD-LARALRKEAEALEKAGVAMIQIDEPILSTGAY--------DLEVAKKAIDIITKGLNVPVAMHV--C-GDVSNII 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 641 HAIHDLDADVISIE--TSRSHGDLIKDFEDINYdlGIGLGVYDIHSPRIPTKEEITTAINRSLQQIDRSLFWVNPDCGLK 718
Cdd:PRK00957 206 DDLLKFNVDILDHEfaSNKKNLEILEEKDLIGK--KIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILIDPDCGMR 283
|
330
....*....|....*....
gi 612673931 719 TRKEEEVKDALTVLVNAVK 737
Cdd:PRK00957 284 MLPRDVAFEKLKNMVEAAR 302
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
415-737 |
1.40e-22 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 99.61 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPQ----SREVRKYRADWKNKRITDEA-YETflkneiarwIKIQEDIGLD-VLVHGEFERNDMVEFFGEKLQ 488
Cdd:PRK01207 4 LITQEIGSFRKpeylSREFHKIEGTDKFYELAERAtLET---------LDVFENAGLDnIGIGGEMFRWEMYEHPAERIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 489 GFLVtkFGWVQSYGSRAVKPPIIYGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIAL 568
Cdd:PRK01207 75 GIIF--YGMVRSFDNRYYRKGSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 569 AINEEVLALEAA------GIKV-IQVDEPAlreglplrSEYHEQYLKDAVLSFKLATSSVRDETQIhtHMCYSQFGQIIH 641
Cdd:PRK01207 153 IINEELKDIKSAwdrkspGRKLeIQIDEPA--------TTTHPDEMDIVVDSINKSVYGIDNEFSI--HVCYSSDYRLLY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 642 -AIHDLDADVISIETS-RSHGDL------------IKDFEDINYDLG----IGLGVYDIHSPRIPTKEEITTAINRSLQQ 703
Cdd:PRK01207 223 dRIPELNIDGYNLEYSnRDTLEPgtsdekrpgfqdLKYFAEHNESLQrkkfIGLGVTDVHIDYVEPVKLIEDRIRYALKI 302
|
330 340 350
....*....|....*....|....*....|....*
gi 612673931 704 I-DRSLFWVNPDCGLKTRKEEEVKDALTVLVNAVK 737
Cdd:PRK01207 303 IkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKN 337
|
|
| PRK09121 |
PRK09121 |
methionine synthase; |
415-742 |
3.20e-22 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 98.60 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 415 LPTTTIGSFPQSR---EVRKYRADWKnkrITDEAYETFLKNEIARWIKIQEDIGLDVLVHGEFERNDMVEFFGEKLQGfl 491
Cdd:PRK09121 3 LPTSTAGSLPKPSwlaEPETLWSPWK---LQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 492 vTKFGWVQSYGSR----AVKPPIIyGDVKWTAPLTVDETVYAQSLTDKPVKGMLTGPVTILNWSFERVDLPRKVVQDQIA 567
Cdd:PRK09121 78 -VDFEKRETVRIRdrydASVPTVV-GAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 568 LAINEEVLALEAAGIKVIQVDEPALREGLPLRSEYHEQYLKDAVLSFKLATSsvrdetqihTHMCYS------------- 634
Cdd:PRK09121 156 KILNQEAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETA---------VHICYGygikantdwkktl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 635 -----QFGQIIHAIHDLDADVISIETSRSH--GDLI-----KDfedinydlgIGLGVYDIHSPRIPTKEEITTAINRSLQ 702
Cdd:PRK09121 227 gsewrQYEEAFPKLQKSNIDIISLECHNSRvpMDLLelirgKK---------VMVGAIDVASDTIETPEEVADTLRKALQ 297
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 612673931 703 QIDRSLFWVNPDCGLKTRKEEEVKDALTVLVNAVKAKRQE 742
Cdd:PRK09121 298 FVDADKLYPCTNCGMAPLSRDVARGKLNALSAGAEIVRRE 337
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
96-328 |
8.70e-12 |
|
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: 66.75 E-value: 8.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 96 FDIARGNKDH---VASALIKW--FNTNYHYIVPEWDNVEPKVSRNVLLDRFKYAQSLNVnaHPVI---VGPITFVKLSKG 167
Cdd:cd00465 43 LDVIPVHEDDvlkVAQALGEWafRYYSQAPSVPEIDEEEDPFREAPALEHITAVRSLEE--FPTAgaaGGPFTFTHHSMS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 168 GH----------QTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSES--------YENITREAYDYFEKAGV 229
Cdd:cd00465 121 MGdalmalyerpEAMHELIEYLTEFILEYAKTLIEAGAKALQIHEPAFSQINSFLgpkmfkkfALPAYKKVAEYKAAGEV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 230 akKLVIQTYFERA-HLKFLSSLPVGGLGLDFVHDNgyNLKQIEagDFDKSKTLYAGIIDGRNVWAS--DIEAKKALIDKL 306
Cdd:cd00465 201 --PIVHHSCYDAAdLLEEMIQLGVDVISFDMTVNE--PKEAIE--KVGEKKTLVGGVDPGYLPATDeeCIAKVEELVERL 274
|
250 260
....*....|....*....|..
gi 612673931 307 LAHTnelVIQPSSSLLHVPVSL 328
Cdd:cd00465 275 GPHY---IINPDCGLGPDSDYK 293
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
15-326 |
2.27e-11 |
|
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been characterized as 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferases, EC:2.1.1.14, mostly from bacteria and plants. This enzyme catalyses the last step in the production of methionine by transferring a methyl group from 5-methyltetrahydrofolate to L-homocysteine without using an intermediate methyl carrier. The active enzyme has a dual (beta-alpha)8-barrel structure, and this model covers both the N-and C-terminal barrel, and some single-barrel sequences, mostly from Archaea. It is assumed that the homologous N-terminal barrel has evolved from the C-terminus via gene duplication and has subsequently lost binding sites, and it seems as if the two barrels forming the active enzyme may sometimes reside on different polypeptides. The C-terminal domain incorporates the Zinc ion, which binds and activates homocysteine. Side chains from both barrels contribute to the binding of the folate substrate.
Pssm-ID: 239426 [Multi-domain] Cd Length: 321 Bit Score: 65.53 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 15 GRKREWKKaiesYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFslYDHILDTSLLFNIIPERFQGRtidddl 94
Cdd:cd03310 13 GVTKEWSI----LEKGAIEPEWPEEALFTALGSFFELQLEAGVEVPTYGQL--GDDMIGRFLEVLVDLETGTRF------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 95 lfdiargnkdhvasalikwFNTNYHYIVPE-----WDNVEPKVsrnvlLDRFKYAQSLNVNAHPVIVGPITFVKLSKGGH 169
Cdd:cd03310 81 -------------------FDNNFFYRPPEakieaFLPLELDY-----LEEVAEAYKEALKVKVVVTGPLTLALLAFLPN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 170 QTF---EEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVTDDSESY---ENITREAYDYFEKAGVAKKLVIQTYferAH 243
Cdd:cd03310 137 GEPdayEDLAKSLAEFLREQVKELKNRGIVVVQIDEPSLGAVGAGAFedlEIVDAALEEVSLKSGGDVEVHLCAP---LD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 244 LKFLSSLPVGGLGLDFVhdnGYNLKQIEAGD-----FDKSKTLYAGIID----GRNVW--ASDIEAKKALIDKLLAHTNE 312
Cdd:cd03310 214 YEALLELGVDVIGFDAA---ALPSKYLEDLKkllriGVRTLILGLVVTDneakGRNAWkeIERLEKLVRRLEEPGEVLDE 290
|
330
....*....|....*
gi 612673931 313 LV-IQPSSSLLHVPV 326
Cdd:cd03310 291 ILyLTPDCGLAFLPP 305
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
137-317 |
8.49e-08 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 54.60 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 137 LLDRFKYAQSLNVNaHPV---IVGPITFVKLSKGGH-QTFEEKVKTLLPLYKEVFESLIDAGAEYIQVDEPILVT--DDS 210
Cdd:PRK04326 114 LVDEFEFAKSVTYT-RPVkvpITGPYTIAEWSFNEYyKDKEELVFDLAKVINEEIKNLVEAGAKYIQIDEPALAThpEDV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 211 EsyenITREAYDYFEKaGVAKKLVIQTYFERAHL--KFLSSLPVGGLGLDFVHDNGYNLKQIEAGDFDKSktLYAGIIDG 288
Cdd:PRK04326 193 E----IAVEALNRIVK-GINAKLGLHVCYGDYSRiaPYILEFPVDQFDLEFANGNYKLLDLLKEYGFDKE--LGLGVIDV 265
|
170 180 190
....*....|....*....|....*....|.
gi 612673931 289 RNVWASDIEAKKALIDKLLAHTN--ELVIQP 317
Cdd:PRK04326 266 HSARVESVEEIKEAIKKGLEYVPpeKLYINP 296
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
22-290 |
3.99e-06 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 22 KAIESYWAKKISKEELDQTLTDLHKENLLLQKYYHLDSIPVGDFSlYDHILDtsLLFNIIperfQGRTIDddllfdiarg 101
Cdd:PRK08575 19 KVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFR-WDDIFD--PTISFI----SGVEKG---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 102 nkdhvasALIKWFNTNYHYIVP--------EWDNVEPKVSRNV--LLDRFKYAQSLNvnahPVIVGPITFVKLSKGGHQT 171
Cdd:PRK08575 82 -------GLQRFYDNNFYYRQPvikekinlKEENPYLQWLESAreIKEEVSLESKLK----AVLPGPLTYAVLSDNEYYK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 172 FEEKvktLLPLYKEVFESLI---DAGAEYIQVDEPILVTDD-SESYENITREAYDYFEKaGVAKKLVIQTYFERAHL--- 244
Cdd:PRK08575 151 NLIE---LMEDYASVVNSLIkelSSVVDAVEIHEPSIFAKGiKRDTLEKLPEVYKTMAK-NVNIEKHLMTYFEINNLkrl 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 612673931 245 KFLSSLPVGGLGLDFVhDNGYNLKQIEagDFDKSKTLYAGIIDGRN 290
Cdd:PRK08575 227 DILFSLPVTYFGIDVI-ENLKKLGRVY--TYLKGRKVYLGILNARN 269
|
|
| CIMS_N_terminal_like |
cd03312 |
CIMS - Cobalamine-independent methonine synthase, or MetE, N-terminal domain_like. Many ... |
517-592 |
8.16e-05 |
|
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: 45.60 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 517 WTAPLtvDETVYAQSLTD--KPVkgmLTGPVTIL------NWSFERVDLprkvvQDQIaLAINEEVLA-LEAAGIKVIQV 587
Cdd:cd03312 133 SNKLL--DEYLEAKALGIntKPV---LLGPVTFLklskakGGGFDRLSL-----LDKL-LPVYKELLKkLAAAGAEWVQI 201
|
....*
gi 612673931 588 DEPAL 592
Cdd:cd03312 202 DEPAL 206
|
|
| Meth_synt_1 |
pfam08267 |
Cobalamin-independent synthase, N-terminal domain; The N-terminal domain and C-terminal ... |
517-592 |
5.76e-04 |
|
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: 42.57 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 517 WTAPLtvDETVYAQSLTD--KPVkgmLTGPVTILnW-------SFERVDLPRKVvqdqiaLAINEEVLA-LEAAGIKVIQ 586
Cdd:pfam08267 132 SNKLL--DEYKEAKALGIetKPV---LLGPVTFL-KlskgkggSFDRLELLPKL------LPVYKELLKeLAAAGAEWVQ 199
|
....*.
gi 612673931 587 VDEPAL 592
Cdd:pfam08267 200 IDEPAL 205
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
128-208 |
9.81e-03 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 38.82 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612673931 128 VEPkVSRNVLLDRFKYAQSL------NVNAHPVIVGPITFVKLSKGG----HQTFEEKVKTLL-PLYKEVfESLIDAGAE 196
Cdd:PRK00957 82 VEP-PAKPITLKDLKYAKKVakkkdpNKGVKGIITGPSTLAYSLRVEpfysDNKDEELIYDLArALRKEA-EALEKAGVA 159
|
90
....*....|..
gi 612673931 197 YIQVDEPILVTD 208
Cdd:PRK00957 160 MIQIDEPILSTG 171
|
|
| |
