|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09121 |
PRK09121 |
methionine synthase; |
3-341 |
0e+00 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 799.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 3 TLLPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDF 82
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 83 EKRETVKIRNRYDASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNE 162
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 163 EAKELEAAGVDIIQFDEPAFNVFFDEVNDWGIACLERAIEGLKCETAVHICYGYGIKANTDWKKTLGTEWRQYEEVFPKL 242
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETAVHICYGYGIKANTDWKKTLGSEWRQYEEAFPKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 243 QQSNIDIISLECHNSHVPLELLELVRGKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCGMAPLPREIA 322
Cdd:PRK09121 241 QKSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADKLYPCTNCGMAPLSRDVA 320
|
330
....*....|....*....
gi 498124300 323 SAKLNALSAGAEIVRKELS 341
Cdd:PRK09121 321 RGKLNALSAGAEIVRRELA 339
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
6-335 |
1.81e-111 |
|
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: 327.26 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 6 PTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFEKr 85
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 86 ETVKIRNRYDASVPtVVGPVSRQKSVFVEDAKFLRQQTD-QPIKWALPGPMTMIDTLYDAH---YKSREKLAWEFAKILN 161
Cdd:cd03311 80 WVQSYGSRYYKPPG-IVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 162 EEAKELEAAGVDIIQFDEPAFNVFFD-----EVNDWGIACLERAIE-GLKCETAVHICYGYGIKANTdwkkTLGTEWRQY 235
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPlepddLAADYLKWANEALADrPDDTQIHTHICYGNFRSTWA----AEGGYEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 236 EEVFPKlqqsNIDIISLECHNS-HVPLELLELV-RGKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCG 313
Cdd:cd03311 235 EYIFEL----DVDVFFLEYDNSrAGGLEPLKELpYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCG 310
|
330 340
....*....|....*....|..
gi 498124300 314 MAPLPREIASAKLNALSAGAEI 335
Cdd:cd03311 311 FATRERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
5-339 |
1.59e-106 |
|
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: 314.39 E-value: 1.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 5 LPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFEK 84
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 85 RETVKIRN-RYdASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNEE 163
Cdd:COG0620 81 NGWVEWFDtNY-HYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 164 AKELEAAGVDIIQFDEPAFNVFF-DEVNDWGIACLERAIEGLK-CETAVHICYGygikantdwkktlgtewrQYEEVFPK 241
Cdd:COG0620 160 LKALEAAGARWIQIDEPALAEDLpDEYLDWAVEAYNRAAAGVPdTKIHLHTCYG------------------GYEDILEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 242 LQQSNIDIISLECHNSHvpLELLELVR----GKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCGMAPL 317
Cdd:COG0620 222 LAALPVDGIHLEFVRSR--AGLLEPLKelpyDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHR 299
|
330 340
....*....|....*....|....*.
gi 498124300 318 P----REIASAKLNALSAGAEIVRKE 339
Cdd:COG0620 300 PvdltREEAWAKLRNMVAFAREVRGE 325
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
5-326 |
1.07e-32 |
|
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: 123.70 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 5 LPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFEK 84
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 85 RETVKIRNRYDASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNEEA 164
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 165 KELEAAGVDIIQFDEPAFN-------VFFDEVNDWGIAC--LERAIEGLKCETAVHICYGygikantdwkktlgtewrQY 235
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALReglplkkLDWAAYLDWAVAAfrLDTCGAADDTQIHTHMCYS------------------DF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 236 EEVFPKLQQSNIDIISLEchNSHVPLELLELVR----GKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTN 311
Cdd:pfam01717 223 NDILSAIAALDADVITIE--ASRSDMELLEAFEewgyGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPD 300
|
330
....*....|....*
gi 498124300 312 CGMAPLPREIASAKL 326
Cdd:pfam01717 301 CGLKTRGWEEARAAL 315
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09121 |
PRK09121 |
methionine synthase; |
3-341 |
0e+00 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 799.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 3 TLLPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDF 82
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 83 EKRETVKIRNRYDASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNE 162
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 163 EAKELEAAGVDIIQFDEPAFNVFFDEVNDWGIACLERAIEGLKCETAVHICYGYGIKANTDWKKTLGTEWRQYEEVFPKL 242
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETAVHICYGYGIKANTDWKKTLGSEWRQYEEAFPKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 243 QQSNIDIISLECHNSHVPLELLELVRGKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCGMAPLPREIA 322
Cdd:PRK09121 241 QKSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADKLYPCTNCGMAPLSRDVA 320
|
330
....*....|....*....
gi 498124300 323 SAKLNALSAGAEIVRKELS 341
Cdd:PRK09121 321 RGKLNALSAGAEIVRRELA 339
|
|
| CIMS_C_terminal_like |
cd03311 |
CIMS - Cobalamine-independent methonine synthase, or MetE, C-terminal domain_like. Many ... |
6-335 |
1.81e-111 |
|
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: 327.26 E-value: 1.81e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 6 PTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFEKr 85
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 86 ETVKIRNRYDASVPtVVGPVSRQKSVFVEDAKFLRQQTD-QPIKWALPGPMTMIDTLYDAH---YKSREKLAWEFAKILN 161
Cdd:cd03311 80 WVQSYGSRYYKPPG-IVGDVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 162 EEAKELEAAGVDIIQFDEPAFNVFFD-----EVNDWGIACLERAIE-GLKCETAVHICYGYGIKANTdwkkTLGTEWRQY 235
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPlepddLAADYLKWANEALADrPDDTQIHTHICYGNFRSTWA----AEGGYEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 236 EEVFPKlqqsNIDIISLECHNS-HVPLELLELV-RGKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCG 313
Cdd:cd03311 235 EYIFEL----DVDVFFLEYDNSrAGGLEPLKELpYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCG 310
|
330 340
....*....|....*....|..
gi 498124300 314 MAPLPREIASAKLNALSAGAEI 335
Cdd:cd03311 311 FATRERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
5-339 |
1.59e-106 |
|
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: 314.39 E-value: 1.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 5 LPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFEK 84
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 85 RETVKIRN-RYdASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNEE 163
Cdd:COG0620 81 NGWVEWFDtNY-HYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 164 AKELEAAGVDIIQFDEPAFNVFF-DEVNDWGIACLERAIEGLK-CETAVHICYGygikantdwkktlgtewrQYEEVFPK 241
Cdd:COG0620 160 LKALEAAGARWIQIDEPALAEDLpDEYLDWAVEAYNRAAAGVPdTKIHLHTCYG------------------GYEDILEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 242 LQQSNIDIISLECHNSHvpLELLELVR----GKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCGMAPL 317
Cdd:COG0620 222 LAALPVDGIHLEFVRSR--AGLLEPLKelpyDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHR 299
|
330 340
....*....|....*....|....*.
gi 498124300 318 P----REIASAKLNALSAGAEIVRKE 339
Cdd:COG0620 300 PvdltREEAWAKLRNMVAFAREVRGE 325
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
3-342 |
2.09e-75 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 235.26 E-value: 2.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 3 TLLPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDF 82
Cdd:PRK04326 7 PFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGFKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 83 EKRETVKIRNRYDAsvPTVVGPVSRQKSVFVEDAKFLRQQT-DQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILN 161
Cdd:PRK04326 87 YGPVRVWGNNYFRK--PSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKVIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 162 EEAKELEAAGVDIIQFDEPAFNVFFDEVnDWGIACLERAIEGLKCETAVHICYGygikantdwkktlgtewrQYEEVFPK 241
Cdd:PRK04326 165 EEIKNLVEAGAKYIQIDEPALATHPEDV-EIAVEALNRIVKGINAKLGLHVCYG------------------DYSRIAPY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 242 LQQSNIDIISLE-CHNSHVPLELL-ELVRGKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCGMAPLPR 319
Cdd:PRK04326 226 ILEFPVDQFDLEfANGNYKLLDLLkEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPR 305
|
330 340
....*....|....*....|...
gi 498124300 320 EIASAKLNALSAGAEIVRKELSA 342
Cdd:PRK04326 306 EIAYQKLVNMVKATREVREELDK 328
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
4-337 |
1.65e-38 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 138.97 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 4 LLPTSTAGSLPkpSWLAQPETLwspwklqGDELTD--GKQDALRVSLHE----QQQAGIDIVSDGeQTRQHFVTTFIEHL 77
Cdd:PRK00957 1 IMITTVVGSYP--VVKGEPETL-------KDKIKGffGLYDPYKPAIEEavadQVKAGIDIISDG-QVRGDMVEIFASNM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 78 NGvdfekretvkIRNRydasvpTVVGPVSR-QKSVFVEDAKFLRQQT-----DQPIKWALPGPMTMIDTLY-DAHYKSR- 149
Cdd:PRK00957 71 PG----------FDGK------RVIGRVEPpAKPITLKDLKYAKKVAkkkdpNKGVKGIITGPSTLAYSLRvEPFYSDNk 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 150 -EKLAWEFAKILNEEAKELEAAGVDIIQFDEPAFNVffdevndwGIACLE---RAIE----GLKCETAVHICYGYGikan 221
Cdd:PRK00957 135 dEELIYDLARALRKEAEALEKAGVAMIQIDEPILST--------GAYDLEvakKAIDiitkGLNVPVAMHVCGDVS---- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 222 tdwkktlgtewrqyeEVFPKLQQSNIDIISLECHNSHVPLELLE--LVRGKKVMVGAIDVATDSIETPEEVASTLRETLK 299
Cdd:PRK00957 203 ---------------NIIDDLLKFNVDILDHEFASNKKNLEILEekDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIE 267
|
330 340 350
....*....|....*....|....*....|....*...
gi 498124300 300 YVDADKLYPCTNCGMAPLPREIASAKLNALSAGAEIVR 337
Cdd:PRK00957 268 ILGAENILIDPDCGMRMLPRDVAFEKLKNMVEAAREIR 305
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
5-326 |
1.07e-32 |
|
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: 123.70 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 5 LPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFEK 84
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 85 RETVKIRNRYDASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNEEA 164
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 165 KELEAAGVDIIQFDEPAFN-------VFFDEVNDWGIAC--LERAIEGLKCETAVHICYGygikantdwkktlgtewrQY 235
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALReglplkkLDWAAYLDWAVAAfrLDTCGAADDTQIHTHMCYS------------------DF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 236 EEVFPKLQQSNIDIISLEchNSHVPLELLELVR----GKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTN 311
Cdd:pfam01717 223 NDILSAIAALDADVITIE--ASRSDMELLEAFEewgyGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPD 300
|
330
....*....|....*
gi 498124300 312 CGMAPLPREIASAKL 326
Cdd:pfam01717 301 CGLKTRGWEEARAAL 315
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
3-340 |
1.07e-31 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 121.57 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 3 TLLPTSTAGSLPKPSWLAQPETlwspwKLQG-DELTDGKQDALRVSLHEQQQAGIDIVS-DGEQTRQHFVTTFIEHLNGV 80
Cdd:PRK01207 2 AALITQEIGSFRKPEYLSREFH-----KIEGtDKFYELAERATLETLDVFENAGLDNIGiGGEMFRWEMYEHPAERIKGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 81 DFEKReTVKIRNRYDASvPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKIL 160
Cdd:PRK01207 77 IFYGM-VRSFDNRYYRK-GSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFARII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 161 NEEAKELEAAGVDI-------IQFDEPAFNVFFDEVnDWGIACLERAIEGLKCETAVHICYGygikantdwkktlgtewR 233
Cdd:PRK01207 155 NEELKDIKSAWDRKspgrkleIQIDEPATTTHPDEM-DIVVDSINKSVYGIDNEFSIHVCYS-----------------S 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 234 QYEEVFPKLQQSNIDIISLECHNSHVP------------------LELLELVRGKKVM-VGAIDVATDSIETPEEVASTL 294
Cdd:PRK01207 217 DYRLLYDRIPELNIDGYNLEYSNRDTLepgtsdekrpgfqdlkyfAEHNESLQRKKFIgLGVTDVHIDYVEPVKLIEDRI 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 498124300 295 RETLKYV-DADKLYPCTNCGMAPLPREIASAKLNALSAGAEIVRKEL 340
Cdd:PRK01207 297 RYALKIIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
4-340 |
1.52e-21 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 95.61 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 4 LLPTSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVDFE 83
Cdd:PLN02475 432 ILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFT 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 84 KRETVKIRNRYDASVPTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNEE 163
Cdd:PLN02475 512 ANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDE 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 164 AKELEAAGVDIIQFDEPAF----------NVFFdevNDWGIACLERAIEGLKCETAV--HICYGygikantdwkktlgte 231
Cdd:PLN02475 592 VEDLEKAGITVIQIDEAALreglplrkseHAFY---LDWAVHSFRITNCGVQDTTQIhtHMCYS---------------- 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 232 wrQYEEVFPKLQQSNIDIISLEchNSHVPLELLELVR-----GKKVMVGAIDVATDSIETPEEVASTLRETLKYVDADKL 306
Cdd:PLN02475 653 --NFNDIIHSIIDMDADVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLESNIL 728
|
330 340 350
....*....|....*....|....*....|....
gi 498124300 307 YPCTNCGMAPLPREIASAKLNALSAGAEIVRKEL 340
Cdd:PLN02475 729 WVNPDCGLKTRKYPEVKPALKNMVAAAKLLRAQL 762
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
6-335 |
3.10e-16 |
|
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: 78.24 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 6 PTSTAGSLPKPSWLAQpetLWSPWKLQGD--ELTDGKQDALRVSLHEQQ-QAGIDIVSDGEQTrQHFVTTFIEHLNGVDF 82
Cdd:cd03310 1 LATGIGSYPLPDGVTK---EWSILEKGAIepEWPEEALFTALGSFFELQlEAGVEVPTYGQLG-DDMIGRFLEVLVDLET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 83 EKRETVkirNRYDASVPTVVGPVS-RQKSVFVEDAKFLRQQTdQPIKWALPGPMTMIDTLYDAHYK--SREKLAWEFAKI 159
Cdd:cd03310 77 GTRFFD---NNFFYRPPEAKIEAFlPLELDYLEEVAEAYKEA-LKVKVVVTGPLTLALLAFLPNGEpdAYEDLAKSLAEF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 160 LNEEAKELEAAGVDIIQFDEPAFNVFFDEVNDWGIACLERAIEGLKCETA---VHICYGygikantdwkktlgtewRQYE 236
Cdd:cd03310 153 LREQVKELKNRGIVVVQIDEPSLGAVGAGAFEDLEIVDAALEEVSLKSGGdveVHLCAP-----------------LDYE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 237 EVFpklqQSNIDIISLECHNSHVPL-----ELLEL-VRGKKVMVGAIDVAT------DSIETPEEVASTLrETLKYVDAD 304
Cdd:cd03310 216 ALL----ELGVDVIGFDAAALPSKYledlkKLLRIgVRTLILGLVVTDNEAkgrnawKEIERLEKLVRRL-EEPGEVLDE 290
|
330 340 350
....*....|....*....|....*....|.
gi 498124300 305 KLYPCTNCGMAPLPREIASAKLNALSAGAEI 335
Cdd:cd03310 291 ILYLTPDCGLAFLPPQEARRKLALLAEAARE 321
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
43-318 |
1.58e-09 |
|
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: 58.28 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 43 ALRVSLHEQQQAGIDIVSDGEQtrqhFVTTFIEHLNGVDFEKREtvkirnrYDASVPTVVGPV-SRQKSVFVEDAKFLRQ 121
Cdd:cd00465 30 EWGITLVEPEEIPLDVIPVHED----DVLKVAQALGEWAFRYYS-------QAPSVPEIDEEEdPFREAPALEHITAVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 122 QTDQPIKWALPGPMTM----------IDTLYDAHYKSREkLAWEFAKILNEEAKELEAAGVDIIQFDEPAF---NVFF-- 186
Cdd:cd00465 99 LEEFPTAGAAGGPFTFthhsmsmgdaLMALYERPEAMHE-LIEYLTEFILEYAKTLIEAGAKALQIHEPAFsqiNSFLgp 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 187 DEVNDWGIACLERAieglkcetavhicygYGIKANTDWKKTLGTEWRQYEEVfPKLQQSNIDIISLEcHNSHVPLELLEL 266
Cdd:cd00465 178 KMFKKFALPAYKKV---------------AEYKAAGEVPIVHHSCYDAADLL-EEMIQLGVDVISFD-MTVNEPKEAIEK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 498124300 267 VRGKKVMVGAIDvATDSIETPEEVASTLRETLKYVDADKLYPCtNCGMAPLP 318
Cdd:cd00465 241 VGEKKTLVGGVD-PGYLPATDEECIAKVEELVERLGPHYIINP-DCGLGPDS 290
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
99-182 |
5.38e-09 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 57.43 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 99 PTVVGPVSRQKSVFVEDAKFLRQQTDQPIKWALPGPMTMidtlydahyksrekLAWEF--------------AKILNEEA 164
Cdd:PRK05222 522 PIIYGDVSRPEPMTVEWIKYAQSLTDKPVKGMLTGPVTI--------------LNWSFvrddqpreetarqiALAIRDEV 587
|
90
....*....|....*...
gi 498124300 165 KELEAAGVDIIQFDEPAF 182
Cdd:PRK05222 588 LDLEAAGIKIIQIDEPAL 605
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
7-339 |
8.65e-09 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 56.28 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 7 TSTAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQHFVTTFIEHLNGVdfEKRE 86
Cdd:PRK08575 5 KALVGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGV--EKGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 87 TVKI-RNRYDASVPTVVGPVSRQKSV-FVEDAKFLRQQTDQ-----PIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKI 159
Cdd:PRK08575 83 LQRFyDNNFYYRQPVIKEKINLKEENpYLQWLESAREIKEEvslesKLKAVLPGPLTYAVLSDNEYYKNLIELMEDYASV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 160 LNEEAKELEaAGVDIIQFDEPAFnvFFDEVNDwgiACLERAIEGLKcETAVhicygyGIKANTDWKKTLGTEWRQYEEVF 239
Cdd:PRK08575 163 VNSLIKELS-SVVDAVEIHEPSI--FAKGIKR---DTLEKLPEVYK-TMAK------NVNIEKHLMTYFEINNLKRLDIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 240 PKLQQS--NIDIISLECHNSHVPLELlelvRGKKVMVGAIdvatDSIETPEEVASTLR---ETLKYVDADKLYPCTNCGM 314
Cdd:PRK08575 230 FSLPVTyfGIDVIENLKKLGRVYTYL----KGRKVYLGIL----NARNTKMEKISTIRrivNKVKRKGVSDIIVGNNTLF 301
|
330 340
....*....|....*....|....*
gi 498124300 315 APLPREIASAKLNALSAGAEIVRKE 339
Cdd:PRK08575 302 DFIPEVVAVKKLKLLGKLEKLEGGE 326
|
|
| PRK06520 |
PRK06520 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; |
9-315 |
1.05e-06 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase;
Pssm-ID: 180601 Cd Length: 368 Bit Score: 49.72 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 9 TAGSLPKPSWLAQPETLWSPWKLQGDELTDGKQDALRVSLHEQQQAGIDIVSDGEQTRQ--HFvtTFIEHLNGVDFEKRE 86
Cdd:PRK06520 12 VVGSFLRPAAIKQARQQFAAGEIDAAALRKIEDMEIRKVVEKQRACGLKVVTDGEFRRAwwHF--DFFDGLQGVERYEAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 87 T------VKIRNRydaSVpTVVGPVS-RQKSVFVEDAKFL-RQQTDQPIKWALPGPMTM--------ID-TLY---DAHY 146
Cdd:PRK06520 90 QgiqfngVQTKAR---GV-RVTGKLDfPDDHPMLEDFRFLkSISGDATPKMTIPSPSVLhfrggrkaIDaTVYpdlDDYF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 147 KsreklawEFAKILNEEAKELEAAGVDIIQFDEPAfnvffdevndWGIAC-------------------------LERAI 201
Cdd:PRK06520 166 D-------DLAKTWRDAIKAFYDAGCRYLQLDDTV----------WAYLCsddqrqqirergddpdelariyarvLNKAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498124300 202 EGLKCETAV--HICYGygiKANTDWKKTLGtewrqYEEVFPKL-QQSNIDIISLECHNSHV----PLELLElvRGKKVMV 274
Cdd:PRK06520 229 AGKPADLTIglHVCRG---NFRSTWISEGG-----YEPVAETLfGGVNVDAFFLEYDNERAggfePLRFIP--PGHQQVV 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 498124300 275 -GAIDVATDSIETPEEVASTLRETLKYVDADKLYPCTNCGMA 315
Cdd:PRK06520 299 lGLITTKNGELENADDVKARLAEAAKFVPLEQLCLSPQCGFA 340
|
|
| |
