|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09121 |
PRK09121 |
methionine synthase; |
3-341 |
0e+00 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 793.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 3 TLLPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 82
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 83 ENRQTVRIRNRYDASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQ 162
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 163 EARELEAAGVDIIQFDEPAFNVFFDEVNDWGIAALERAIEGLKCETAVHICYGYGIKANTDWKKTLGSEWRQYEEAFPKL 242
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETAVHICYGYGIKANTDWKKTLGSEWRQYEEAFPKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 243 QTSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCGMAPLSRQVA 322
Cdd:PRK09121 241 QKSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADKLYPCTNCGMAPLSRDVA 320
|
330
....*....|....*....
gi 754493210 323 NGKLKALSAGAEIIRKELG 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 |
2.31e-113 |
|
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: 332.27 E-value: 2.31e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 6 PTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFENr 85
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 86 QTVRIRNRYDASVPTVVsAVARQKPVFVDDAKYLRQLTD-KPIKWALPGPMTMIDTLYDAH---YKSREKLAWEFAKILN 161
Cdd:cd03311 80 WVQSYGSRYYKPPGIVG-DVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 162 QEARELEAAGVDIIQFDEPAFNVFFD-----EVNDWGIAALERAIE-GLKCETAVHICYGYGIKANTdwkkTLGSEWRQY 235
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPlepddLAADYLKWANEALADrPDDTQIHTHICYGNFRSTWA----AEGGYEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 236 EEAFPKlqtsNIDIISLECHNSR-VPMDLLELI-RGKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCG 313
Cdd:cd03311 235 EYIFEL----DVDVFFLEYDNSRaGGLEPLKELpYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCG 310
|
330 340
....*....|....*....|..
gi 754493210 314 MAPLSRQVANGKLKALSAGAEI 335
Cdd:cd03311 311 FATRERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
5-339 |
6.65e-107 |
|
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: 315.54 E-value: 6.65e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 5 LPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFEN 84
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 85 RQTVRIRN-RYdASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQE 163
Cdd:COG0620 81 NGWVEWFDtNY-HYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 164 ARELEAAGVDIIQFDEPAFNVFF-DEVNDWGIAALERAIEGLK-CETAVHICYGygikantdwkktlgsewrQYEEAFPK 241
Cdd:COG0620 160 LKALEAAGARWIQIDEPALAEDLpDEYLDWAVEAYNRAAAGVPdTKIHLHTCYG------------------GYEDILEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 242 LQTSNIDIISLECHNSRvpMDLLELIR----GKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCGMAP- 316
Cdd:COG0620 222 LAALPVDGIHLEFVRSR--AGLLEPLKelpyDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHr 299
|
330 340
....*....|....*....|....*.
gi 754493210 317 ---LSRQVANGKLKALSAGAEIIRKE 339
Cdd:COG0620 300 pvdLTREEAWAKLRNMVAFAREVRGE 325
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
5-334 |
3.77e-35 |
|
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: 130.25 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 5 LPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFEN 84
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 85 RQTVRIRNRYDASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQEA 164
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 165 RELEAAGVDIIQFDEPAFN-------VFFDEVNDWGIAA--LERAIEGLKCETAVHICYgygikantdwkktlgSEwrqY 235
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALReglplkkLDWAAYLDWAVAAfrLDTCGAADDTQIHTHMCY---------------SD---F 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 236 EEAFPKLQTSNIDIISLEchNSRVPMDLLELIR----GKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTN 311
Cdd:pfam01717 223 NDILSAIAALDADVITIE--ASRSDMELLEAFEewgyGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPD 300
|
330 340
....*....|....*....|...
gi 754493210 312 CGMAPLSRQVANGKLKALSAGAE 334
Cdd:pfam01717 301 CGLKTRGWEEARAALRNMVDAAK 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09121 |
PRK09121 |
methionine synthase; |
3-341 |
0e+00 |
|
methionine synthase;
Pssm-ID: 181659 Cd Length: 339 Bit Score: 793.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 3 TLLPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 82
Cdd:PRK09121 1 TLLPTSTAGSLPKPSWLAEPETLWSPWKLQGEELIEGKQDALRLSLQEQEDAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 83 ENRQTVRIRNRYDASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQ 162
Cdd:PRK09121 81 EKRETVRIRDRYDASVPTVVGAVSRQKPVFVEDAKFLRQQTTQPIKWALPGPMTMIDTLYDDHYKSREKLAWEFAKILNQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 163 EARELEAAGVDIIQFDEPAFNVFFDEVNDWGIAALERAIEGLKCETAVHICYGYGIKANTDWKKTLGSEWRQYEEAFPKL 242
Cdd:PRK09121 161 EAKELEAAGVDIIQFDEPAFNVFFDEVNDWGVAALERAIEGLKCETAVHICYGYGIKANTDWKKTLGSEWRQYEEAFPKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 243 QTSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCGMAPLSRQVA 322
Cdd:PRK09121 241 QKSNIDIISLECHNSRVPMDLLELIRGKKVMVGAIDVASDTIETPEEVADTLRKALQFVDADKLYPCTNCGMAPLSRDVA 320
|
330
....*....|....*....
gi 754493210 323 NGKLKALSAGAEIIRKELG 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 |
2.31e-113 |
|
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: 332.27 E-value: 2.31e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 6 PTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFENr 85
Cdd:cd03311 1 PTTTVGSFPRPKELREARAKFKKGEISAEELREAEDDAIADAVKDQEEAGLDVVTDGEFRRSDMVEYFLERLDGFEFTG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 86 QTVRIRNRYDASVPTVVsAVARQKPVFVDDAKYLRQLTD-KPIKWALPGPMTMIDTLYDAH---YKSREKLAWEFAKILN 161
Cdd:cd03311 80 WVQSYGSRYYKPPGIVG-DVSRRPPMTVEEGKIAQSLTHpKPLKGILTGPVTIPSPSFVRFrgyYPSREELAMDLALALR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 162 QEARELEAAGVDIIQFDEPAFNVFFD-----EVNDWGIAALERAIE-GLKCETAVHICYGYGIKANTdwkkTLGSEWRQY 235
Cdd:cd03311 159 EEIRDLYDAGCRYIQIDEPALAEGLPlepddLAADYLKWANEALADrPDDTQIHTHICYGNFRSTWA----AEGGYEPIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 236 EEAFPKlqtsNIDIISLECHNSR-VPMDLLELI-RGKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCG 313
Cdd:cd03311 235 EYIFEL----DVDVFFLEYDNSRaGGLEPLKELpYDKKVGLGVVDVKSPEVESPEEVKDRIEEAAKYVPLEQLWVSPDCG 310
|
330 340
....*....|....*....|..
gi 754493210 314 MAPLSRQVANGKLKALSAGAEI 335
Cdd:cd03311 311 FATRERGNALTKLENMVKAALV 332
|
|
| MetE |
COG0620 |
Methionine synthase II (cobalamin-independent) [Amino acid transport and metabolism]; ... |
5-339 |
6.65e-107 |
|
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: 315.54 E-value: 6.65e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 5 LPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFEN 84
Cdd:COG0620 1 LPTTTVGSFPRPRELKKAREAYWAGEISAEELREAADEAIAEVVRKQEEAGLDVVTDGEFRRYDMVGYFPERLDGYAFAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 85 RQTVRIRN-RYdASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQE 163
Cdd:COG0620 81 NGWVEWFDtNY-HYVPEITGDVSFSGPMTVEEFRFAKSLTGKPVKPVLPGPVTLLLLSKVRDYKDREELLDDLAPAYREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 164 ARELEAAGVDIIQFDEPAFNVFF-DEVNDWGIAALERAIEGLK-CETAVHICYGygikantdwkktlgsewrQYEEAFPK 241
Cdd:COG0620 160 LKALEAAGARWIQIDEPALAEDLpDEYLDWAVEAYNRAAAGVPdTKIHLHTCYG------------------GYEDILEA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 242 LQTSNIDIISLECHNSRvpMDLLELIR----GKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCGMAP- 316
Cdd:COG0620 222 LAALPVDGIHLEFVRSR--AGLLEPLKelpyDKVLGLGVIDGRNPWVEDPEEVAARIEEALKYVPPERLWVSPDCGLKHr 299
|
330 340
....*....|....*....|....*.
gi 754493210 317 ---LSRQVANGKLKALSAGAEIIRKE 339
Cdd:COG0620 300 pvdLTREEAWAKLRNMVAFAREVRGE 325
|
|
| PRK04326 |
PRK04326 |
methionine synthase; Provisional |
3-342 |
3.79e-77 |
|
methionine synthase; Provisional
Pssm-ID: 179825 [Multi-domain] Cd Length: 330 Bit Score: 239.88 E-value: 3.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 3 TLLPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDF 82
Cdd:PRK04326 7 PFLPTTVVGSYPKPKWLREAIRLHKAGKISEEDLHEAFDDAVRLVVKDHERAGVDIPVDGEMRREEMVEYFAERIEGFKF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 83 ENRQTVRIRNRYDAsvPTVVSAVARQKPVFVDDAKYLRQLT-DKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILN 161
Cdd:PRK04326 87 YGPVRVWGNNYFRK--PSVVGKIEYKEPMLVDEFEFAKSVTyTRPVKVPITGPYTIAEWSFNEYYKDKEELVFDLAKVIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 162 QEARELEAAGVDIIQFDEPAFNVFFDEVnDWGIAALERAIEGLKCETAVHICYGygikantdwkktlgsewrQYEEAFPK 241
Cdd:PRK04326 165 EEIKNLVEAGAKYIQIDEPALATHPEDV-EIAVEALNRIVKGINAKLGLHVCYG------------------DYSRIAPY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 242 LQTSNIDIISLECHNSRV-PMDLL-ELIRGKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTNCGMAPLSR 319
Cdd:PRK04326 226 ILEFPVDQFDLEFANGNYkLLDLLkEYGFDKELGLGVIDVHSARVESVEEIKEAIKKGLEYVPPEKLYINPDCGLKLLPR 305
|
330 340
....*....|....*....|...
gi 754493210 320 QVANGKLKALSAGAEIIRKELGA 342
Cdd:PRK04326 306 EIAYQKLVNMVKATREVREELDK 328
|
|
| PRK00957 |
PRK00957 |
methionine synthase; Provisional |
4-337 |
1.06e-41 |
|
methionine synthase; Provisional
Pssm-ID: 234875 [Multi-domain] Cd Length: 305 Bit Score: 147.44 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 4 LLPTSTAGSLPkpTWLAQPETLwsPWKLQDqelLAGKQDALRLSLDE----QIRAGIDIVSDGeQTRQHFVTTFIEHLSG 79
Cdd:PRK00957 1 IMITTVVGSYP--VVKGEPETL--KDKIKG---FFGLYDPYKPAIEEavadQVKAGIDIISDG-QVRGDMVEIFASNMPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 80 vdFENRqtvrirnrydasvpTVVSAV-ARQKPVFVDDAKYLRQLT-----DKPIKWALPGPMTMIDTLY-DAHYKSR--E 150
Cdd:PRK00957 73 --FDGK--------------RVIGRVePPAKPITLKDLKYAKKVAkkkdpNKGVKGIITGPSTLAYSLRvEPFYSDNkdE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 151 KLAWEFAKILNQEARELEAAGVDIIQFDEPAFNVFFDEVnDWGIAALERAIEGLKCETAVHICYGYGikantdwkktlgs 230
Cdd:PRK00957 137 ELIYDLARALRKEAEALEKAGVAMIQIDEPILSTGAYDL-EVAKKAIDIITKGLNVPVAMHVCGDVS------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 231 ewrqyeEAFPKLQTSNIDIISLECHNSRVPMDLLE--LIRGKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYP 308
Cdd:PRK00957 203 ------NIIDDLLKFNVDILDHEFASNKKNLEILEekDLIGKKIGFGCVDTKSKSVESVDEIKALIEEGIEILGAENILI 276
|
330 340
....*....|....*....|....*....
gi 754493210 309 STNCGMAPLSRQVANGKLKALSAGAEIIR 337
Cdd:PRK00957 277 DPDCGMRMLPRDVAFEKLKNMVEAAREIR 305
|
|
| Meth_synt_2 |
pfam01717 |
Cobalamin-independent synthase, Catalytic domain; This is a family of vitamin-B12 independent ... |
5-334 |
3.77e-35 |
|
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: 130.25 E-value: 3.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 5 LPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFEN 84
Cdd:pfam01717 1 FPTTTIGSFPQTAEIRAARVEFKKGEISLEEYELRIRGEIEDAVRRQERLGLDVLVHGEPERGDMVEYFGEALGGFAFTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 85 RQTVRIRNRYDASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQEA 164
Cdd:pfam01717 81 NGWVQSYGSRCVRPPIIYGDVSRPAPMTVKWSAYAQSTTDKPVKGMLTGPVTILNWSFVRDDQPRAAIAMQIALALRDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 165 RELEAAGVDIIQFDEPAFN-------VFFDEVNDWGIAA--LERAIEGLKCETAVHICYgygikantdwkktlgSEwrqY 235
Cdd:pfam01717 161 ADLEAAGIAVIQIDEPALReglplkkLDWAAYLDWAVAAfrLDTCGAADDTQIHTHMCY---------------SD---F 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 236 EEAFPKLQTSNIDIISLEchNSRVPMDLLELIR----GKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPSTN 311
Cdd:pfam01717 223 NDILSAIAALDADVITIE--ASRSDMELLEAFEewgyGRGIGPGVYDIHSPRVPSMEEIAALIVAALDVVPAERLWVNPD 300
|
330 340
....*....|....*....|...
gi 754493210 312 CGMAPLSRQVANGKLKALSAGAE 334
Cdd:pfam01717 301 CGLKTRGWEEARAALRNMVDAAK 323
|
|
| PRK01207 |
PRK01207 |
methionine synthase; Provisional |
3-340 |
3.23e-31 |
|
methionine synthase; Provisional
Pssm-ID: 100814 Cd Length: 343 Bit Score: 120.41 E-value: 3.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 3 TLLPTSTAGSLPKPTWLAQP-ETLWSPWKLQDqelLAGKqdALRLSLDEQIRAGIDIVS-DGEQTRQHFVTTFIEHLSGV 80
Cdd:PRK01207 2 AALITQEIGSFRKPEYLSREfHKIEGTDKFYE---LAER--ATLETLDVFENAGLDNIGiGGEMFRWEMYEHPAERIKGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 81 DFENrqTVR-IRNRYDASvPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKI 159
Cdd:PRK01207 77 IFYG--MVRsFDNRYYRK-GSIIDRMERRSSFHLDEVEFVADNTKKPIKVPITGPYTMMDWSFNDFYRDRYDLAMEFARI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 160 LNQEARELEAAGVDI-------IQFDEPAFNVFFDEVnDWGIAALERAIEGLKCETAVHICYgygikantdwkktlGSEW 232
Cdd:PRK01207 154 INEELKDIKSAWDRKspgrkleIQIDEPATTTHPDEM-DIVVDSINKSVYGIDNEFSIHVCY--------------SSDY 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 233 RQYEEAFPKLqtsNIDIISLECHNSrvpmDLLE-----------------------LIRGKKVMVGAIDVATNTVETPEE 289
Cdd:PRK01207 219 RLLYDRIPEL---NIDGYNLEYSNR----DTLEpgtsdekrpgfqdlkyfaehnesLQRKKFIGLGVTDVHIDYVEPVKL 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 754493210 290 VADTLRKALQFV-DADKLYPSTNCGMAPLSRQVANGKLKALSAGAEIIRKEL 340
Cdd:PRK01207 292 IEDRIRYALKIIkDPELVRLNPDCGLRTRSREIGEQKLRNMVAAKNNILKEL 343
|
|
| PLN02475 |
PLN02475 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase |
4-341 |
1.71e-25 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Pssm-ID: 215264 [Multi-domain] Cd Length: 766 Bit Score: 107.55 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 4 LLPTSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVDFE 83
Cdd:PLN02475 432 ILPTTTIGSFPQTVELRRVRREYKAKKISEEDYVKAIKEEIAKVVKLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFT 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 84 NRQTVRIRNRYDASVPTVVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMIDTLYDAHYKSREKLAWEFAKILNQE 163
Cdd:PLN02475 512 ANGWVQSYGSRCVKPPIIYGDVSRPKAMTVFWSSVAQSMTKRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDE 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 164 ARELEAAGVDIIQFDEPAFNVFF-------DEVNDWGIAALERAIEGLKCETAV--HICYgygikantdwkktlgSEWRQ 234
Cdd:PLN02475 592 VEDLEKAGITVIQIDEAALREGLplrksehAFYLDWAVHSFRITNCGVQDTTQIhtHMCY---------------SNFND 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 235 YEEAFPKLQTsniDIISLEchNSRVPMDLLELIR-----GKKVMVGAIDVATNTVETPEEVADTLRKALQFVDADKLYPS 309
Cdd:PLN02475 657 IIHSIIDMDA---DVITIE--NSRSDEKLLSVFRegvkyGAGIGPGVYDIHSPRIPSTEEIADRINKMLAVLESNILWVN 731
|
330 340 350
....*....|....*....|....*....|....
gi 754493210 310 TNCGMAplSRQVANGK--LKALSAGAEIIRKELG 341
Cdd:PLN02475 732 PDCGLK--TRKYPEVKpaLKNMVAAAKLLRAQLA 763
|
|
| CIMS_like |
cd03310 |
CIMS - Cobalamine-independent methonine synthase, or MetE. Many members have been ... |
6-335 |
1.99e-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: 78.62 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 6 PTSTAGSLPKPTWLAQPETLWspWKLQDQELLAGKQDALRLS--LDEQIRAGIDIVSDGEQTrQHFVTTFIEHLSGVDFE 83
Cdd:cd03310 1 LATGIGSYPLPDGVTKEWSIL--EKGAIEPEWPEEALFTALGsfFELQLEAGVEVPTYGQLG-DDMIGRFLEVLVDLETG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 84 NRQTVrirNRYDASVPtvvsaVARQKPVFVDDAKYLRQLTD-----KPIKWALPGPMTMIDTLYDAHYK--SREKLAWEF 156
Cdd:cd03310 78 TRFFD---NNFFYRPP-----EAKIEAFLPLELDYLEEVAEaykeaLKVKVVVTGPLTLALLAFLPNGEpdAYEDLAKSL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 157 AKILNQEARELEAAGVDIIQFDEPAF-----NVFFD-EVNDWGIAALERAIEGlkcETAVHICYGygikantdwkktlgs 230
Cdd:cd03310 150 AEFLREQVKELKNRGIVVVQIDEPSLgavgaGAFEDlEIVDAALEEVSLKSGG---DVEVHLCAP--------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 231 ewRQYEEAfpkLQTsNIDIISLECHNSRVPMD-----LLEL-IRGKKVMVGAIDVA---TNTVETPEEVAdTLRKALQFV 301
Cdd:cd03310 212 --LDYEAL---LEL-GVDVIGFDAAALPSKYLedlkkLLRIgVRTLILGLVVTDNEakgRNAWKEIERLE-KLVRRLEEP 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 754493210 302 DADK---LYPSTNCGMAPLSRQVANGKLKALSAGAEI 335
Cdd:cd03310 285 GEVLdeiLYLTPDCGLAFLPPQEARRKLALLAEAARE 321
|
|
| PRK05222 |
PRK05222 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional |
105-342 |
2.88e-13 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional
Pssm-ID: 235367 [Multi-domain] Cd Length: 758 Bit Score: 70.53 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 105 VARQKPVFVDDAKYLRQLTDKPIKWALPGPMTMidtlydahyksrekLAWEF--------------AKILNQEARELEAA 170
Cdd:PRK05222 528 VSRPEPMTVEWIKYAQSLTDKPVKGMLTGPVTI--------------LNWSFvrddqpreetarqiALAIRDEVLDLEAA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 171 GVDIIQFDEPAFNvffdEV-----NDWGiAALERAIE-------GLKCETAV--HICYgygikantdwkktlgSEWRQYE 236
Cdd:PRK05222 594 GIKIIQIDEPALR----EGlplrrSDWD-AYLDWAVEafrlatsGVKDETQIhtHMCY---------------SEFNDII 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 237 EAFPKLqtsNIDIISLEchNSRVPMDLLELIRGKK----VMVGAIDVATNTVETPEEVADTLRKALQFVDADKL--YPSt 310
Cdd:PRK05222 654 DAIAAL---DADVISIE--TSRSDMELLDAFEDFGypneIGPGVYDIHSPRVPSVEEIEELLRKALEVIPAERLwvNPD- 727
|
250 260 270
....*....|....*....|....*....|....
gi 754493210 311 nCGMAplSRQVANGK--LKALSAGAEIIRKELGA 342
Cdd:PRK05222 728 -CGLK--TRGWEETIaaLKNMVAAAKELRAELAA 758
|
|
| PRK08575 |
PRK08575 |
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional |
7-329 |
4.63e-10 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; Provisional
Pssm-ID: 236299 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 7 TSTAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQHFVTTFIEHLSGVD----- 81
Cdd:PRK08575 5 KALVGSYPRPVKLAKVISWYNSGKISKEKLEKAINENTKRFFELAKDVGIDYTTDGLFRWDDIFDPTISFISGVEkgglq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 82 --FEN----RQTV---RIRNRYDASVPTVVSAVARQKPVFVDDAKylrqltdkpIKWALPGPMTMIDTLYDAHYKSREKL 152
Cdd:PRK08575 85 rfYDNnfyyRQPVikeKINLKEENPYLQWLESAREIKEEVSLESK---------LKAVLPGPLTYAVLSDNEYYKNLIEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 153 AWEFAKILNQEARELEaAGVDIIQFDEPAFnvFFDEVNDWGIAALERA----IEGLKCEtaVHICYGYGIkANTDWKKTL 228
Cdd:PRK08575 156 MEDYASVVNSLIKELS-SVVDAVEIHEPSI--FAKGIKRDTLEKLPEVyktmAKNVNIE--KHLMTYFEI-NNLKRLDIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 229 GSEWRQYeeafpklqtSNIDIISLECHNSRVPmdllELIRGKKVMVGAIdvatNTVETPEEVADTLRKALQFV---DADK 305
Cdd:PRK08575 230 FSLPVTY---------FGIDVIENLKKLGRVY----TYLKGRKVYLGIL----NARNTKMEKISTIRRIVNKVkrkGVSD 292
|
330 340
....*....|....*....|....
gi 754493210 306 LYPSTNCGMAPLSRQVANGKLKAL 329
Cdd:PRK08575 293 IIVGNNTLFDFIPEVVAVKKLKLL 316
|
|
| URO-D_CIMS_like |
cd00465 |
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ... |
97-318 |
1.12e-07 |
|
The URO-D_CIMS_like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases, as well as cobalamine (B12) independent methionine synthases. Despite their sequence similarities, members of this family have clearly different functions. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane, and methionine synthases transfer a methyl group from a folate cofactor to L-homocysteine in a reaction requiring zinc.
Pssm-ID: 238261 [Multi-domain] Cd Length: 306 Bit Score: 52.50 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 97 SVPT-VVSAVARQKPVFVDDAKYLRQLTDKPIKWALPGPMTM----------IDTLYDAHYKSREkLAWEFAKILNQEAR 165
Cdd:cd00465 73 SVPEiDEEEDPFREAPALEHITAVRSLEEFPTAGAAGGPFTFthhsmsmgdaLMALYERPEAMHE-LIEYLTEFILEYAK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 166 ELEAAGVDIIQFDEPAF---NVFF--DEVNDWGIAALERAIEGLKC-ETAVHICYGYgikantDWkktlgsewrqyEEAF 239
Cdd:cd00465 152 TLIEAGAKALQIHEPAFsqiNSFLgpKMFKKFALPAYKKVAEYKAAgEVPIVHHSCY------DA-----------ADLL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 240 PKLQTSNIDIISLEcHNSRVPMDLLELIRGKKVMVGAIDvatnTVETPEEVADTLRKALQFVDA-DKLY-PSTNCGMAPL 317
Cdd:cd00465 215 EEMIQLGVDVISFD-MTVNEPKEAIEKVGEKKTLVGGVD----PGYLPATDEECIAKVEELVERlGPHYiINPDCGLGPD 289
|
.
gi 754493210 318 S 318
Cdd:cd00465 290 S 290
|
|
| PRK06520 |
PRK06520 |
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; |
9-315 |
1.80e-05 |
|
5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase;
Pssm-ID: 180601 Cd Length: 368 Bit Score: 45.87 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 9 TAGSLPKPTWLAQPETLWSPWKLQDQELLAGKQDALRLSLDEQIRAGIDIVSDGEQTRQ--HFvtTFIEHLSGVD-FENR 85
Cdd:PRK06520 12 VVGSFLRPAAIKQARQQFAAGEIDAAALRKIEDMEIRKVVEKQRACGLKVVTDGEFRRAwwHF--DFFDGLQGVErYEAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 86 QTVR---IRNRYDASVPTVVSAVARQKPVfVDDAKYLRQLTDKPI-KWALPGPMTM--------ID-TLY---DAHYKsr 149
Cdd:PRK06520 90 QGIQfngVQTKARGVRVTGKLDFPDDHPM-LEDFRFLKSISGDATpKMTIPSPSVLhfrggrkaIDaTVYpdlDDYFD-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 150 eklawEFAKILNQEARELEAAGVDIIQFDEP--AFNVFFDE---VNDWG--------IAA--LERAIEGLKCETAV--HI 212
Cdd:PRK06520 167 -----DLAKTWRDAIKAFYDAGCRYLQLDDTvwAYLCSDDQrqqIRERGddpdelarIYArvLNKALAGKPADLTIglHV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 213 CYGygikantDWKKTLGSEwRQYEE-AFPKLQTSNIDIISLECHNSRV----PMDLLEliRGKKVMV-GAIDVATNTVET 286
Cdd:PRK06520 242 CRG-------NFRSTWISE-GGYEPvAETLFGGVNVDAFFLEYDNERAggfePLRFIP--PGHQQVVlGLITTKNGELEN 311
|
330 340
....*....|....*....|....*....
gi 754493210 287 PEEVADTLRKALQFVDADKLYPSTNCGMA 315
Cdd:PRK06520 312 ADDVKARLAEAAKFVPLEQLCLSPQCGFA 340
|
|
| Mta_CmuA_like |
cd03307 |
MtaA_CmuA_like family. MtaA/CmuA, also MtsA, or methyltransferase 2 (MT2) MT2-A and MT2-M ... |
164-329 |
1.83e-04 |
|
MtaA_CmuA_like family. MtaA/CmuA, also MtsA, or methyltransferase 2 (MT2) MT2-A and MT2-M isozymes, are methylcobamide:Coenzyme M methyltransferases, which play a role in metabolic pathways of methane formation from various substrates, such as methylated amines and methanol. Coenzyme M, 2-mercaptoethylsulfonate or CoM, is methylated during methanogenesis in a reaction catalyzed by three proteins. A methyltransferase methylates the corrinoid cofactor, which is bound to a second polypeptide, a corrinoid protein. The methylated corrinoid protein then serves as a substrate for MT2-A and related enzymes, which methylate CoM.
Pssm-ID: 239423 Cd Length: 326 Bit Score: 42.66 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 164 ARELEAAGVDIIQFDEPAFN------VFFDEVndwGIAALERAIEGLK-CETAVHICygygikANTDwkktlgsewrqye 236
Cdd:cd03307 177 AKAQLEAGADIITIADPTASpelispEFYEEF---ALPYHKKIVKELHgCPTILHIC------GNTT------------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754493210 237 EAFPKLQTSNIDIISLEchnSRVPM-DLLELIRGKKVMVGAID-VATNTVETPEEVADTLRKALQFvDADKLYPStnCGM 314
Cdd:cd03307 235 PILEYIAQCGFDGISVD---EKVDVkTAKEIVGGRAALIGNVSpSQTLLNGTPEDVKAEARKCLED-GVDILAPG--CGI 308
|
170
....*....|....*
gi 754493210 315 APLSrqvANGKLKAL 329
Cdd:cd03307 309 APRT---PLANLKAM 320
|
|
| |
