|
Name |
Accession |
Description |
Interval |
E-value |
| cysG |
PRK10637 |
siroheme synthase CysG; |
1-457 |
0e+00 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 984.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 1 MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80
Cdd:PRK10637 1 MDHLPIFCQLRDRDCLLVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 81 DDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQ 160
Cdd:PRK10637 81 DDDAVNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAITETTEQLINEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240
Cdd:PRK10637 161 LRGRVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320
Cdd:PRK10637 241 QADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMP 400
Cdd:PRK10637 321 GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHLKTGGELDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMP 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446272000 401 GEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMNSPSLIIIGRVVGLRDKLNWFSNH 457
Cdd:PRK10637 401 ADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNSPSLIIVGRVVGLRDKLNWFSNH 457
|
|
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
215-456 |
5.17e-144 |
|
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; Uroporphyrinogen-III methylase (siroheme synthase) is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 439778 [Multi-domain] Cd Length: 245 Bit Score: 411.39 E-value: 5.17e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGK 294
Cdd:COG0007 1 KGKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 295 RVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGG-ELDWENLAA 373
Cdd:COG0007 81 RVVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKlDLDWAALAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 374 EKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVVGLRDKL 451
Cdd:COG0007 161 PGGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGlkSPALIVVGEVVALREKL 240
|
....*
gi 446272000 452 NWFSN 456
Cdd:COG0007 241 SWFEA 245
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
221-445 |
4.31e-127 |
|
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen III methyltransferase, SUMT); SUMT is an enzyme of the cobalamin and siroheme biosynthetic pathway. It catalyzes the first of three steps leading to the formation of siroheme from uroporphyrinogen III; it transfers two methyl groups from S-adenosyl-L-methionine to the C-2 and C-7 atoms of uroporphyrinogen III to yield precorrin-2 via the intermediate formation of precorrin-1. Precorrin-2 is also a precursor for the biosynthesis of vitamin B12, coenzyme F430, siroheme and heme d1. This family includes proteins in which the SUMT domain is fused to other functional domains, such as to a uroporphyrinogen-III synthase domain to form bifunctional uroporphyrinogen-III methylase/uroporphyrinogen-III synthase, or to a dual function dehydrogenase-chelatase domain, as in the case of the multifunctional S-adenosyl-L-methionine (SAM)-dependent bismethyltransferase/dehydrogenase/ferrochelatase CysG, which catalyzes all three steps that transform uroporphyrinogen III into siroheme.
Pssm-ID: 381169 Cd Length: 228 Bit Score: 367.53 E-value: 4.31e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 221 VGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVVRLK 300
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 301 GGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGGELD-WENLAAEKQTLV 379
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDdDAALARPGGTLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272000 380 FYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVV 445
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGirSPALIVVGEVV 228
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
216-454 |
2.95e-122 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 356.06 E-value: 2.95e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKR 295
Cdd:PRK06136 3 GKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKGKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGG---ELDWENLA 372
Cdd:PRK06136 83 VVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKlepEVNWSALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 373 AEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVVGLRDK 450
Cdd:PRK06136 163 DGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDiqSPAIIVIGEVVALRAK 242
|
....
gi 446272000 451 LNWF 454
Cdd:PRK06136 243 LAWF 246
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
218-448 |
1.76e-114 |
|
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with uroporphyrin-III C-methyltransferase activity. This enzyme catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). Cobalamin contains cobalt while siroheme contains iron. Siroheme is a cofactor for nitrite and sulfite reductases and therefore plays a role in cysteine biosynthesis; many members of this family are CysG, siroheme synthase, with an additional N-terminal domain and with additional oxidation and iron insertion activities. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273643 Cd Length: 236 Bit Score: 335.73 E-value: 1.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKRVV 297
Cdd:TIGR01469 2 VYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 298 RLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGG--ELDWENLAAEK 375
Cdd:TIGR01469 82 RLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKalEVDWEALAKGA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272000 376 QTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVVGLR 448
Cdd:TIGR01469 162 GTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANlkSPALIVIGEVVALR 236
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
212-457 |
3.65e-101 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 303.09 E-value: 3.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 212 LDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQ 291
Cdd:PLN02625 11 LEGPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 292 KGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTGGE---LDW 368
Cdd:PLN02625 91 AGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTdplDVA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 369 ENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVVG 446
Cdd:PLN02625 171 EAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGlvSPTVIVVGEVVA 250
|
250
....*....|.
gi 446272000 447 LRDKLNWFSNH 457
Cdd:PLN02625 251 LSPLWPWAAEE 261
|
|
| CysG2 |
COG1648 |
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ... |
1-212 |
5.78e-95 |
|
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 441254 [Multi-domain] Cd Length: 211 Bit Score: 285.12 E-value: 5.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 1 MDHLPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAAT 80
Cdd:COG1648 1 MDYFPIFLDLEGRRVLVVGGGEVAARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 81 DDDALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQ 160
Cdd:COG1648 81 DDEEVNARVAAAARARGILVNVVDDPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446272000 161 LRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAITETTEQLINEPL 212
Cdd:COG1648 161 LRERVKARLPDGAERRRFWERLL-DGPLAELLRAGDEEEAEALLEELLAEAA 211
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
216-453 |
1.15e-72 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 236.81 E-value: 1.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEEINQILLREAQKGKR 295
Cdd:PRK07168 3 GYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKtgGEL----DWENL 371
Cdd:PRK07168 83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAK--GPLtdhgKYNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 372 aAEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVVGLRD 449
Cdd:PRK07168 161 -HNSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENisNPSMTIVGDVVSLRN 239
|
....
gi 446272000 450 KLNW 453
Cdd:PRK07168 240 QIAW 243
|
|
| cysG_Nterm |
TIGR01470 |
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ... |
4-207 |
3.26e-72 |
|
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal region-related sequences. All sequences in the seed alignment for this model are N-terminal regions of known or predicted siroheme synthases. The C-terminal region of each is uroporphyrin-III C-methyltransferase (EC 2.1.1.107), which catalyzes the first step committed to the biosynthesis of either siroheme or cobalamin (vitamin B12) rather than protoheme (heme). The region represented by this model completes the process of oxidation and iron insertion to yield siroheme. Siroheme is a cofactor for nitrite and sulfite reductases, so siroheme synthase is CysG of cysteine biosynthesis in some organisms. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 130536 [Multi-domain] Cd Length: 205 Bit Score: 226.52 E-value: 3.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 4 LPIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAATDDD 83
Cdd:TIGR01470 1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 84 ALNQRVSEAAEARRIFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAKYAGQLRG 163
Cdd:TIGR01470 81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446272000 164 RVKQQFATMGERRRFWEKLFVNDRLAQSLANNDQKAITETTEQL 207
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAGREEQAERVLATRL 204
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
218-426 |
8.90e-52 |
|
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function. This family includes the methylase Dipthine synthase.
Pssm-ID: 425769 [Multi-domain] Cd Length: 209 Bit Score: 173.68 E-value: 8.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVYDR-LVSDDIMNLVRRDADRVFvGKRAGYHCVPQEEINQILLREAQKGKRV 296
Cdd:pfam00590 2 LYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLYFPM-TEDKEPLEEAYEEIAEALAAALRAGKDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVrLITGHLKTGGELDWENLAAEKQ 376
Cdd:pfam00590 81 ARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSV-LFLPGLARIELRLLEALLANGD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446272000 377 TLVFYMGLNQAATIQQKLIEHGmPGEMPVAIVENGTAVTQRVIDGTLTQL 426
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELY-PDTTPVAVVERAGTPDEKVVRGTLGEL 208
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
221-446 |
1.34e-49 |
|
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. In the aerobic pathway, CobM catalyzes the methylation of precorrin-4 at C-11 to yield precorrin-5. In the anaerobic pathway, CibF catalyzes the methylation of cobalt-precorrin-4 to cobalt-precorrin-5. Both CibF and CobM, which are homologous, are included in this model. There are about 30 enzymes involved in vitamin B12 synthetic pathway. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared in both pathways and several of these enzymes are pathway-specific.
Pssm-ID: 381168 [Multi-domain] Cd Length: 225 Bit Score: 168.34 E-value: 1.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 221 VGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNLVRRDADRVfvgKRAGyhcVPQEEINQILLREAQKGKRVVRL 299
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIV---DSAG---MTLEEIIEVMREAAREGKDVVRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 300 KGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKTG---GElDWENLAAEKQ 376
Cdd:cd11641 75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTPvpeGE-SLRELAKHGA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272000 377 TLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTltqLGELAQQM-----NSPSLIIIGRVVG 446
Cdd:cd11641 154 TLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGT---LADLAEKVkeagiTRTALILVGPALG 225
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
218-449 |
3.66e-45 |
|
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-3B C17-methyltransferase, EC 2.1.1.131). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 200107 Cd Length: 247 Bit Score: 157.49 E-value: 3.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNLVRRDADrvfVGKRAGYHCvpqEEINQILLREAQKGKRV 296
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAE---VVNSAGMSL---EEIVDIMSDAHREGKDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 297 VRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKT---GGElDWENLAA 373
Cdd:TIGR01465 75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTpmpEGE-KLADLAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272000 374 EKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMN--SPSLIIIGRVVGLRD 449
Cdd:TIGR01465 154 HGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGiyRTTLILVGPALDPRI 231
|
|
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
215-446 |
7.91e-45 |
|
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 442122 [Multi-domain] Cd Length: 256 Bit Score: 156.76 E-value: 7.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNLVRRDADRVfvgKRAGYHcvpQEEINQILLREAQKG 293
Cdd:COG2875 2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIV---DSASMT---LEEIIALMKEAAAEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 294 KRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLKT---GGElDWEN 370
Cdd:COG2875 76 KDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTpmpEGE-SLAS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272000 371 LAAEKQTLVFYMGLNQAATIQQKLIEHgMPGEMPVAIVENGTAVTQRVIDGTLTQLGEL--AQQMNSPSLIIIGRVVG 446
Cdd:COG2875 155 LAAHGATLAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRGTLADIAEKvkEAGITRTALILVGPALG 231
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
221-442 |
3.54e-36 |
|
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.
Pssm-ID: 381167 [Multi-domain] Cd Length: 219 Bit Score: 132.90 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 221 VGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSddimnlvRRDADRVFVGKRAGYHCVP------QEEINQILLREAQKGK 294
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDS-------KLLSLVLRAILKDGKRIYDlhdpnvEEEMAELLLEEARQGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 295 RVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLthrdyAQSVRLITGHLKTGGE--LDWENLA 372
Cdd:cd09815 74 DVAFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASDLLENPrlLVLKALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446272000 373 AEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGEL-AQQMNSPSLIIIG 442
Cdd:cd09815 149 KERRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAErTERGKPLTTILVG 219
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
6-115 |
4.56e-34 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 123.36 E-value: 4.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 6 IFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVnalafIPQFTAWADAGMLTLVEGPFDESLLDTcWLAIAATDDDAL 85
Cdd:pfam13241 1 LFLDLRGKRVLVVGGGEVAARKARKLLEAGAKVTV-----VSPEITPFLEGLLDLIRREFEGDLDGA-DLVIAATDDPEL 74
|
90 100 110
....*....|....*....|....*....|
gi 446272000 86 NQRVSEAAEARRIFCNVVDAPKAASFIMPS 115
Cdd:pfam13241 75 NERIAALARARGILVNVADDPELCDFYFPA 104
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
217-446 |
9.11e-33 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 124.87 E-value: 9.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 217 EVVLVGAGPGDAGLLTLKGLQQIQQADVVVY-DRLVSDDIMNLVRRDADRvfvGKRAGYHCvpqEEINQILLREAQKGKR 295
Cdd:PRK15473 9 CVWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAEC---HDSAELHL---EQIIDLMEAGVKAGKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 296 VVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVrLIT---GHLKTGGELDWENLA 372
Cdd:PRK15473 83 VVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSL-IITrmeGRTPVPAREQLESFA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446272000 373 AEKQTLVFYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQ--MNSPSLIIIGRVVG 446
Cdd:PRK15473 162 SHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDagIRKTALILVGNFLG 237
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
220-442 |
1.65e-31 |
|
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily use S-AdoMet (S-adenosyl-L-methionine or SAM) in the methylation of diverse substrates. Most members catalyze various methylation steps in cobalamin (vitamin B12) biosynthesis. There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. The enzymes involved in the aerobic pathway are prefixed Cob and those of the anaerobic pathway Cbi. Most of the enzymes are shared by both pathways and a few enzymes are pathway-specific. Diphthine synthase and Ribosomal RNA small subunit methyltransferase I (RsmI) are two superfamily members that are not involved in cobalamin biosynthesis. Diphthine synthase participates in the posttranslational modification of a specific histidine residue in elongation factor 2 (EF-2) of eukaryotes and archaea to diphthamide. RsmI catalyzes the 2-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA. Other superfamily members not involved in cobalamin biosynthesis include the N-terminal tetrapyrrole methylase domain of Bacillus subtilis YabN whose specific function is unknown, and Omphalotus olearius omphalotin methyltransferase which catalyzes the automethylation of its own C-terminus; this C terminus is subsequently released and macrocyclized to give Omphalotin A, a potent nematicide.
Pssm-ID: 381178 [Multi-domain] Cd Length: 243 Bit Score: 120.74 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 220 LVGAGPGDAGLLTLKGLQQIQQADVVVY-------------DRLVSDD----IMNLVRRDADRVFVGKRAGYHCVPQEEI 282
Cdd:cd11724 4 LVGVGPGDPDLITLRALKAIKKADVVFAppdlrkrfaeylaGKEVLDDphglFTYYGKKCSPLEEAEKECEELEKQRAEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 283 NQIlLREA-QKGKRVVRLKGGDPFIFGRGGEELETLcnAGIPFSVVPGITAASGCSAYSGIPLTHRDYAQSVRLITGHLK 361
Cdd:cd11724 84 VQK-IREAlAQGKNVALLDSGDPTIYGPWIWYLEEF--ADLNPEVIPGVSSFNAANAALKRSLTGGGDSRSVILTAPFAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 362 TGGELDWENLAAEKQTLVFYMGLNQAATIQQKLiEHGMPGEMPVAIVEN-GTAVTQRVIDGTLTQLGELAQQMNSP--SL 438
Cdd:cd11724 161 KENEDLLEDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIVYHaGYSEKEKVIRGTLDDILEKLGGEKEPflGL 239
|
....
gi 446272000 439 IIIG 442
Cdd:cd11724 240 IYVG 243
|
|
| CobJ |
COG1010 |
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
215-442 |
1.74e-20 |
|
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440634 Cd Length: 250 Bit Score: 90.51 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADVVV----YDRLVSDDIMNLVRRD------ADRVfvgKRAgyhcvpqeeinq 284
Cdd:COG1010 3 RGKLYVVGLGPGSAELMTPRARAALAEADVVVgygtYLDLIPPLLPGKEVHAsgmreeVERA---REA------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 285 ilLREAQKGKRVVRLKGGDPFIFGRGG---EELETLCNA-GIPFSVVPGITAASGCSAYSGIPLTHrDYAqSVRLiTGHL 360
Cdd:COG1010 68 --LELAAEGKTVAVVSSGDPGVYGMAGlvlEVLEEGGAWrDVEVEVVPGITAAQAAAARLGAPLGH-DFC-VISL-SDLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 361 KtggelDWE------NLAAEKQ-TLVFYmglN--------QAATIQQKLIEHGmPGEMPVAIVENGTAVTQRVidgTLTQ 425
Cdd:COG1010 143 T-----PWEviekrlRAAAEADfVIALY---NprsrkrpwQLERALEILLEHR-PPDTPVGIVRNAGRPDESV---TVTT 210
|
250 260
....*....|....*....|
gi 446272000 426 LGELAQQ---MNspSLIIIG 442
Cdd:COG1010 211 LGELDPEevdML--TTVIIG 228
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
216-441 |
5.73e-20 |
|
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441844 [Multi-domain] Cd Length: 229 Bit Score: 88.23 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADVVVY---------------DRLVSD-DIMNL---VRRDADRvfvgKRAGYHc 276
Cdd:COG2243 3 GKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslareivAPYLPPaRIVELvfpMTTDYEA----LVAAWD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 277 vpqEEINQILlREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLI 356
Cdd:COG2243 78 ---EAAARIA-EELEAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEGD--EPLTVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 357 TGhlkTGGELDWENLAAEKQTLVFyMGLNQA-ATIQQKLIEHGMPGEmpVAIVENGTAVTQRVIDGtltqLGELAQQmNS 435
Cdd:COG2243 152 PG---TLLEEELERALDDFDTVVI-MKVGRNfPKVREALEEAGLLDR--AWYVERAGMPDERIVPG----LAEVDIE-EA 220
|
....*...
gi 446272000 436 P--SLIII 441
Cdd:COG2243 221 PyfSLILV 228
|
|
| Precorrin_3B_C17_MT |
cd11646 |
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
220-442 |
1.81e-19 |
|
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. This model includes CobJ of the aerobic pathway and CbiH of the anaerobic pathway, both as stand-alone enzymes and when CobJ or CbiH form part of bifunctional enzymes, such as in Mycobacterium tuberculosis CobIJ where CobJ fuses with a precorrin-2 C(20)-methyltransferase domain, or Bacillus megaterium CbiH60, where CbiH is fused to a nitrite and sulfite reductase-like domain. In the aerobic pathway, once CobG has generated precorrin-3b, CobJ catalyzes the methylation of precorrin-3b at C-17 to form precorrin-4 (the extruded methylated C-20 fragment is left attached as an acyl group at C-1). In the corresponding anaerobic pathway, CbiH carries out this ring contraction, using cobalt-precorrin-3b as a substrate to generate a tetramethylated delta-lactone.
Pssm-ID: 381173 [Multi-domain] Cd Length: 238 Bit Score: 87.09 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 220 LVGAGPGDAGLLTLKGLQQIQQADVVV----YDRLVSDDI---------MnlvRRDADRVfvgKRAgyhcvpqeeinqil 286
Cdd:cd11646 3 VVGIGPGSADLMTPRAREALEEADVIVgyktYLDLIEDLLpgkevissgM---GEEVERA---REA-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 287 LREAQKGKRVVRLKGGDPFIFGRGGEELETLC--NAGIPFSVVPGITAASGCSAYSGIPLTHrDYAqsvrLIT--GHLKt 362
Cdd:cd11646 63 LELALEGKRVALVSSGDPGIYGMAGLVLELLDerWDDIEVEVVPGITAALAAAALLGAPLGH-DFA----VISlsDLLT- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 363 ggelDWE------NLAAEKQ-TLVFY--------MGLNQAATIqqkLIEHgMPGEMPVAIVENGTAVTQRVidgTLTQLG 427
Cdd:cd11646 137 ----PWEviekrlRAAAEADfVIALYnprskkrpWQLEKALEI---LLEH-RPPDTPVGIVRNAGREGEEV---TITTLG 205
|
250
....*....|....*.
gi 446272000 428 EL-AQQMNSPSLIIIG 442
Cdd:cd11646 206 ELdPEDVDMFTTVIIG 221
|
|
| PRK06718 |
PRK06718 |
NAD(P)-binding protein; |
5-148 |
3.34e-19 |
|
NAD(P)-binding protein;
Pssm-ID: 180667 [Multi-domain] Cd Length: 202 Bit Score: 85.47 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 5 PIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNAlafiPQFTA----WADAGMLTLVEGPFDESLLDTCWLAIAAT 80
Cdd:PRK06718 3 PLMIDLSNKRVVIVGGGKVAGRRAITLLKYGAHIVVIS----PELTEnlvkLVEEGKIRWKQKEFEPSDIVDAFLVIAAT 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272000 81 DDDALNQRVSEAAEARRIFcNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLP 148
Cdd:PRK06718 79 NDPRVNEQVKEDLPENALF-NVITDAESGNVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYD 145
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
221-441 |
8.44e-19 |
|
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase (also known as S-adenosyl-L-methionine--precorrin-2 methyltransferase) participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. Precorrin-2 C20-methyltransferase catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 using S-adenosylmethionine as a methyl group source to produce precorrin-3A. In the anaerobic pathway, cobalt is inserted into precorrin-2 by CbiK to generate cobalt-precorrin-2, which is the substrate for CbiL, a C20 methyltransferase. In Clostridium difficile, CbiK and CbiL are fused into a bifunctional enzyme. In the aerobic pathway, the precorrin-2 C20-methyltransferase is named CobI. This family includes CbiL and CobI precorrin-2 C20-methyltransferases, both as stand-alone enzymes and when CbiL forms part of a bifunctional enzyme.
Pssm-ID: 381172 [Multi-domain] Cd Length: 223 Bit Score: 84.87 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 221 VGAGPGDAGLLTLKGLQQIQQADVVVY-------DRLVSDDIMNLVRRDADRVFV--------GKRAGYHcvpqEEINQI 285
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggeGSAALIIAAALLIPDKEIIPLefpmtkdrEELEEAW----DEAAEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 286 LLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLITGhlkTGGE 365
Cdd:cd11645 77 IAEELKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPA---TYDE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446272000 366 LDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEmpVAIVENGTAVTQRVIDGTLTQLGElaqqmNSP--SLIII 441
Cdd:cd11645 152 EELEKALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYTDLEELKEE-----KLPyfSLIIV 222
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
215-442 |
1.49e-16 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 79.06 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADVVV----YDRLVSDDImnlvrrDADRVFVGKRagyhcvpQEEI--NQILLR 288
Cdd:PRK05765 1 MGKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIgyntYLRLISDLL------DGKEVIGARM-------KEEIfrANTAIE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 289 EAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIP--FSVVPGITAASGCSAYSGIPLThRDYAqSVRL---------IT 357
Cdd:PRK05765 68 KALEGNIVALVSSGDPQVYGMAGLVFELISRRKLDvdVEVIPGVTAALAAAARLGSPLS-LDFV-VISLsdllipreeIL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 358 GHLKTGGELDWenlaaekqTLVFYMGLNQAATIQ-QKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMNSP 436
Cdd:PRK05765 146 HRVTKAAEADF--------VIVFYNPINENLLIEvMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEHMDEIGMT 217
|
....*.
gi 446272000 437 SLIIIG 442
Cdd:PRK05765 218 TTMIIG 223
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
218-442 |
1.88e-16 |
|
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273641 [Multi-domain] Cd Length: 239 Bit Score: 78.50 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVV----YDRLVSDdimnlVRRDADRVFVGKRagyhcvpqEEIN--QILLREAQ 291
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIVgyktYLDLIED-----LIPGKEVVTSGMR--------EEIAraELAIELAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 292 KGKRVVRLKGGDPFIFGRGGEELETL--CNAGIPFSVVPGITAASGCSAYSGIPLTHrDYAqSVRLiTGHLKTggeldWE 369
Cdd:TIGR01466 68 EGRTVALVSSGDPGIYGMAALVFEALekKGAEVDIEVIPGITAASAAASLLGAPLGH-DFC-VISL-SDLLTP-----WP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 370 ------NLAAEKQ-TLVFYMGLNQAATIQ----QKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQLGELAQQMNspSL 438
Cdd:TIGR01466 140 eiekrlRAAAEADfVIAIYNPRSKRRPEQfrraMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAELDEELIDML--TT 217
|
....
gi 446272000 439 IIIG 442
Cdd:TIGR01466 218 VIIG 221
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
221-441 |
2.15e-16 |
|
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also known as cobalt-precorrin-7 C(5)-methyltransferase, also known as cobalt-precorrin-6Y C(5)-methyltransferase) catalyzes the methylation of C-5 in cobalt-precorrin-7 to form cobalt-precorrin-8. It participates in the pathway toward the biosynthesis of cobalamin (vitamin B12). There are two distinct cobalamin biosynthetic pathways in bacteria. The aerobic pathway requires oxygen, and cobalt is inserted late in the pathway; the anaerobic pathway does not require oxygen, and cobalt insertion is the first committed step towards cobalamin synthesis. CbiE functions in the anaerobic pathway, it is a subunit of precorrin-6Y C5,15-methyltransferase, a bifunctional enzyme: cobalt-precorrin-7 C(5)-methyltransferase (CbiE)/cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (CbiT), that catalyzes two methylations (at C-5 and C-15) in precorrin-6Y, as well as the decarboxylation of the acetate side chain located in ring C, in order to generate precorrin-8X. CbiE and CbiT can be found fused (CbiET, also called CobL), or on separate protein chains (CbiE and CbiT). In the aerobic pathway, a single enzyme called CobL catalyzes the methylations at C-5 and C-15, and the decarboxylation of the C-12 acetate side chain of precorrin-6B.
Pssm-ID: 381171 [Multi-domain] Cd Length: 198 Bit Score: 77.15 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 221 VGAGPGDAGLLTLKGLQQIQQADVVV-YDRLVsddimNLVRRDADRVFVgkragyhcVPQEEINQILLREAQKGKRVVRL 299
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVIgAKRLL-----ELFPDLGAEKIP--------LPSEDIAELLEEIAEAGKRVVVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 300 KGGDPFIFGRGGEELETLcnAGIPFSVVPGITAASGCSAYSGIPLthrdyaQSVRLITGHLKTGGELDWEnLAAEKQTLV 379
Cdd:cd11644 68 ASGDPGFYGIGKTLLRRL--GGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLHGRDLENLRRA-LRRGRKVFV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446272000 380 FYMGLNQAATIQQKLIEHGMpGEMPVAIVENGTAVTQRVIDGTLTQLgeLAQQMNSPSLIII 441
Cdd:cd11644 139 LTDGKNTPAEIARLLLERGL-GDSRVTVGENLGYPDERITEGTAEEL--AEEEFSDLNVVLI 197
|
|
| PRK06719 |
PRK06719 |
precorrin-2 dehydrogenase; Validated |
5-156 |
2.00e-15 |
|
precorrin-2 dehydrogenase; Validated
Pssm-ID: 180668 [Multi-domain] Cd Length: 157 Bit Score: 73.46 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 5 PIFCQLRDRDCLIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTawaDAGMLTLVEGPFDESLLDTCWLAIAATDDDA 84
Cdd:PRK06719 6 PLMFNLHNKVVVIIGGGKIAYRKASGLKDTGAFVTVVSPEICKEMK---ELPYITWKQKTFSNDDIKDAHLIYAATNQHA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446272000 85 LNQRVSEAAEARRiFCNVVDAPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPLHLGQVAK 156
Cdd:PRK06719 83 VNMMVKQAAHDFQ-WVNVVSDGTESSFHTPGVIRNDEYVVTISTSGKDPSFTKRLKQELTSILPKLIKKISR 153
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
221-421 |
2.79e-15 |
|
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, one of several closely related S-adenosylmethionine-dependent methyltransferases involved in cobalamin (vitamin B12) biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273642 [Multi-domain] Cd Length: 230 Bit Score: 75.04 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 221 VGAGPGDAGLLTLKGLQQIQQADVVVYDR-----------LVSDDIMNLVRRDADRVF-VGKRAGYHCVPQEEINQILLR 288
Cdd:TIGR01467 6 VGVGPGDPELITVKALEALRSADVIAVPAskkgreslarkIVEDYLKPNDTRILELVFpMTKDRDELEKAWDEAAEAVAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 289 EAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLITGhlkTGGELDW 368
Cdd:TIGR01467 86 ELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGD--ESLAILPA---TAGEAEL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446272000 369 ENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPGEmpVAIVENGTAVTQRVIDG 421
Cdd:TIGR01467 161 EKALAEFDTVVLMKVGRNLPQIKEALAKLGRLDA--AVVVERATMPDEKIVDL 211
|
|
| CbiE |
TIGR02467 |
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ... |
220-426 |
4.38e-15 |
|
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes the CbiE methylase which is responsible, in part (along with CbiT), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiT subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL.
Pssm-ID: 274146 [Multi-domain] Cd Length: 204 Bit Score: 73.89 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 220 LVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKragyhcvPQEEINQiLLREAQKGKRVVRL 299
Cdd:TIGR02467 1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIILTYK-------DLDELLE-FIAATRKEKRVVVL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 300 KGGDPFIFGRGGEELETLCNAGIpfSVVPGITAASGCSAYSGIPLthrdyaQSVRLITGHLKTGGELDWENLAAEKQTLV 379
Cdd:TIGR02467 73 ASGDPLFYGIGRTLAERLGKERL--EIIPGISSVQYAFARLGLPW------QDAVVISLHGRELDELLLALLRGHRKVAV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446272000 380 FYMGLNQAATIQQKLIEHGMPGEMPVAIVENGTAVTQRVIDGTLTQL 426
Cdd:TIGR02467 145 LTDPRNGPAEIARELIELGIGGSYELTVGENLGYEDERITEGTLEEI 191
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
218-410 |
3.59e-13 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 68.36 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRagyhcvpqEEINQilLREAQKGKRVV 297
Cdd:PRK05787 2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGLR--------DLLEW--LELAAKGKNVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 298 RLKGGDPFIFGRGGEELEtLCNAGIPFSVVPGITAASGCSAYSGIPLTHrdyaqsVRLITGHLKTGGELDWENLAAEKQT 377
Cdd:PRK05787 72 VLSTGDPLFSGLGKLLKV-RRAVAEDVEVIPGISSVQYAAARLGIDMND------VVFTTSHGRGPNFEELEDLLKNGRK 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 446272000 378 LVF----YMGLNQAAtiqQKLIEHGMPgEMPVAIVEN 410
Cdd:PRK05787 145 VIMlpdpRFGPKEIA---AELLERGKL-ERRIVVGEN 177
|
|
| CysG_dimerizer |
pfam10414 |
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ... |
152-208 |
9.18e-13 |
|
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the iron-containing porphinoid sirohaem. CysG, S-adenosyl-L-methionine (SAM)-dependent bis-methyltransferase, dehydrogenase and ferrochelatase, synthesizes sirohaem from uroporphyrinogen III via reactions which encompass two branchpoint intermediates in tetrapyrrole biosynthesis, diverting flux first from protoporphyrin IX biosynthesis and then from cobalamin (vitamin B12) biosynthesis. CysG is a dimer of two structurally similar protomers held together asymmetrically through a number of salt-bridges across complementary residues in the CysG_dimerizer region to produce a series of active sites, accounting for CysG's multifunctionality, catalysing four diverse reactions: two SAM-dependent methylations, NAD+-dependent tetrapyrrole dehydrogenation and metal chelation. The CysG_dimerizer region holding the two protomers together is of 74 residues.
Pssm-ID: 431269 [Multi-domain] Cd Length: 56 Bit Score: 62.57 E-value: 9.18e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446272000 152 GQVAKYAGQLRGRVKQQFATMGERRRFWEKLFvNDRLAQSLANNDQKAITETTEQLI 208
Cdd:pfam10414 1 GRLAALAGRFRDRVKARLPDVAARRRFWERVF-DGPVAELVLAGDEDEAEALLEQAL 56
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
216-403 |
1.51e-12 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 66.86 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 216 GEVVLVGAGPGDAGLLTLKGLQQIQQADVVV--YDRLVSDDI-MNLVRRDAD---RVFV-----GKRAGYHCVPQEEINQ 284
Cdd:PRK05576 2 GKLYGIGLGPGDPELLTVKAARILEEADVVYapASRKGGGSLaLNIVRPYLKeetEIVElhfpmSKDEEEKEAVWKENAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 285 ILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTHRDyaQSVRLITGhlkTGG 364
Cdd:PRK05576 82 EIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGD--ESLAIIPA---TRE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446272000 365 ELDWENLAAEKqTLVFYMGLNQAATIQQKLIEHG----------MPGEM 403
Cdd:PRK05576 157 ALIEQALTDFD-SVVLMKVYKNFALIEELLEEGYldalyvrrayMEGEQ 204
|
|
| CobL |
COG2241 |
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
218-441 |
1.48e-10 |
|
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441842 [Multi-domain] Cd Length: 207 Bit Score: 60.54 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 218 VVLVGAGPGDAGLLTLKGLQQIQQADVVV-YDRLVSddimnLVR-RDADRVFVGkragyhcVPQEE-INQILlrEAQKGK 294
Cdd:COG2241 4 LTVVGIGPGGPDGLTPAAREAIAEADVVVgGKRHLE-----LFPdLGAERIVWP-------SPLSElLEELL--ALLRGR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 295 RVVRLKGGDPFIFGRGGEELETLCNAgiPFSVVPGITAASGCSAYSGIPLthrdyaQSVRLITGHLKTGGELDwENLAAE 374
Cdd:COG2241 70 RVVVLASGDPLFYGIGATLARHLPAE--EVRVIPGISSLQLAAARLGWPW------QDAAVVSLHGRPLERLL-PALAPG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446272000 375 KQTLVFYMGLNQAATIQQKLIEHGMpGEMPVAIVENGTAVTQRVIDGTLTQLgeLAQQMNSPSLIII 441
Cdd:COG2241 141 RRVLVLTDDGNTPAAIARLLLERGF-GDSRLTVLENLGGPDERITRGTAEEL--ADADFSDLNVVAI 204
|
|
| PRK05990 |
PRK05990 |
precorrin-2 C(20)-methyltransferase; Reviewed |
215-441 |
5.82e-10 |
|
precorrin-2 C(20)-methyltransferase; Reviewed
Pssm-ID: 180341 Cd Length: 241 Bit Score: 59.62 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVY--------------DRLVSDDIMNL-----VRRDADRvfvgKRAGYH 275
Cdd:PRK05990 2 KGRLIGLGVGPGDPELLTLKALRLLQAAPVVAYfvakgkkgnafgivEAHLSPGQTLLplvypVTTEILP----PPLCYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 276 CVPQ---EEINQILLREAQKGKRVVRLKGGDPFIFG-------RGGEELETlcnagipfSVVPGITAASGCSAYSGIPLT 345
Cdd:PRK05990 78 TVIAdfyDTSAEAVAAHLDAGRDVAVICEGDPFFYGsymylhdRLAPRYET--------EVIPGVCSMLGCWSVLGAPLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 346 HRDyaQSVRLITGHLKTgGELDwENLAAEKQTLVFYMGLNqAATIQQKLIEHGMPGEmpvAI-VENGTAVTQRVIdgtlt 424
Cdd:PRK05990 150 YRN--QSLSVLSGVLPE-EELR-RRLADADAAVIMKLGRN-LDKVRRVLAALGLLDR---ALyVERATMANQRIV----- 216
|
250
....*....|....*....
gi 446272000 425 QLGELAqQMNSP--SLIII 441
Cdd:PRK05990 217 PLAEVD-PMASPyfSLILV 234
|
|
| cbiH |
PRK15478 |
precorrin-3B C(17)-methyltransferase; |
220-346 |
2.06e-08 |
|
precorrin-3B C(17)-methyltransferase;
Pssm-ID: 185375 [Multi-domain] Cd Length: 241 Bit Score: 54.89 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 220 LVGAGPGDAGLLTLKGLQQIQQADVVV----YDRLVsddimnlvrrdadRVFVGKRAGYHCVPQEEIN--QILLREAQKG 293
Cdd:PRK15478 4 VIGIGPGSQAMMTMEAIEALQAAEIVVgyktYTHLV-------------KAFTGDKQVIKTGMCKEIErcQAAIELAQAG 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446272000 294 KRVVRLKGGDPFIFGRGGEELETLCNAGIPFSV--VPGITAASGCSAYSGIPLTH 346
Cdd:PRK15478 71 HNVALISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPLMH 125
|
|
| PRK05562 |
PRK05562 |
NAD(P)-dependent oxidoreductase; |
16-147 |
1.94e-07 |
|
NAD(P)-dependent oxidoreductase;
Pssm-ID: 235504 Cd Length: 223 Bit Score: 51.57 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 16 LIVGGGDVAERKARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAATDDDALNQRVSEAAEA 95
Cdd:PRK05562 29 LIIGGGKAAFIKGKTFLKKGCYVYILSKKFSKEFLDLKKYGNLKLIKGNYDKEFIKDKHLIVIATDDEKLNNKIRKHCDR 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 446272000 96 R-RIFCNVVDaPKAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLL 147
Cdd:PRK05562 109 LyKLYIDCSD-YKKGLCIIPYQRSTKNFVFALNTKGGSPKTSVFIGEKVKNFL 160
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
219-337 |
1.01e-06 |
|
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester synthase (DHP5) and archaeal diphthamide synthase (DphB) participate in the second step of the biosynthetic pathway of diphthamide. The eukaryotic enzyme catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester; the archaeal enzyme, catalyzes only 3 methylations, producing diphthine. Diphtheria toxin ADP-ribosylates diphthamide leading to inhibition of protein synthesis in the eukaryotic host cells.
Pssm-ID: 381174 Cd Length: 241 Bit Score: 49.72 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 219 VLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVS-------DDIMNLVRRD---ADRVFVgkragyhcvpqEEINQILLR 288
Cdd:cd11647 3 YLIGLGLGDEKDITLEGLEALKKADKVYLEAYTSilpgsklEELEKLIGKKiilLDREDL-----------EEESEEILE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446272000 289 EAQKgKRVVRLKGGDPFIfgrggeeletlcnA-------------GIPFSVVPG---ITAASGCS 337
Cdd:cd11647 72 EAKK-KDVALLVPGDPLI-------------AtthidlrleakkrGIKVKVIHNasiLSAAGSTS 122
|
|
| PRK05991 |
PRK05991 |
precorrin-3B C17-methyltransferase; Provisional |
215-442 |
3.32e-06 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 180342 [Multi-domain] Cd Length: 250 Bit Score: 48.20 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 215 RGEVVLVGAGPGDAGLLTLKGLQQIQQADVVV-----YDRLvsDDIMNLVRRDADRvfvgkragyhcvpQEEIN--QILL 287
Cdd:PRK05991 2 SGRLFVIGTGPGNPEQMTPEALAAVEAATDFFgygpyLDRL--PLRADQLRHASDN-------------REELDraGAAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 288 REAQKGKRVVRLKGGDPFIFGRGGEELETLCNA-----GIPFSVVPGITAASGCSAYSGIPLTHRDYAQSvrlITGHLKT 362
Cdd:PRK05991 67 AMAAAGANVCVVSGGDPGVFAMAAAVCEAIENGpaawrAVDLTIVPGVTAMLAVAARIGAPLGHDFCAIS---LSDNLKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 363 GGELDWENLAAEKQTLV--FYMGLNQAATIQQ----KLIEHGMPGEMPVAIVENGTAVTQRVidgTLTQLGEL-AQQMNS 435
Cdd:PRK05991 144 WELIEKRLRLAAEAGFViaLYNPISRARPWQLgeafDLLREHLPATVPVIFGRAAGRPDERI---AVAPLAEAdASMADM 220
|
....*..
gi 446272000 436 PSLIIIG 442
Cdd:PRK05991 221 ATCVIIG 227
|
|
| PTZ00175 |
PTZ00175 |
diphthine synthase; Provisional |
220-442 |
8.17e-06 |
|
diphthine synthase; Provisional
Pssm-ID: 185500 Cd Length: 270 Bit Score: 47.26 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 220 LVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSddIMNLVRRDADRVFVGKR---AGYHCVpqEEINQILLREAqKGKRV 296
Cdd:PTZ00175 5 IIGLGLGDEKDITVKGLEAVKSADVVYLESYTS--ILINSNKEKLEEFYGKPvieADREMV--EEGCDEILEEA-KEKNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 297 VRLKGGDPF-------IFGRGGEeletlcnAGIPFSVV--PGITAASGCsaySGIPLtHRdYAQSVRL------------ 355
Cdd:PTZ00175 80 AFLVVGDPFcatthtdLYLRAKK-------KGIEVEVIhnASIMNAIGC---TGLQL-YR-FGETVSIpfftetwkpdsf 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446272000 356 ---ITGHLKTG-----------GELDWENLAaeKQTLVF----YMGLNQAatIQQKL-IEHGMPGE------MPVAIVEN 410
Cdd:PTZ00175 148 ydkIKANRDNGlhtlclldikvKERSVENLM--KGRKIYepprYMTINQA--IEQLLeVEEKKGGGviaedtLVVGVARV 223
|
250 260 270
....*....|....*....|....*....|....
gi 446272000 411 GTAvTQRVIDGTLTQLgeLAQQMNSP--SLIIIG 442
Cdd:PTZ00175 224 GSD-DQQIVSGTLEDL--LDVDFGPPlhSLVICA 254
|
|
| Sirohm_synth_M |
pfam14824 |
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ... |
122-146 |
5.62e-05 |
|
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme which catalyzes the biosynthesis of sirohaem. Both of the catalytic activities of this enzyme (precorrin-2 dehydrogenase EC:1.3.1.76) and sirohydrochlorin ferrochelatase (EC:4.99.1.4) are located in the N-terminal domain of this enzyme, pfam13241.
Pssm-ID: 464336 [Multi-domain] Cd Length: 25 Bit Score: 39.68 E-value: 5.62e-05
|
| |
