|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
226-462 |
1.31e-115 |
|
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: 339.74 E-value: 1.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 226 GHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGKR 305
Cdd:COG0007 2 GKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 306 VVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPGWAKLAVS 385
Cdd:COG0007 82 VVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALARP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVAGAA 462
Cdd:COG0007 162 GGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALRE 238
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
227-461 |
2.24e-110 |
|
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: 326.10 E-value: 2.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 227 HVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGKRV 306
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 307 VRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLP-GWAKLAVS 385
Cdd:TIGR01469 81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALEvDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVAGA 461
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
231-458 |
1.09e-106 |
|
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: 316.30 E-value: 1.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGKRVVRLK 310
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 311 SGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPGWAKLAVSGATIA 390
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489059161 391 VYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAV 458
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
224-468 |
8.77e-104 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 309.84 E-value: 8.77e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 224 ASGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEG 303
Cdd:PRK06136 1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 304 KRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPG--WAK 381
Cdd:PRK06136 81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLEPEvnWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 382 LAVSGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVAGA 461
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240
|
....*..
gi 489059161 462 AIGRAQA 468
Cdd:PRK06136 241 AKLAWFE 247
|
|
| CysG2 |
COG1648 |
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ... |
36-222 |
8.16e-54 |
|
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: 179.58 E-value: 8.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 36 LNKARLVAQTAARLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDEAGDRAAAAAARARKIPVNVVD 115
Cdd:COG1648 25 ARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAATDDEEVNARVAAAARARGILVNVVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 116 RPALCDFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRPLVERALPKGLARRGFWRTFFS 195
Cdd:COG1648 105 DPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGRLRERVKARLPDGAERRRFWERLLD 184
|
170 180
....*....|....*....|....*..
gi 489059161 196 GKVARAVESGDHEAAHRAAAELIGQGQ 222
Cdd:COG1648 185 GPLAELLRAGDEEEAEALLEELLAEAA 211
|
|
| cysG_Nterm |
TIGR01470 |
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ... |
15-205 |
4.86e-50 |
|
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: 169.51 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 15 FPAFFRVSGEVVAVVGGGEEALNKARLVAQTAARLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDE 94
Cdd:TIGR01470 1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 95 AGDRAAAAAARARKIPVNVVDRPALCDFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRP 174
Cdd:TIGR01470 81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160
|
170 180 190
....*....|....*....|....*....|.
gi 489059161 175 LVERALPKGLARRGFWRTFFSGKVARAVESG 205
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAG 191
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
227-438 |
2.20e-49 |
|
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: 167.90 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 227 HVWLVGAGPGAEDLLTLRAQRVLMEADVIVHD-ALVPEGVIAMGRRDAERlPVGKRKGCHSKSQGEINRLLVKLGQEGKR 305
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdSRALEILLDLLPEDLYF-PMTEDKEPLEEAYEEIAEALAAALRAGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 306 VVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLpgWAKLAVS 385
Cdd:pfam00590 80 VARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRL--LEALLAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLhEDTAVAVVENASRSNKRMFHGTLKDLP 438
Cdd:pfam00590 158 GDTVVLLYGPRRLAELAELLLELYP-DTTPVAVVERAGTPDEKVVRGTLGELA 209
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
38-126 |
1.06e-10 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 58.26 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 38 KARLVAQTAARLRIIAekaePHLAAFIESHgVEHIASPFaPELLDGAKLVFVATGDEAGDRAAAAAARARKIPVNVVDRP 117
Cdd:pfam13241 22 KARKLLEAGAKVTVVS----PEITPFLEGL-LDLIRREF-EGDLDGADLVIAATDDPELNERIAALARARGILVNVADDP 95
|
....*....
gi 489059161 118 ALCDFLTPA 126
Cdd:pfam13241 96 ELCDFYFPA 104
|
|
| PRK06718 |
PRK06718 |
NAD(P)-binding protein; |
41-178 |
5.08e-03 |
|
NAD(P)-binding protein;
Pssm-ID: 180667 [Multi-domain] Cd Length: 202 Bit Score: 38.09 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 41 LVAQTAaRLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDEAGDRAAAAAARARKIpVNVVDRPALC 120
Cdd:PRK06718 29 LLKYGA-HIVVISPELTENLVKLVEEGKIRWKQKEFEPSDIVDAFLVIAATNDPRVNEQVKEDLPENAL-FNVITDAESG 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489059161 121 DFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRPLVER 178
Cdd:PRK06718 107 NVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYECRQKIKE 164
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
226-462 |
1.31e-115 |
|
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: 339.74 E-value: 1.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 226 GHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGKR 305
Cdd:COG0007 2 GKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAELIYVGKRGGRHSLPQEEINALLVELARAGKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 306 VVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPGWAKLAVS 385
Cdd:COG0007 82 VVRLKGGDPFVFGRGGEEAEALAAAGIPFEVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLDWAALARP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVAGAA 462
Cdd:COG0007 162 GGTLVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVALRE 238
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
227-461 |
2.24e-110 |
|
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: 326.10 E-value: 2.24e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 227 HVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGKRV 306
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEINRLLVELAREGKKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 307 VRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLP-GWAKLAVS 385
Cdd:TIGR01469 81 VRLKGGDPFVFGRGGEEAEALAEAGIPFEVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALEvDWEALAKG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVAGA 461
Cdd:TIGR01469 161 AGTLVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVALR 236
|
|
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
231-458 |
1.09e-106 |
|
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: 316.30 E-value: 1.09e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGKRVVRLK 310
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 311 SGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPGWAKLAVSGATIA 390
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAGIPFEVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAALARPGGTLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489059161 391 VYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAV 458
Cdd:cd11642 161 IYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
224-468 |
8.77e-104 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 309.84 E-value: 8.77e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 224 ASGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEG 303
Cdd:PRK06136 1 MMGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEINRLLVDYARKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 304 KRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPG--WAK 381
Cdd:PRK06136 81 KVVVRLKGGDPFVFGRGGEELEALEAAGIPYEVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLEPEvnWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 382 LAVSGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVAGA 461
Cdd:PRK06136 161 LADGADTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEVVALR 240
|
....*..
gi 489059161 462 AIGRAQA 468
Cdd:PRK06136 241 AKLAWFE 247
|
|
| cysG |
PRK10637 |
siroheme synthase CysG; |
38-459 |
1.79e-101 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 311.31 E-value: 1.79e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 38 KARLVAQTAARLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDEAGDRAAAAAARARKIPVNVVDRP 117
Cdd:PRK10637 27 KARLLLDAGARLTVNALAFIPQFTAWADAGMLTLVEGPFDESLLDTCWLAIAATDDDAVNQRVSEAAEARRIFCNVVDAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 118 ALCDFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRPLVERALPKGLARRGFWRTFF-SG 196
Cdd:PRK10637 107 KAASFIMPSIIDRSPLMVAVSSGGTSPVLARLLREKLESLLPQHLGQVAKYAGQLRGRVKQQFATMGERRRFWEKLFvND 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 197 KVARAVESGDHEAAHRAAAELIGQGQDASGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERL 276
Cdd:PRK10637 187 RLAQSLANNDQKAVTETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 277 PVGKRKGCHSKSQGEINRLLVKLGQEGKRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTL 356
Cdd:PRK10637 267 FVGKRAGYHCVPQEEINQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAGIPFSVVPGITAASGCSAYSGIPLTH 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 357 RGVASSLVFTTGHDMTGDVLpGWAKLAVSGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKD 436
Cdd:PRK10637 347 RDYAQSVRLVTGHLKTGGEL-DWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSGTLTQ 425
|
410 420
....*....|....*....|...
gi 489059161 437 LPQLEnrKELSGPVMVVIGDAVA 459
Cdd:PRK10637 426 LGELA--QQVNSPSLIIVGRVVG 446
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
223-459 |
1.93e-76 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 240.30 E-value: 1.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 223 DASGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQE 302
Cdd:PLN02625 12 EGPGNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSFAEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 303 GKRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTG--DVLPGWA 380
Cdd:PLN02625 92 GKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGgtDPLDVAE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489059161 381 KLAVSGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVA 459
Cdd:PLN02625 172 AAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEVVA 250
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
231-459 |
1.76e-58 |
|
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: 192.22 E-value: 1.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVH-DALVPEGVIAMGRRDAERLPVgkrkgcHSKSQGEINRLLVKLGQEGKRVVRL 309
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIYaGSLVPPELLAYAKPGAEIVDS------AGMTLEEIIEVMREAAREGKDVVRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 310 KSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGdVLPG--WAKLAVSGA 387
Cdd:cd11641 75 HTGDPSLYGAIREQIDALDKLGIPYEVVPGVSSFFAAAAALGTELTLPEVSQTVILTRLEGRTP-VPEGesLRELAKHGA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489059161 388 TIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVA 459
Cdd:cd11641 154 TLAIFLSAALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
|
|
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
225-465 |
7.83e-56 |
|
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: 186.42 E-value: 7.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 225 SGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVH-DALVPEGVIAMGRRDAERLPVGkrkgchSKSQGEINRLLVKLGQEG 303
Cdd:COG2875 2 KGTVYFVGAGPGDPDLITVKGRRLLEEADVVLYaGSLVPPELLAYCKPGAEIVDSA------SMTLEEIIALMKEAAAEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 304 KRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMT----GDVLpgw 379
Cdd:COG2875 76 KDVVRLHSGDPSLYGAIAEQMRRLDALGIPYEVVPGVSAFAAAAAALGRELTLPEVSQTVILTRAEGRTpmpeGESL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 380 AKLAVSGATIAVYMGSTVAASVASRLIaAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVA 459
Cdd:COG2875 153 ASLAAHGATLAIYLSAHRIDEVVEELL-EGYPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALG 231
|
....*.
gi 489059161 460 GAAIGR 465
Cdd:COG2875 232 AEDFAR 237
|
|
| CysG2 |
COG1648 |
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ... |
36-222 |
8.16e-54 |
|
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: 179.58 E-value: 8.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 36 LNKARLVAQTAARLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDEAGDRAAAAAARARKIPVNVVD 115
Cdd:COG1648 25 ARKARLLLKAGARVTVVAPEFSPELAALAEEGRIELIKRAFEPEDLDGAFLVIAATDDEEVNARVAAAARARGILVNVVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 116 RPALCDFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRPLVERALPKGLARRGFWRTFFS 195
Cdd:COG1648 105 DPELCDFIVPAIVDRGPLVIAISTGGASPVLARRLRERLEALLPPEYGDLAELLGRLRERVKARLPDGAERRRFWERLLD 184
|
170 180
....*....|....*....|....*..
gi 489059161 196 GKVARAVESGDHEAAHRAAAELIGQGQ 222
Cdd:COG1648 185 GPLAELLRAGDEEEAEALLEELLAEAA 211
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
228-459 |
5.97e-52 |
|
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: 175.98 E-value: 5.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 228 VWLVGAGPGAEDLLTLRAQRVLMEADVIVH-DALVPEGVIAMGRRDAERLPVGkrkgchSKSQGEINRLLVKLGQEGKRV 306
Cdd:TIGR01465 1 VYFIGAGPGDPDLITVKGRKLIESADVILYaGSLVPPELLAHCRPGAEVVNSA------GMSLEEIVDIMSDAHREGKDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 307 VRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMT----GDVLpgwAKL 382
Cdd:TIGR01465 75 ARLHSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRTpmpeGEKL---ADL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489059161 383 AVSGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVA 459
Cdd:TIGR01465 152 AKHGATMAIFLSAHILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALD 228
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
225-459 |
2.36e-50 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 178.26 E-value: 2.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 225 SGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKGCHSKSQGEINRLLVKLGQEGK 304
Cdd:PRK07168 2 NGYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 305 RVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLPGWAKLAV 384
Cdd:PRK07168 82 IVVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHAKGPLTDHGKYNSSH 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489059161 385 SGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENRKELSGPVMVVIGDAVA 459
Cdd:PRK07168 162 NSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVVS 236
|
|
| cysG_Nterm |
TIGR01470 |
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ... |
15-205 |
4.86e-50 |
|
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: 169.51 E-value: 4.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 15 FPAFFRVSGEVVAVVGGGEEALNKARLVAQTAARLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDE 94
Cdd:TIGR01470 1 LPVFANLEGRAVLVVGGGDVALRKARLLLKAGAQLRVIAEELESELTLLAEQGGITWLARCFDADILEGAFLVIAATDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 95 AGDRAAAAAARARKIPVNVVDRPALCDFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRP 174
Cdd:TIGR01470 81 ELNRRVAHAARARGVPVNVVDDPELCSFIFPSIVDRSPVVVAISSGGAAPVLARLLRERIETLLPPSLGDLATLAATWRD 160
|
170 180 190
....*....|....*....|....*....|.
gi 489059161 175 LVERALPKGLARRGFWRTFFSGKVARAVESG 205
Cdd:TIGR01470 161 AVKKRLPNGAARRRFWEKFFDGAFAERVLAG 191
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
227-438 |
2.20e-49 |
|
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: 167.90 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 227 HVWLVGAGPGAEDLLTLRAQRVLMEADVIVHD-ALVPEGVIAMGRRDAERlPVGKRKGCHSKSQGEINRLLVKLGQEGKR 305
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDdSRALEILLDLLPEDLYF-PMTEDKEPLEEAYEEIAEALAAALRAGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 306 VVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTGHDMTGDVLpgWAKLAVS 385
Cdd:pfam00590 80 VARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRL--LEALLAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLhEDTAVAVVENASRSNKRMFHGTLKDLP 438
Cdd:pfam00590 158 GDTVVLLYGPRRLAELAELLLELYP-DTTPVAVVERAGTPDEKVVRGTLGELA 209
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
227-455 |
1.92e-28 |
|
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: 112.65 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 227 HVWLVGAGPGAEDLLTLRAQRVLMEADVI------------------VHDAlvPEGVIA-MGRRDAERLPVGKRKGCHSK 287
Cdd:cd11724 1 KLYLVGVGPGDPDLITLRALKAIKKADVVfappdlrkrfaeylagkeVLDD--PHGLFTyYGKKCSPLEEAEKECEELEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 288 SQGEINRLLVKLGQEGKRVVRLKSGDPLVFGRAGEEMAALraAGIGFEVVPGItSAFAAA-ADMELPLTLRGVASSLVFT 366
Cdd:cd11724 79 QRAEIVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEF--ADLNPEVIPGV-SSFNAAnAALKRSLTGGGDSRSVILT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 367 TGHDMTGDVLPGwAKLAVSGATIAVYMGSTVAASVASRLiAAGLHEDTAVAVVENASRSNK-RMFHGTLKDLPQLENRKE 445
Cdd:cd11724 156 APFALKENEDLL-EDLAATGDTLVIFMMRLDLDELVEKL-KKHYPPDTPVAIVYHAGYSEKeKVIRGTLDDILEKLGGEK 233
|
250
....*....|
gi 489059161 446 LSGPVMVVIG 455
Cdd:cd11724 234 EPFLGLIYVG 243
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
231-454 |
6.05e-27 |
|
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: 107.86 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEG---VIAMGRRD-AERLPVGkrkgcHSKSQGEINRLLVKLGQEGKRV 306
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAEDKDSKLlslVLRAILKDgKRIYDLH-----DPNVEEEMAELLLEEARQGKDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 307 VRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLtlrgvASSLVFTTGHDMTGDVLP-GWAKLAVS 385
Cdd:cd09815 76 AFLSPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDL-----GESFLFVTASDLLENPRLlVLKALAKE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLenRKELSGPVMVVI 454
Cdd:cd09815 151 RRHLVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAE--RTERGKPLTTIL 217
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
228-437 |
7.33e-27 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 108.69 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 228 VWLVGAGPGAEDLLTLRAQRVLMEADVIVH-DALVPEGVIAMGRRDAErlpvgkrkgCHSKSQ---GEINRLLVKLGQEG 303
Cdd:PRK15473 10 VWFVGAGPGDKELITLKGYRLLQQAQVVIYaGSLINTELLDYCPAQAE---------CHDSAElhlEQIIDLMEAGVKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 304 KRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLVFTTghdMTGDV-LPGWAKL 382
Cdd:PRK15473 81 KTVVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITR---MEGRTpVPAREQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489059161 383 ---AVSGATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDL 437
Cdd:PRK15473 158 esfASHQTSMAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADI 215
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
231-444 |
2.52e-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: 86.41 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVH-------DALVPEGVIAMGRRDAERL----PVGKRKGCHSKSQGEINRLLVKL 299
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIFVpvskggeGSAALIIAAALLIPDKEIIplefPMTKDREELEEAWDEAAEEIAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 300 GQEGKRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGvaSSLVfttghdmtgdVLPG- 378
Cdd:cd11645 81 LKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLA----------ILPAt 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489059161 379 -----WAKLAVSGATIAVYMGSTVAASVASRLIAAGLHEDtaVAVVENASRSNKRMFHgtlkDLPQLENRK 444
Cdd:cd11645 149 ydeeeLEKALENFDTVVLMKVGRNLEEIKELLEELGLLDK--AVYVERCGMEGERIYT----DLEELKEEK 213
|
|
| Precorrin_3B_C17_MT |
cd11646 |
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
228-438 |
8.12e-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: 85.54 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 228 VWLVGAGPGAEDLLTLRAQRVLMEADVIVhdalvpegviamG-RRDAERL-PVGKRKGCHSKSQG-EINR--LLVKLGQE 302
Cdd:cd11646 1 LYVVGIGPGSADLMTPRAREALEEADVIV------------GyKTYLDLIeDLLPGKEVISSGMGeEVERarEALELALE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 303 GKRVVRLKSGDPLVFGRAGE--EMAALRAAGIGFEVVPGITSAFAAAADMELPLtlrgvasslvfttGHDMT----GDVL 376
Cdd:cd11646 69 GKRVALVSSGDPGIYGMAGLvlELLDERWDDIEVEVVPGITAALAAAALLGAPL-------------GHDFAvislSDLL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489059161 377 PGW------AKLAVSGA-TIAVY----MGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLP 438
Cdd:cd11646 136 TPWeviekrLRAAAEADfVIALYnprsKKRPWQLEKALEILLEHRPPDTPVGIVRNAGREGEEVTITTLGELD 208
|
|
| CobJ |
COG1010 |
Precorrin-3B methylase [Coenzyme transport and metabolism]; Precorrin-3B methylase is part of ... |
224-348 |
2.24e-18 |
|
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: 84.35 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 224 ASGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHD----ALVPEGviamgRRDAERLPVGKRKgchsksqgEINR--LLV 297
Cdd:COG1010 2 MRGKLYVVGLGPGSAELMTPRARAALAEADVVVGYgtylDLIPPL-----LPGKEVHASGMRE--------EVERarEAL 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489059161 298 KLGQEGKRVVRLKSGDPLVFGRAG---EEMAALRAA-GIGFEVVPGITSAFAAAA 348
Cdd:COG1010 69 ELAAEGKTVAVVSSGDPGVYGMAGlvlEVLEEGGAWrDVEVEVVPGITAAQAAAA 123
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
231-454 |
1.08e-17 |
|
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: 81.00 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVhdalvpeGviamGRRDAERLPVGKRKGCHSKSQgEINRLLVKLGQEGKRVVRLK 310
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVI-------G----AKRLLELFPDLGAEKIPLPSE-DIAELLEEIAEAGKRVVVLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 311 SGDPLVFGRAGEEMAALraAGIGFEVVPGITSAFAAAADMELPLtlrgvaSSLVFTTGHdmtGDVLPGWAKLAVSGATIA 390
Cdd:cd11644 69 SGDPGFYGIGKTLLRRL--GGEEVEVIPGISSVQLAAARLGLPW------EDARLVSLH---GRDLENLRRALRRGRKVF 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489059161 391 VYMGSTV-AASVASRLIAAGLhEDTAVAVVENASRSNKRMFHGTLKDLpqleNRKELSGPVMVVI 454
Cdd:cd11644 138 VLTDGKNtPAEIARLLLERGL-GDSRVTVGENLGYPDERITEGTAEEL----AEEEFSDLNVVLI 197
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
225-441 |
5.06e-17 |
|
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: 80.14 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 225 SGHVWLVGAGPGAEDLLTLRAQRVLMEADVIVH---------------DALVPEGVI-----AMgRRDAERLpvgkrKGC 284
Cdd:COG2243 2 MGKLYGVGVGPGDPELLTLKAVRALREADVIAYpakgagkaslareivAPYLPPARIvelvfPM-TTDYEAL-----VAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 285 HSKSQGEINRLLvklgQEGKRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGvaSSLV 364
Cdd:COG2243 76 WDEAAARIAEEL----EAGRDVAFLTEGDPSLYSTFMYLLERLRERGFEVEVIPGITSFSAAAAALGIPLAEGD--EPLT 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489059161 365 FTTGhdmTGDVlPGWAKLAVSGATIAVYMGSTVAASVASRLIAAGLHEDtaVAVVENASRSNKRMFHGtLKDLPQLE 441
Cdd:COG2243 150 VLPG---TLLE-EELERALDDFDTVVIMKVGRNFPKVREALEEAGLLDR--AWYVERAGMPDERIVPG-LAEVDIEE 219
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
228-437 |
1.19e-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: 79.27 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 228 VWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEgVIAMGRRDAERLPVGKRKgchsksqgEINR--LLVKLGQEGKR 305
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLD-LIEDLIPGKEVVTSGMRE--------EIARaeLAIELAAEGRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 306 VVRLKSGDPLVFGRAGE--EMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSLvfttghdmtGDVLPGWA--- 380
Cdd:TIGR01466 72 VALVSSGDPGIYGMAALvfEALEKKGAEVDIEVIPGITAASAAASLLGAPLGHDFCVISL---------SDLLTPWPeie 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489059161 381 ----KLAVSGATIAVY----MGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDL 437
Cdd:TIGR01466 143 krlrAAAEADFVIAIYnprsKRRPEQFRRAMEILLEHRKPDTPVGIVRNAGREGEEVEITTLAEL 207
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
228-453 |
1.31e-15 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 75.29 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 228 VWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMGRRDAERLPVGKRKgchsksqgEINRLlvKLGQEGKRVV 307
Cdd:PRK05787 2 IYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGLRD--------LLEWL--ELAAKGKNVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 308 RLKSGDPLVFGrAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTlrgvasSLVFTTGHDmTGDVLPGWAKLAVSGA 387
Cdd:PRK05787 72 VLSTGDPLFSG-LGKLLKVRRAVAEDVEVIPGISSVQYAAARLGIDMN------DVVFTTSHG-RGPNFEELEDLLKNGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489059161 388 TIAVymgstVAAS------VASRLIAAGLHEDTAVaVVENASRSNKRMFHGTLKDLPQLENRkELSgpVMVV 453
Cdd:PRK05787 144 KVIM-----LPDPrfgpkeIAAELLERGKLERRIV-VGENLSYPDERIHKLTLSEIEPLEFS-DMS--VVVI 206
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
231-355 |
4.09e-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: 74.65 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVH-------DALVPEGVIAMGRRDAERL-----PVGKRKGCHSKSQGEINRLLVK 298
Cdd:TIGR01467 6 VGVGPGDPELITVKALEALRSADVIAVpaskkgrESLARKIVEDYLKPNDTRIlelvfPMTKDRDELEKAWDEAAEAVAA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 489059161 299 LGQEGKRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITSAFAAAADMELPLT 355
Cdd:TIGR01467 86 ELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLV 142
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
226-457 |
5.80e-15 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 74.43 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 226 GHVWLVGAGPGAEDLLTLRAQRVLMEADVIVhdalVPEGVIAMgrrdAERLPVGKrKGCHSKSQGEINR--LLVKLGQEG 303
Cdd:PRK05765 2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVII----GYNTYLRL----ISDLLDGK-EVIGARMKEEIFRanTAIEKALEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 304 KRVVRLKSGDPLVFGRAGE--EMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSL--VFTTGHDMTGDVLpgw 379
Cdd:PRK05765 73 NIVALVSSGDPQVYGMAGLvfELISRRKLDVDVEVIPGVTAALAAAARLGSPLSLDFVVISLsdLLIPREEILHRVT--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 380 aKLAVSGATIAVY----MGSTVAasvASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLENrkELSGPVMVVIG 455
Cdd:PRK05765 150 -KAAEADFVIVFYnpinENLLIE---VMDIVSKHRKPNTPVGLVKSAYRNNENVVITTLSSWKEHMD--EIGMTTTMIIG 223
|
..
gi 489059161 456 DA 457
Cdd:PRK05765 224 NS 225
|
|
| CbiE |
TIGR02467 |
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ... |
230-441 |
5.98e-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: 73.50 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 230 LVGAGPGAEDLLTLRAQRVLMEADVIV----HDALVPEGviamgrrDAERLPVGKrkgcHSKSQGEINRLLVKLGQEgKR 305
Cdd:TIGR02467 1 VVGIGPGGPELLTPAAIEAIRKADLVVggerHLELLAEL-------IGEKREIIL----TYKDLDELLEFIAATRKE-KR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 306 VVRLKSGDPLVFGRagEEMAALRAAGIGFEVVPGITSAFAAAADMELPLTLRGVASSlvftTGHDMTGDVLpgwAKLAVS 385
Cdd:TIGR02467 69 VVVLASGDPLFYGI--GRTLAERLGKERLEIIPGISSVQYAFARLGLPWQDAVVISL----HGRELDELLL---ALLRGH 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489059161 386 GATIAVYMGSTVAASVASRLIAAGLHEDTAVAVVENASRSNKRMFHGTLKDLPQLE 441
Cdd:TIGR02467 140 RKVAVLTDPRNGPAEIARELIELGIGGSYELTVGENLGYEDERITEGTLEEIAAAQ 195
|
|
| CobL |
COG2241 |
Precorrin-6B methylase 1 [Coenzyme transport and metabolism]; Precorrin-6B methylase 1 is part ... |
230-454 |
7.31e-15 |
|
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: 73.26 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 230 LVGAGPGAEDLLTLRAQRVLMEADVIV----HDALVPEgviamgrRDAERLPVGkrkgchsksqGEINRLLVKLGQE--G 303
Cdd:COG2241 6 VVGIGPGGPDGLTPAAREAIAEADVVVggkrHLELFPD-------LGAERIVWP----------SPLSELLEELLALlrG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 304 KRVVRLKSGDPLVFGRAGEEMAALRAAGIgfEVVPGITSAFAAAADMELPLTlrgvasSLVFTTGHdmtGDVLPGWAKLA 383
Cdd:COG2241 69 RRVVVLASGDPLFYGIGATLARHLPAEEV--RVIPGISSLQLAAARLGWPWQ------DAAVVSLH---GRPLERLLPAL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489059161 384 VSGATIAVYM--GSTVAAsVASRLIAAGLhEDTAVAVVENASRSNKRMFHGTLKDLPQlenrKELSGPVMVVI 454
Cdd:COG2241 138 APGRRVLVLTddGNTPAA-IARLLLERGF-GDSRLTVLENLGGPDERITRGTAEELAD----ADFSDLNVVAI 204
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
231-352 |
5.40e-13 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 68.40 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 231 VGAGPGAEDLLTLRAQRVLMEADVIVhdalVPEGViAMGRRDAERL------PVGKRKGCH---SKSQGEINRLLVKLGQ 301
Cdd:PRK05576 7 IGLGPGDPELLTVKAARILEEADVVY----APASR-KGGGSLALNIvrpylkEETEIVELHfpmSKDEEEKEAVWKENAE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 302 E-------GKRVVRLKSGDPLVFGRAGEEMAALRAAGIGFEVVPGITS--AFAAAADMEL 352
Cdd:PRK05576 82 EiaaeaeeGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSftAIASRAGVPL 141
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
38-126 |
1.06e-10 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 58.26 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 38 KARLVAQTAARLRIIAekaePHLAAFIESHgVEHIASPFaPELLDGAKLVFVATGDEAGDRAAAAAARARKIPVNVVDRP 117
Cdd:pfam13241 22 KARKLLEAGAKVTVVS----PEITPFLEGL-LDLIRREF-EGDLDGADLVIAATDDPELNERIAALARARGILVNVADDP 95
|
....*....
gi 489059161 118 ALCDFLTPA 126
Cdd:pfam13241 96 ELCDFYFPA 104
|
|
| CysG_dimerizer |
pfam10414 |
Sirohaem synthase dimerization region; Bacterial sulfur metabolism depends on the ... |
163-206 |
3.70e-10 |
|
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: 55.25 E-value: 3.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489059161 163 GELAHFAESWRPLVERALPKGLARRGFWRTFFSGKVARAVESGD 206
Cdd:pfam10414 1 GRLAALAGRFRDRVKARLPDVAARRRFWERVFDGPVAELVLAGD 44
|
|
| cbiH |
PRK15478 |
precorrin-3B C(17)-methyltransferase; |
230-354 |
8.86e-07 |
|
precorrin-3B C(17)-methyltransferase;
Pssm-ID: 185375 [Multi-domain] Cd Length: 241 Bit Score: 49.88 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 230 LVGAGPGAEDLLTLRAQRVLMEADVIVHDALVPEGVIAMgRRDAERLPVGKRKgchsksqgEINRLL--VKLGQEGKRVV 307
Cdd:PRK15478 4 VIGIGPGSQAMMTMEAIEALQAAEIVVGYKTYTHLVKAF-TGDKQVIKTGMCK--------EIERCQaaIELAQAGHNVA 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489059161 308 RLKSGDPLVFGRAGEEMAALRAAGIGFEV--VPGITSAFAAAADMELPL 354
Cdd:PRK15478 75 LISSGDAGIYGMAGLVLELVSKQKLDVEVrlIPGMTASIAAASLLGAPL 123
|
|
| PRK05948 |
PRK05948 |
precorrin-2 C(20)-methyltransferase; |
226-441 |
1.77e-06 |
|
precorrin-2 C(20)-methyltransferase;
Pssm-ID: 180320 Cd Length: 238 Bit Score: 49.26 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 226 GHVWLVGAGPGAEDLLTLRAQRVLMEADVIVHDALV------PEGVIAMG-RRDAERLP-----VGKRKGCHSKSQGEIN 293
Cdd:PRK05948 4 GTLYGISVGPGDPELITLKGLRLLQSAPVVAFPAGLagqpglAEQIIAPWlSPQQIKLPlyfpyVQDEEQLEQAWQAAAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 294 RLLVKLGQeGKRVVRLKSGDPLVFGRAGEEMAALRA--AGIGFEVVPGITSAFAAAADMELPLTLRgvasslvfttghDM 371
Cdd:PRK05948 84 QVWHYLEQ-GEDVAFACEGDVSFYSTFTYLAQTLQElyPQVAIQTIPGVCSPLAAAAALGIPLTLG------------SQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489059161 372 TGDVLPGWAKL-----AVSGATIAVYMG-STVAASVASRLIAAGLHEDTavAVVENASRSNKRMFHgTLKDLPQLE 441
Cdd:PRK05948 151 RLAILPALYHLeeleqALTWADVVVLMKvSSVYPQVWQWLKARNLLEQA--SLVERATTPEQVIYR-NLEDYPDLR 223
|
|
| DHP5_DphB |
cd11647 |
diphthine methyl ester synthase and diphthine synthase; Eukaryotic diphthine methyl ester ... |
229-348 |
4.35e-03 |
|
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: 38.94 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 229 WLVGAGPGAEDLLTLRAQRVLMEADVIVHDA---LVPEG------------VIAMGRRDAErlpvgkrkgchsksqgEIN 293
Cdd:cd11647 3 YLIGLGLGDEKDITLEGLEALKKADKVYLEAytsILPGSkleelekligkkIILLDREDLE----------------EES 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489059161 294 RLLVKLGQEgKRVVRLKSGDPLVfgrageemA------ALRA--AGIGFEVVPGItSAFAAAA 348
Cdd:cd11647 67 EEILEEAKK-KDVALLVPGDPLI--------AtthidlRLEAkkRGIKVKVIHNA-SILSAAG 119
|
|
| PRK06718 |
PRK06718 |
NAD(P)-binding protein; |
41-178 |
5.08e-03 |
|
NAD(P)-binding protein;
Pssm-ID: 180667 [Multi-domain] Cd Length: 202 Bit Score: 38.09 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489059161 41 LVAQTAaRLRIIAEKAEPHLAAFIESHGVEHIASPFAPELLDGAKLVFVATGDEAGDRAAAAAARARKIpVNVVDRPALC 120
Cdd:PRK06718 29 LLKYGA-HIVVISPELTENLVKLVEEGKIRWKQKEFEPSDIVDAFLVIAATNDPRVNEQVKEDLPENAL-FNVITDAESG 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489059161 121 DFLTPAIVNRAPVTIAIGSQGTAPVLAQMVRARIDAAFSPRLGELAHFAESWRPLVER 178
Cdd:PRK06718 107 NVVFPSALHRGKLTISVSTDGASPKLAKKIRDELEALYDESYESYIDFLYECRQKIKE 164
|
|
| |
