|
Name |
Accession |
Description |
Interval |
E-value |
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
331-556 |
4.35e-90 |
|
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: 277.40 E-value: 4.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLESLDNGLKVVRLK 410
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 411 QGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIPE--FVESRTT 487
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAG-IPFeVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAalARPGGTL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365329 488 VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAV 556
Cdd:cd11642 160 VIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
326-557 |
1.01e-73 |
|
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: 235.74 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTE-TFIAKKfPGNAERAQQE----LLAKGLEsl 400
Cdd:COG0007 2 GKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAElIYVGKR-GGRHSLPQEEinalLVELARA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 401 dnGLKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPI-I 478
Cdd:COG0007 79 --GKRVVRLKGGDPFVFGRGGEEAEALAAAG-IPFeVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLdW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 479 PEFVESRTT-VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVN 557
Cdd:COG0007 156 AALARPGGTlVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVA 235
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
320-557 |
4.78e-68 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 221.43 E-value: 4.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 320 EGPkklGKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLES 399
Cdd:PLN02625 12 EGP---GNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 400 LDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPII- 478
Cdd:PLN02625 89 AEAGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTDPLd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 479 ---PEFVESRTTVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKA 555
Cdd:PLN02625 169 vaeAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEV 248
|
..
gi 398365329 556 VN 557
Cdd:PLN02625 249 VA 250
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
327-557 |
3.27e-59 |
|
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: 197.45 E-value: 3.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQE----LLAKGLEsldn 402
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEinrlLVELARE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 403 GLKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIP-- 479
Cdd:TIGR01469 77 GKKVVRLKGGDPFVFGRGGEEAEALAEAG-IPFeVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALEVDwe 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365329 480 EFVESRTT-VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVN 557
Cdd:TIGR01469 156 ALAKGAGTlVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVA 234
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
327-533 |
6.90e-42 |
|
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: 150.19 E-value: 6.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSADIILADK-LVPQAILDLIPPKTEtFIAKKFPGNAERAQQELLAKGLESLDNGLK 405
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLY-FPMTEDKEPLEEAYEEIAEALAAALRAGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 406 VVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIPEFVESR 485
Cdd:pfam00590 80 VARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLEALLANGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365329 486 TTVFLMALHRANVLITGLLKHGwDGDVPAAIVERGSCPDQRVTRTLLK 533
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELY-PDTTPVAVVERAGTPDEKVVRGTLG 206
|
|
| CysG2 |
COG1648 |
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ... |
26-209 |
1.87e-13 |
|
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: 69.41 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 26 LLIGTGStdsvsVCKNRIHSILNAGGNPIVVnpsSPSHTKQLQlEFGKFAKFEIVEREFRLSDLTtlGRVLVCKVVDRVF 105
Cdd:COG1648 16 LVVGGGE-----VAARKARLLLKAGARVTVV---APEFSPELA-ALAEEGRIELIKRAFEPEDLD--GAFLVIAATDDEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 106 VDlpitqsrlcEEIFWQCQKLRIPINTFHKPEFSTFNMiPTWVDpkGSGLQISVTTNGNGYILANRIKRDIISHLPPNIS 185
Cdd:COG1648 85 VN---------ARVAAAARARGILVNVVDDPELCDFIV-PAIVD--RGPLVIAISTGGASPVLARRLRERLEALLPPEYG 152
|
170 180
....*....|....*....|....*....
gi 398365329 186 EVVINMGYLKDRIIN-----EDHKALLEE 209
Cdd:COG1648 153 DLAELLGRLRERVKArlpdgAERRRFWER 181
|
|
| cysG_Nterm |
TIGR01470 |
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ... |
26-198 |
1.74e-06 |
|
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: 48.94 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 26 LLIGTGStdsvsVCKNRIHSILNAGGNPIVVNPSSPShtkQLQLeFGKFAKFEIVEREFRLSDLTtlGRVLVCKVVDrvf 105
Cdd:TIGR01470 13 LVVGGGD-----VALRKARLLLKAGAQLRVIAEELES---ELTL-LAEQGGITWLARCFDADILE--GAFLVIAATD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 106 vdlpitQSRLCEEIFWQCQKLRIPINTFHKPEFSTFnMIPTWVDPkgSGLQISVTTNGNGYILANRIKRDIISHLPPNIS 185
Cdd:TIGR01470 79 ------DEELNRRVAHAARARGVPVNVVDDPELCSF-IFPSIVDR--SPVVVAISSGGAAPVLARLLRERIETLLPPSLG 149
|
170
....*....|...
gi 398365329 186 EVVINMGYLKDRI 198
Cdd:TIGR01470 150 DLATLAATWRDAV 162
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
21-141 |
4.53e-05 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 42.85 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 21 TDQVHLLIGTGStdsvsVCKNRIHSILNAGGNPIVVnpsSPSHTKQLQlefgkfAKFEIVEREFRlSDLttLGRVLVCKV 100
Cdd:pfam13241 6 RGKRVLVVGGGE-----VAARKARKLLEAGAKVTVV---SPEITPFLE------GLLDLIRREFE-GDL--DGADLVIAA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 398365329 101 VDrvfvdlpitQSRLCEEIFWQCQKLRIPINTFHKPEFSTF 141
Cdd:pfam13241 69 TD---------DPELNERIAALARARGILVNVADDPELCDF 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SUMT |
cd11642 |
Uroporphyrin-III C-methyltransferase (also known as S-Adenosyl-L-methionine:uroporphyrinogen ... |
331-556 |
4.35e-90 |
|
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: 277.40 E-value: 4.35e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLESLDNGLKVVRLK 410
Cdd:cd11642 1 VGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALAPPGAELIYVGKRPGRHSVPQEEINELLVELAREGKRVVRLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 411 QGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIPE--FVESRTT 487
Cdd:cd11642 81 GGDPFVFGRGGEEIEALREAG-IPFeVVPGITSAIAAAAYAGIPLTHRGVASSVTFVTGHEADGKLPDDDAalARPGGTL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365329 488 VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAV 556
Cdd:cd11642 160 VIYMGVSNLEEIAERLIAAGLPPDTPVAIVENATTPDQRVVVGTLAELAEKAAEAGIRSPALIVVGEVV 228
|
|
| CysG |
COG0007 |
Uroporphyrinogen-III methylase (siroheme synthase) [Coenzyme transport and metabolism]; ... |
326-557 |
1.01e-73 |
|
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: 235.74 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTE-TFIAKKfPGNAERAQQE----LLAKGLEsl 400
Cdd:COG0007 2 GKVYLVGAGPGDPDLLTLKALRALQQADVVLYDRLVSPEILALARPDAElIYVGKR-GGRHSLPQEEinalLVELARA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 401 dnGLKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPI-I 478
Cdd:COG0007 79 --GKRVVRLKGGDPFVFGRGGEEAEALAAAG-IPFeVVPGITAAIAAPAYAGIPLTHRGVASSVTFVTGHEKDGKLDLdW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 479 PEFVESRTT-VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVN 557
Cdd:COG0007 156 AALARPGGTlVIYMGVKNLPEIAAALIAAGRSPDTPVAVIENGTTPDQRVVTGTLATLAELAAEAGLKSPALIVVGEVVA 235
|
|
| PLN02625 |
PLN02625 |
uroporphyrin-III C-methyltransferase |
320-557 |
4.78e-68 |
|
uroporphyrin-III C-methyltransferase
Pssm-ID: 178232 [Multi-domain] Cd Length: 263 Bit Score: 221.43 E-value: 4.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 320 EGPkklGKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLES 399
Cdd:PLN02625 12 EGP---GNVFLVGTGPGDPDLLTLKALRLLQTADVVLYDRLVSPDILDLVPPGAELLYVGKRGGYHSRTQEEIHELLLSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 400 LDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPII- 478
Cdd:PLN02625 89 AEAGKTVVRLKGGDPLVFGRGGEEMDALRKNGIPVTVVPGITAAIGAPAELGIPLTHRGVATSVRFLTGHDREGGTDPLd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 479 ---PEFVESRTTVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKA 555
Cdd:PLN02625 169 vaeAAADPDTTLVVYMGLGTLPSLAEKLIAAGLPPDTPAAAVERGTTPEQRVVFGTLEDIAEDVAAAGLVSPTVIVVGEV 248
|
..
gi 398365329 556 VN 557
Cdd:PLN02625 249 VA 250
|
|
| cobA_cysG_Cterm |
TIGR01469 |
uroporphyrin-III C-methyltransferase; This model represents enzymes, or enzyme domains, with ... |
327-557 |
3.27e-59 |
|
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: 197.45 E-value: 3.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQE----LLAKGLEsldn 402
Cdd:TIGR01469 1 KVYLVGAGPGDPELLTLKALRLLQEADVVLYDALVSPEILAYAPPQAELIDVGKRPGCHSKKQEEinrlLVELARE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 403 GLKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIP-- 479
Cdd:TIGR01469 77 GKKVVRLKGGDPFVFGRGGEEAEALAEAG-IPFeVVPGVTSAIAAAAYAGIPLTHRGVASSVTFVTGHEADDKALEVDwe 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365329 480 EFVESRTT-VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVN 557
Cdd:TIGR01469 156 ALAKGAGTlVIYMGVRNLPEIAKELIEHGRSPDTPVAVVEWATTPNQRVLIGTLGDLAEKAAEANLKSPALIVIGEVVA 234
|
|
| PRK06136 |
PRK06136 |
uroporphyrinogen-III C-methyltransferase; |
325-558 |
7.33e-57 |
|
uroporphyrinogen-III C-methyltransferase;
Pssm-ID: 235711 Cd Length: 249 Bit Score: 191.58 E-value: 7.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 325 LGKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQE----LLAKGLEsl 400
Cdd:PRK06136 2 MGKVYLVGAGPGDPDLITLKGVRLLEQADVVLYDDLVSPEILAYAKPDAELIYVGKRAGRHSTKQEEinrlLVDYARK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 401 dnGLKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPI-- 477
Cdd:PRK06136 80 --GKVVVRLKGGDPFVFGRGGEELEALEAAG-IPYeVVPGITAAIAAAAYAGIPLTHRGVARSVTFVTGHEAAGKLEPev 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 478 -IPEFVESR-TTVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKA 555
Cdd:PRK06136 157 nWSALADGAdTLVIYMGVRNLPYIAAQLLAAGRAPDTPVAIIENGTTPEQRVVRGTLGTIAEGAAAEDIQSPAIIVIGEV 236
|
...
gi 398365329 556 VNA 558
Cdd:PRK06136 237 VAL 239
|
|
| cysG |
PRK10637 |
siroheme synthase CysG; |
312-562 |
4.47e-43 |
|
siroheme synthase CysG;
Pssm-ID: 182606 [Multi-domain] Cd Length: 457 Bit Score: 160.31 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 312 QLSEVKKEEGPKKLGKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQE 391
Cdd:PRK10637 202 ETTEQLFSEPLDHRGEVVLVGAGPGDAGLLTLKGLQQIQQADVVVYDRLVSDDIMNLVRRDADRVFVGKRAGYHCVPQEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 392 LLAKGLESLDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIADQVLICTGTG 470
Cdd:PRK10637 282 INQILLREAQKGKRVVRLKGGDPFIFGRGGEELETLCNAG-IPFsVVPGITAASGCSAYSGIPLTHRDYAQSVRLVTGHL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 471 RKGA-LPIIPEFVESRTTVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSrpPGV 549
Cdd:PRK10637 361 KTGGeLDWENLAAEKQTLVFYMGLNQAATIQQKLIEHGMPADMPVALVENGTSVTQRVVSGTLTQLGELAQQVNS--PSL 438
|
250
....*....|...
gi 398365329 550 LVVGKAVnALVEK 562
Cdd:PRK10637 439 IIVGRVV-GLRDK 450
|
|
| TP_methylase |
pfam00590 |
Tetrapyrrole (Corrin/Porphyrin) Methylases; This family uses S-AdoMet in the methylation of ... |
327-533 |
6.90e-42 |
|
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: 150.19 E-value: 6.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSADIILADK-LVPQAILDLIPPKTEtFIAKKFPGNAERAQQELLAKGLESLDNGLK 405
Cdd:pfam00590 1 KLYLVGVGPGDPDLLTLRALRALKEADVVLGDDsRALEILLDLLPEDLY-FPMTEDKEPLEEAYEEIAEALAAALRAGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 406 VVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKGALPIIPEFVESR 485
Cdd:pfam00590 80 VARLVSGDPLVYGTGSYLVEALRAAGIDVEVVPGVSSAQAAAARLGIPLTEGGEVLSVLFLPGLARIELRLLEALLANGD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365329 486 TTVFLMALHRANVLITGLLKHGwDGDVPAAIVERGSCPDQRVTRTLLK 533
Cdd:pfam00590 160 TVVLLYGPRRLAELAELLLELY-PDTTPVAVVERAGTPDEKVVRGTLG 206
|
|
| CobM |
COG2875 |
Precorrin-4 methylase [Coenzyme transport and metabolism]; Precorrin-4 methylase is part of ... |
326-558 |
3.75e-30 |
|
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: 119.01 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIIL-ADKLVPQAILDLIPPKTETFiakkfpgN-AERAQQELLAKGLESLDNG 403
Cdd:COG2875 3 GTVYFVGAGPGDPDLITVKGRRLLEEADVVLyAGSLVPPELLAYCKPGAEIV-------DsASMTLEEIIALMKEAAAEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 404 LKVVRLKQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIAdQVLICTGTGRKGALP---IIP 479
Cdd:COG2875 76 KDVVRLHSGDPSLYGAIAEQMRRLDALG-IPYeVVPGVSAFAAAAAALGRELTLPEVS-QTVILTRAEGRTPMPegeSLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 480 EFVESRTT-VFLMALHRANVLITGLLKHgWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVNA 558
Cdd:COG2875 154 SLAAHGATlAIYLSAHRIDEVVEELLEG-YPPDTPVAVVYRASWPDEKIVRGTLADIAEKVKEAGITRTALILVGPALGA 232
|
|
| PRK07168 |
PRK07168 |
uroporphyrin-III C-methyltransferase; |
326-557 |
4.15e-30 |
|
uroporphyrin-III C-methyltransferase;
Pssm-ID: 180864 [Multi-domain] Cd Length: 474 Bit Score: 123.56 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLESLDNGLK 405
Cdd:PRK07168 3 GYVYLVGAGPGDEGLITKKAIECLKRADIVLYDRLLNPFFLSYTKQTCELMYCGKMPKNHIMRQEMINAHLLQFAKEGKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 406 VVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGrKGALPIIPEF---V 482
Cdd:PRK07168 83 VVRLKGGDPSIFGRVGEEAETLAAANIPYEIVPGITSSIAASSYAGIPLTHRNYSNSVTLLTGHA-KGPLTDHGKYnssH 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365329 483 ESRTTVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVN 557
Cdd:PRK07168 162 NSDTIAYYMGIKNLPTICENLRQAGKKEDTPVAVIEWGTTGKQRVVTGTLSTIVSIVKNENISNPSMTIVGDVVS 236
|
|
| Precorrin-4_C11-MT |
cd11641 |
Precorrin-4 C11-methyltransferase (CbiF/CobM); Precorrin-4 C11-methyltransferase participates ... |
331-557 |
5.11e-30 |
|
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: 117.49 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADIIL-ADKLVPQAILDLIPPKTETFiakkfpGNAERAQQELLAKGLESLDNGLKVVRL 409
Cdd:cd11641 1 VGAGPGDPELITVKGARLLEEADVVIyAGSLVPPELLAYAKPGAEIV------DSAGMTLEEIIEVMREAAREGKDVVRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 410 KQGDPYIFGRGGEEFNFFKDHGyIPV-VLPGISSSLACTVLAQIPATQRDIAdQVLICTGTGRKGALPI---IPEFVESR 485
Cdd:cd11641 75 HTGDPSLYGAIREQIDALDKLG-IPYeVVPGVSSFFAAAAALGTELTLPEVS-QTVILTRLEGRTPVPEgesLRELAKHG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365329 486 TT--VFLMAlHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVN 557
Cdd:cd11641 153 ATlaIFLSA-ALIEEVVEELLAGGYPPDTPVAVVYKASWPDEKIIRGTLADLAEKVKEAGITRTALILVGPALG 225
|
|
| cobM_cbiF |
TIGR01465 |
precorrin-4 C11-methyltransferase; This model represents precorrin-4 C11-methyltransferase, ... |
331-558 |
3.41e-27 |
|
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: 110.49 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADIIL-ADKLVPQAILDLIPPKTEtfIAKkfpgNAERAQQELLAKGLESLDNGLKVVRL 409
Cdd:TIGR01465 4 IGAGPGDPDLITVKGRKLIESADVILyAGSLVPPELLAHCRPGAE--VVN----SAGMSLEEIVDIMSDAHREGKDVARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 410 KQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKgALP---IIPEFVESRT 486
Cdd:TIGR01465 78 HSGDPSIYGAIAEQMRLLEALGIPYEVVPGVSSFFAAAAALGAELTVPEVSQTVILTRASGRT-PMPegeKLADLAKHGA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398365329 487 T--VFLMAlHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGKAVNA 558
Cdd:TIGR01465 157 TmaIFLSA-HILDKVVKELIEHGYSEDTPVAVVYRATWPDEKIVRGTLADLADLVREEGIYRTTLILVGPALDP 229
|
|
| TP_methylase |
cd11724 |
uncharacterized family of the tetrapyrrole methylase superfamily; Members of this superfamily ... |
327-553 |
5.51e-25 |
|
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: 103.79 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPK-----------------TETFIAKKFPGNAERAQ 389
Cdd:cd11724 1 KLYLVGVGPGDPDLITLRALKAIKKADVVFAPPDLRKRFAEYLAGKevlddphglftyygkkcSPLEEAEKECEELEKQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 390 QELLAKGLESLDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHgyIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGT 469
Cdd:cd11724 81 AEIVQKIREALAQGKNVALLDSGDPTIYGPWIWYLEEFADL--NPEVIPGVSSFNAANAALKRSLTGGGDSRSVILTAPF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 470 GRKGALPIIPEFVESRTT-VFLMALHRANVLITGLLKHgWDGDVPAAIVER-GSCPDQRVTRTLLKWVPEVVEEIGSRPP 547
Cdd:cd11724 159 ALKENEDLLEDLAATGDTlVIFMMRLDLDELVEKLKKH-YPPDTPVAIVYHaGYSEKEKVIRGTLDDILEKLGGEKEPFL 237
|
....*.
gi 398365329 548 GVLVVG 553
Cdd:cd11724 238 GLIYVG 243
|
|
| TP_methylase |
cd09815 |
S-AdoMet-dependent tetrapyrrole methylases; This superfamily uses S-AdoMet ... |
331-553 |
7.52e-24 |
|
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: 100.16 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADIILA-DKLVPQAILDLIppKTETFIAKKFPGNAERAQQELLAKGLESLDNGLKVVRL 409
Cdd:cd09815 1 VGVGPGDPDLLTLRALEILRAADVVVAeDKDSKLLSLVLR--AILKDGKRIYDLHDPNVEEEMAELLLEEARQGKDVAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 410 KQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRdiadqVLICTGTGRKG---ALPIIPEFVESRT 486
Cdd:cd09815 79 SPGDPGVAGTGAELVERAEREGVEVKVIPGVSAADAAAAALGIDLGES-----FLFVTASDLLEnprLLVLKALAKERRH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365329 487 TVFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEiGSRPPGVLVVG 553
Cdd:cd09815 154 LVLFLDGHRFLKALERLLKELGEDDTPVVLVANAGSEGEVIRTGTVKELRAERTE-RGKPLTTILVG 219
|
|
| CobF |
COG2243 |
Precorrin-2 methylase [Coenzyme transport and metabolism]; Precorrin-2 methylase is part of ... |
324-531 |
7.92e-16 |
|
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: 77.06 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 324 KLGKISLVGSGPGSVSMLTIGALQEIKSADIIladkLVP----------QAILD-LIPPKTETFIAkkFP-----GNAER 387
Cdd:COG2243 1 MMGKLYGVGVGPGDPELLTLKAVRALREADVI----AYPakgagkaslaREIVApYLPPARIVELV--FPmttdyEALVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 388 AQQELLAKGLESLDNGLKVVRLKQGDP-------YIFGRggeefnfFKDHGYIPVVLPGISSSLACTVLAQIPATQRDia 460
Cdd:COG2243 75 AWDEAAARIAEELEAGRDVAFLTEGDPslystfmYLLER-------LRERGFEVEVIPGITSFSAAAAALGIPLAEGD-- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365329 461 DQVLICTGTGRKGALpiiPEFVESRTTVFLMALHRANVLITGLLK-HGWDGDvpAAIVERGSCPDQRVTRTL 531
Cdd:COG2243 146 EPLTVLPGTLLEEEL---ERALDDFDTVVIMKVGRNFPKVREALEeAGLLDR--AWYVERAGMPDERIVPGL 212
|
|
| cbiF |
PRK15473 |
cobalt-precorrin-4 methyltransferase; |
327-554 |
6.88e-15 |
|
cobalt-precorrin-4 methyltransferase;
Pssm-ID: 185370 Cd Length: 257 Bit Score: 74.79 E-value: 6.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSAD-IILADKLVPQAILDLIPPKTETFiakkfpGNAERAQQELLAKGLESLDNGLK 405
Cdd:PRK15473 9 CVWFVGAGPGDKELITLKGYRLLQQAQvVIYAGSLINTELLDYCPAQAECH------DSAELHLEQIIDLMEAGVKAGKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 406 VVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKgalPIIPE----- 480
Cdd:PRK15473 83 VVRLQTGDVSLYGSIREQGEELTKRGIDFQVVPGVSSFLGAAAELGVEYTVPEVSQSLIITRMEGRT---PVPAReqles 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365329 481 FVESRTT-VFLMALHRANVLITGLLKHGWDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVEEIGSRPPGVLVVGK 554
Cdd:PRK15473 160 FASHQTSmAIFLSVQRIHRVAERLIAGGYPATTPVAVIYKATWPESQTVRGTLADIAEKVRDAGIRKTALILVGN 234
|
|
| CysG2 |
COG1648 |
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ... |
26-209 |
1.87e-13 |
|
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: 69.41 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 26 LLIGTGStdsvsVCKNRIHSILNAGGNPIVVnpsSPSHTKQLQlEFGKFAKFEIVEREFRLSDLTtlGRVLVCKVVDRVF 105
Cdd:COG1648 16 LVVGGGE-----VAARKARLLLKAGARVTVV---APEFSPELA-ALAEEGRIELIKRAFEPEDLD--GAFLVIAATDDEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 106 VDlpitqsrlcEEIFWQCQKLRIPINTFHKPEFSTFNMiPTWVDpkGSGLQISVTTNGNGYILANRIKRDIISHLPPNIS 185
Cdd:COG1648 85 VN---------ARVAAAARARGILVNVVDDPELCDFIV-PAIVD--RGPLVIAISTGGASPVLARRLRERLEALLPPEYG 152
|
170 180
....*....|....*....|....*....
gi 398365329 186 EVVINMGYLKDRIIN-----EDHKALLEE 209
Cdd:COG1648 153 DLAELLGRLRERVKArlpdgAERRRFWER 181
|
|
| Precorrin_2_C20_MT |
cd11645 |
Precorrin-2 C20-methyltransferase, also named CobI or CbiL; Precorrin-2 C20-methyltransferase ... |
331-537 |
2.98e-12 |
|
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: 66.38 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADII-----------LADKLVPQAILDLIPPKTETFIAKKFPGNAERAQQELLAKGLES 399
Cdd:cd11645 1 VGVGPGDPELLTLKAVRILKEADVIfvpvskggegsAALIIAAALLIPDKEIIPLEFPMTKDREELEEAWDEAAEEIAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 400 LDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDiaDQVLICTGTGRKGALPIIP 479
Cdd:cd11645 81 LKEGKDVAFLTLGDPSLYSTFSYLLERLRAPGVEVEIIPGITSFSAAAARLGIPLAEGD--ESLAILPATYDEEELEKAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 398365329 480 EFVEsrtTVFLMALHRANVLITGLLK-HGWDGDvpAAIVERGSCPDQRVTRTLLKWVPE 537
Cdd:cd11645 159 ENFD---TVVLMKVGRNLEEIKELLEeLGLLDK--AVYVERCGMEGERIYTDLEELKEE 212
|
|
| cobI_cbiL |
TIGR01467 |
precorrin-2 C(20)-methyltransferase; This model represents precorrin-2 C(20)-methyltransferase, ... |
326-529 |
4.95e-11 |
|
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: 63.10 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIIL-------ADKLVPQAILDLIPPKTETFIAKKFPGNA-----ERAQQELL 393
Cdd:TIGR01467 1 GKLYGVGVGPGDPELITVKALEALRSADVIAvpaskkgRESLARKIVEDYLKPNDTRILELVFPMTKdrdelEKAWDEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 394 AKGLESLDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDiaDQVLICTGTGrkg 473
Cdd:TIGR01467 81 EAVAAELEEGRDVAFLTLGDPSLYSTFSYLLQRLQGMGIEVEVVPGITSFAACASAAGLPLVEGD--ESLAILPATA--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 474 alpiIPEFVESRT----TVFLMALHRANVLITGLLKHGWDGDVpAAIVERGSCPDQRVTR 529
Cdd:TIGR01467 156 ----GEAELEKALaefdTVVLMKVGRNLPQIKEALAKLGRLDA-AVVVERATMPDEKIVD 210
|
|
| PRK05787 |
PRK05787 |
cobalt-precorrin-7 (C(5))-methyltransferase; |
327-540 |
2.70e-10 |
|
cobalt-precorrin-7 (C(5))-methyltransferase;
Pssm-ID: 235609 [Multi-domain] Cd Length: 210 Bit Score: 60.27 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 327 KISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKfpgNAERAQQELLAKglesldnGLKV 406
Cdd:PRK05787 1 MIYIVGIGPGDPEYLTLKALEAIRKADVVVGSKRVLELFPELIDGEAFVLTAGL---RDLLEWLELAAK-------GKNV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 407 VRLKQGDPYIFGRGGEEFNFFKDHGYIPVVlPGISS-SLACtvlAQIpatQRDIADQVLIcTGTGRKGALPIIPEFVESR 485
Cdd:PRK05787 71 VVLSTGDPLFSGLGKLLKVRRAVAEDVEVI-PGISSvQYAA---ARL---GIDMNDVVFT-TSHGRGPNFEELEDLLKNG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 398365329 486 TTVFLMALHRANV--LITGLLKHGwDGDVPAAIVERGSCPDQRVTRTLLKWVPEVVE 540
Cdd:PRK05787 143 RKVIMLPDPRFGPkeIAAELLERG-KLERRIVVGENLSYPDERIHKLTLSEIEPLEF 198
|
|
| Precorrin-6Y-MT |
cd11644 |
Precorrin-6Y methyltransferase (also named CbiE); CbiE (precorrin-6Y methyltransferase, also ... |
331-552 |
1.17e-09 |
|
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: 58.27 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 331 VGSGPGSVSMLTIGALQEIKSADIILADKlvpqAILDLIPPktetFIAKKFPGNAERaqqelLAKGLESLDN-GLKVVRL 409
Cdd:cd11644 1 IGIGPGGPEYLTPEAREAIEEADVVIGAK----RLLELFPD----LGAEKIPLPSED-----IAELLEEIAEaGKRVVVL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 410 KQGDPYIFGRGgeefNFFKDH--GYIPVVLPGISS-SLACtvlAQIpatQRDIADqVLICTGTGRKGALpiIPEFVESRT 486
Cdd:cd11644 68 ASGDPGFYGIG----KTLLRRlgGEEVEVIPGISSvQLAA---ARL---GLPWED-ARLVSLHGRDLEN--LRRALRRGR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365329 487 TVFLMALHRANV--LITGLLKHGWdGDVPAAIVERGSCPDQRVTRTLLKwvpEVVEEIGSrPPGVLVV 552
Cdd:cd11644 135 KVFVLTDGKNTPaeIARLLLERGL-GDSRVTVGENLGYPDERITEGTAE---ELAEEEFS-DLNVVLI 197
|
|
| Precorrin_3B_C17_MT |
cd11646 |
Precorrin-3B C(17)-methyltransferase (also named CobJ or CbiH); Precorrin-3B C(17) ... |
328-446 |
7.38e-09 |
|
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: 56.65 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 328 ISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKteTFIAKKFPGNAERAQqellaKGLESLDNGLKVV 407
Cdd:cd11646 1 LYVVGIGPGSADLMTPRAREALEEADVIVGYKTYLDLIEDLLPGK--EVISSGMGEEVERAR-----EALELALEGKRVA 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 398365329 408 RLKQGDPYIFGRGGEEFNFFKDHGY-IPV-VLPGISSSLAC 446
Cdd:cd11646 74 LVSSGDPGIYGMAGLVLELLDERWDdIEVeVVPGITAALAA 114
|
|
| PRK05576 |
PRK05576 |
cobalt-factor II C(20)-methyltransferase; |
326-541 |
1.42e-08 |
|
cobalt-factor II C(20)-methyltransferase;
Pssm-ID: 235512 [Multi-domain] Cd Length: 229 Bit Score: 55.69 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIILA-------DKLVPQAILDLIPPKTETFIaKKFPGNA-----ERAQQELL 393
Cdd:PRK05576 2 GKLYGIGLGPGDPELLTVKAARILEEADVVYApasrkggGSLALNIVRPYLKEETEIVE-LHFPMSKdeeekEAVWKENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 394 AKGLESLDNGLKVVRLKQGDPYIFGRGGEEFNFFKDHGYIPVVLPGISSSLACTVLAQIPATQRDIADQVLICTGTGRKG 473
Cdd:PRK05576 81 EEIAAEAEEGKNVAFITLGDPNLYSTFSHLLEYLKCHDIEVETVPGISSFTAIASRAGVPLAMGDESLAIIPATREALIE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365329 474 ALPIIPEFVesrttVFLMALHRANvLITGLLKhgwDGDVPAAIVERGSCPDQRVTRtllkWVPEVVEE 541
Cdd:PRK05576 161 QALTDFDSV-----VLMKVYKNFA-LIEELLE---EGYLDALYVRRAYMEGEQILR----RLEEILDD 215
|
|
| PRK05765 |
PRK05765 |
precorrin-3B C17-methyltransferase; Provisional |
326-445 |
8.63e-08 |
|
precorrin-3B C17-methyltransferase; Provisional
Pssm-ID: 235597 Cd Length: 246 Bit Score: 53.63 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKteTFIAKKFPGNAERAQQElLAKGLEsldnGLK 405
Cdd:PRK05765 2 GKLYIVGIGPGSKEQRTIKAQEAIEKSNVIIGYNTYLRLISDLLDGK--EVIGARMKEEIFRANTA-IEKALE----GNI 74
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 398365329 406 VVRLKQGDPYIFGRGGEEFNFFKDHGyIPV---VLPGISSSLA 445
Cdd:PRK05765 75 VALVSSGDPQVYGMAGLVFELISRRK-LDVdveVIPGVTAALA 116
|
|
| cobJ_cbiH |
TIGR01466 |
precorrin-3B C17-methyltransferase; This model represents precorrin-3B C17-methyltransferase, ... |
328-446 |
2.92e-07 |
|
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: 51.92 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 328 ISLVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTetFIAKKFPGNAERAQqELLAKGLEsldnGLKVV 407
Cdd:TIGR01466 1 LYVVGIGPGAEELMTPEAKEALAEADVIVGYKTYLDLIEDLIPGKE--VVTSGMREEIARAE-LAIELAAE----GRTVA 73
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 398365329 408 RLKQGDPYIFGRGGEEFNFFKDHGYIP--VVLPGISSSLAC 446
Cdd:TIGR01466 74 LVSSGDPGIYGMAALVFEALEKKGAEVdiEVIPGITAASAA 114
|
|
| CbiE |
TIGR02467 |
precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; This model recognizes ... |
330-533 |
3.15e-07 |
|
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: 51.16 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 330 LVGSGPGSVSMLTIGALQEIKSADIILADKLVPQAILDLIPPKTETFIAKKfpgnaerAQQELLAKgLESLDNGLKVVRL 409
Cdd:TIGR02467 1 VVGIGPGGPELLTPAAIEAIRKADLVVGGERHLELLAELIGEKREIILTYK-------DLDELLEF-IAATRKEKRVVVL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 410 KQGDPYIFGRGG-EEFNFFKDhgyIPVVLPGISS-SLACtvlAQIpatQRDIADQVLIcTGTGRkGALPIIPEFVESRTT 487
Cdd:TIGR02467 73 ASGDPLFYGIGRtLAERLGKE---RLEIIPGISSvQYAF---ARL---GLPWQDAVVI-SLHGR-ELDELLLALLRGHRK 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 398365329 488 VFLMALHRANVLITG--LLKHGWDGDVPAAIVERGSCPDQRVTRTLLK 533
Cdd:TIGR02467 142 VAVLTDPRNGPAEIAreLIELGIGGSYELTVGENLGYEDERITEGTLE 189
|
|
| PRK05990 |
PRK05990 |
precorrin-2 C(20)-methyltransferase; Reviewed |
326-464 |
1.62e-06 |
|
precorrin-2 C(20)-methyltransferase; Reviewed
Pssm-ID: 180341 Cd Length: 241 Bit Score: 49.60 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 326 GKISLVGSGPGSVSMLTIGALQEIKSADI---------------ILADKLVP-QAILDLIPPKT----------ETFIAK 379
Cdd:PRK05990 3 GRLIGLGVGPGDPELLTLKALRLLQAAPVvayfvakgkkgnafgIVEAHLSPgQTLLPLVYPVTteilppplcyETVIAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 380 KFPGNAeraqqELLAkglESLDNGLKVVRLKQGDPYIFGrggeEFNFFKD---HGYIPVVLPGISSSLACTVLAQIPATQ 456
Cdd:PRK05990 83 FYDTSA-----EAVA---AHLDAGRDVAVICEGDPFFYG----SYMYLHDrlaPRYETEVIPGVCSMLGCWSVLGAPLVY 150
|
....*...
gi 398365329 457 RdiaDQVL 464
Cdd:PRK05990 151 R---NQSL 155
|
|
| cysG_Nterm |
TIGR01470 |
siroheme synthase, N-terminal domain; This model represents a subfamily of CysG N-terminal ... |
26-198 |
1.74e-06 |
|
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: 48.94 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 26 LLIGTGStdsvsVCKNRIHSILNAGGNPIVVNPSSPShtkQLQLeFGKFAKFEIVEREFRLSDLTtlGRVLVCKVVDrvf 105
Cdd:TIGR01470 13 LVVGGGD-----VALRKARLLLKAGAQLRVIAEELES---ELTL-LAEQGGITWLARCFDADILE--GAFLVIAATD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 106 vdlpitQSRLCEEIFWQCQKLRIPINTFHKPEFSTFnMIPTWVDPkgSGLQISVTTNGNGYILANRIKRDIISHLPPNIS 185
Cdd:TIGR01470 79 ------DEELNRRVAHAARARGVPVNVVDDPELCSF-IFPSIVDR--SPVVVAISSGGAAPVLARLLRERIETLLPPSLG 149
|
170
....*....|...
gi 398365329 186 EVVINMGYLKDRI 198
Cdd:TIGR01470 150 DLATLAATWRDAV 162
|
|
| cbiH |
PRK15478 |
precorrin-3B C(17)-methyltransferase; |
328-453 |
1.52e-05 |
|
precorrin-3B C(17)-methyltransferase;
Pssm-ID: 185375 [Multi-domain] Cd Length: 241 Bit Score: 46.80 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 328 ISLVGSGPGSVSMLTIGALQEIKSADIILAdklvpqaildlipPKTETFIAKKFPGNAERAQQ------ELLAKGLESLD 401
Cdd:PRK15478 2 LSVIGIGPGSQAMMTMEAIEALQAAEIVVG-------------YKTYTHLVKAFTGDKQVIKTgmckeiERCQAAIELAQ 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 398365329 402 NGLKVVRLKQGDPYIFGRGGEEFNFFKDHGY-IPVVL-PGISSSLACTVLAQIP 453
Cdd:PRK15478 69 AGHNVALISSGDAGIYGMAGLVLELVSKQKLdVEVRLiPGMTASIAAASLLGAP 122
|
|
| NAD_binding_7 |
pfam13241 |
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria. |
21-141 |
4.53e-05 |
|
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
Pssm-ID: 433055 [Multi-domain] Cd Length: 104 Bit Score: 42.85 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365329 21 TDQVHLLIGTGStdsvsVCKNRIHSILNAGGNPIVVnpsSPSHTKQLQlefgkfAKFEIVEREFRlSDLttLGRVLVCKV 100
Cdd:pfam13241 6 RGKRVLVVGGGE-----VAARKARKLLEAGAKVTVV---SPEITPFLE------GLLDLIRREFE-GDL--DGADLVIAA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 398365329 101 VDrvfvdlpitQSRLCEEIFWQCQKLRIPINTFHKPEFSTF 141
Cdd:pfam13241 69 TD---------DPELNERIAALARARGILVNVADDPELCDF 100
|
|
| Sirohm_synth_M |
pfam14824 |
Sirohaem biosynthesis protein central; This is the central domain of a multifunctional enzyme ... |
155-179 |
9.55e-04 |
|
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: 36.60 E-value: 9.55e-04
|
| |
