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Conserved domains on  [gi|15608313|ref|NP_215689|]
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FO synthase [Mycobacterium tuberculosis H37Rv]

Protein Classification

radical SAM protein( domain architecture ID 11483668)

radical SAM protein generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfer of a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fbiC PRK09234
FO synthase; Reviewed
15-856 0e+00

FO synthase; Reviewed


:

Pssm-ID: 236422 [Multi-domain]  Cd Length: 843  Bit Score: 1636.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   15 PVVPPQANASALRRVLRRARDGVTLNVDEAAIAMTARGDELADLCASAARVRDAGLVSAGRHGPsgrlaISYSRKVFIPV 94
Cdd:PRK09234   3 PPQSPTPTASAMRRALRRARDGVTLDVDEAAVLLTARGDDLADLCASAARVRDAGLGAAGRPGV-----VTYSRKVFIPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   95 TRLCRDNCHYCTFVTVPGKLRAqgssTYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGERGYDSTLSYV 174
Cdd:PRK09234  78 TRLCRDRCHYCTFATVPGKLEA----AYLSPDEVLDIARAGAAAGCKEALFTLGDRPEDRWPEAREWLDERGYDSTLDYV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  175 RAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLFETKGLAHYGSPDKDPAVRLRVLTDAGRLSIP 254
Cdd:PRK09234 154 RAMAIRVLEETGLLPHLNPGVMSWSELARLKPVAPSMGMMLETTSRRLFEEKGGPHYGSPDKDPAVRLRVLEDAGRLSVP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  255 FTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLVLGPGMRIQAP 334
Cdd:PRK09234 234 FTTGILIGIGETLAERAESLFAIRKLHREYGHIQEVIVQNFRAKPDTAMAGVPDAGLEELLATIAVARLVLGPKMRIQAP 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  335 PNLVSGDECRALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGAAWIDPRVRGHV 414
Cdd:PRK09234 314 PNLVSGDECAALLGAGIDDWGGVSPLTPDHVNPERPWPQLDELAAVTAEAGFTLVERLTAYPEYVRAGEPWIDPRLRGHV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  415 VALADPATGLAR-DVNPVGMPWQEPDDVASWGRVDLGAAIDTQGRNTAVRSDLASAFGDWESIREqvHELAVRAPERIDT 493
Cdd:PRK09234 394 AALADPETGLAReDAWPVGRPWQEPDEGWSSGRTDLHTAIDTEGRTTDRRSDFDSAYGDWESIRE--QVHEGRAPERIDT 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  494 DVLAALRSAERAPAGCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGD 573
Cdd:PRK09234 472 DVLAALRAAERDPAGLTDDEALALFTADGPALEAVCRLADDLRRDVVGDDVTYVVNRNINFTNICYTGCRFCAFAQRKTD 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  574 ADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWL 653
Cdd:PRK09234 552 ADAYTLSLDEVADRAWEAWVAGATEVCMQGGIHPELPGTGYADLVRAVKARVPSMHVHAFSPMEIVNGAARLGLSIREWL 631
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  654 IGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRT 733
Cdd:PRK09234 632 TALREAGLDTIPGTAAEILDDEVRWVLTKGKLPTAEWIEVVTTAHEVGLRSSSTMMYGHVDTPRHWVAHLRVLRDIQDRT 711
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  734 GGFTEFVPLPFVHQNSPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLME 813
Cdd:PRK09234 712 GGFTEFVPLPFVHQNAPLYLAGAARPGPTHRENRAVHALARIMLHGRIDNIQTSWVKLGVEGTRAMLRGGANDLGGTLME 791
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 15608313  814 ETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTYALLAA 856
Cdd:PRK09234 792 ETISRMAGSEHGSAKTVAELEAIAEGAGRPARQRTTLYGPVAA 834
 
Name Accession Description Interval E-value
fbiC PRK09234
FO synthase; Reviewed
15-856 0e+00

FO synthase; Reviewed


Pssm-ID: 236422 [Multi-domain]  Cd Length: 843  Bit Score: 1636.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   15 PVVPPQANASALRRVLRRARDGVTLNVDEAAIAMTARGDELADLCASAARVRDAGLVSAGRHGPsgrlaISYSRKVFIPV 94
Cdd:PRK09234   3 PPQSPTPTASAMRRALRRARDGVTLDVDEAAVLLTARGDDLADLCASAARVRDAGLGAAGRPGV-----VTYSRKVFIPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   95 TRLCRDNCHYCTFVTVPGKLRAqgssTYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGERGYDSTLSYV 174
Cdd:PRK09234  78 TRLCRDRCHYCTFATVPGKLEA----AYLSPDEVLDIARAGAAAGCKEALFTLGDRPEDRWPEAREWLDERGYDSTLDYV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  175 RAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLFETKGLAHYGSPDKDPAVRLRVLTDAGRLSIP 254
Cdd:PRK09234 154 RAMAIRVLEETGLLPHLNPGVMSWSELARLKPVAPSMGMMLETTSRRLFEEKGGPHYGSPDKDPAVRLRVLEDAGRLSVP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  255 FTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLVLGPGMRIQAP 334
Cdd:PRK09234 234 FTTGILIGIGETLAERAESLFAIRKLHREYGHIQEVIVQNFRAKPDTAMAGVPDAGLEELLATIAVARLVLGPKMRIQAP 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  335 PNLVSGDECRALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGAAWIDPRVRGHV 414
Cdd:PRK09234 314 PNLVSGDECAALLGAGIDDWGGVSPLTPDHVNPERPWPQLDELAAVTAEAGFTLVERLTAYPEYVRAGEPWIDPRLRGHV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  415 VALADPATGLAR-DVNPVGMPWQEPDDVASWGRVDLGAAIDTQGRNTAVRSDLASAFGDWESIREqvHELAVRAPERIDT 493
Cdd:PRK09234 394 AALADPETGLAReDAWPVGRPWQEPDEGWSSGRTDLHTAIDTEGRTTDRRSDFDSAYGDWESIRE--QVHEGRAPERIDT 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  494 DVLAALRSAERAPAGCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGD 573
Cdd:PRK09234 472 DVLAALRAAERDPAGLTDDEALALFTADGPALEAVCRLADDLRRDVVGDDVTYVVNRNINFTNICYTGCRFCAFAQRKTD 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  574 ADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWL 653
Cdd:PRK09234 552 ADAYTLSLDEVADRAWEAWVAGATEVCMQGGIHPELPGTGYADLVRAVKARVPSMHVHAFSPMEIVNGAARLGLSIREWL 631
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  654 IGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRT 733
Cdd:PRK09234 632 TALREAGLDTIPGTAAEILDDEVRWVLTKGKLPTAEWIEVVTTAHEVGLRSSSTMMYGHVDTPRHWVAHLRVLRDIQDRT 711
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  734 GGFTEFVPLPFVHQNSPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLME 813
Cdd:PRK09234 712 GGFTEFVPLPFVHQNAPLYLAGAARPGPTHRENRAVHALARIMLHGRIDNIQTSWVKLGVEGTRAMLRGGANDLGGTLME 791
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 15608313  814 ETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTYALLAA 856
Cdd:PRK09234 792 ETISRMAGSEHGSAKTVAELEAIAEGAGRPARQRTTLYGPVAA 834
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
509-851 0e+00

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 616.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   509 CTDGEYLALATADGpALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRA 588
Cdd:TIGR03551   1 ITKEEALELFEARG-NLFELFRLADELRRDIVGDTVTYVVNRNINFTNVCYGGCGFCAFRKRKGDADAYLLSLEEIAERA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   589 WEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTA 668
Cdd:TIGR03551  80 AEAWKAGATEVCIQGGIHPDLDGDFYLDILRAVKEEVPGMHIHAFSPMEVYYGARNSGLSVEEALKRLKEAGLDSMPGTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   669 AEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQN 748
Cdd:TIGR03551 160 AEILDDEVRKVICPDKLSTAEWIEIIKTAHKLGIPTTATIMYGHVETPEHWVDHLLILREIQEETGGFTEFVPLPFVHYN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   749 SPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAK 828
Cdd:TIGR03551 240 APLYLKGMARPGPTGREDLKVHAIARILLHGLIDNIQASWVKLGKKLAQVALRCGANDLGGTLMEESISRAAGASHGEYL 319
                         330       340
                  ....*....|....*....|...
gi 15608313   829 TVAELVAIAEGIGRPARQRTTTY 851
Cdd:TIGR03551 320 SPEELEAIIEDAGRIPKQRTTLY 342
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
494-851 3.80e-164

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 480.78  E-value: 3.80e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 494 DVLAALRSAERapagCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGD 573
Cdd:COG1060   1 EILEKALAGER----LSLEDALALLSPAAADLEELAELADELRRRRFGNTVTFVVNRPINLTNVCVNGCKFCAFSRDNGD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 574 ADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWL 653
Cdd:COG1060  77 IDRYTLSPEEILEEAEEAKALGATEILLVGGEHPDLPLEYYLDLLRAIKERFPNIHIHALSPEEIAHLARASGLSVEEVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 654 IGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRT 733
Cdd:COG1060 157 ERLKEAGLDSLPGGGAEILDDEVRHPIGPGKIDYEEWLEVMERAHELGIRTTATMLYGHVETREERVDHLLHLRELQDET 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 734 GGFTEFVPLPFVHQNSPLYLagaARPGPSHRDNRAVHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLME 813
Cdd:COG1060 237 GGFTEFIPLRFRPANTPLYL---ERPGVSDRELLKLIAVARLFLPN-IGNIQASWVSLGTRLRQLALSLGANDLGGTSME 312
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15608313 814 ETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTY 851
Cdd:COG1060 313 ENIVRAAGGEEGDERSVEELIRLIREAGRIPVERDTLY 350
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
554-712 2.40e-15

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 74.10  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   554 FTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGiDPELPVTGYADLVRAVKARVPSMHVHAF 633
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGG-EPLLLPDLVELLERLLKLELAEGIRITL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608313   634 SpmeiangvTKSGLSIREWLIGLREAGLDTIpGTAAEILDDEVRWvLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGH 712
Cdd:pfam04055  80 E--------TNGTLLDEELLELLKEAGLDRV-SIGLESGDDEVLK-LINRGHTFEEVLEALELLREAGIPVVTDNIVGL 148
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
552-721 2.11e-11

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 64.28  E-value: 2.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 552 INFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGiDPELPVtGYADLVRAVKARVPSMHVH 631
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGG-EPLLYP-ELAELLRRLKKELPGFEIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 632 AfspmeiangVTKSGLSIREWLIGLREAGLDTIpGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYG 711
Cdd:cd01335  79 I---------ETNGTLLTEELLKELKELGLDGV-GVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVG 148
                       170
                ....*....|
gi 15608313 712 HVDSPRHWVA 721
Cdd:cd01335 149 LGDEDEEDDL 158
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
88-308 3.24e-09

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 57.80  E-value: 3.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313     88 RKVFIPVTRLCRDNCHYCTFVTVPGKLRaqgsSTYMEP--DEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGER 165
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGKLR----SRYLEAlvREIELLAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    166 gydstLSYVRAMAIRVleqtGLLPHLNPGVMSWS---EMSRLKPVAPSMGmmLETTSRRLFETKGLAHygsPDKDPAVRL 242
Cdd:smart00729  77 -----IREILGLAKDV----EITIETRPDTLTEElleALKEAGVNRVSLG--VQSGDDEVLKAINRGH---TVEDVLEAV 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608313    243 RVLTDAGRLSIpfTTGLLVGI-GETLSERADTLHAIRKshkefGHIQEVIVQNFRAKEHTAMAAFPD 308
Cdd:smart00729 143 ELLREAGPIKV--STDLIVGLpGETEEDFEETLKLLKE-----LGPDRVSIFPLSPRPGTPLAKMYK 202
 
Name Accession Description Interval E-value
fbiC PRK09234
FO synthase; Reviewed
15-856 0e+00

FO synthase; Reviewed


Pssm-ID: 236422 [Multi-domain]  Cd Length: 843  Bit Score: 1636.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   15 PVVPPQANASALRRVLRRARDGVTLNVDEAAIAMTARGDELADLCASAARVRDAGLVSAGRHGPsgrlaISYSRKVFIPV 94
Cdd:PRK09234   3 PPQSPTPTASAMRRALRRARDGVTLDVDEAAVLLTARGDDLADLCASAARVRDAGLGAAGRPGV-----VTYSRKVFIPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   95 TRLCRDNCHYCTFVTVPGKLRAqgssTYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGERGYDSTLSYV 174
Cdd:PRK09234  78 TRLCRDRCHYCTFATVPGKLEA----AYLSPDEVLDIARAGAAAGCKEALFTLGDRPEDRWPEAREWLDERGYDSTLDYV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  175 RAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLFETKGLAHYGSPDKDPAVRLRVLTDAGRLSIP 254
Cdd:PRK09234 154 RAMAIRVLEETGLLPHLNPGVMSWSELARLKPVAPSMGMMLETTSRRLFEEKGGPHYGSPDKDPAVRLRVLEDAGRLSVP 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  255 FTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLVLGPGMRIQAP 334
Cdd:PRK09234 234 FTTGILIGIGETLAERAESLFAIRKLHREYGHIQEVIVQNFRAKPDTAMAGVPDAGLEELLATIAVARLVLGPKMRIQAP 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  335 PNLVSGDECRALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGAAWIDPRVRGHV 414
Cdd:PRK09234 314 PNLVSGDECAALLGAGIDDWGGVSPLTPDHVNPERPWPQLDELAAVTAEAGFTLVERLTAYPEYVRAGEPWIDPRLRGHV 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  415 VALADPATGLAR-DVNPVGMPWQEPDDVASWGRVDLGAAIDTQGRNTAVRSDLASAFGDWESIREqvHELAVRAPERIDT 493
Cdd:PRK09234 394 AALADPETGLAReDAWPVGRPWQEPDEGWSSGRTDLHTAIDTEGRTTDRRSDFDSAYGDWESIRE--QVHEGRAPERIDT 471
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  494 DVLAALRSAERAPAGCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGD 573
Cdd:PRK09234 472 DVLAALRAAERDPAGLTDDEALALFTADGPALEAVCRLADDLRRDVVGDDVTYVVNRNINFTNICYTGCRFCAFAQRKTD 551
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  574 ADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWL 653
Cdd:PRK09234 552 ADAYTLSLDEVADRAWEAWVAGATEVCMQGGIHPELPGTGYADLVRAVKARVPSMHVHAFSPMEIVNGAARLGLSIREWL 631
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  654 IGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRT 733
Cdd:PRK09234 632 TALREAGLDTIPGTAAEILDDEVRWVLTKGKLPTAEWIEVVTTAHEVGLRSSSTMMYGHVDTPRHWVAHLRVLRDIQDRT 711
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  734 GGFTEFVPLPFVHQNSPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLME 813
Cdd:PRK09234 712 GGFTEFVPLPFVHQNAPLYLAGAARPGPTHRENRAVHALARIMLHGRIDNIQTSWVKLGVEGTRAMLRGGANDLGGTLME 791
                        810       820       830       840
                 ....*....|....*....|....*....|....*....|...
gi 15608313  814 ETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTYALLAA 856
Cdd:PRK09234 792 ETISRMAGSEHGSAKTVAELEAIAEGAGRPARQRTTLYGPVAA 834
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
509-851 0e+00

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 616.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   509 CTDGEYLALATADGpALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRA 588
Cdd:TIGR03551   1 ITKEEALELFEARG-NLFELFRLADELRRDIVGDTVTYVVNRNINFTNVCYGGCGFCAFRKRKGDADAYLLSLEEIAERA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   589 WEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTA 668
Cdd:TIGR03551  80 AEAWKAGATEVCIQGGIHPDLDGDFYLDILRAVKEEVPGMHIHAFSPMEVYYGARNSGLSVEEALKRLKEAGLDSMPGTA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   669 AEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQN 748
Cdd:TIGR03551 160 AEILDDEVRKVICPDKLSTAEWIEIIKTAHKLGIPTTATIMYGHVETPEHWVDHLLILREIQEETGGFTEFVPLPFVHYN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   749 SPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAK 828
Cdd:TIGR03551 240 APLYLKGMARPGPTGREDLKVHAIARILLHGLIDNIQASWVKLGKKLAQVALRCGANDLGGTLMEESISRAAGASHGEYL 319
                         330       340
                  ....*....|....*....|...
gi 15608313   829 TVAELVAIAEGIGRPARQRTTTY 851
Cdd:TIGR03551 320 SPEELEAIIEDAGRIPKQRTTLY 342
F420_cofG TIGR03550
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents ...
85-414 0e+00

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents either a subunit or a domain, depending on whether or not the genes are fused, of a bifunctional protein that completes the synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, or FO. FO is the chromophore of coenzyme F(420), involved in methanogenesis in methanogenic archaea but found in certain other lineages as well. The chromophore also occurs as a cofactor in DNA photolyases in Cyanobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132589 [Multi-domain]  Cd Length: 322  Bit Score: 572.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    85 SYSRKVFIPVTRLCRDNCHYCTFVTVPGKLRAQgsstYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGE 164
Cdd:TIGR03550   1 TYSRNVFIPLTRLCRNRCGYCTFRRPPGELEAA----LLSPEEVLEILRKGAAAGCTEALFTFGEKPEERYPEAREWLAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   165 RGYDSTLSYVRAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLfeTKGLAHYGSPDKDPAVRLRV 244
Cdd:TIGR03550  77 MGYDSTLEYLRELCELALEETGLLPHTNPGVMSRDELARLKPVNASMGLMLETTSERL--CKGEAHYGSPGKDPAVRLET 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   245 LTDAGRLSIPFTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLV 324
Cdd:TIGR03550 155 IEDAGRLKIPFTTGILIGIGETREERAESLLAIRELHERYGHIQEVIVQNFRAKPGTPMENHPEPSLEEMLRTVAVARLI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   325 LGPGMRIQAPPNLVSGDeCRALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGaa 404
Cdd:TIGR03550 235 LPPDISIQVPPNLNRED-YRLLLDAGIDDWGGVSPVTPDHVNPEAPWPEIDELARATEEAGFTLKERLPVYPEYVREG-- 311
                         330
                  ....*....|
gi 15608313   405 WIDPRVRGHV 414
Cdd:TIGR03550 312 WLSPRISEHI 321
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
517-851 1.78e-167

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 490.17  E-value: 1.78e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  517 LATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGA 596
Cdd:PRK07360  29 LETTEPRRIFEILELADRLRKEQVGDTVTYVVNRNINFTNICEGHCGFCAFRRDEGDHGAFWLTIAEILEKAAEAVKRGA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  597 TEVCMQGGIDPELPVTG-YADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDE 675
Cdd:PRK07360 109 TEVCIQGGLHPAADSLEfYLEILEAIKEEFPDIHLHAFSPMEVYFAAREDGLSYEEVLKALKDAGLDSMPGTAAEILVDE 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  676 VRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPLYLAG 755
Cdd:PRK07360 189 VRRIICPEKIKTAEWIEIVKTAHKLGLPTTSTMMYGHVETPEHRIDHLLILREIQQETGGITEFVPLPFVHENAPLYERG 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  756 AARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKTVAELVA 835
Cdd:PRK07360 269 RVKGGAPGLEDLLLYAVSRIFLGNWIKNIQASWVKLGLKLAQVALNCGANDLGGTLMEEHITKMAGASGGTYMSVEELQW 348
                        330
                 ....*....|....*.
gi 15608313  836 IAEGIGRPARQRTTTY 851
Cdd:PRK07360 349 MIKSIGRIPKQRDTLY 364
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
494-851 3.80e-164

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 480.78  E-value: 3.80e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 494 DVLAALRSAERapagCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGD 573
Cdd:COG1060   1 EILEKALAGER----LSLEDALALLSPAAADLEELAELADELRRRRFGNTVTFVVNRPINLTNVCVNGCKFCAFSRDNGD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 574 ADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWL 653
Cdd:COG1060  77 IDRYTLSPEEILEEAEEAKALGATEILLVGGEHPDLPLEYYLDLLRAIKERFPNIHIHALSPEEIAHLARASGLSVEEVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 654 IGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRT 733
Cdd:COG1060 157 ERLKEAGLDSLPGGGAEILDDEVRHPIGPGKIDYEEWLEVMERAHELGIRTTATMLYGHVETREERVDHLLHLRELQDET 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 734 GGFTEFVPLPFVHQNSPLYLagaARPGPSHRDNRAVHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLME 813
Cdd:COG1060 237 GGFTEFIPLRFRPANTPLYL---ERPGVSDRELLKLIAVARLFLPN-IGNIQASWVSLGTRLRQLALSLGANDLGGTSME 312
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15608313 814 ETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTY 851
Cdd:COG1060 313 ENIVRAAGGEEGDERSVEELIRLIREAGRIPVERDTLY 350
cofG PRK06245
FO synthase subunit 1; Reviewed
84-426 3.39e-155

FO synthase subunit 1; Reviewed


Pssm-ID: 180485 [Multi-domain]  Cd Length: 336  Bit Score: 457.43  E-value: 3.39e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   84 ISYSRKVFIPVTRLCRDNCHYCTFVTVPGKlraqgsSTYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLG 163
Cdd:PRK06245   8 VTYSRNVFIPLTYECRNRCGYCTFRRDPGQ------PSLLSPEEVKEILRRGADAGCTEALFTFGEVPDESYERIKEQLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  164 ERGYDSTLSYVRAMAIRVLEQtGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLFETkglAHYGSPDKDPAVRLR 243
Cdd:PRK06245  82 EMGYSSILEYLYDLCELALEE-GLLPHTNAGILTREEMEKLKEVNASMGLMLEQTSPRLLNT---VHRGSPGKDPELRLE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  244 VLTDAGRLSIPFTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARL 323
Cdd:PRK06245 158 TIENAGKLKIPFTTGILIGIGETWEDRAESLEAIAELHERYGHIQEVIIQNFSPKPGIPMENHPEPSLEEMLRVVALARL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  324 VLGPGMRIQAPPNLVSGDECrALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGa 403
Cdd:PRK06245 238 ILPPDISIQVPPNLNRDTGL-LLLDAGADDLGGISPVTKDYVNPEYPWPDIEELREILEEAGWPLKERLPVYPKYIKEG- 315
                        330       340
                 ....*....|....*....|...
gi 15608313  404 aWIDPRVRGHVVALADPAtGLAR 426
Cdd:PRK06245 316 -WLSERLQELIEALSDAG-GYRR 336
TIGR00423 TIGR00423
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
544-854 1.85e-132

radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of coenzyme F(420) biosynthesis from Methanocaldococcus jannaschii, but appears to hit genomes more broadly than just the subset that make coenzyme F(420), so that narrower group is being built as a separate family. [Hypothetical proteins, Conserved]


Pssm-ID: 273071 [Multi-domain]  Cd Length: 309  Bit Score: 397.92  E-value: 1.85e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   544 VTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKA 623
Cdd:TIGR00423   1 VTFVVNRNINFTNICVGKCKFCAFRAREKDKDAYVLSLEEILEKVKEAVAKGATEVCIQGGLNPQLDIEYYEELFRAIKQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   624 RVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLR 703
Cdd:TIGR00423  81 EFPDVHIHAFSPMEVYFLAKNEGLSIEEVLKRLKKAGLDSMPGTGAEILDDSVRRKICPNKLSSDEWLEVIKTAHRLGIP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   704 SSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPlYLAGAARPGPSHRDNRAVHALARIMLhGRISH 783
Cdd:TIGR00423 161 TTATMMFGHVENPEHRVEHLLRIRKIQEKTGGFTEFIPLPFQPENNP-YLEGEVRKGASGIDDLKVIAISRILL-NNIRN 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608313   784 IQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTYALL 854
Cdd:TIGR00423 239 IQASWVKLGLKLAQVALEFGANDLGGTLMEENISKAAGAKSGVGLTVEELIEAIKDAGRVPAQRDTLYNIL 309
menaquin_MqnC TIGR03699
dehypoxanthine futalosine cyclase; members of this protein family are involved in menaquinone ...
511-854 2.70e-115

dehypoxanthine futalosine cyclase; members of this protein family are involved in menaquinone biosynthesis by an alternate pathway via futalosine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 274731 [Multi-domain]  Cd Length: 340  Bit Score: 354.64  E-value: 2.70e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   511 DGEYLaLATADgpaLEAVAALADSLRRDV-VGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAW 589
Cdd:TIGR03699   7 EALEL-YKEAD---LLALGALADEVRRRRhPGNVVTFVVDRNINYTNICVVGCKFCAFYRPPGHPEGYVLSVEEILQKIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   590 EAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAA 669
Cdd:TIGR03699  83 ELVAYGGTQILLQGGVNPDLGLDYYEDLFRAIKARFPHIHIHGFSPVEIVYIAKKEGLSLREVLERLKEAGLDSIPGGGA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   670 EILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNS 749
Cdd:TIGR03699 163 EILSDRVRRIISPKKISSEEWLEVMETAHKLGLPTTATMMFGHVETLEERIEHLERIRELQDKTGGFTAFIPWTFQPGNT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   750 PLylaGAARPGPSHRDNRAVhALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKt 829
Cdd:TIGR03699 243 EL---GKKRPATSTEYLKVL-AISRIFLDN-IPNIQASWVTQGKEVGQLALHFGANDFGSTMIEENVVAAAGASHRASR- 316
                         330       340
                  ....*....|....*....|....*
gi 15608313   830 vAELVAIAEGIGRPARQRTTTYALL 854
Cdd:TIGR03699 317 -EEIIRIIREAGFIPAQRDTLYNIL 340
mena_SCO4494 TIGR03700
putative menaquinone biosynthesis radical SAM enzyme, SCO4494 family; Members of this protein ...
516-851 9.83e-100

putative menaquinone biosynthesis radical SAM enzyme, SCO4494 family; Members of this protein family appear to be involved in menaquinone biosynthesis by an alternate pathway via futalosine, based on close phylogenetic correlation with known markers of the futalosine pathway, gene clustering in many organisms, and paralogy with the SCO4550 protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 213851 [Multi-domain]  Cd Length: 351  Bit Score: 314.31  E-value: 9.83e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   516 ALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAG 595
Cdd:TIGR03700  16 GLFLYASDDLLTLGELAALVRERKHGDKVYFNVNRHLNYTNICVNGCAFCAFQRERGEPGAYAMSLEEIVARVKEAYAPG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   596 ATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDE 675
Cdd:TIGR03700  96 ATEVHIVGGLHPNLPFEWYLDMIRTLKEAYPDLHVKAFTAVEIHHFSKISGLPTEEVLDELKEAGLDSMPGGGAEIFAEE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   676 VRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSplYLAG 755
Cdd:TIGR03700 176 VRQQICPEKISAERWLEIHRTAHELGLKTNATMLYGHIETPAHRVDHMLRLRELQDETGGFQAFIPLAFQPDNN--RLNR 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   756 AARPGPSHRDNRAVHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKTVAELVA 835
Cdd:TIGR03700 254 LLAKGPTGLDDLKTLAVSRLYLDN-IPHIKAYWVMLGLKLAQVALAFGVNDLDGTVVEEKIGHDAGAKSPQALSKDELVR 332
                         330
                  ....*....|....*.
gi 15608313   836 IAEGIGRPARQRTTTY 851
Cdd:TIGR03700 333 LIRDAGRVPVERDTLY 348
PRK08445 PRK08445
dehypoxanthine futalosine cyclase;
545-854 3.78e-76

dehypoxanthine futalosine cyclase;


Pssm-ID: 181427 [Multi-domain]  Cd Length: 348  Bit Score: 251.57  E-value: 3.78e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  545 TFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKAR 624
Cdd:PRK08445  39 TFIVDRNINYTNICWVDCKFCAFYRHLKEDDAYILSFEEIDKKIEELLAIGGTQILFQGGVHPKLKIEWYENLVSHIAQK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  625 VPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRS 704
Cdd:PRK08445 119 YPTITIHGFSAVEIDYIAKISKISIKEVLERLQAKGLSSIPGAGAEILSDRVRDIIAPKKLDSDRWLEVHRQAHLIGMKS 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  705 SSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPLYLAGAA-RPGPSHRDNRAVhALARIMLHgRISH 783
Cdd:PRK08445 199 TATMMFGTVENDEEIIEHWERIRDLQDETGGFRAFILWSFQPDNTPLKEEIPEiKKQSSNRYLRLL-AVSRLFLD-NFKN 276
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608313  784 IQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKtvAELVAIAEGIGRPARQRTTTYALL 854
Cdd:PRK08445 277 IQSSWVTQGSYIGQLALLFGANDLGSTMMEENVVKAAGASFRMNQ--AEMIELIKDIGEIPAKRNTAYEIL 345
PRK05927 PRK05927
dehypoxanthine futalosine cyclase;
525-839 1.20e-59

dehypoxanthine futalosine cyclase;


Pssm-ID: 135660 [Multi-domain]  Cd Length: 350  Bit Score: 207.04  E-value: 1.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  525 LEAVAALADSLRRD-VVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQG 603
Cdd:PRK05927  21 LEELQEHADSLRKQrYPQNTVTYVLDANPNYTNICKIDCTFCAFYRKPHSSDAYLLSFDEFRSLMQRYVSAGVKTVLLQG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  604 GIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKG 683
Cdd:PRK05927 101 GVHPQLGIDYLEELVRITVKEFPSLHPHFFSAVEIAHAAQVSGISTEQALERLWDAGQRTIPGGGAEILSERVRKIISPK 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  684 KLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPL--YLAGAARPGP 761
Cdd:PRK05927 181 KMGPDGWIQFHKLAHRLGFRSTATMMFGHVESPEDILLHLQTLRDAQDENPGFYSFIPWSYKPGNTALgrRVPHQASPEL 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15608313  762 SHRdnraVHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKTVAELVAIAEG 839
Cdd:PRK05927 261 YYR----ILAVARIFLDN-FDHIAASWFGEGKEEGAKGLHYGADDFGGTILDESVHKCTGWDLQSSEEEICAMILSEG 333
PRK08444 PRK08444
aminofutalosine synthase MqnE;
529-834 2.34e-59

aminofutalosine synthase MqnE;


Pssm-ID: 181426 [Multi-domain]  Cd Length: 353  Bit Score: 206.08  E-value: 2.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  529 AALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAF-AQRKGDaDAYSLSVGEVADRAWEAHVAGATEVCMQGGIDP 607
Cdd:PRK08444  30 GKYADKKRTKLHGKKVYFNVNRHINPTNICADVCKFCAFsAHRKNP-NPYTMSHEEILEIVKNSVKRGIKEVHIVSAHNP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  608 ELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPT 687
Cdd:PRK08444 109 NYGYEWYLEIFKKIKEAYPNLHVKAMTAAEVDFLSRKFGKSYEEVLEDMLEYGVDSMPGGGAEIFDEEVRKKICKGKVSS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  688 SLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLpfVHQNSPLYLAGAARPGPShrDNR 767
Cdd:PRK08444 189 ERWLEIHKYWHKKGKMSNATMLFGHIENREHRIDHMLRLRDLQDKTGGFNAFIPL--VYQRENNYLKVEKFPSSQ--EIL 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  768 AVHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAG--SEHG-SAKTVAELV 834
Cdd:PRK08444 265 KTIAISRILLDN-IPHIKAYWATLTLNLALVAQEFGANDLDGTIEKESIQSAAGakSANGlSLEDFIFLI 333
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
35-393 5.93e-59

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 204.98  E-value: 5.93e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  35 DGVTLNVDEAAIAMTARGDELADLCASAARVRDAglvsagRHGPSgrlaISYSRKVFIPVTRLCRDNCHYCTFVTVPGKL 114
Cdd:COG1060   8 AGERLSLEDALALLSPAAADLEELAELADELRRR------RFGNT----VTFVVNRPINLTNVCVNGCKFCAFSRDNGDI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 115 RAqgssTYMEPDEILDVARRGAEFGCKEALFTLGDRPearwrqarewlgergyDSTLSYVRAMAIRVLEQtglLPHLNPG 194
Cdd:COG1060  78 DR----YTLSPEEILEEAEEAKALGATEILLVGGEHP----------------DLPLEYYLDLLRAIKER---FPNIHIH 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 195 VMSWSEMSRLKPV-------------APSMGMMLETTSRRLFETkgLAHYGSPDKDPAV-RLRVLTDAGRLSIPFTTGLL 260
Cdd:COG1060 135 ALSPEEIAHLARAsglsveevlerlkEAGLDSLPGGGAEILDDE--VRHPIGPGKIDYEeWLEVMERAHELGIRTTATML 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 261 VGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKeHTAMA-AFPDAGIEDYLATVAVARLVLGPGMRIQAPPNLVS 339
Cdd:COG1060 213 YGHVETREERVDHLLHLRELQDETGGFTEFIPLRFRPA-NTPLYlERPGVSDRELLKLIAVARLFLPNIGNIQASWVSLG 291
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15608313 340 GDECRALVGAGVDDWGGVSPLtpDHVNP-----ERPWPALDELAAVTAEAGYDMVQRLT 393
Cdd:COG1060 292 TRLRQLALSLGANDLGGTSME--ENIVRaaggeEGDERSVEELIRLIREAGRIPVERDT 348
PRK05926 PRK05926
hypothetical protein; Provisional
526-823 2.26e-48

hypothetical protein; Provisional


Pssm-ID: 168296 [Multi-domain]  Cd Length: 370  Bit Score: 175.81  E-value: 2.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  526 EAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAgATEVCMQGGI 605
Cdd:PRK05926  46 RALWSFADLIRANRVGDTVYYSSTLYLYPTNFCQFNCTFCSFYAKPGDPKGWFYTPDQLVQSIKENPSP-ITETHIVAGC 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  606 DPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKGKL 685
Cdd:PRK05926 125 FPSCNLAYYEELFSKIKQNFPDLHIKALTAIEYAYLSKLDNLPVKEVLQTLKIAGLDSIPGGGAEILVDEIRETLAPGRL 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  686 PTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPLylaGAA--RPGPSH 763
Cdd:PRK05926 205 SSQGFLEIHKTAHSLGIPSNATMLCYHRETPEDIVTHMSKLRALQDKTSGFKNFILLKFASENNAL---GKRlrKMGSRH 281
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15608313  764 RDNRA-VHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSE 823
Cdd:PRK05926 282 SIPPAsIIAVARLFLDN-FPNIKALWNYLGIEVALHLLSCGANDLSSTHQGEKVFQMASSQ 341
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
554-712 2.40e-15

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 74.10  E-value: 2.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   554 FTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGiDPELPVTGYADLVRAVKARVPSMHVHAF 633
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGG-EPLLLPDLVELLERLLKLELAEGIRITL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15608313   634 SpmeiangvTKSGLSIREWLIGLREAGLDTIpGTAAEILDDEVRWvLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGH 712
Cdd:pfam04055  80 E--------TNGTLLDEELLELLKEAGLDRV-SIGLESGDDEVLK-LINRGHTFEEVLEALELLREAGIPVVTDNIVGL 148
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
38-325 3.22e-13

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 71.23  E-value: 3.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  38 TLNVDEAAIAMTARGDELADLCASAARVRDA---------GLVSAgrhgPSGRlaisysrkvfipvtrlCRDNCHYCtfv 108
Cdd:COG0502   1 DLTREEALALLELPDEELEDLLAAADEVREHffgnkvqlcGLINI----KSGG----------------CPEDCKYC--- 57
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 109 tvpgklrAQgSSTY---------MEPDEILDVARRGAEFGCKEalFTLGdrpearwrQArewlGERGYDSTLSYVRAMAI 179
Cdd:COG0502  58 -------GQ-SAHNktgieryrlLSVEEILEAARAAKEAGARR--FCLV--------AS----GRDPSDRDFEKVLEIVR 115
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 180 RVLEQTGLLPHLNPGVMSWSEMSRLKpvapSMGMM-----LETtSRRlfetkglaHYGS--PDKDPAVRLRVLTDAGRLS 252
Cdd:COG0502 116 AIKEELGLEVCASLGELSEEQAKRLK----EAGVDrynhnLET-SPE--------LYPKicTTHTYEDRLDTLKNAREAG 182
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15608313 253 IPFTTGLLVGIGETLSERADTLHAIRKShkefgHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLVL 325
Cdd:COG0502 183 LEVCSGGIVGMGETLEDRADLLLTLAEL-----DPDSVPINPLIPIPGTPLEDAPPLDPEEFLRTIAVARLLL 250
CofH_C pfam19288
CofH/MqnC C-terminal region; This entry represents the C-terminal half of the CofH and MqnC ...
735-851 3.74e-12

CofH/MqnC C-terminal region; This entry represents the C-terminal half of the CofH and MqnC enzymes. This entry is found to the C-terminus of pfam04055.


Pssm-ID: 437120 [Multi-domain]  Cd Length: 125  Bit Score: 64.03  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   735 GFTEFVPLPFVHQNSPLYLAGAARPGPSHRDNRAVHALARIMLHGrISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEE 814
Cdd:pfam19288   3 GFIAFIPWPFQDEGTLLKRLRGVRNDVSGDEYIRMIALSRIMLPN-IKNIQASWLTVGKQTAQICLHAGANDFGSIMIEE 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15608313   815 TISRMAGSEHG-SAKTVAElvAIAEGIGRPaRQRTTTY 851
Cdd:pfam19288  82 NVVSAAGAPHRfTAEGIQQ--AIREAGFEP-QLRNQLY 116
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
552-721 2.11e-11

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 64.28  E-value: 2.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 552 INFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGiDPELPVtGYADLVRAVKARVPSMHVH 631
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGG-EPLLYP-ELAELLRRLKKELPGFEIS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 632 AfspmeiangVTKSGLSIREWLIGLREAGLDTIpGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYG 711
Cdd:cd01335  79 I---------ETNGTLLTEELLKELKELGLDGV-GVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVG 148
                       170
                ....*....|
gi 15608313 712 HVDSPRHWVA 721
Cdd:cd01335 149 LGDEDEEDDL 158
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
510-662 8.49e-11

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 63.91  E-value: 8.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 510 TDGEYLALATADGPALEAVAALADSLRRDVVGDEV---TFvvnrnINF-TNICYTGCRFCAfaQRKG---DADAYSL-SV 581
Cdd:COG0502   3 TREEALALLELPDEELEDLLAAADEVREHFFGNKVqlcGL-----INIkSGGCPEDCKYCG--QSAHnktGIERYRLlSV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 582 GEVADRAWEAHVAGATEVCM-QGGIDP-ELPVTGYADLVRAVKARVpsmhvhafsPMEIAngvtksgLSI----REWLIG 655
Cdd:COG0502  76 EEILEAARAAKEAGARRFCLvASGRDPsDRDFEKVLEIVRAIKEEL---------GLEVC-------ASLgelsEEQAKR 139

                ....*..
gi 15608313 656 LREAGLD 662
Cdd:COG0502 140 LKEAGVD 146
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
94-273 1.64e-09

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 57.54  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    94 VTRLCRDNCHYCTFvtvpGKLRAQGSSTYMEPDEILDVARRGAEFGCKEALFTlGDRPEARWRQAREWLgergydstlsy 173
Cdd:pfam04055   1 ITRGCNLRCTYCAF----PSIRARGKGRELSPEEILEEAKELKRLGVEVVILG-GGEPLLLPDLVELLE----------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   174 vRAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPS-MGMMLETTSRRLfetkgLAHYGsPDKDPAVRLRVLTDAGRLS 252
Cdd:pfam04055  65 -RLLKLELAEGIRITLETNGTLLDEELLELLKEAGLDrVSIGLESGDDEV-----LKLIN-RGHTFEEVLEALELLREAG 137
                         170       180
                  ....*....|....*....|..
gi 15608313   253 IPFTTGLLVGI-GETLSERADT 273
Cdd:pfam04055 138 IPVVTDNIVGLpGETDEDLEET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
88-308 3.24e-09

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 57.80  E-value: 3.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313     88 RKVFIPVTRLCRDNCHYCTFVTVPGKLRaqgsSTYMEP--DEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGER 165
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFPSLRGKLR----SRYLEAlvREIELLAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    166 gydstLSYVRAMAIRVleqtGLLPHLNPGVMSWS---EMSRLKPVAPSMGmmLETTSRRLFETKGLAHygsPDKDPAVRL 242
Cdd:smart00729  77 -----IREILGLAKDV----EITIETRPDTLTEElleALKEAGVNRVSLG--VQSGDDEVLKAINRGH---TVEDVLEAV 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608313    243 RVLTDAGRLSIpfTTGLLVGI-GETLSERADTLHAIRKshkefGHIQEVIVQNFRAKEHTAMAAFPD 308
Cdd:smart00729 143 ELLREAGPIKV--STDLIVGLpGETEEDFEETLKLLKE-----LGPDRVSIFPLSPRPGTPLAKMYK 202
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
92-315 2.71e-08

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 55.03  E-value: 2.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313  92 IPVTRLCRDNCHYCTFVTVPGKLRaqgsSTYMEPDEILDVARRGAEFGCKEALFTLGDrPEARWRQARewlgergydstl 171
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGRGP----ESPPEIEEILDIVLEAKERGVEVVILTGGE-PLLYPELAE------------ 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313 172 sYVRAmAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPS-MGMMLETtsrrlFETKGLAHYGSPDKDPAVRLRVLTDAGR 250
Cdd:cd01335  64 -LLRR-LKKELPGFEISIETNGTLLTEELLKELKELGLDgVGVSLDS-----GDEEVADKIRGSGESFKERLEALKELRE 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15608313 251 LSIPFTTGLLVG-IGETLSERADTLHAIRkshkEFGHIQEVIVQNFRAKEHTAMA-AFPDAGIEDYL 315
Cdd:cd01335 137 AGLGLSTTLLVGlGDEDEEDDLEELELLA----EFRSPDRVSLFRLLPEEGTPLElAAPVVPAEKLL 199
TIGR00423 TIGR00423
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
92-333 1.52e-06

radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of coenzyme F(420) biosynthesis from Methanocaldococcus jannaschii, but appears to hit genomes more broadly than just the subset that make coenzyme F(420), so that narrower group is being built as a separate family. [Hypothetical proteins, Conserved]


Pssm-ID: 273071 [Multi-domain]  Cd Length: 309  Bit Score: 50.86  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    92 IPVTRLCRDNCHYCTFvtvpGKLRAQGSSTYMEPDEILDVARRGAEFGCKEALFTLGDRPEArwrqarewlgerGYDSTL 171
Cdd:TIGR00423   9 INFTNICVGKCKFCAF----RAREKDKDAYVLSLEEILEKVKEAVAKGATEVCIQGGLNPQL------------DIEYYE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   172 SYVRAMAirvleqtGLLPHLNPGVMSWSEMSRLkpvAPSMGMMLETTSRRLFETkGLAHY---GSPDKDPAVR------- 241
Cdd:TIGR00423  73 ELFRAIK-------QEFPDVHIHAFSPMEVYFL---AKNEGLSIEEVLKRLKKA-GLDSMpgtGAEILDDSVRrkicpnk 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   242 ------LRVLTDAGRLSIPFTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRaKEHTAM---AAFPDAGIE 312
Cdd:TIGR00423 142 lssdewLEVIKTAHRLGIPTTATMMFGHVENPEHRVEHLLRIRKIQEKTGGFTEFIPLPFQ-PENNPYlegEVRKGASGI 220
                         250       260
                  ....*....|....*....|.
gi 15608313   313 DYLATVAVARLVLGPGMRIQA 333
Cdd:TIGR00423 221 DDLKVIAISRILLNNIRNIQA 241
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
552-752 1.38e-05

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 47.01  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    552 INFTNICYTGCRFCAFAQRKGDADAYSL-SVGEVADRAWEAHVAG--ATEVCMQGGIDPELPVTGYADLVRAVKARVPSM 628
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYLeALVREIELLAEKGEKEglVGTVFIGGGTPTLLSPEQLEELLEAIREILGLA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    629 HVHAFSPmeIANGVTKSglsiREWLIGLREAGLDTIpGTAAEILDDEVRWVLTKGKlPTSLWIEIVTTAHEVG-LRSSST 707
Cdd:smart00729  85 KDVEITI--ETRPDTLT----EELLEALKEAGVNRV-SLGVQSGDDEVLKAINRGH-TVEDVLEAVELLREAGpIKVSTD 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 15608313    708 MMYGHVD-SPRHWVAHLNVLRDIQ-DRTGGFTeFVPLPfvhqNSPLY 752
Cdd:smart00729 157 LIVGLPGeTEEDFEETLKLLKELGpDRVSIFP-LSPRP----GTPLA 198
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
39-356 2.73e-04

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313    39 LNVDEAAIAMTARGDeLADLCASAARVRDAglvSAGRHgpsgrlaISYSRKVFIPVTRLCRDNCHYCTFVTVPGKLRAQg 118
Cdd:TIGR03551   1 ITKEEALELFEARGN-LFELFRLADELRRD---IVGDT-------VTYVVNRNINFTNVCYGGCGFCAFRKRKGDADAY- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   119 sstYMEPDEILDVARRGAEFGCKEALFTLGDRPEArwrqarewlgerGYDSTLSYVRAMAIRVleqtgllPHLNpgVMSW 198
Cdd:TIGR03551  69 ---LLSLEEIAERAAEAWKAGATEVCIQGGIHPDL------------DGDFYLDILRAVKEEV-------PGMH--IHAF 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   199 SEMSRLKPVAPSmGMMLETTSRRLFETkGLahyGS------------------PDKDP-AVRLRVLTDAGRLSIPFTTGL 259
Cdd:TIGR03551 125 SPMEVYYGARNS-GLSVEEALKRLKEA-GL---DSmpgtaaeilddevrkvicPDKLStAEWIEIIKTAHKLGIPTTATI 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15608313   260 LVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKE----HTAMAAFPDAGIEDyLATVAVARLVLGPGMR-IQAP 334
Cdd:TIGR03551 200 MYGHVETPEHWVDHLLILREIQEETGGFTEFVPLPFVHYNaplyLKGMARPGPTGRED-LKVHAIARILLHGLIDnIQAS 278
                         330       340
                  ....*....|....*....|..
gi 15608313   335 PNLVSGDECRALVGAGVDDWGG 356
Cdd:TIGR03551 279 WVKLGKKLAQVALRCGANDLGG 300
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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