|
Name |
Accession |
Description |
Interval |
E-value |
| PFL1 |
cd01678 |
Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, ... |
15-760 |
0e+00 |
|
Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.
Pssm-ID: 153087 [Multi-domain] Cd Length: 738 Bit Score: 1388.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 15 AWAGFCGEEWKNAVNVRDFIQHNYTPYEGDEAFLAQATPATTALWQKVMVGIRQENATHAPVDFDTNIATTITAHGPGYI 94
Cdd:cd01678 1 AWEGFKGGKWQEEIDVRDFIQKNYTPYEGDESFLAGPTERTKKLWDKLEELLEEERAKGGVLDVDTKTVSTITSHKAGYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 95 DQELETIVGLQTDKPLKRALHPYGGINMIRSSFEAYGREMDPQFEYLFTDLRKTHNQGVFDVYSPEMMRCRKSGVLTGLP 174
Cdd:cd01678 81 DKELEVIVGLQTDKPLKRAIMPFGGIRMAEQALKAYGYELDPELKKIFTKYRKTHNDGVFDAYTPEIRRARHSGIITGLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 175 DGYGRGRIIGDYRRVALYGISYLVRERELQFADLQGKLergdDLEATIRLREELAEHKRALLQIQQMAANYGFDISRPAM 254
Cdd:cd01678 161 DAYGRGRIIGDYRRVALYGVDRLIEEKKKDLDNLGGDE----MTDDTIRLREEVAEQIKALKELKQMAASYGLDISRPAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 255 NAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRMVRFLRTPEFDTLFSG 334
Cdd:cd01678 237 NAQEAIQWTYFGYLAAIKEQNGAAMSLGRVSTFLDIYIERDLKAGTITEAEAQELIDQFIMKLRMVRFLRTPEYNELFSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 335 DPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMGPAPEPNLTILWSEQLPIAFKKYAAQVSIVTSSLQYENDDLMRADF 414
Cdd:cd01678 317 DPTWVTESIGGMGNDGRSLVTKTSFRFLNTLYNLGPAPEPNLTVLWSEKLPENFKRFCAKVSIDTSSIQYENDDLMRPDW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 415 NSDDYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTEPLLDEVLDYDTVMASLDHFMDWLAVQ 494
Cdd:cd01678 397 GGDDYGIACCVSAMRIGKQMQFFGARANLAKALLYAINGGRDEKTGDQVGPDIEPITSDYLDYDEVMENYDKSMDWLADT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 495 YISALNLIHYMHDKYSYEASLMALHDRDVYRTMACGIAGLSVAADSLSAIKYATVKPVRDHTGLAVDFVIEGDYPQYGNN 574
Cdd:cd01678 477 YVNALNIIHYMHDKYAYEALQMALHDTDVRRTMAFGIAGLSVAADSLSAIKYAKVKPIRDEDGLAVDFEIEGDFPRYGND 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 575 DDRVDSIACDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKGAVASLT 654
Cdd:cd01678 557 DDRADDIAVWVVKTFMNKLRKHKTYRNAEPTQSVLTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDKKGALASLA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 655 SVAKLPFTYAKDGISYTFSIVPQALGKDELVRKTNLVGLLDGYFHHeatieGGQHLNVNVMNREMLLDAIAHPENYPNLT 734
Cdd:cd01678 637 SVAKLPYRDANDGISNTFSIVPNALGKTDEERIDNLVGILDGYFTK-----GGHHLNVNVLNRETLLDAMEHPEKYPQLT 711
|
730 740
....*....|....*....|....*.
gi 1995764507 735 IRVSGYAVRFNALTREQQQDVISRTF 760
Cdd:cd01678 712 IRVSGYAVNFVKLTREQQLDVISRTF 737
|
|
| pyr_form_ly_1 |
TIGR01255 |
formate acetyltransferase 1; Alternate names: pyruvate formate-lyase; formate ... |
15-764 |
0e+00 |
|
formate acetyltransferase 1; Alternate names: pyruvate formate-lyase; formate C-acetyltransferase This enzyme converts formate + acetyl-CoA into pyruvate + CoA. This model describes formate acetyltransferase 1. More distantly related putative formate acetyltransferases have also been identified, including formate acetyltransferase 2 from E. coli, which is excluded from this model. [Energy metabolism, Fermentation]
Pssm-ID: 273525 [Multi-domain] Cd Length: 744 Bit Score: 1244.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 15 AWAGFCGEEWKNAVNVRDFIQHNYTPYEGDEAFLAQATPATTALWQKVMvGIRQENATHAPVDFDTNIATTITAHGPGYI 94
Cdd:TIGR01255 1 AWEGFTKGDWQNEVNVRDFIQKNYKPYEGDESFLAGPTEATTKVWDKVM-EVKLENRTHAPVDFDTAVASTITSHDAGYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 95 DQELETIVGLQTDKPLKRALHPYGGINMIRSSFEAYGREMDPQFEYLFTDLRKTHNQGVFDVYSPEMMRCRKSGVLTGLP 174
Cdd:TIGR01255 80 DKQLEKIVGLQTEAPLKRALIPFGGIRMAEGSLKEYGRELDPMIHKIFTEYRKTHNQGVFDAYTPDIRRARKAGVLTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 175 DGYGRGRIIGDYRRVALYGISYLVRERELQFADLQGklergDDLEATIRLREELAEHKRALLQIQQMAANYGFDISRPAM 254
Cdd:TIGR01255 160 DAYGRGRIIGDYRRVALYGIDYLMKEKLKQFTSLQA-----DLENELIRLREEIAEQHRALGEMKEMAAKYGYDISRPAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 255 NAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRMVRFLRTPEFDTLFSG 334
Cdd:TIGR01255 235 NAKEAIQWTYFGYLAAVKSQNGAAMSLGRTSTFLDIYIERDLKAGKITEQEAQEMVDHFVMKLRMVRFLRTPEYDELFSG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 335 DPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMGPAPEPNLTILWSEQLPIAFKKYAAQVSIVTSSLQYENDDLMRADF 414
Cdd:TIGR01255 315 DPTWATESIAGMGLDGRTLVTKNSFRFLNTLYTMGPAPEPNMTVLWSEKLPLSFKKFAAKMSIDTSSIQYENDDLMRPDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 415 NSDDYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTEPLLDEVLDYDTVMASLDHFMDWLAVQ 494
Cdd:TIGR01255 395 NNDDYAIACCVSPMIVGKQMQFFGARANLAKTMLYAINGGVDEKLKMQVVPDIEPIKDEVLDYDEVMENMDKFLDWLAKQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 495 YISALNLIHYMHDKYSYEASLMALHDRDVYRTMACGIAGLSVAADSLSAIKYATVKPVRDHTGLAVDFVIEGDYPQYGNN 574
Cdd:TIGR01255 475 YVTAMNIIHYMHDKYSYEASQMALHDTKVIRTMAFGIAGFSVAADSLSAIKYAKVKPIRDENGLAIDFEIEGDFPQYGND 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 575 DDRVDSIACDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKGAVASLT 654
Cdd:TIGR01255 555 DDRVDDIAVDLVERFMKKLQKHHTYRNAIPTQSVLTITSNVVYGKKTGNTPDGRRVGAPFGPGANPMHGRDQKGALASLT 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 655 SVAKLPFTYAKDGISYTFSIVPQALGKDELVRKTNLVGLLDGYFHHEATIEGGQHLNVNVMNREMLLDAIAHPENYPNLT 734
Cdd:TIGR01255 635 SVAKLPFAYAKDGISYTFSIVPNALGKDDDVRKTNLVGIMDGYFHHEASIEGGQHLNVNVMNREMLLDAMENPEKYPQLT 714
|
730 740 750
....*....|....*....|....*....|
gi 1995764507 735 IRVSGYAVRFNALTREQQQDVISRTFTQAI 764
Cdd:TIGR01255 715 IRVSGYAVNFNSLTKEQQQEVITRTFHESL 744
|
|
| PflD |
COG1882 |
Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of ... |
45-760 |
0e+00 |
|
Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 441486 [Multi-domain] Cd Length: 789 Bit Score: 995.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 45 EAFLAQATPATTALWQKVM---VGIRQENATH-----------APVDFDTNIATTITAHGPGYIdQELETIVGLQTDKPL 110
Cdd:COG1882 1 ESFLAGPTERTKRLREKLLeakPLIDIERARLftesyketeglPVIIRRAKAFSHILEHKPIYI-KDDELIVGLQTDKPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 111 KRALHPYGGINMIRSSFEAY------GREMDPQFEYLFTDL-----RKTHNQGVFDVYSPEMMRCRKSGVLTGLPDGYGR 179
Cdd:COG1882 80 KRPIFPEGGIRWVEDELDALptrpqdGFEISPEDKEIFREIapywkGKTHNDGVFDAYPEEIRKARKAGIITGLPDAYGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 180 GRIIGDYRRVALYGISYLVRERELQFADLQGKLERGDD-----------LEATIRLREELAEHKRALLQ----------I 238
Cdd:COG1882 160 GHIIGDYRRVLLYGLDGLIEEAKEKLAELDLTDPEDIEkidfykamiivCEAVIRLAERYAELARELAEketdpkrkaeL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 239 QQMAANYGFDISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIR 318
Cdd:COG1882 240 LEIAEICGFVPANPARTFWEAVQWVWFVYLAAIKEQNGAAMSLGRFDQYLYPYYERDLEEGRLTEEEAQELLDCFWIKLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 319 MVRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMgPAPEPNLTILWSEQLPIAFKKYAAQ-VSI 397
Cdd:COG1882 320 EVRFLRTPEYAELFAGYPTWVTLTIGGMTPDGRDAVNELSYLILETLRNL-PLPEPNLTVRWSEKLPEGFLKKAAEvISI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 398 VTSSLQYENDDLMRADF--------NSDDYAIACCVSPMVIGKQMQFFGA-RANLAKTLLYAINGGVDEKLKIQVGPKTE 468
Cdd:COG1882 399 GTGSPQYENDDLMIPMLlnkgvtleDARDYGIAGCVEPMVPGKQMQFFGAgRINLAKALEYALNNGVDEKTGKQVGPETG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 469 PlLDEVLDYDTVMASLDHFMDWLAVQYISALNLIHYMHDKYSYEASLMALHDRDVYRTM------------ACGIAGLSV 536
Cdd:COG1882 479 D-PTDFLTYDEVMEAFKKQLDYLADLYVNALNIIHYMHDKYAPEPFLSALHDDCIERGKdlneggarynfgAIGIAGLSV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 537 AADSLSAIK---YATVKPVRD--HTGLAVDFviEG---------DYPQYGNNDDRVDSIACDLVERFMKKIQALPTYRNA 602
Cdd:COG1882 558 VADSLSAIKklvFDKKKVTMDelLEALAANF--EGyeelrqlllNAPKYGNDDDYVDEIAVELVETFMDEIRKYKTYRGG 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 603 VPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKGAVASLTSVAKLPFTYAKDGISYTFSIVPQALGKD 682
Cdd:COG1882 636 TYTLSILTITSNVPYGKKTGATPDGRKAGEPLADGASPMHGRDKNGPTAVLKSVAKLPYEKATDGILLNQKFSPSALGGE 715
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995764507 683 ElvRKTNLVGLLDGYFHHeatieGGQHLNVNVMNREMLLDAIAHPENYPNLTIRVSGYAVRFNALTREQQQDVISRTF 760
Cdd:COG1882 716 E--GIENLVSLLRTYFDL-----GGHHIQFNVVDRETLLDAQKHPEKYPDLTVRVAGYSAYFVELSKEQQDDIIARTE 786
|
|
| PFL-like |
pfam02901 |
Pyruvate formate lyase-like; This family of enzymes includes pyruvate formate lyase, choline ... |
34-618 |
0e+00 |
|
Pyruvate formate lyase-like; This family of enzymes includes pyruvate formate lyase, choline trimethylamine lyase, glycerol dehydratase, 4-hydroxyphenylacetate decarboxylase, and benzylsuccinate synthase.
Pssm-ID: 427048 Cd Length: 647 Bit Score: 710.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 34 IQHNYTPYEGDEAFLaqatpattalWQKVMVGIRQENATHAPVDFDTNIATT---ITAHGPGYIdQELETIVGLQTDKPL 110
Cdd:pfam02901 8 LKENYTLYTGDPSLS----------WERARLLTESYKETEGVLPVDIRRAKAlkkILSHLPGYI-RDDELIVGLQTDKPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 111 KRALHPYGGINMIRSSFEAY------GREMDPQFEYLFTDL-----RKTHNQGVFDVYSPEMMRCRKSGVLTGLPDGYGR 179
Cdd:pfam02901 77 KRAIYPEGGIRWVEDELDYLntrpqdGFEISEEDKKIFREIfpywkGKTHNEGVFDAYTPEMKAARESGIFTGLPDAYGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 180 GRIIGDYRRVALYGISYLVRERELQFADLQGK---LERGDDLEA--------------TIRLREELAEHK---RALLQIQ 239
Cdd:pfam02901 157 GHIIGDYRRVLLYGLDGLIEEKEEKLAKLDTDpedIEKIEFYKAmiiscdavieyaerYARLAEELAEQEtdpKRKAELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 240 QMAANYGFDISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRM 319
Cdd:pfam02901 237 EIAEICGRVPARPAETFQEAIQWFWFVYLAAVKEQNGAAMSLGRLDQYLYPYYERDLEEGRLTEEEAQELIDCFWIKLRE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 320 VRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMgPAPEPNLTILWSEQLPIAFKKYAAQVSI-V 398
Cdd:pfam02901 317 VRFLRTPEYNKLFAGYDPFQNLTIGGQGRDGRDAVNKLSYLILEALDNL-PLPEPNLTVRWSKKLPEEFLKKAAEVSRkG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 399 TSSLQYENDDLMRADFNSD--------DYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTEPl 470
Cdd:pfam02901 396 TGSPQYENDDVMIPALLNRgvsledarDYGIAGCVEPMKPGKEMQFFGARINLAKALEYALNGGRDELTGKQVGPKTGP- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 471 LDEVLDYDTVMASLDHFMDWLAVQYISALNLIHYMHDKYSYEASLMALHDRDVYRTMACGI------------AGLSVAA 538
Cdd:pfam02901 475 VTEFLSFEEVMEAFKKQLDYLADLYVNALNIIHYMHDKYAPEPFLSALHDDCIERGKDVGIggarynfsgpqgAGLANVA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 539 DSLSAIKY----ATVKPVRD-HTGLAVDFVIEG--------DYPQYGNNDDRVDSIACDLVERFMKKIQALPTYRNAVPT 605
Cdd:pfam02901 555 DSLSAIKKlvfdDKVYTLRElEDALAADFEGEEelrqdllnDAPKYGNDDDRVDDIAVEVVETFMDEVRKYKNYRGGKFT 634
|
650
....*....|...
gi 1995764507 606 QSILTITSNVVYG 618
Cdd:pfam02901 635 PSLLTITSNVPYG 647
|
|
| pflD |
PRK09983 |
putative formate acetyltransferase 2; Provisional |
178-762 |
2.01e-43 |
|
putative formate acetyltransferase 2; Provisional
Pssm-ID: 182181 [Multi-domain] Cd Length: 765 Bit Score: 168.46 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 178 GRGRIIGDYRRVALYGISYLVrerelqfADLQGKLERGDD----------LEATIR-------LREELAEH------KRA 234
Cdd:PRK09983 153 GQGHIIIDYPRLLNHGLGELV-------AQMQQHCQQQPEnhfyqaalllLEASQKhilryaeLAETMAANctdaqrREE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 235 LLQIqqmAANYGFDISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRlNEVQAQELIDHFI 314
Cdd:PRK09983 226 LLTI---AEISRHNAQHKPQTFWQACQLFWYMNIILQYESNASSLSLGRFDQYMLPFYQASLTQGE-DPAFLKELLESLW 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 315 MKIRMVRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMgPAPEPNLTILWSEQLPIAF-KKYAA 393
Cdd:PRK09983 302 VKCNDIVLLRSTSSARYFAGFPTGYTALLGGLTENGRSAVNVLSFLCLDAYQSV-QLPQPNLGVRTNALIDTPFlMKTAE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 394 QVSIVTSSLQYENDDLMRADF--------NSDDYAIACCVSPMVIGKQmqfFG----ARANLAKTL---LYAINGgvdek 458
Cdd:PRK09983 381 TIRLGTGIPQIFNDEVVVPAFlnrgvsleDARDYSVVGCVELSIPGRT---YGlhdiAMFNLLKVMeicLHENEG----- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 459 lkiQVGPKTEPLLDEVLD----YDTVMASLDHFMD-----WLAVQYISAL--NLIHYMHD------KYSYEAslmalhdr 521
Cdd:PRK09983 453 ---NAALTYEGLLEQIRAkishYITLMVEGSNICDighrdWAPVPLLSSFisDCLEKGRDitdggaRYNFSG-------- 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 522 dvyrTMACGIAGLSvaaDSLSAIKyatvKPVRDHTGLAVDFVIE-------------------GDYPQYGNNDDRVDSIA 582
Cdd:PRK09983 522 ----VQGIGIANLS---DSLHALK----GMVFDQQRLSFDELLSvlkanfatpegekvrarliNRFEKYGNDIDEVDNIS 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 583 CDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGA-NPMHGRDRKGAVASLTSVAKLPF 661
Cdd:PRK09983 591 AELLRHYCKEVEKYQNPRGGYFTPGSYTVSAHVPLGSVVGATPDGRFAGEQLADGGlSPMLGQDAQGPTAVLKSVSKLDN 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 662 TYAKDGISYTFSIVPQALGKDELVRKtnLVGLLDGYFHHEAtieggQHLNVNVMNREMLLDAIAHPENYPNLTIRVSGYA 741
Cdd:PRK09983 671 TLLSNGTLLNVKFTPATLEGEAGLRK--LADFLRAFTQLKL-----QHIQFNVVNADTLREAQQRPQDYAGLVVRVAGYS 743
|
650 660
....*....|....*....|.
gi 1995764507 742 VRFNALTREQQQDVISRTFTQ 762
Cdd:PRK09983 744 AFFVELSKEIQDDIIRRTAHQ 764
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PFL1 |
cd01678 |
Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, ... |
15-760 |
0e+00 |
|
Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.
Pssm-ID: 153087 [Multi-domain] Cd Length: 738 Bit Score: 1388.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 15 AWAGFCGEEWKNAVNVRDFIQHNYTPYEGDEAFLAQATPATTALWQKVMVGIRQENATHAPVDFDTNIATTITAHGPGYI 94
Cdd:cd01678 1 AWEGFKGGKWQEEIDVRDFIQKNYTPYEGDESFLAGPTERTKKLWDKLEELLEEERAKGGVLDVDTKTVSTITSHKAGYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 95 DQELETIVGLQTDKPLKRALHPYGGINMIRSSFEAYGREMDPQFEYLFTDLRKTHNQGVFDVYSPEMMRCRKSGVLTGLP 174
Cdd:cd01678 81 DKELEVIVGLQTDKPLKRAIMPFGGIRMAEQALKAYGYELDPELKKIFTKYRKTHNDGVFDAYTPEIRRARHSGIITGLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 175 DGYGRGRIIGDYRRVALYGISYLVRERELQFADLQGKLergdDLEATIRLREELAEHKRALLQIQQMAANYGFDISRPAM 254
Cdd:cd01678 161 DAYGRGRIIGDYRRVALYGVDRLIEEKKKDLDNLGGDE----MTDDTIRLREEVAEQIKALKELKQMAASYGLDISRPAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 255 NAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRMVRFLRTPEFDTLFSG 334
Cdd:cd01678 237 NAQEAIQWTYFGYLAAIKEQNGAAMSLGRVSTFLDIYIERDLKAGTITEAEAQELIDQFIMKLRMVRFLRTPEYNELFSG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 335 DPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMGPAPEPNLTILWSEQLPIAFKKYAAQVSIVTSSLQYENDDLMRADF 414
Cdd:cd01678 317 DPTWVTESIGGMGNDGRSLVTKTSFRFLNTLYNLGPAPEPNLTVLWSEKLPENFKRFCAKVSIDTSSIQYENDDLMRPDW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 415 NSDDYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTEPLLDEVLDYDTVMASLDHFMDWLAVQ 494
Cdd:cd01678 397 GGDDYGIACCVSAMRIGKQMQFFGARANLAKALLYAINGGRDEKTGDQVGPDIEPITSDYLDYDEVMENYDKSMDWLADT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 495 YISALNLIHYMHDKYSYEASLMALHDRDVYRTMACGIAGLSVAADSLSAIKYATVKPVRDHTGLAVDFVIEGDYPQYGNN 574
Cdd:cd01678 477 YVNALNIIHYMHDKYAYEALQMALHDTDVRRTMAFGIAGLSVAADSLSAIKYAKVKPIRDEDGLAVDFEIEGDFPRYGND 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 575 DDRVDSIACDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKGAVASLT 654
Cdd:cd01678 557 DDRADDIAVWVVKTFMNKLRKHKTYRNAEPTQSVLTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDKKGALASLA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 655 SVAKLPFTYAKDGISYTFSIVPQALGKDELVRKTNLVGLLDGYFHHeatieGGQHLNVNVMNREMLLDAIAHPENYPNLT 734
Cdd:cd01678 637 SVAKLPYRDANDGISNTFSIVPNALGKTDEERIDNLVGILDGYFTK-----GGHHLNVNVLNRETLLDAMEHPEKYPQLT 711
|
730 740
....*....|....*....|....*.
gi 1995764507 735 IRVSGYAVRFNALTREQQQDVISRTF 760
Cdd:cd01678 712 IRVSGYAVNFVKLTREQQLDVISRTF 737
|
|
| pyr_form_ly_1 |
TIGR01255 |
formate acetyltransferase 1; Alternate names: pyruvate formate-lyase; formate ... |
15-764 |
0e+00 |
|
formate acetyltransferase 1; Alternate names: pyruvate formate-lyase; formate C-acetyltransferase This enzyme converts formate + acetyl-CoA into pyruvate + CoA. This model describes formate acetyltransferase 1. More distantly related putative formate acetyltransferases have also been identified, including formate acetyltransferase 2 from E. coli, which is excluded from this model. [Energy metabolism, Fermentation]
Pssm-ID: 273525 [Multi-domain] Cd Length: 744 Bit Score: 1244.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 15 AWAGFCGEEWKNAVNVRDFIQHNYTPYEGDEAFLAQATPATTALWQKVMvGIRQENATHAPVDFDTNIATTITAHGPGYI 94
Cdd:TIGR01255 1 AWEGFTKGDWQNEVNVRDFIQKNYKPYEGDESFLAGPTEATTKVWDKVM-EVKLENRTHAPVDFDTAVASTITSHDAGYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 95 DQELETIVGLQTDKPLKRALHPYGGINMIRSSFEAYGREMDPQFEYLFTDLRKTHNQGVFDVYSPEMMRCRKSGVLTGLP 174
Cdd:TIGR01255 80 DKQLEKIVGLQTEAPLKRALIPFGGIRMAEGSLKEYGRELDPMIHKIFTEYRKTHNQGVFDAYTPDIRRARKAGVLTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 175 DGYGRGRIIGDYRRVALYGISYLVRERELQFADLQGklergDDLEATIRLREELAEHKRALLQIQQMAANYGFDISRPAM 254
Cdd:TIGR01255 160 DAYGRGRIIGDYRRVALYGIDYLMKEKLKQFTSLQA-----DLENELIRLREEIAEQHRALGEMKEMAAKYGYDISRPAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 255 NAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRMVRFLRTPEFDTLFSG 334
Cdd:TIGR01255 235 NAKEAIQWTYFGYLAAVKSQNGAAMSLGRTSTFLDIYIERDLKAGKITEQEAQEMVDHFVMKLRMVRFLRTPEYDELFSG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 335 DPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMGPAPEPNLTILWSEQLPIAFKKYAAQVSIVTSSLQYENDDLMRADF 414
Cdd:TIGR01255 315 DPTWATESIAGMGLDGRTLVTKNSFRFLNTLYTMGPAPEPNMTVLWSEKLPLSFKKFAAKMSIDTSSIQYENDDLMRPDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 415 NSDDYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTEPLLDEVLDYDTVMASLDHFMDWLAVQ 494
Cdd:TIGR01255 395 NNDDYAIACCVSPMIVGKQMQFFGARANLAKTMLYAINGGVDEKLKMQVVPDIEPIKDEVLDYDEVMENMDKFLDWLAKQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 495 YISALNLIHYMHDKYSYEASLMALHDRDVYRTMACGIAGLSVAADSLSAIKYATVKPVRDHTGLAVDFVIEGDYPQYGNN 574
Cdd:TIGR01255 475 YVTAMNIIHYMHDKYSYEASQMALHDTKVIRTMAFGIAGFSVAADSLSAIKYAKVKPIRDENGLAIDFEIEGDFPQYGND 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 575 DDRVDSIACDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKGAVASLT 654
Cdd:TIGR01255 555 DDRVDDIAVDLVERFMKKLQKHHTYRNAIPTQSVLTITSNVVYGKKTGNTPDGRRVGAPFGPGANPMHGRDQKGALASLT 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 655 SVAKLPFTYAKDGISYTFSIVPQALGKDELVRKTNLVGLLDGYFHHEATIEGGQHLNVNVMNREMLLDAIAHPENYPNLT 734
Cdd:TIGR01255 635 SVAKLPFAYAKDGISYTFSIVPNALGKDDDVRKTNLVGIMDGYFHHEASIEGGQHLNVNVMNREMLLDAMENPEKYPQLT 714
|
730 740 750
....*....|....*....|....*....|
gi 1995764507 735 IRVSGYAVRFNALTREQQQDVISRTFTQAI 764
Cdd:TIGR01255 715 IRVSGYAVNFNSLTKEQQQEVITRTFHESL 744
|
|
| PflD |
COG1882 |
Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of ... |
45-760 |
0e+00 |
|
Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 441486 [Multi-domain] Cd Length: 789 Bit Score: 995.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 45 EAFLAQATPATTALWQKVM---VGIRQENATH-----------APVDFDTNIATTITAHGPGYIdQELETIVGLQTDKPL 110
Cdd:COG1882 1 ESFLAGPTERTKRLREKLLeakPLIDIERARLftesyketeglPVIIRRAKAFSHILEHKPIYI-KDDELIVGLQTDKPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 111 KRALHPYGGINMIRSSFEAY------GREMDPQFEYLFTDL-----RKTHNQGVFDVYSPEMMRCRKSGVLTGLPDGYGR 179
Cdd:COG1882 80 KRPIFPEGGIRWVEDELDALptrpqdGFEISPEDKEIFREIapywkGKTHNDGVFDAYPEEIRKARKAGIITGLPDAYGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 180 GRIIGDYRRVALYGISYLVRERELQFADLQGKLERGDD-----------LEATIRLREELAEHKRALLQ----------I 238
Cdd:COG1882 160 GHIIGDYRRVLLYGLDGLIEEAKEKLAELDLTDPEDIEkidfykamiivCEAVIRLAERYAELARELAEketdpkrkaeL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 239 QQMAANYGFDISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIR 318
Cdd:COG1882 240 LEIAEICGFVPANPARTFWEAVQWVWFVYLAAIKEQNGAAMSLGRFDQYLYPYYERDLEEGRLTEEEAQELLDCFWIKLR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 319 MVRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMgPAPEPNLTILWSEQLPIAFKKYAAQ-VSI 397
Cdd:COG1882 320 EVRFLRTPEYAELFAGYPTWVTLTIGGMTPDGRDAVNELSYLILETLRNL-PLPEPNLTVRWSEKLPEGFLKKAAEvISI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 398 VTSSLQYENDDLMRADF--------NSDDYAIACCVSPMVIGKQMQFFGA-RANLAKTLLYAINGGVDEKLKIQVGPKTE 468
Cdd:COG1882 399 GTGSPQYENDDLMIPMLlnkgvtleDARDYGIAGCVEPMVPGKQMQFFGAgRINLAKALEYALNNGVDEKTGKQVGPETG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 469 PlLDEVLDYDTVMASLDHFMDWLAVQYISALNLIHYMHDKYSYEASLMALHDRDVYRTM------------ACGIAGLSV 536
Cdd:COG1882 479 D-PTDFLTYDEVMEAFKKQLDYLADLYVNALNIIHYMHDKYAPEPFLSALHDDCIERGKdlneggarynfgAIGIAGLSV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 537 AADSLSAIK---YATVKPVRD--HTGLAVDFviEG---------DYPQYGNNDDRVDSIACDLVERFMKKIQALPTYRNA 602
Cdd:COG1882 558 VADSLSAIKklvFDKKKVTMDelLEALAANF--EGyeelrqlllNAPKYGNDDDYVDEIAVELVETFMDEIRKYKTYRGG 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 603 VPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKGAVASLTSVAKLPFTYAKDGISYTFSIVPQALGKD 682
Cdd:COG1882 636 TYTLSILTITSNVPYGKKTGATPDGRKAGEPLADGASPMHGRDKNGPTAVLKSVAKLPYEKATDGILLNQKFSPSALGGE 715
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995764507 683 ElvRKTNLVGLLDGYFHHeatieGGQHLNVNVMNREMLLDAIAHPENYPNLTIRVSGYAVRFNALTREQQQDVISRTF 760
Cdd:COG1882 716 E--GIENLVSLLRTYFDL-----GGHHIQFNVVDRETLLDAQKHPEKYPDLTVRVAGYSAYFVELSKEQQDDIIARTE 786
|
|
| PFL-like |
pfam02901 |
Pyruvate formate lyase-like; This family of enzymes includes pyruvate formate lyase, choline ... |
34-618 |
0e+00 |
|
Pyruvate formate lyase-like; This family of enzymes includes pyruvate formate lyase, choline trimethylamine lyase, glycerol dehydratase, 4-hydroxyphenylacetate decarboxylase, and benzylsuccinate synthase.
Pssm-ID: 427048 Cd Length: 647 Bit Score: 710.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 34 IQHNYTPYEGDEAFLaqatpattalWQKVMVGIRQENATHAPVDFDTNIATT---ITAHGPGYIdQELETIVGLQTDKPL 110
Cdd:pfam02901 8 LKENYTLYTGDPSLS----------WERARLLTESYKETEGVLPVDIRRAKAlkkILSHLPGYI-RDDELIVGLQTDKPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 111 KRALHPYGGINMIRSSFEAY------GREMDPQFEYLFTDL-----RKTHNQGVFDVYSPEMMRCRKSGVLTGLPDGYGR 179
Cdd:pfam02901 77 KRAIYPEGGIRWVEDELDYLntrpqdGFEISEEDKKIFREIfpywkGKTHNEGVFDAYTPEMKAARESGIFTGLPDAYGR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 180 GRIIGDYRRVALYGISYLVRERELQFADLQGK---LERGDDLEA--------------TIRLREELAEHK---RALLQIQ 239
Cdd:pfam02901 157 GHIIGDYRRVLLYGLDGLIEEKEEKLAKLDTDpedIEKIEFYKAmiiscdavieyaerYARLAEELAEQEtdpKRKAELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 240 QMAANYGFDISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRM 319
Cdd:pfam02901 237 EIAEICGRVPARPAETFQEAIQWFWFVYLAAVKEQNGAAMSLGRLDQYLYPYYERDLEEGRLTEEEAQELIDCFWIKLRE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 320 VRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMgPAPEPNLTILWSEQLPIAFKKYAAQVSI-V 398
Cdd:pfam02901 317 VRFLRTPEYNKLFAGYDPFQNLTIGGQGRDGRDAVNKLSYLILEALDNL-PLPEPNLTVRWSKKLPEEFLKKAAEVSRkG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 399 TSSLQYENDDLMRADFNSD--------DYAIACCVSPMVIGKQMQFFGARANLAKTLLYAINGGVDEKLKIQVGPKTEPl 470
Cdd:pfam02901 396 TGSPQYENDDVMIPALLNRgvsledarDYGIAGCVEPMKPGKEMQFFGARINLAKALEYALNGGRDELTGKQVGPKTGP- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 471 LDEVLDYDTVMASLDHFMDWLAVQYISALNLIHYMHDKYSYEASLMALHDRDVYRTMACGI------------AGLSVAA 538
Cdd:pfam02901 475 VTEFLSFEEVMEAFKKQLDYLADLYVNALNIIHYMHDKYAPEPFLSALHDDCIERGKDVGIggarynfsgpqgAGLANVA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 539 DSLSAIKY----ATVKPVRD-HTGLAVDFVIEG--------DYPQYGNNDDRVDSIACDLVERFMKKIQALPTYRNAVPT 605
Cdd:pfam02901 555 DSLSAIKKlvfdDKVYTLRElEDALAADFEGEEelrqdllnDAPKYGNDDDRVDDIAVEVVETFMDEVRKYKNYRGGKFT 634
|
650
....*....|...
gi 1995764507 606 QSILTITSNVVYG 618
Cdd:pfam02901 635 PSLLTITSNVPYG 647
|
|
| PFL2_DhaB_BssA |
cd01677 |
Pyruvate formate lyase 2 and related enzymes; This family includes pyruvate formate lyase 2 ... |
86-759 |
9.38e-82 |
|
Pyruvate formate lyase 2 and related enzymes; This family includes pyruvate formate lyase 2 (PFL2), B12-independent glycerol dehydratase (DhaB) and the alpha subunit of benzylsuccinate synthase (BssA), all of which have a highly conserved ten-stranded alpha/beta barrel domain, which is similar to those of PFL1 (pyruvate formate lyase 1) and RNR (ribonucleotide reductase). Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. DhaB catalyzes the first step in the conversion of glycerol to 1,3-propanediol while BssA catalyzes the first step in the anaerobic mineralization of both toluene and m-xylene.
Pssm-ID: 153086 [Multi-domain] Cd Length: 781 Bit Score: 277.24 E-value: 9.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 86 ITAHGPGYI-DQELetIVGLQTDKP-----------------LKRALHPYGGINMIRSSFEAYGREMDPQFEylftdlRK 147
Cdd:cd01677 49 ILENATIYIqDDEL--IVGNRGGKPravpvfpelsvhwvedeLDDLPKRPGDPFVISEDKKEYLEEIFPYWK------GK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 148 THNQGVFDVYSPEMMRCRKSGVLTGLPDGY-GRGRIIGDYRRVALYGISYLVRERELQFADLQGK----LERGDDLEATI 222
Cdd:cd01677 121 TLRDRCFKYFPEETLIAMAAGVFTEFMYFFsGPGHVAVDYPKVLEKGLDGLIEEAKEAIEALDLTgpedIDKIYFYQAMI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 223 --------------RLREELAE------HKRALLQIQQmaanygfdISR-----PAMNAQEAVQWVYFAYLAAVKSQNGG 277
Cdd:cd01677 201 ivceavityakryaELAKELAAketdpkRKAELLEIAE--------ICRrvpahPPRTFWEALQSFWFIHLILQIESNGH 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 278 AMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKIRMVRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKN 357
Cdd:cd01677 273 SISPGRFDQYLYPFYKQDIEEGRLTREGAIELLECLWIKINEINKVRSGASAKYFAGYNTFQNLTIGGQTEDGSDATNEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 358 SFRYLHTLHTMgPAPEPNLTILWSEQLPIAFKKYAAQVsiVTSSL---QYENDD-----LMRADFNSDD---YAIACCVS 426
Cdd:cd01677 353 SYLILEATRRV-RLPQPSLTVRYHAKSPDKFLKKAAEV--IRLGLgypAFFNDEvvipaLLRKGVSLEDardYGLIGCVE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 427 PMVIGKQMQFFGARA-NLAKTLLYAINGGVDEKLKIQVGPKTEPL-----LDEVldYDTVMASLDHFMDWLavqyISALN 500
Cdd:cd01677 430 TGAPGRKYRWTGTGYiNLAKVLEITLNNGKDPRSGKQVGPETGDAtdfktFEEL--WEAFKKQLRHFIKLS----VRANN 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 501 LIHYMHDKYSYEASLMALHD------RDVYRTMA---------CGIAglsVAADSLSAIKYA-------TVKPVRDhtGL 558
Cdd:cd01677 504 ISDIAHAEVAPAPFLSALVDdciekgKDINAGGArynfggiqgVGIA---TLGDSLAAIKKLvfeekklTMEELLE--AL 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 559 AVDFViEG---------DYPQYGNNDDRVDSIACDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRR 629
Cdd:cd01677 579 KANFA-EGyeerrrllnNAPKYGNDDDYADNIARRVYEWYCKEVEKYQNPRGGKFYPGTYSVSANVPFGSVTGATPDGRL 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 630 GGTPFAPGANPMHGRDRKGAVASLTSVAKLPFTYAKDGISYTFSIVPQALGKDELVRKtnLVGLLDGYFhheatIEGGQH 709
Cdd:cd01677 658 AGTPLSDGVSPSQGTDKKGPTAVIKSVSKLDHFNISGGTLLNQKFSPSTLEGEEGLKK--LAALIRTYF-----DLGGHH 730
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1995764507 710 LNVNVMNREMLLDAIAHPENYPNLTIRVSGYAVRFNALTREQQQDVISRT 759
Cdd:cd01677 731 IQFNVVSAETLRDAQKHPEKYRDLIVRVAGYSAYFVELSKEVQDEIIART 780
|
|
| RNR_PFL |
cd00576 |
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and ... |
159-714 |
9.76e-71 |
|
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL) are believed to have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical.
Pssm-ID: 153083 [Multi-domain] Cd Length: 401 Bit Score: 237.05 E-value: 9.76e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 159 PEMMRCRKSGVLTGL-PDGYGRGRIIGDYRRVALYGISYlvrerelqfadlqgklergddleatirlreelaehkrallq 237
Cdd:cd00576 2 ERIYEAVKSGVITVGrPDLPFTGCVLVDYGDSLDPGIKG----------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 238 iqqmaanygfdISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEVQAQELIDHFIMKI 317
Cdd:cd00576 41 -----------VNETAKSINEAIQKTYQIIALAASNQNGGGVSFARASSILSPYGSRDYAKGSGTETDAVEAADAFNLAL 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 318 RMVRFLrtpefdtlfSGDPIWATEVIGGMGLDgrtLVTKNSFRYLHTLHTMG----PAPEPNLTILWSEQLP------IA 387
Cdd:cd00576 110 KEVGQG---------NGRTGAATGFIGGVHKG---KGDKISQEFLNLALANGgegiPLNFPNLSVRVSSDKPgilvkaVE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 388 FKKYAAQVSIVTSSLQYENDdlmradfnsddyaIACcvspmvigkqmqfFGARANLAKTLLYAINGgvdeklkiqvgpkt 467
Cdd:cd00576 178 LKQLIAEEARKTGSPGIFND-------------ELC-------------NLVSLNLARIMEKAING-------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 468 eplldevldydtVMASLDHFMDWLAVQYISALNLIHYMHDKYSYEaslmALHDRDVYRTMACGIAGLSVAADSLSAIKYA 547
Cdd:cd00576 218 ------------SMDVVLEELEELAFLAVRALDCVIDSHDERIPT----IELGGDERRTVGLGIAGVADLLIKLGLEKVG 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 548 tvkpvrdhtglavdfviegdypqygnnDDRVDSIACDLVERFMKKIQALPTYRNAVPTQSILTITSNvvygqktgntpdg 627
Cdd:cd00576 282 ---------------------------DPEADDLAAELVDQLKKHLVKATNERGFNFLLGLSPSESN------------- 321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 628 rRGGTPFAPGANPMHGR------DRKGAVASLTSVAKLPFtYAKDGISYTFSIVPQALGKDelvrktNLVGLLDGYFHHe 701
Cdd:cd00576 322 -SSGAPATNGVSPSRG*iaivlnGDIGPEESLASVAILQF-YADNGISDTITIPDSATNLD------QLLAVIDGAAAI- 392
|
570
....*....|...
gi 1995764507 702 atieGGQHLNVNV 714
Cdd:cd00576 393 ----KTTHVRVNP 401
|
|
| Gly_radical |
pfam01228 |
Glycine radical; |
634-745 |
1.74e-49 |
|
Glycine radical;
Pssm-ID: 426140 [Multi-domain] Cd Length: 106 Bit Score: 168.89 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 634 FAPGANPMHGRDRKGAVASLTSVAKLPFTYAKDGISYTFSIVPQALGKDELVRKTNLVGLLDGYFHheatieGGQHLNVN 713
Cdd:pfam01228 1 VAPGISPSHGADFEGPTAVLNSVGKIDYEVELDGISLNQKFLPAVLGYYDEEGYANLNTLIDTYFE------GGHHLQFN 74
|
90 100 110
....*....|....*....|....*....|..
gi 1995764507 714 VMNREMLLDAIAHPENYPNLTIRVSGYAVRFN 745
Cdd:pfam01228 75 VVDRETLPDAQKHPEKYPDLTVRVSGYSANFV 106
|
|
| pflD |
PRK09983 |
putative formate acetyltransferase 2; Provisional |
178-762 |
2.01e-43 |
|
putative formate acetyltransferase 2; Provisional
Pssm-ID: 182181 [Multi-domain] Cd Length: 765 Bit Score: 168.46 E-value: 2.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 178 GRGRIIGDYRRVALYGISYLVrerelqfADLQGKLERGDD----------LEATIR-------LREELAEH------KRA 234
Cdd:PRK09983 153 GQGHIIIDYPRLLNHGLGELV-------AQMQQHCQQQPEnhfyqaalllLEASQKhilryaeLAETMAANctdaqrREE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 235 LLQIqqmAANYGFDISRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRlNEVQAQELIDHFI 314
Cdd:PRK09983 226 LLTI---AEISRHNAQHKPQTFWQACQLFWYMNIILQYESNASSLSLGRFDQYMLPFYQASLTQGE-DPAFLKELLESLW 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 315 MKIRMVRFLRTPEFDTLFSGDPIWATEVIGGMGLDGRTLVTKNSFRYLHTLHTMgPAPEPNLTILWSEQLPIAF-KKYAA 393
Cdd:PRK09983 302 VKCNDIVLLRSTSSARYFAGFPTGYTALLGGLTENGRSAVNVLSFLCLDAYQSV-QLPQPNLGVRTNALIDTPFlMKTAE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 394 QVSIVTSSLQYENDDLMRADF--------NSDDYAIACCVSPMVIGKQmqfFG----ARANLAKTL---LYAINGgvdek 458
Cdd:PRK09983 381 TIRLGTGIPQIFNDEVVVPAFlnrgvsleDARDYSVVGCVELSIPGRT---YGlhdiAMFNLLKVMeicLHENEG----- 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 459 lkiQVGPKTEPLLDEVLD----YDTVMASLDHFMD-----WLAVQYISAL--NLIHYMHD------KYSYEAslmalhdr 521
Cdd:PRK09983 453 ---NAALTYEGLLEQIRAkishYITLMVEGSNICDighrdWAPVPLLSSFisDCLEKGRDitdggaRYNFSG-------- 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 522 dvyrTMACGIAGLSvaaDSLSAIKyatvKPVRDHTGLAVDFVIE-------------------GDYPQYGNNDDRVDSIA 582
Cdd:PRK09983 522 ----VQGIGIANLS---DSLHALK----GMVFDQQRLSFDELLSvlkanfatpegekvrarliNRFEKYGNDIDEVDNIS 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 583 CDLVERFMKKIQALPTYRNAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGA-NPMHGRDRKGAVASLTSVAKLPF 661
Cdd:PRK09983 591 AELLRHYCKEVEKYQNPRGGYFTPGSYTVSAHVPLGSVVGATPDGRFAGEQLADGGlSPMLGQDAQGPTAVLKSVSKLDN 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 662 TYAKDGISYTFSIVPQALGKDELVRKtnLVGLLDGYFHHEAtieggQHLNVNVMNREMLLDAIAHPENYPNLTIRVSGYA 741
Cdd:PRK09983 671 TLLSNGTLLNVKFTPATLEGEAGLRK--LADFLRAFTQLKL-----QHIQFNVVNADTLREAQQRPQDYAGLVVRVAGYS 743
|
650 660
....*....|....*....|.
gi 1995764507 742 VRFNALTREQQQDVISRTFTQ 762
Cdd:PRK09983 744 AFFVELSKEIQDDIIRRTAHQ 764
|
|
| choline_CutC |
TIGR04394 |
choline trimethylamine-lyase; Members of this family, homologs to pyruvate formate-lyases and ... |
225-759 |
9.38e-40 |
|
choline trimethylamine-lyase; Members of this family, homologs to pyruvate formate-lyases and benzylsuccinate synthases, are glycine radical enzymes that appear to act as choline TMA-lyase, that is, to perform a C-N bond cleavage turning choline into trimethylamine (TMA) plus acetaldehyde. The gene symbol is cutC, for choline utilization. The activase, CutD, is a radical SAM enzyme. [Energy metabolism, Amino acids and amines]
Pssm-ID: 275187 [Multi-domain] Cd Length: 789 Bit Score: 157.27 E-value: 9.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 225 REELAEHKRALLQIQQMAANYGfdiSRPAMNAQEAVQWVYFAYLAAVKSQNGGAMSLGRTASFLDIYIERDMQAGRLNEV 304
Cdd:TIGR04394 228 KEQDPKRKAELEKIAEVNARVP---AHKPRTFWEAIQSVWTVESLLVVEENQTGMSIGRVDQYMYPFYKADIEAGRMTEY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 305 QAQELIDHFIMKIRMVRFLRTPEFDTLFSGDPIWATEVIGGMGLDGR------TLVTKNSFRYLHTLhtmgpapEPNLTI 378
Cdd:TIGR04394 305 EAFELAGCMLIKMSEMMWLTSEGGSKFFAGYQPFVNMCVGGVTREGGdatndlTYLLMDAVRHVKVY-------QPSLAC 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 379 LWSEQLPiafKKYAAQ-VSIVTSSLQYEN---DD----LMRA---DF-NSDDYAIACCVSPMVIGKQMQFFG-ARANLAK 445
Cdd:TIGR04394 378 RIHNKSP---QKYLKKiVDVVRAGMGFPAchfDDahikMMLAkgvSIeDARDYCLMGCVEPQKSGRLYQWTStAYTQWPI 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 446 TLLYAINGGVDEKLKIQVGPKTEPL--LDEVLDYD-TVMASLDHFMDWLAVQYISALNLIHYMHDKysyeaSLMAL---- 518
Cdd:TIGR04394 455 CIELVLNHGVPLWYGKQVCPDTGDLsqFDTYEKFDaAVKEQIKYITKWSAVATVISQRVHRDLAPK-----PLMSLmyeg 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 519 ---HDRDVYRTMAC-----GI--AGLSVAADSLSAI--------KYaTVKPVRDhtGLAVDFviEG---------DYPQY 571
Cdd:TIGR04394 530 cmeKGKDVSAGGAMynfgpGVvwSGLATYADSMAAIkklvyddkKY-TLEQLNE--ALKANF--EGyeqiradclDAPKY 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 572 GNNDDRVDSIACDLV---ERFMKKIQALptYrnAVPTQSILTITSNVVYGQKTGNTPDGRRGGTPFAPGANPMHGRDRKG 648
Cdd:TIGR04394 605 GNDDDYADLIAADLVnftEREHRKYKTL--Y--SHLSHGTLSISNNTPFGQLTGASANGRLAWTPLSDGISPTQGADFKG 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764507 649 AVASLTSVAKLPFTYAKDGISYTFSIVPQALGKDElvRKTNLVGLLdgyfhHEATIEGGQHLNVNVMNREMLLDAIAHPE 728
Cdd:TIGR04394 681 PTAIIKSVSKMANDSMNIGMVHNFKLMSGLLDTPE--GENGLITLL-----RTASILGNGEMQFNYLDNETLLDAQQHPE 753
|
570 580 590
....*....|....*....|....*....|.
gi 1995764507 729 NYPNLTIRVSGYAVRFNALTREQQQDVISRT 759
Cdd:TIGR04394 754 KYRDLVVRVAGYSAFFVELCKDVQDEIISRT 784
|
|
| PRK11127 |
PRK11127 |
autonomous glycyl radical cofactor GrcA; Provisional |
704-764 |
6.89e-38 |
|
autonomous glycyl radical cofactor GrcA; Provisional
Pssm-ID: 182983 [Multi-domain] Cd Length: 127 Bit Score: 137.28 E-value: 6.89e-38
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1995764507 704 IEGGQHLNVNVMNREMLLDAIAHPENYPNLTIRVSGYAVRFNALTREQQQDVISRTFTQAI 764
Cdd:PRK11127 67 VEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSLTPEQQRDVIARTFTESL 127
|
|
| spare_glycyl |
TIGR04365 |
autonomous glycyl radical cofactor GrcA; This small protein, previously designated YfiD in E. ... |
700-764 |
7.82e-36 |
|
autonomous glycyl radical cofactor GrcA; This small protein, previously designated YfiD in E. coli, is closely homologous to pyruvate formate_lyase (PFL) in a region surrounding the stable glycyl radical that is prepared by the action of pyruvate formate-lyase activase, a radical SAM enzyme. When damage at the site of this radical breaks the main chain of PFL, this protein acts as a spare part that reintroduces the needed stable glycyl radical. Cutoffs for this model are set to exclude a set of closely related phage proteins that appear to have a corresponding function.
Pssm-ID: 213978 [Multi-domain] Cd Length: 124 Bit Score: 131.46 E-value: 7.82e-36
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995764507 700 HEATIEGGQHLNVNVMNREMLLDAIAHPENYPNLTIRVSGYAVRFNALTREQQQDVISRTFTQAI 764
Cdd:TIGR04365 60 APAKVEGGQHLNVNVLTRETLEDAVKNPEKYPQLTIRVSGYAVRFNSLTPEQQRDVITRTFTESL 124
|
|
| |
