|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-704 |
0e+00 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 1296.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPrtggdapdqtttiiranstvtaaePLKMSHVETLLSSNQQDV 80
Cdd:PRK05632 6 YLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP------------------------PLTMSEVEALLASGQLDE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 81 LMEEIIARYHENTKDAEVVLVEGLVPTRKHQFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARSSFGGSKNKN 160
Cdd:PRK05632 62 LLEEIVARYHALAKDCDVVLVEGLDPTRKHPFEFSLNAEIAKNLGAEVVLVSSGGNDTPEELAERIELAASSFGGAKNAN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 161 ITGVIINKLNAPVDEQGRTRPDLSEIFDDSTKAsvaNIDPTQLFANSPLPVLGCIPWSFELIATRAIDMAKHLNARIINE 240
Cdd:PRK05632 142 ILGVIINKLNAPVDEQGRTRPDLSEIFDDSSKA---NVDPSKLFASSPLPLLGVVPWSPDLIAPRVIDIAKHLGATVLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 241 GDVKTRRVKSVTFCARSIPHMLEHFRPGSLLVTSADRPDVLVSACLAAMNGVEIGAILLTGGYEIDARINSLCERAFQTG 320
Cdd:PRK05632 219 GDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPPIAGLLLTGGYEPDPRIAKLCEGAFETG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 321 LPVFMVETNTWQTSLSLQSFNLEVPADDHQRVEKLQQYVASHINAD-WINSLSAHSERSRRLSPPAFRYQLTELARKAGK 399
Cdd:PRK05632 299 LPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDTDeLLERLTATSERSRRLSPPAFRYQLTERARAAKK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 400 RIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGKGIEIVDPVAVREEYVARLVELRKSKGMTEVV 479
Cdd:PRK05632 379 RIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQGVDLPAGIEIIDPSEVRERYVAPLVELRKHKGMTEEV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 480 AREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAINPDPTAEQ 559
Cdd:PRK05632 459 AREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPALQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAEQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 560 LSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIMADVAQSKAPNSPV 639
Cdd:PRK05632 539 LAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKVREATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSPV 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774007702 640 AGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQS 704
Cdd:PRK05632 619 AGRATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRKPVNDLSRGALVDDIVNTIAITAIQA 683
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-703 |
0e+00 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 831.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPRTGGDAPDQTTTIIRANSTVTA----AEPLKMSHVETLLSSN 76
Cdd:COG0857 6 YIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLVGGGERDEDVELIREHLGLDLpyedASPVTLDEVETLLAEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 77 QQDVLMEEIIARYHENTKDAEVVLVEGLVPTRKH-QFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARSSFGG 155
Cdd:COG0857 86 DPDELLERIVERYEALAAECDVVLVEGSDPTGVGsPFELSLNARIAKNLGAPVLLVASGGGRTPEELVDALLLAADEFRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 156 sKNKNITGVIINKLNAPVDEQGRTrpdlseifddstkasvaniDPTQLFANSPLPVLGCIPWSFELIATRAIDMAKHLNA 235
Cdd:COG0857 166 -EGARVLGVIINRVPPEKLEEVRE-------------------ALRPFLEGSGIPVLGVIPENPELAAPTVRDLAEALGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 236 RIINEGDVKTRRVKSVTFCARSIPHMLEHFRPGSLLVTSADRPDVLVSACLAAMNGV-EIGAILLTGGYEIDARINSLCE 314
Cdd:COG0857 226 EVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTpSIAGLILTGGLPPDPAVLRLAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 315 RAFQTgLPVFMVETNTWQTSLSLQSFNLEVPADDHQRVEKLQQYVASHINADWInsLSAHSERSRRLSPPAFRYQLTELA 394
Cdd:COG0857 306 GLGQT-LPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWL--LSRLGLPRSRLSPPAFFYYLLERA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 395 RKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGKGIEIVDPVAVREEYVARLVELRKSKG 474
Cdd:COG0857 383 ARAAKRIVLPEGGEDRRILAAAICLLRRIAACVLLGGPEEIIRVAAAQGGLLLDGIEIIDPPDSRLRYVAAEVYLRRRKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 475 MTEVVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAINPD 554
Cdd:COG0857 463 KGVTVAAAQLEDDVVLYTGMMMVHEGDGLGMGSGATTTTTTTIPPQLIITKTGPGVVSSSSFFLMLLQVVVVGDCACAPN 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 555 PTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIMADVAQSKA 634
Cdd:COG0857 543 PPPEELALAAIISSSSAAAAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRRRDLLLDGPGPYQAAAAADVVVAKA 622
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774007702 635 PNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQ 703
Cdd:COG0857 623 KPSPVAGAAAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGVVDIDITIALTIIA 691
|
|
| pta |
TIGR00651 |
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ... |
401-701 |
4.41e-171 |
|
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]
Pssm-ID: 273196 [Multi-domain] Cd Length: 303 Bit Score: 491.95 E-value: 4.41e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 401 IVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIkrVAAAQGVTLGKGIEIVDPVAV---REEYVARLVELRKSKGMTE 477
Cdd:TIGR00651 1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEI--QPKAAGCNLDLGHVVIIDPDVspdRESYAERYVELRKHKGMTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 478 VVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAINPDPTA 557
Cdd:TIGR00651 79 AQARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 558 EQLSEIAIQSADSAAAFG-IEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIMADVAQSKAPN 636
Cdd:TIGR00651 159 EQLAEIAIQSANSAKSFGeIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKRPDLTIDGELQFDAAFVEKVAEKKAPN 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774007702 637 SPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTA 701
Cdd:TIGR00651 239 SPVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNTGAITA 303
|
|
| PTA_PTB |
pfam01515 |
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ... |
386-701 |
7.54e-158 |
|
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.
Pssm-ID: 396207 [Multi-domain] Cd Length: 318 Bit Score: 458.70 E-value: 7.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 386 FRYQLTELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGkGIEIVDPVAVR--EEYV 463
Cdd:pfam01515 1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDLD-GIEIVDPETSPrlEEYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 464 ARLVELRKSKGMTEVVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQV 543
Cdd:pfam01515 80 DFYYELRKRKGMTPEIAREIVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 544 LVYGDCAINPDPTAEQLSEIAIQSADSAAAFG-IEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYD 622
Cdd:pfam01515 160 LFFADCAVNPNPTAEELAEIALMSAKTAKRFGiIEPRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQFD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774007702 623 AAIMADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTA 701
Cdd:pfam01515 240 AALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAITA 318
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
1-189 |
4.13e-29 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 114.59 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPRTGGDAPDqtTTIIRANS----TVTAAEPLKMS-HVETLLSS 75
Cdd:cd03109 4 FVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCPGLEDSD--AELLRKLAglllDLELINPYRFEaPLSPHLAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 76 NQQ--DVLMEEIIARYHENTKDAEVVLVEGLVPTRKHQFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARssf 153
Cdd:cd03109 82 ELEgrDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEALK--- 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1774007702 154 ggSKNKNITGVIINKlnapVDEQGRTRPDLSEIFDD 189
Cdd:cd03109 159 --SRGLDVAGVVLNG----IPPEPEAEADNAETLKE 188
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-704 |
0e+00 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 1296.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPrtggdapdqtttiiranstvtaaePLKMSHVETLLSSNQQDV 80
Cdd:PRK05632 6 YLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP------------------------PLTMSEVEALLASGQLDE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 81 LMEEIIARYHENTKDAEVVLVEGLVPTRKHQFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARSSFGGSKNKN 160
Cdd:PRK05632 62 LLEEIVARYHALAKDCDVVLVEGLDPTRKHPFEFSLNAEIAKNLGAEVVLVSSGGNDTPEELAERIELAASSFGGAKNAN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 161 ITGVIINKLNAPVDEQGRTRPDLSEIFDDSTKAsvaNIDPTQLFANSPLPVLGCIPWSFELIATRAIDMAKHLNARIINE 240
Cdd:PRK05632 142 ILGVIINKLNAPVDEQGRTRPDLSEIFDDSSKA---NVDPSKLFASSPLPLLGVVPWSPDLIAPRVIDIAKHLGATVLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 241 GDVKTRRVKSVTFCARSIPHMLEHFRPGSLLVTSADRPDVLVSACLAAMNGVEIGAILLTGGYEIDARINSLCERAFQTG 320
Cdd:PRK05632 219 GDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPPIAGLLLTGGYEPDPRIAKLCEGAFETG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 321 LPVFMVETNTWQTSLSLQSFNLEVPADDHQRVEKLQQYVASHINAD-WINSLSAHSERSRRLSPPAFRYQLTELARKAGK 399
Cdd:PRK05632 299 LPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDTDeLLERLTATSERSRRLSPPAFRYQLTERARAAKK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 400 RIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGKGIEIVDPVAVREEYVARLVELRKSKGMTEVV 479
Cdd:PRK05632 379 RIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAAQGVDLPAGIEIIDPSEVRERYVAPLVELRKHKGMTEEV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 480 AREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAINPDPTAEQ 559
Cdd:PRK05632 459 AREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPALQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAEQ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 560 LSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIMADVAQSKAPNSPV 639
Cdd:PRK05632 539 LAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKVREATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSPV 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774007702 640 AGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQS 704
Cdd:PRK05632 619 AGRATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRKPVNDLSRGALVDDIVNTIAITAIQA 683
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-703 |
0e+00 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 831.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPRTGGDAPDQTTTIIRANSTVTA----AEPLKMSHVETLLSSN 76
Cdd:COG0857 6 YIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLVGGGERDEDVELIREHLGLDLpyedASPVTLDEVETLLAEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 77 QQDVLMEEIIARYHENTKDAEVVLVEGLVPTRKH-QFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARSSFGG 155
Cdd:COG0857 86 DPDELLERIVERYEALAAECDVVLVEGSDPTGVGsPFELSLNARIAKNLGAPVLLVASGGGRTPEELVDALLLAADEFRG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 156 sKNKNITGVIINKLNAPVDEQGRTrpdlseifddstkasvaniDPTQLFANSPLPVLGCIPWSFELIATRAIDMAKHLNA 235
Cdd:COG0857 166 -EGARVLGVIINRVPPEKLEEVRE-------------------ALRPFLEGSGIPVLGVIPENPELAAPTVRDLAEALGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 236 RIINEGDVKTRRVKSVTFCARSIPHMLEHFRPGSLLVTSADRPDVLVSACLAAMNGV-EIGAILLTGGYEIDARINSLCE 314
Cdd:COG0857 226 EVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTpSIAGLILTGGLPPDPAVLRLAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 315 RAFQTgLPVFMVETNTWQTSLSLQSFNLEVPADDHQRVEKLQQYVASHINADWInsLSAHSERSRRLSPPAFRYQLTELA 394
Cdd:COG0857 306 GLGQT-LPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWL--LSRLGLPRSRLSPPAFFYYLLERA 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 395 RKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGKGIEIVDPVAVREEYVARLVELRKSKG 474
Cdd:COG0857 383 ARAAKRIVLPEGGEDRRILAAAICLLRRIAACVLLGGPEEIIRVAAAQGGLLLDGIEIIDPPDSRLRYVAAEVYLRRRKK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 475 MTEVVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAINPD 554
Cdd:COG0857 463 KGVTVAAAQLEDDVVLYTGMMMVHEGDGLGMGSGATTTTTTTIPPQLIITKTGPGVVSSSSFFLMLLQVVVVGDCACAPN 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 555 PTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIMADVAQSKA 634
Cdd:COG0857 543 PPPEELALAAIISSSSAAAAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRRRDLLLDGPGPYQAAAAADVVVAKA 622
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774007702 635 PNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQ 703
Cdd:COG0857 623 KPSPVAGAAAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGVVDIDITIALTIIA 691
|
|
| pta |
TIGR00651 |
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ... |
401-701 |
4.41e-171 |
|
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from E.coli coding for ethanolamine utilization protein (euti) and also contains similarity to malate oxidoreductases [Central intermediary metabolism, Other, Energy metabolism, Fermentation]
Pssm-ID: 273196 [Multi-domain] Cd Length: 303 Bit Score: 491.95 E-value: 4.41e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 401 IVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIkrVAAAQGVTLGKGIEIVDPVAV---REEYVARLVELRKSKGMTE 477
Cdd:TIGR00651 1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEI--QPKAAGCNLDLGHVVIIDPDVspdRESYAERYVELRKHKGMTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 478 VVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAINPDPTA 557
Cdd:TIGR00651 79 AQARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 558 EQLSEIAIQSADSAAAFG-IEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIMADVAQSKAPN 636
Cdd:TIGR00651 159 EQLAEIAIQSANSAKSFGeIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKRPDLTIDGELQFDAAFVEKVAEKKAPN 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774007702 637 SPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTA 701
Cdd:TIGR00651 239 SPVAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNTGAITA 303
|
|
| Pta |
COG0280 |
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ... |
385-703 |
2.29e-169 |
|
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production and conversion];
Pssm-ID: 440049 [Multi-domain] Cd Length: 320 Bit Score: 488.04 E-value: 2.29e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 385 AFRYQLTELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLgKGIEIVDPV--AVREEY 462
Cdd:COG0280 1 KFFRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEELGLDL-SGFEIIDPEdsPRYEEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 463 VARLVELRKSKGMTEVVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQ 542
Cdd:COG0280 80 AEAYYELRKRKGVTPEEARELVRDAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIGLRPGVKRVSHVFLMELPDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 543 VLVYGDCAINPDPTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYD 622
Cdd:COG0280 160 LLFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKGPSTDKVREATKMARGQIPDLEVDGELQFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 623 AAIMADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAI 702
Cdd:COG0280 240 AALSPEAAKRKGPDSPVAGDANVLVFPDLEAGNILYKLLQRLAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNSIALAAV 319
|
.
gi 1774007702 703 Q 703
Cdd:COG0280 320 Q 320
|
|
| PTA_PTB |
pfam01515 |
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ... |
386-701 |
7.54e-158 |
|
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase and phosphate butaryltransferase. These enzymes catalyze the transfer of an acetyl or butaryl group to orthophosphate.
Pssm-ID: 396207 [Multi-domain] Cd Length: 318 Bit Score: 458.70 E-value: 7.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 386 FRYQLTELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGkGIEIVDPVAVR--EEYV 463
Cdd:pfam01515 1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDLD-GIEIVDPETSPrlEEYA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 464 ARLVELRKSKGMTEVVAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQV 543
Cdd:pfam01515 80 DFYYELRKRKGMTPEIAREIVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 544 LVYGDCAINPDPTAEQLSEIAIQSADSAAAFG-IEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYD 622
Cdd:pfam01515 160 LFFADCAVNPNPTAEELAEIALMSAKTAKRFGiIEPRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQFD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774007702 623 AAIMADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTA 701
Cdd:pfam01515 240 AALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAITA 318
|
|
| eutD |
PRK09653 |
phosphotransacetylase; |
389-704 |
1.05e-152 |
|
phosphotransacetylase;
Pssm-ID: 236609 [Multi-domain] Cd Length: 324 Bit Score: 445.83 E-value: 1.05e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 389 QLTELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLgKGIEIVDPV--AVREEYVARL 466
Cdd:PRK09653 6 SLKEKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDL-DGVEIIDPEtyPLLEEFAEAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 467 VELRKSKGMTEVvAREQLEDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVY 546
Cdd:PRK09653 85 VELRKGKGTEED-AAELLKDPNYFGTMLVKLGKADGMVSGAIHSTADTLRPALQIIKTKPGVKTVSSVFIMVKGDERYIF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 547 GDCAINPDPTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIM 626
Cdd:PRK09653 164 ADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLSFSTKGSAKGPEVDKVQEATEIAKELAPDLKIDGELQFDAAFV 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774007702 627 ADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQS 704
Cdd:PRK09653 244 PEVAAKKAPGSPVAGKANVFVFPSLEAGNIGYKIAQRLGGFEAVGPILQGLNKPVNDLSRGCSVEDIYNLALITAAQA 321
|
|
| PRK07232 |
PRK07232 |
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed |
389-703 |
4.48e-90 |
|
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
Pssm-ID: 235976 [Multi-domain] Cd Length: 752 Bit Score: 297.39 E-value: 4.48e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 389 QLTELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTL--GKGIEIVDPV--AVREEYVA 464
Cdd:PRK07232 430 PIFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIKKLGLDLkaGVDFEIVNPEddPRYEEYWQ 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 465 RLVELRKSKGMTEVVAREQLE-DNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQV 543
Cdd:PRK07232 510 YYYELLQRKGVTPEDARRLVRrDRTVIGAMMVARGDADAMICGLTGRYHEHLRPVRQVIGLRPGVHTAAAMNALLLKGGN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 544 LVYGDCAINPDPTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDA 623
Cdd:PRK07232 590 LFIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPSARKMREAVELLRERAPDLEVDGEMHGDA 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 624 AIMADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQ 703
Cdd:PRK07232 670 ALNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILLGMAKPVHILTPSATVRRIVNMTALAVVD 749
|
|
| PRK12862 |
PRK12862 |
malic enzyme; Reviewed |
392-701 |
1.02e-65 |
|
malic enzyme; Reviewed
Pssm-ID: 183799 [Multi-domain] Cd Length: 763 Bit Score: 231.70 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 392 ELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTL--GKGIEIVDPV--AVREEYVARLV 467
Cdd:PRK12862 441 AAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVIEARIERAGLRLrpGVDFEIVNPEddPRYRDYWDTYH 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 468 ELRKSKGMTEVVAREQL-EDNVVLGTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLVY 546
Cdd:PRK12862 521 ALMGRKGVTPEMARREVrRRTTLIGAMMVKRGEADAMICGTEGRYERHLEFVLQVIGKRPGVRVYAAMSLLILPGRTLFL 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 547 GDCAINPDPTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAIM 626
Cdd:PRK12862 601 ADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGSSDSPSARKMREALEILRERAPDLEVDGEMHGDAALD 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774007702 627 ADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSA-DLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTA 701
Cdd:PRK12862 681 EELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAAgNGLAVGPILLGAAKPVHILTPSATVRRIVNMTALAV 756
|
|
| PRK12861 |
PRK12861 |
malic enzyme; Reviewed |
392-704 |
3.10e-44 |
|
malic enzyme; Reviewed
Pssm-ID: 183798 [Multi-domain] Cd Length: 764 Bit Score: 170.07 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 392 ELARKAGK-RIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQG--VTLGKGIEIVDPVAVRE--EYVARL 466
Cdd:PRK12861 441 QLVRDGGKaRIVFTEGEDERVLRAVQVIVDEKLARPILVGRPEVLLARIERFGlrLRLGQDVEVTNPEYDERfpQYWTTY 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 467 VELRKSKGMTEVVAREQLEDNVVL-GTLMLEQGNVDGLVSGAVHTTANTIRPPLQLIKTAPGSSLVSSVFFMLLPDQVLV 545
Cdd:PRK12861 521 WELRCRDGISKEMARVEMRRRLTLiGAMMVRLGDADGMICGTVGEYHNHLRFVDEVIGRKPGASTYAAMNILLLDQRTVA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 546 YGDCAINPDPTAEQLSEIAIQSADSAAAFGIEPRVAMISYSTGNSGAGSDVEKVREATRLAQEKRPDLIIDGPLQYDAAI 625
Cdd:PRK12861 601 LVDTHVNDNPDAEQIAEFTIAAARQMEWLNLTPKVALLSRSNFGSGSAASGVKMRRALEIVREQAPDLEADGEMHGDCAL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 626 MADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSA-DLVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAIQS 704
Cdd:PRK12861 681 DEGLRARLLPMSPLKGAANLLVCPNVDAGNIAYNLLKTEAgSNVAVGPFLLGVNAPVNILTSSATVRRIVNMAALTVIEA 760
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
1-225 |
2.05e-40 |
|
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.
Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 147.02 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPRTGGDAPDQTTTIIRANSTVTAAEPLKMSH-VETLLSSNQQ- 78
Cdd:pfam13500 4 FVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTGLVEDGDSELVKRLLGLDQSYEDPEPFRLSApLSPHLAARQEg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 79 -DVLMEEIIaryHENTKDAEVVLVEGLVPTRKHQFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARssfggSK 157
Cdd:pfam13500 84 vTIDLEKII---YELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALR-----QR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774007702 158 NKNITGVIINKLNAPVDEQgrtrpdlseifddstkasvanidptQLFANSPLPVLGCIPWSFELIATR 225
Cdd:pfam13500 156 GIPVLGVILNGVPNPENVR-------------------------TIFAFGGVPVLGAVPYLPDLTAPT 198
|
|
| DRTGG |
pfam07085 |
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ... |
228-340 |
1.23e-29 |
|
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).
Pssm-ID: 429285 [Multi-domain] Cd Length: 105 Bit Score: 112.98 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 228 DMAKHLNARIINEGDVKTRRVKSVTFCARSIPHMLEHFRPGSLLVTSADRPDVLVSACLAAmngveIGAILLTGGYEIDA 307
Cdd:pfam07085 1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITPGDREDIQLAALEAG-----IAGLILTGGFEPSP 75
|
90 100 110
....*....|....*....|....*....|...
gi 1774007702 308 RINSLCERAfqtGLPVFMVETNTWQTSLSLQSF 340
Cdd:pfam07085 76 EVLKLAEEL---GLPVLSTPYDTFTTASRINRA 105
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
1-189 |
4.13e-29 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 114.59 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 1 MLIPTGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAQPRTGGDAPDqtTTIIRANS----TVTAAEPLKMS-HVETLLSS 75
Cdd:cd03109 4 FVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCPGLEDSD--AELLRKLAglllDLELINPYRFEaPLSPHLAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 76 NQQ--DVLMEEIIARYHENTKDAEVVLVEGLVPTRKHQFANALNYEIAKTLNAEIVFVLALGNDSPAQLKERIELARssf 153
Cdd:cd03109 82 ELEgrDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEALK--- 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1774007702 154 ggSKNKNITGVIINKlnapVDEQGRTRPDLSEIFDD 189
Cdd:cd03109 159 --SRGLDVAGVVLNG----IPPEPEAEADNAETLKE 188
|
|
| PRK05805 |
PRK05805 |
phosphate butyryltransferase; Validated |
407-702 |
1.23e-18 |
|
phosphate butyryltransferase; Validated
Pssm-ID: 180267 Cd Length: 301 Bit Score: 87.07 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 407 DEP--RTVKAAAlcaERGIAECVLLGNPDEIKRVAAAQGVTLGKgIEIVDPVAVREeyvarlvelrkskgmtevVAREQL 484
Cdd:PRK05805 27 DEPvlEAVKEAK---ELGIANAILVGDKEKIKEIAKEIDMDLED-FEIIDEKDNRK------------------AALKAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 485 EdnvvlgtlMLEQGNVDGLVSGAVHTtANTIRPPLQLIKTAPGSSLVSSVFFMLLP--DQVLVYGDCAINPDPTAEQLSE 562
Cdd:PRK05805 85 E--------LVSSGKADMVMKGLVDT-ANFLRAVLNKEIGLRTGKTMSHVAVFEVPkyDRLLFLTDAAFNIAPDLKEKID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 563 IAIQSADSAAAFGIE-PRVAMISystgnsgagsDVEKVR-------EATRLAQEKR----PDLIIDGPLQYDAAIMADVA 630
Cdd:PRK05805 156 IINNAVTVAHAIGIEnPKVAPIC----------AVEVVNpkmpatlDAALLSKMSDrgqiKGCIVDGPLALDNALSEEAA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774007702 631 QSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADlVSIGPMLQGMRKPVNDLSRGALVDDIVYTVALTAI 702
Cdd:PRK05805 226 KHKGIDGPVAGNADILLVPNIEAGNVMYKTLTYFAD-CKNGGLLVGTSAPVVLTSRADSHETKLNSIALAAL 296
|
|
| PRK08190 |
PRK08190 |
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated |
401-681 |
3.74e-17 |
|
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
Pssm-ID: 236180 [Multi-domain] Cd Length: 466 Bit Score: 84.93 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 401 IVLPEgdEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGkGIEIVDpVAVREEYVARLVELrkskgmtevvA 480
Cdd:PRK08190 181 VVHPC--DAESLRGALEAAEAGLIEPVLVGPEAKIRAAAEEAGLDLS-GVRIVD-VPHSHAAAARAVAL----------A 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 481 ReqlednvvlgtlmleQGNVDGLVSGAVHT---TANTIRPPLQLiKTApgsSLVSSVFFMLLP--DQVLVYGDCAINPDP 555
Cdd:PRK08190 247 R---------------AGEVEALMKGSLHTdelLSAVVARDSGL-RTE---RRISHVFAMDVPtyPRPLLITDAAINIAP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 556 TAEQLSEIaIQSA-DSAAAFGIE-PRVAMISYstgnsgagsdVEKVREATR-----LAQEKRPDL------IIDGPLQYD 622
Cdd:PRK08190 308 TLEDKRDI-VQNAiDLAHALGVEePKVAILSA----------VETVNPKMPstldaAALCKMADRgqitggIVDGPLAFD 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1774007702 623 AAIMADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLqGMRKPV 681
Cdd:PRK08190 377 NAISAEAARTKGIVSPVAGQADILVVPDLEAGNMLAKQLTYLAGADAAGIVL-GARVPI 434
|
|
| PRK07742 |
PRK07742 |
phosphate butyryltransferase; Validated |
386-699 |
4.61e-16 |
|
phosphate butyryltransferase; Validated
Pssm-ID: 236086 Cd Length: 299 Bit Score: 79.37 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 386 FRYQLTELARKAGKRIVLPEGDEPRTVKAAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGKGIEIVDpvAVREEYVAR 465
Cdd:PRK07742 3 LEHLIDQAAGQPKKTVAVAVAEDEEVIEAVAKAIELQLARFRLYGNQEKIMGMLQEHGLQTSEHIEIIH--AQSSAEAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 466 LVelrkskgmteVVAREQLEDNVvlgtLMleQGNVdglvsgavhTTANTIRPPLQLIKTAPGSSLVSSVFFMLLP--DQV 543
Cdd:PRK07742 81 LA----------VKAVRNGEADV----LM--KGNV---------PTANILKAVLNKEWGLRKGSVLSHVAVFEVPnyDRL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 544 LVYGDCAINPDPTAEQLSEIAIQSADSAAAFGIE-PRVAMIsystgnsGAGSDVEKVREAT----RLAQEKR----PDLI 614
Cdd:PRK07742 136 IFVTDAAMNIAPDLEQKAAIIQNAVEVARAIGIDlPKVAPL-------AAVEVVNPAMQATidaaALTQMNRrgqiKNCV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 615 IDGPLQYDAAIMADVAQSKAPNSPVAGKATVFIFPDLNTGNTTYKAVQRSADlVSIGPMLQGMRKPVNDLSRGALVDDIV 694
Cdd:PRK07742 209 VDGPLALDNAVSQIAAEHKGIVSDVAGKADILLVPTIEAGNVLYKSLVYFAD-AKVGAMIAGAKAPIVLTSRADSAETKL 287
|
....*
gi 1774007702 695 YTVAL 699
Cdd:PRK07742 288 YSLAL 292
|
|
| PRK11890 |
PRK11890 |
phosphate acetyltransferase; Provisional |
414-686 |
2.15e-14 |
|
phosphate acetyltransferase; Provisional
Pssm-ID: 183361 Cd Length: 312 Bit Score: 74.64 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 414 AAALCAERGIAECVLLGNPDEIKRVAAAQGVTLGkGIEIVDpVAVREEYVARLVELrkskgmtevvAREqlednvvlgtl 493
Cdd:PRK11890 38 GAVEAAQLGLITPILVGPRARIEAVAAECGLDLS-GYEIVD-APHSHAAAAKAVEL----------VRE----------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 494 mleqGNVDGLVSGAVHTTantirpplQLIK--TAPGSSL-----VSSVFFMLLP--DQVLVYGDCAINPDPTAEQLSEIA 564
Cdd:PRK11890 95 ----GEAEALMKGSLHTD--------ELMSavVARDTGLrterrISHVFVMDVPgyPKPLIITDAAVNIAPTLEDKADIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 565 IQSADSAAAFGI-EPRVAMIS-YSTGNSGAGSDVEkvreATRLAqeKRPD------LIIDGPLQYDAAIMADVAQSKAPN 636
Cdd:PRK11890 163 QNAIDLAHALGFdEPRVAILSaVETVNPKIPSTLD----AAALC--KMADrgqitgAILDGPLAFDNAISPEAARIKGIV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1774007702 637 SPVAGKATVFIFPDLNTGNTTYKAVQRSADLVSIGPMLqGMRKPVNDLSR 686
Cdd:PRK11890 237 SPVAGDADILVVPDLEAGNMLAKQLTFLAGADAAGIVL-GARVPIILTSR 285
|
|
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
5-217 |
6.65e-07 |
|
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439902 [Multi-domain] Cd Length: 222 Bit Score: 50.93 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 5 TGTSVGLTSVSLGVIRAMEQKGVSLSIFKPIAqprTGGDAPDQT-----TTIIRANSTVtaaePLKMSHVETL------- 72
Cdd:COG0132 9 TDTDVGKTVVTAALAAALRAAGLRVGYYKPVQ---TGCEETDGGlrngdAELLRRLSGL----PLSYELVNPYrfeepls 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 73 --LSSNQ--QDVLMEEIIARYHENTKDAEVVLVEG----LVP-TRKHQFAnalnyEIAKTLNAEIVFV--LALG--NDSP 139
Cdd:COG0132 82 phLAARLegVPIDLDKILAALRALAARYDLVLVEGagglLVPlTEDLTLA-----DLAKALGLPVILVvrARLGtiNHTL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774007702 140 AQlkerIELARssfggSKNKNITGVIINKLNAPVDEQGRTRPDLSEIfddstkasvanidptqlfanSPLPVLGCIPW 217
Cdd:COG0132 157 LT----VEALR-----ARGLPLAGIVLNGVPPPDLAERDNLETLERL--------------------TGAPVLGVLPY 205
|
|
| CobB_N |
cd05388 |
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
5-216 |
1.72e-04 |
|
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.
Pssm-ID: 349773 [Multi-domain] Cd Length: 193 Bit Score: 42.97 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 5 TGTSVGLTSVSLGVIRAMEQKGVSLSIFKpiaqprTGgdaPDQTTTIIraNSTVTAAEplkmshvetllSSNQQDVLM-- 82
Cdd:cd05388 8 TSSGSGKTTITLGLMRALARRGLRVQPFK------VG---PDYIDPGF--HEAATGRP-----------SRNLDSWMMge 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 83 EEIIARYHENTKDAEVVLVEGL------VPTRKHQFANAlnyEIAKTLNAEIVFVL---ALGNDSPAQLKERIELarssf 153
Cdd:cd05388 66 DGVRELFARAAGGADVAIIEGVmglydgRDTDSDEGSTA---ELARLLGAPVLLVLdckGMARSAAAIVKGYKEF----- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774007702 154 ggSKNKNITGVIINKLNAPVDEQGRTRpdlseifddstkasvanidptQLFANSPLPVLGCIP 216
Cdd:cd05388 138 --DPDLNLAGVILNRVGSPRHAELLKE---------------------AIEEYTGIPVLGYLP 177
|
|
| DsbA_HCCA_Iso |
cd03022 |
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ... |
383-468 |
2.87e-04 |
|
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).
Pssm-ID: 239320 [Multi-domain] Cd Length: 192 Bit Score: 42.62 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774007702 383 PPAFRYQLTELARKAGKR---IVLPEGDEPRTVKAAAL---CAERG-----IAECVL---------LGNPDEIKRVAAAQ 442
Cdd:cd03022 54 PAKGRYRLRDLERWARRYgipLRFPPRFPPNTLRAMRAalaAQAEGdaaeaFARAVFralwgegldIADPAVLAAVAAAA 133
|
90 100
....*....|....*....|....*.
gi 1774007702 443 GVTLGKGIEIVDPVAVREEYVARLVE 468
Cdd:cd03022 134 GLDADELLAAADDPAVKAALRANTEE 159
|
|
| |
