|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-727 |
0e+00 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 960.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 1 MARSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIARSkhkpdyvlelllnhlqagkpagtnpatqpaltydecv 80
Cdd:PRK05632 1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 81 GVTYDDVHA-----DPDAALARIVARYKAVEAQCDAVVVIGSDFTDVgSPTELAYNARIAANLGVPVLLVLAGRvgfgqg 155
Cdd:PRK05632 44 PLTMSEVEAllasgQLDELLEEIVARYHALAKDCDVVLVEGLDPTRK-HPFEFSLNAEIAKNLGAEVVLVSSGG------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 156 eglsqsdqlgqsePRTSDDIRQLTDVALTELQ-SEHVSLLGVVVNR--ADPENLNGLIAAVREGVDNLPDTPDAM----- 227
Cdd:PRK05632 117 -------------NDTPEELAERIELAASSFGgAKNANILGVIINKlnAPVDEQGRTRPDLSEIFDDSSKANVDPsklfa 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 228 HAAVVPVWAIPEDAFLVAPSMKTILEATHGTLVqGDPELLSREALSVVVAAMSMVNVLPRLTEGAVVVIPSDRPEVLLAA 307
Cdd:PRK05632 184 SSPLPLLGVVPWSPDLIAPRVIDIAKHLGATVL-NEGDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 308 LMANSSAtfPSLAGVVLVGGFPLPESIEQLMKGLAPS-VPIIRTDLASYEAALRITHTRGRLAADSQRKHDTALALFEQH 386
Cdd:PRK05632 263 LLAAMNG--PPIAGLLLTGGYEPDPRIAKLCEGAFETgLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASH 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 387 VDGGALLDRLKV--SRADVVTPLMFEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIG 464
Cdd:PRK05632 341 VDTDELLERLTAtsERSRRLSPPAFRYQLTERARAAKKRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 465 LGLDL-AKATVVSPfdDVLRMRFAEEYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSF 543
Cdd:PRK05632 421 QGVDLpAGIEIIDP--SEVRERYVAPLVELRKHKGMTEEVAREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPAL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 544 EIIKTRPGVSVVSSVFLMALADRVLVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKV 623
Cdd:PRK05632 499 QLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAEQLAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 624 REATAIVRERRPDLAVEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRK 703
Cdd:PRK05632 579 REATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSPVAGRATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRK 658
|
730 740
....*....|....*....|....
gi 1054830065 704 PINDLSRGALVQDIVNTVAITAIQ 727
Cdd:PRK05632 659 PVNDLSRGALVDDIVNTIAITAIQ 682
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-727 |
0e+00 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 737.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 1 MARSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIARS---KHKPDYVLELLLNHLQAGKPagtnpatqpaltYD 77
Cdd:COG0857 1 MMKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSlvgGGERDEDVELIREHLGLDLP------------YE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 78 ECVGVTYDDVHA-----DPDAALARIVARYKAVEAQCDAVVVIGSDFTDVGSPTELAYNARIAANLGVPVLLVLAGRVgf 152
Cdd:COG0857 69 DASPVTLDEVETllaegDPDELLERIVERYEALAAECDVVLVEGSDPTGVGSPFELSLNARIAKNLGAPVLLVASGGG-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 153 gqgeglsqsdqlgqsepRTSDDIRQLTDVALTELQSEHVSLLGVVVNRADPENLNGLIAAVREGVDNLPdtpdamhaaVV 232
Cdd:COG0857 147 -----------------RTPEELVDALLLAADEFRGEGARVLGVIINRVPPEKLEEVREALRPFLEGSG---------IP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 233 PVWAIPEDAFLVAPSMKTILEATHGTLVQGdPELLSREALSVVVAAMSMVNVLPRLTEGAVVVIPSDRPEVLLAALMANS 312
Cdd:COG0857 201 VLGVIPENPELAAPTVRDLAEALGAEVLNG-GELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAAL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 313 SATfPSLAGVVLVGGFPLPESIEQLMKGLAPSVPIIRTDLASYEAALRITHTRGRLAADSQRKHDTALALFEQHVDGGAL 392
Cdd:COG0857 280 SGT-PSIAGLILTGGLPPDPAVLRLAEGLGQTLPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 393 LDRLKVSRADVVTPLMFEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKA 472
Cdd:COG0857 359 LSRLGLPRSRLSPPAFFYYLLERAARAAKRIVLPEGGEDRRILAAAICLLRRIAACVLLGGPEEIIRVAAAQGGLLLDGI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 473 TVVSPFDDVLRMRFAEEYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGV 552
Cdd:COG0857 439 EIIDPPDSRLRYVAAEVYLRRRKKKGVTVAAAQLEDDVVLYTGMMMVHEGDGLGMGSGATTTTTTTIPPQLIITKTGPGV 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 553 SVVSSVFLMALADRVLVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRE 632
Cdd:COG0857 519 VSSSSFFLMLLQVVVVGDCACAPNPPPEELALAAIISSSSAAAAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 633 RRPDLAVEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGA 712
Cdd:COG0857 599 RDLLLDGPGPYQAAAAADVVVAKAKPSPVAGAAAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGV 678
|
730
....*....|....*
gi 1054830065 713 LVQDIVNTVAITAIQ 727
Cdd:COG0857 679 VDIDITIALTIIAAQ 693
|
|
| PTA_PTB |
pfam01515 |
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ... |
409-725 |
2.65e-148 |
|
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: 435.20 E-value: 2.65e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 409 FEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDVLRMRFAE 488
Cdd:pfam01515 1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDLDGIEIVDPETSPRLEEYAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 489 EYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRVL 568
Cdd:pfam01515 81 FYYELRKRKGMTPEIAREIVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 569 VYGDCAVNPDPTAAQLADIAISASETALEFG-IEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDA 647
Cdd:pfam01515 161 FFADCAVNPNPTAEELAEIALMSAKTAKRFGiIEPRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQFDA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054830065 648 AADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITA 725
Cdd:pfam01515 241 ALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAITA 318
|
|
| pta |
TIGR00651 |
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ... |
424-725 |
3.65e-137 |
|
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: 406.05 E-value: 3.65e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 424 IVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDVLRMRFAEEYARLRAHKGVTIDQ 503
Cdd:TIGR00651 1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGCNLDLGHVVIIDPDVSPDRESYAERYVELRKHKGMTEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 504 ARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRVLVYGDCAVNPDPTAAQ 583
Cdd:TIGR00651 81 ARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 584 LADIAISASETALEFG-IEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDAAADAAVAAAKMPDSD 662
Cdd:TIGR00651 161 LAEIAIQSANSAKSFGeIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKRPDLTIDGELQFDAAFVEKVAEKKAPNSP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054830065 663 VAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITA 725
Cdd:TIGR00651 241 VAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNTGAITA 303
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
3-206 |
7.15e-07 |
|
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: 50.26 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 3 RSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIarskhkpdyvlelllnhlQAGKPAGTNP-------ATQPALT 75
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPV------------------QTGCPGLEDSdaellrkLAGLLLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 76 YDECVGVTYDDvHADPDAA---------LARIVARYKAVEAQCDAVVVIGSDFTDVGSPTELaYNARIAANLGVPVLLVL 146
Cdd:cd03109 63 LELINPYRFEA-PLSPHLAaelegrdidLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGY-LNADLARALGLPVILVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 147 AGRVGfgqgeglsqsdqlgqseprtsdDIRQLTDvALTELQSEHVSLLGVVVNRADPENL 206
Cdd:cd03109 141 RGGLG----------------------TINHTLL-TLEALKSRGLDVAGVVLNGIPPEPE 177
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-727 |
0e+00 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 960.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 1 MARSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIARSkhkpdyvlelllnhlqagkpagtnpatqpaltydecv 80
Cdd:PRK05632 1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 81 GVTYDDVHA-----DPDAALARIVARYKAVEAQCDAVVVIGSDFTDVgSPTELAYNARIAANLGVPVLLVLAGRvgfgqg 155
Cdd:PRK05632 44 PLTMSEVEAllasgQLDELLEEIVARYHALAKDCDVVLVEGLDPTRK-HPFEFSLNAEIAKNLGAEVVLVSSGG------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 156 eglsqsdqlgqsePRTSDDIRQLTDVALTELQ-SEHVSLLGVVVNR--ADPENLNGLIAAVREGVDNLPDTPDAM----- 227
Cdd:PRK05632 117 -------------NDTPEELAERIELAASSFGgAKNANILGVIINKlnAPVDEQGRTRPDLSEIFDDSSKANVDPsklfa 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 228 HAAVVPVWAIPEDAFLVAPSMKTILEATHGTLVqGDPELLSREALSVVVAAMSMVNVLPRLTEGAVVVIPSDRPEVLLAA 307
Cdd:PRK05632 184 SSPLPLLGVVPWSPDLIAPRVIDIAKHLGATVL-NEGDILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 308 LMANSSAtfPSLAGVVLVGGFPLPESIEQLMKGLAPS-VPIIRTDLASYEAALRITHTRGRLAADSQRKHDTALALFEQH 386
Cdd:PRK05632 263 LLAAMNG--PPIAGLLLTGGYEPDPRIAKLCEGAFETgLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASH 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 387 VDGGALLDRLKV--SRADVVTPLMFEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIG 464
Cdd:PRK05632 341 VDTDELLERLTAtsERSRRLSPPAFRYQLTERARAAKKRIVLPEGDEPRTLKAAAICLERGIADCVLLGNPEEIRRVAAA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 465 LGLDL-AKATVVSPfdDVLRMRFAEEYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSF 543
Cdd:PRK05632 421 QGVDLpAGIEIIDP--SEVRERYVAPLVELRKHKGMTEEVAREQLEDNVYFGTMMLALGEVDGLVSGAVHTTANTIRPAL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 544 EIIKTRPGVSVVSSVFLMALADRVLVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKV 623
Cdd:PRK05632 499 QLIKTAPGSSLVSSVFFMLLPDQVLVYGDCAVNPDPTAEQLAEIAIQSADSAAAFGIEPRVAMLSYSTGTSGSGADVEKV 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 624 REATAIVRERRPDLAVEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRK 703
Cdd:PRK05632 579 REATRLARERRPDLLIDGPLQYDAAVDPSVARSKAPNSPVAGRATVFIFPDLNTGNTTYKAVQRSAGAVSIGPMLQGLRK 658
|
730 740
....*....|....*....|....
gi 1054830065 704 PINDLSRGALVQDIVNTVAITAIQ 727
Cdd:PRK05632 659 PVNDLSRGALVDDIVNTIAITAIQ 682
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-727 |
0e+00 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 737.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 1 MARSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIARS---KHKPDYVLELLLNHLQAGKPagtnpatqpaltYD 77
Cdd:COG0857 1 MMKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSlvgGGERDEDVELIREHLGLDLP------------YE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 78 ECVGVTYDDVHA-----DPDAALARIVARYKAVEAQCDAVVVIGSDFTDVGSPTELAYNARIAANLGVPVLLVLAGRVgf 152
Cdd:COG0857 69 DASPVTLDEVETllaegDPDELLERIVERYEALAAECDVVLVEGSDPTGVGSPFELSLNARIAKNLGAPVLLVASGGG-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 153 gqgeglsqsdqlgqsepRTSDDIRQLTDVALTELQSEHVSLLGVVVNRADPENLNGLIAAVREGVDNLPdtpdamhaaVV 232
Cdd:COG0857 147 -----------------RTPEELVDALLLAADEFRGEGARVLGVIINRVPPEKLEEVREALRPFLEGSG---------IP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 233 PVWAIPEDAFLVAPSMKTILEATHGTLVQGdPELLSREALSVVVAAMSMVNVLPRLTEGAVVVIPSDRPEVLLAALMANS 312
Cdd:COG0857 201 VLGVIPENPELAAPTVRDLAEALGAEVLNG-GELLDRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAAL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 313 SATfPSLAGVVLVGGFPLPESIEQLMKGLAPSVPIIRTDLASYEAALRITHTRGRLAADSQRKHDTALALFEQHVDGGAL 392
Cdd:COG0857 280 SGT-PSIAGLILTGGLPPDPAVLRLAEGLGQTLPILSVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 393 LDRLKVSRADVVTPLMFEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKA 472
Cdd:COG0857 359 LSRLGLPRSRLSPPAFFYYLLERAARAAKRIVLPEGGEDRRILAAAICLLRRIAACVLLGGPEEIIRVAAAQGGLLLDGI 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 473 TVVSPFDDVLRMRFAEEYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGV 552
Cdd:COG0857 439 EIIDPPDSRLRYVAAEVYLRRRKKKGVTVAAAQLEDDVVLYTGMMMVHEGDGLGMGSGATTTTTTTIPPQLIITKTGPGV 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 553 SVVSSVFLMALADRVLVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRE 632
Cdd:COG0857 519 VSSSSFFLMLLQVVVVGDCACAPNPPPEELALAAIISSSSAAAAGFGPEPAMISLSSSTSGSGGGVDVVKVATATALVRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 633 RRPDLAVEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGA 712
Cdd:COG0857 599 RDLLLDGPGPYQAAAAADVVVAKAKPSPVAGAAAAFVFPFLDTNNTNNTAKARQASAGAVAPGPQGLGLPVNDLDLSRGV 678
|
730
....*....|....*
gi 1054830065 713 LVQDIVNTVAITAIQ 727
Cdd:COG0857 679 VDIDITIALTIIAAQ 693
|
|
| Pta |
COG0280 |
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production ... |
408-727 |
5.34e-155 |
|
Phosphotransacetylase (includes Pta, EutD and phosphobutyryltransferase) [Energy production and conversion];
Pssm-ID: 440049 [Multi-domain] Cd Length: 320 Bit Score: 452.22 E-value: 5.34e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 408 MFEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDVLRMRFA 487
Cdd:COG0280 1 KFFRPLIERAKAAPKRIVFAEGEDERVLRAAQEALDEGLAEPILVGRPEKIEARAEELGLDLSGFEIIDPEDSPRYEEYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 488 EEYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRV 567
Cdd:COG0280 81 EAYYELRKRKGVTPEEARELVRDAAYFAAMMVRLGEADGLVKGAVGTTADLLRPVLQIIGLRPGVKRVSHVFLMELPDRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 568 LVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDA 647
Cdd:COG0280 161 LFITDTAVNIDPTAEQLADIAINAADTARAFGIEPKVALLSASEFGSPKGPSTDKVREATKMARGQIPDLEVDGELQFDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 648 AADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITAIQ 727
Cdd:COG0280 241 ALSPEAAKRKGPDSPVAGDANVLVFPDLEAGNILYKLLQRLAGAEAIGPILLGLAKPVHLLSRGDSVRDIVNSIALAAVQ 320
|
|
| eutD |
PRK09653 |
phosphotransacetylase; |
408-727 |
1.47e-150 |
|
phosphotransacetylase;
Pssm-ID: 236609 [Multi-domain] Cd Length: 324 Bit Score: 441.21 E-value: 1.47e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 408 MFEyTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDVLRMRFA 487
Cdd:PRK09653 3 LFE-SLKEKAKGKKKKIVLPEGEDERVLKAAKRLQKEGLVEPILLGNPEEIRAKAKELGLDLDGVEIIDPETYPLLEEFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 488 EEYARLRAHKGvTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRV 567
Cdd:PRK09653 82 EAFVELRKGKG-TEEDAAELLKDPNYFGTMLVKLGKADGMVSGAIHSTADTLRPALQIIKTKPGVKTVSSVFIMVKGDER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 568 LVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDA 647
Cdd:PRK09653 161 YIFADCAVNPNPTAEQLAEIAINSAETAKAFGIDPKVAMLSFSTKGSAKGPEVDKVQEATEIAKELAPDLKIDGELQFDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 648 AADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITAIQ 727
Cdd:PRK09653 241 AFVPEVAAKKAPGSPVAGKANVFVFPSLEAGNIGYKIAQRLGGFEAVGPILQGLNKPVNDLSRGCSVEDIYNLALITAAQ 320
|
|
| PTA_PTB |
pfam01515 |
Phosphate acetyl/butaryl transferase; This family contains both phosphate acetyltransferase ... |
409-725 |
2.65e-148 |
|
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: 435.20 E-value: 2.65e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 409 FEYTLLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDVLRMRFAE 488
Cdd:pfam01515 1 FLERIFERAKKAKKRIVFPEGEDERVLKAAQKLLQQGIADPILIGDEIEIKAKALGLDLDLDGIEIVDPETSPRLEEYAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 489 EYARLRAHKGVTIDQARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRVL 568
Cdd:pfam01515 81 FYYELRKRKGMTPEIAREIVRDPNYFAAMLVKLGEADGMVSGAVNTTADTLRPALQIIGTKPGVKTVSSVFIMLLPDGLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 569 VYGDCAVNPDPTAAQLADIAISASETALEFG-IEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDA 647
Cdd:pfam01515 161 FFADCAVNPNPTAEELAEIALMSAKTAKRFGiIEPRVALLSYSTFGSGKGEDVEKVREATKIVRERAPDLVVDGELQFDA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054830065 648 AADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITA 725
Cdd:pfam01515 241 ALVEEVAAQKAPDSPVAGKANVFVFPDLEAGNIGYKIAQRLGGAEAIGPILQGLAKPVNDLSRGASVEDIVNTAAITA 318
|
|
| pta |
TIGR00651 |
phosphate acetyltransferase; Alternate name: phosphotransacetylase Model contains a gene from ... |
424-725 |
3.65e-137 |
|
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: 406.05 E-value: 3.65e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 424 IVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDVLRMRFAEEYARLRAHKGVTIDQ 503
Cdd:TIGR00651 1 IVFPEGWEPRVLKAAALLAERGIATPVVLGNPEEIQPKAAGCNLDLGHVVIIDPDVSPDRESYAERYVELRKHKGMTEAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 504 ARDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRVLVYGDCAVNPDPTAAQ 583
Cdd:TIGR00651 81 ARKQLRDESYFATMMVALGEADGLVSGAVHTTADTLRPALQIIKTLPGVKIVSSVFIMDLGEEVLVFADCAVNPDPNAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 584 LADIAISASETALEFG-IEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDAAADAAVAAAKMPDSD 662
Cdd:TIGR00651 161 LAEIAIQSANSAKSFGeIEPKVALLSYSTKGSGKGEEVEKVREATRIAKEKRPDLTIDGELQFDAAFVEKVAEKKAPNSP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1054830065 663 VAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITA 725
Cdd:TIGR00651 241 VAGSANVFVFPDLDAGNIGYKIVQRLGDAEAIGPILQGLNKPVNDLSRGCSVEDIVNTGAITA 303
|
|
| PRK07232 |
PRK07232 |
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed |
413-727 |
4.48e-89 |
|
bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed
Pssm-ID: 235976 [Multi-domain] Cd Length: 752 Bit Score: 295.47 E-value: 4.48e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 413 LLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKA---TVVSPFDDVLRMRFAEE 489
Cdd:PRK07232 431 IFAKAKKDPKRVVFAEGEEERVLRAAQEVVDEGLAKPILIGRPEVIEARIKKLGLDLKAGvdfEIVNPEDDPRYEEYWQY 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 490 YARLRAHKGVTIDQA-RDVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRVL 568
Cdd:PRK07232 511 YYELLQRKGVTPEDArRLVRRDRTVIGAMMVARGDADAMICGLTGRYHEHLRPVRQVIGLRPGVHTAAAMNALLLKGGNL 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 569 VYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDAA 648
Cdd:PRK07232 591 FIADTYVNEDPTAEELAEIALMAAEEVRRFGIEPRVALLSHSNFGSSDSPSARKMREAVELLRERAPDLEVDGEMHGDAA 670
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1054830065 649 ADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITAIQ 727
Cdd:PRK07232 671 LNEEIRKDLYPFSRLKGPANVLVMPNLEAANISYNLLKELGGGVTIGPILLGMAKPVHILTPSATVRRIVNMTALAVVD 749
|
|
| PRK12862 |
PRK12862 |
malic enzyme; Reviewed |
413-725 |
7.05e-70 |
|
malic enzyme; Reviewed
Pssm-ID: 183799 [Multi-domain] Cd Length: 763 Bit Score: 243.64 E-value: 7.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 413 LLERARQNRMRIVLPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDL---AKATVVSPFDDVLRMRFAEE 489
Cdd:PRK12862 439 VFAAAKAAPKRVVFAEGEDERVLRAAQVVVDEGLAKPILIGRPAVIEARIERAGLRLrpgVDFEIVNPEDDPRYRDYWDT 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 490 YARLRAHKGVTIDQARDVV-TDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVFLMALADRVL 568
Cdd:PRK12862 519 YHALMGRKGVTPEMARREVrRRTTLIGAMMVKRGEADAMICGTEGRYERHLEFVLQVIGKRPGVRVYAAMSLLILPGRTL 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 569 VYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAVEGPIQYDAA 648
Cdd:PRK12862 599 FLADTHVNEDPTAEELAEITILAAEEVRRFGIEPKVALLSHSNFGSSDSPSARKMREALEILRERAPDLEVDGEMHGDAA 678
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1054830065 649 ADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAG-AVAIGPVLQGLRKPINDLSRGALVQDIVNTVAITA 725
Cdd:PRK12862 679 LDEELRDRIFPDSRLEGEANLLVFPNLDAANIAYNLLKTAAGnGLAVGPILLGAAKPVHILTPSATVRRIVNMTALAV 756
|
|
| PRK12861 |
PRK12861 |
malic enzyme; Reviewed |
409-727 |
7.93e-47 |
|
malic enzyme; Reviewed
Pssm-ID: 183798 [Multi-domain] Cd Length: 764 Bit Score: 178.16 E-value: 7.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 409 FEYTLLERARQ-----NRMRIVLPEGDDDRVLRAAATLLARDVADLIILG--EEFEVRSRAIGLGLDLAK-ATVVSPFDD 480
Cdd:PRK12861 431 FMKPLFAAARQlvrdgGKARIVFTEGEDERVLRAVQVIVDEKLARPILVGrpEVLLARIERFGLRLRLGQdVEVTNPEYD 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 481 VLRMRFAEEYARLRAHKGVTIDQAR-DVVTDVSYFGTMMVQLGLADGMVSGASHTTAHTIRPSFEIIKTRPGVSVVSSVF 559
Cdd:PRK12861 511 ERFPQYWTTYWELRCRDGISKEMARvEMRRRLTLIGAMMVRLGDADGMICGTVGEYHNHLRFVDEVIGRKPGASTYAAMN 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 560 LMALADRVLVYGDCAVNPDPTAAQLADIAISASETALEFGIEPRIAMLSYSTGISGNGADVEKVREATAIVRERRPDLAV 639
Cdd:PRK12861 591 ILLLDQRTVALVDTHVNDNPDAEQIAEFTIAAARQMEWLNLTPKVALLSRSNFGSGSAASGVKMRRALEIVREQAPDLEA 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 640 EGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGA-VAIGPVLQGLRKPINDLSRGALVQDIV 718
Cdd:PRK12861 671 DGEMHGDCALDEGLRARLLPMSPLKGAANLLVCPNVDAGNIAYNLLKTEAGSnVAVGPFLLGVNAPVNILTSSATVRRIV 750
|
....*....
gi 1054830065 719 NTVAITAIQ 727
Cdd:PRK12861 751 NMAALTVIE 759
|
|
| DRTGG |
pfam07085 |
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ... |
251-364 |
2.07e-21 |
|
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: 89.48 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 251 ILEATHGTLVQGDPELLsREALSVVVAAMSMVNVLPRLTEGAVVVIPSDRPEVLLAALMAnssatfpSLAGVVLVGGFPL 330
Cdd:pfam07085 2 IARILGAEVLNGGDGLL-RRVGKVVVGAMSVENMLKYLRPGDLVITPGDREDIQLAALEA-------GIAGLILTGGFEP 73
|
90 100 110
....*....|....*....|....*....|....
gi 1054830065 331 PESIEQLMKGLapSVPIIRTDLASYEAALRITHT 364
Cdd:pfam07085 74 SPEVLKLAEEL--GLPVLSTPYDTFTTASRINRA 105
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
3-205 |
3.68e-15 |
|
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: 74.60 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 3 RSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIarskhkpdyvlelllnhlQAGKPAGTNPATQPAL-----TYD 77
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPV------------------QTGLVEDGDSELVKRLlgldqSYE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 78 ECVGVTYDDVHADPDAA--------LARIVaryKAVEAQCDAVVVIGSDFTDVGsPTELAYNARIAANLGVPVLLVLAGR 149
Cdd:pfam13500 63 DPEPFRLSAPLSPHLAArqegvtidLEKII---YELPADADPVVVEGAGGLLVP-INEDLLNADIAANLGLPVILVARGG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1054830065 150 VGfgqgeglsqsdqlgqseprtsddirQLTDVALT--ELQSEHVSLLGVVVNR-ADPEN 205
Cdd:pfam13500 139 LG-------------------------TINHTLLTleALRQRGIPVLGVILNGvPNPEN 172
|
|
| PRK05805 |
PRK05805 |
phosphate butyryltransferase; Validated |
413-726 |
3.07e-08 |
|
phosphate butyryltransferase; Validated
Pssm-ID: 180267 Cd Length: 301 Bit Score: 55.87 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 413 LLERARQNRMRIV-LPEGDDDRVLRAAATLLARDVADLIILGEEFEVRSRAIGLGLDLAKATVVSPFDDvlrmrfaeeya 491
Cdd:PRK05805 8 ILSKAKEQPPKTIsVAVAQDEPVLEAVKEAKELGIANAILVGDKEKIKEIAKEIDMDLEDFEIIDEKDN----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 492 rlrahkgvtIDQARDVVTDVSYFGTMMVQLGLADgmvsgashtTAHTIRPSFEI-IKTRPGvSVVS--SVFLMALADRVL 568
Cdd:PRK05805 77 ---------RKAALKAVELVSSGKADMVMKGLVD---------TANFLRAVLNKeIGLRTG-KTMShvAVFEVPKYDRLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 569 VYGDCAVNPDPTAAQLADIAISASETALEFGIE-PRIAMLSYSTGISGN------GADVEKVREATAIvrerrPDLAVEG 641
Cdd:PRK05805 138 FLTDAAFNIAPDLKEKIDIINNAVTVAHAIGIEnPKVAPICAVEVVNPKmpatldAALLSKMSDRGQI-----KGCIVDG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 642 PIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAvAIGPVLQGLRKPINDLSRGALVQDIVNTV 721
Cdd:PRK05805 213 PLALDNALSEEAAKHKGIDGPVAGNADILLVPNIEAGNVMYKTLTYFADC-KNGGLLVGTSAPVVLTSRADSHETKLNSI 291
|
....*
gi 1054830065 722 AITAI 726
Cdd:PRK05805 292 ALAAL 296
|
|
| PRK11890 |
PRK11890 |
phosphate acetyltransferase; Provisional |
555-710 |
2.46e-07 |
|
phosphate acetyltransferase; Provisional
Pssm-ID: 183361 Cd Length: 312 Bit Score: 53.07 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 555 VSSVFLMALA--DRVLVYGDCAVNPDPTAAQLADIAISASETALEFGI-EPRIAMLSYSTGISgngADVEKVREATAIVR 631
Cdd:PRK11890 127 ISHVFVMDVPgyPKPLIITDAAVNIAPTLEDKADIVQNAIDLAHALGFdEPRVAILSAVETVN---PKIPSTLDAAALCK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 632 --ERR--PDLAVEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVAIGPVLqGLRKPIND 707
Cdd:PRK11890 204 maDRGqiTGAILDGPLAFDNAISPEAARIKGIVSPVAGDADILVVPDLEAGNMLAKQLTFLAGADAAGIVL-GARVPIIL 282
|
...
gi 1054830065 708 LSR 710
Cdd:PRK11890 283 TSR 285
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
3-206 |
7.15e-07 |
|
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: 50.26 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 3 RSIYITSAEGNTGKSTIALGVLDTLLHSIERVGVFRPIarskhkpdyvlelllnhlQAGKPAGTNP-------ATQPALT 75
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPV------------------QTGCPGLEDSdaellrkLAGLLLD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 76 YDECVGVTYDDvHADPDAA---------LARIVARYKAVEAQCDAVVVIGSDFTDVGSPTELaYNARIAANLGVPVLLVL 146
Cdd:cd03109 63 LELINPYRFEA-PLSPHLAaelegrdidLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGY-LNADLARALGLPVILVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 147 AGRVGfgqgeglsqsdqlgqseprtsdDIRQLTDvALTELQSEHVSLLGVVVNRADPENL 206
Cdd:cd03109 141 RGGLG----------------------TINHTLL-TLEALKSRGLDVAGVVLNGIPPEPE 177
|
|
| PRK07742 |
PRK07742 |
phosphate butyryltransferase; Validated |
553-710 |
3.17e-06 |
|
phosphate butyryltransferase; Validated
Pssm-ID: 236086 Cd Length: 299 Bit Score: 49.71 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 553 SVVS--SVFLMALADRVLVYGDCAVNPDPTAAQLADIAISASETALEFGIE-PRIAMLsystgisgngADVEKVR----- 624
Cdd:PRK07742 119 SVLShvAVFEVPNYDRLIFVTDAAMNIAPDLEQKAAIIQNAVEVARAIGIDlPKVAPL----------AAVEVVNpamqa 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 625 --EATAIV----RERRPDLAVEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAvAIGPVL 698
Cdd:PRK07742 189 tiDAAALTqmnrRGQIKNCVVDGPLALDNAVSQIAAEHKGIVSDVAGKADILLVPTIEAGNVLYKSLVYFADA-KVGAMI 267
|
170
....*....|..
gi 1054830065 699 QGLRKPINDLSR 710
Cdd:PRK07742 268 AGAKAPIVLTSR 279
|
|
| PRK14869 |
PRK14869 |
putative manganese-dependent inorganic diphosphatase; |
244-361 |
2.57e-05 |
|
putative manganese-dependent inorganic diphosphatase;
Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 47.52 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 244 VAPSMKTILEATHGTLVQGDPELLsREALSVVVAAMSMVNVLPRLTEGAVVVIpSDRPEVLLAALMANSSAtfpslagVV 323
Cdd:PRK14869 136 SPTSLENIIRTLDGEVLVGAEEDK-VEEGKVVVAAMAPESLLERIEEGDIVIV-GDREDIQLAAIEAGVRL-------LI 206
|
90 100 110
....*....|....*....|....*....|....*...
gi 1054830065 324 LVGGFPLPESIEQLMKglAPSVPIIRTDLASYEAALRI 361
Cdd:PRK14869 207 ITGGAPVSEDVLELAK--ENGVTVISTPYDTFTTARLI 242
|
|
| PRK08190 |
PRK08190 |
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated |
555-705 |
4.46e-05 |
|
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
Pssm-ID: 236180 [Multi-domain] Cd Length: 466 Bit Score: 46.80 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 555 VSSVFLMALAD--RVLVYGDCAVNPDPTAAQLADIAISASETALEFGIE-PRIAMLSystgisgngadvekvreATAIVR 631
Cdd:PRK08190 281 ISHVFAMDVPTypRPLLITDAAINIAPTLEDKRDIVQNAIDLAHALGVEePKVAILS-----------------AVETVN 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054830065 632 ERRP---DLA---------------VEGPIQYDAAADAAVAAAKMPDSDVAGKATVFIFPDLNTGNNTYKAVQRSAGAVA 693
Cdd:PRK08190 344 PKMPstlDAAalckmadrgqitggiVDGPLAFDNAISAEAARTKGIVSPVAGQADILVVPDLEAGNMLAKQLTYLAGADA 423
|
170
....*....|..
gi 1054830065 694 IGPVLqGLRKPI 705
Cdd:PRK08190 424 AGIVL-GARVPI 434
|
|
| MPP_GpdQ |
cd07402 |
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ... |
90-146 |
9.55e-04 |
|
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277347 [Multi-domain] Cd Length: 240 Bit Score: 41.49 E-value: 9.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1054830065 90 DPDAALARIVARYKAVEAQCDAVVVIGsDFTDVGSPTELAYNARIAANLGVPVLLVL 146
Cdd:cd07402 21 DTAARLAAAVAQVNALHPRPDLVVVTG-DLSDDGSPESYERLRELLAPLPAPVYWIP 76
|
|
| |
