|
Name |
Accession |
Description |
Interval |
E-value |
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
1-376 |
0e+00 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 779.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 1 MIRLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISREKPDFVV 80
Cdd:COG0027 1 MTTIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 81 PEIEAIATDTLIALEQEGQRVVPCAKAAKLTMNREGIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSS 160
Cdd:COG0027 81 PEIEAIATDALVELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 161 SGKGQSFIRDSSTLDKAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCDPIGHRQEDGDYRESWQPQQM 239
Cdd:COG0027 161 SGKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVDGpTHFCEPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 240 SALALERAQAIARKTVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:COG0027 241 SEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 320 PAASAVILPQLTSQNVTFDNVDAAVG-AGLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:COG0027 321 PAASAVILAEGESWAPAFDGLAEALAvPGTDLRLFGKPEAYGRRRMGVALATADDVEE 378
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
1-376 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 772.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 1 MIRLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISREKPDFVV 80
Cdd:PRK09288 1 MTRLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 81 PEIEAIATDTLIALEQEGQRVVPCAKAAKLTMNREGIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSS 160
Cdd:PRK09288 81 PEIEAIATDALVELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 161 SGKGQSFIRDSSTLDKAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVD-GVHFCDPIGHRQEDGDYRESWQPQQM 239
Cdd:PRK09288 161 SGKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVDgGTHFCAPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 240 SALALERAQAIARKTVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:PRK09288 241 SPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 320 PAASAVILPQLTSQNVTFDNVDAAVG-AGLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:PRK09288 321 PAASAVILAEGESANPSFDGLAEALAvPGTDVRLFGKPEIRGGRRMGVALATGEDVEE 378
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
14-376 |
0e+00 |
|
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN (TIGR00639) [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 130212 Cd Length: 380 Bit Score: 649.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 14 RVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISREKPDFVVPEIEAIATDTLIA 93
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 94 LEQEGQRVVPCAKAAKLTMNREGIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSST 173
Cdd:TIGR01142 81 LEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 174 LDKAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCDPIGHRQEDGDYRESWQPQQMSALALERAQAIAR 252
Cdd:TIGR01142 161 IEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGnTTFCAPIGHRQIDGDYHESWQPQEMSEKALEEAQRIAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 253 KTVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQLTS 332
Cdd:TIGR01142 241 RITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 544824433 333 QNVTFDNVDAAVG-AGLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:TIGR01142 321 YSPAFRGLEKALSvPNTQVRLFGKPEAYVGRRLGVALATAKSVEA 365
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
123-294 |
1.74e-70 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 218.66 E-value: 1.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 123 EELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVK-PVMSSSGKGQSFIRDSSTLDKAWEYAqqggraGAGRVIVEGVVKFD 201
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEEL------GDGPVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 202 FEITLLTVSAVDG-VHFCDPIGHRQEDGDYRESWQPQQMSALALERAQAIARKTVLALGGYGLFGVELFVCGD-EVIFSE 279
Cdd:pfam02222 75 RELSVLVVRSVDGeTAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgDLLINE 154
|
170
....*....|....*
gi 544824433 280 VSPRPHDTGMVTLIS 294
Cdd:pfam02222 155 LAPRPHNSGHYTLDG 169
|
|
| dTDP_HR_like_SDR_e |
cd05254 |
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ... |
14-80 |
2.19e-05 |
|
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187564 [Multi-domain] Cd Length: 280 Bit Score: 45.70 E-value: 2.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 14 RVMLLG-SGELGKEVAIECQRLGVEVIAVDRyADApamhvahRSYVINMLDGDALRELISREKPDFVV 80
Cdd:cd05254 1 KILITGaTGMLGRALVRLLKERGYEVIGTGR-SRA-------SLFKLDLTDPDAVEEAIRDYKPDVII 60
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
1-376 |
0e+00 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 779.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 1 MIRLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISREKPDFVV 80
Cdd:COG0027 1 MTTIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 81 PEIEAIATDTLIALEQEGQRVVPCAKAAKLTMNREGIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSS 160
Cdd:COG0027 81 PEIEAIATDALVELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 161 SGKGQSFIRDSSTLDKAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCDPIGHRQEDGDYRESWQPQQM 239
Cdd:COG0027 161 SGKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVDGpTHFCEPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 240 SALALERAQAIARKTVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:COG0027 241 SEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 320 PAASAVILPQLTSQNVTFDNVDAAVG-AGLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:COG0027 321 PAASAVILAEGESWAPAFDGLAEALAvPGTDLRLFGKPEAYGRRRMGVALATADDVEE 378
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
1-376 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 772.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 1 MIRLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISREKPDFVV 80
Cdd:PRK09288 1 MTRLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 81 PEIEAIATDTLIALEQEGQRVVPCAKAAKLTMNREGIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSS 160
Cdd:PRK09288 81 PEIEAIATDALVELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 161 SGKGQSFIRDSSTLDKAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVD-GVHFCDPIGHRQEDGDYRESWQPQQM 239
Cdd:PRK09288 161 SGKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVDgGTHFCAPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 240 SALALERAQAIARKTVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:PRK09288 241 SPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 320 PAASAVILPQLTSQNVTFDNVDAAVG-AGLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:PRK09288 321 PAASAVILAEGESANPSFDGLAEALAvPGTDVRLFGKPEIRGGRRMGVALATGEDVEE 378
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
14-376 |
0e+00 |
|
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN (TIGR00639) [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 130212 Cd Length: 380 Bit Score: 649.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 14 RVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISREKPDFVVPEIEAIATDTLIA 93
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 94 LEQEGQRVVPCAKAAKLTMNREGIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSST 173
Cdd:TIGR01142 81 LEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 174 LDKAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCDPIGHRQEDGDYRESWQPQQMSALALERAQAIAR 252
Cdd:TIGR01142 161 IEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGnTTFCAPIGHRQIDGDYHESWQPQEMSEKALEEAQRIAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 253 KTVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQLTS 332
Cdd:TIGR01142 241 RITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 544824433 333 QNVTFDNVDAAVG-AGLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:TIGR01142 321 YSPAFRGLEKALSvPNTQVRLFGKPEAYVGRRLGVALATAKSVEA 365
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
123-294 |
1.74e-70 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 218.66 E-value: 1.74e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 123 EELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVK-PVMSSSGKGQSFIRDSSTLDKAWEYAqqggraGAGRVIVEGVVKFD 201
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEEL------GDGPVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 202 FEITLLTVSAVDG-VHFCDPIGHRQEDGDYRESWQPQQMSALALERAQAIARKTVLALGGYGLFGVELFVCGD-EVIFSE 279
Cdd:pfam02222 75 RELSVLVVRSVDGeTAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgDLLINE 154
|
170
....*....|....*
gi 544824433 280 VSPRPHDTGMVTLIS 294
Cdd:pfam02222 155 LAPRPHNSGHYTLDG 169
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
23-376 |
9.06e-55 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 184.12 E-value: 9.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 23 LGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELIsrEKPDFVVPEIEAIATDTLIALEQEGqRVV 102
Cdd:COG0026 2 LGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFA--ERCDVVTFEFENVPAEALEALEAEV-PVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 103 PCAKAAKLTMNRegIR-RLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPV-MSSSGKGQSFIRDSSTLDKAWEy 180
Cdd:COG0026 79 PGPEALEIAQDR--LLeKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrGGYDGKGQVVIKSAADLEAAWA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 181 aqqggRAGAGRVIVEGVVKFDFEITLLTVSAVDG--VHFcdPIGH-RQEDGDYRESWQPQQMSALALERAQAIARKTVLA 257
Cdd:COG0026 156 -----ALGGGPCILEEFVPFERELSVIVARSPDGevATY--PVVEnVHRNGILDESIAPARISEALAAEAEEIAKRIAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 258 LGGYGLFGVELFVCGD-EVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQltsqnVT 336
Cdd:COG0026 229 LDYVGVLAVEFFVTKDgELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGDTELLSPAVMVNLLGD-----DW 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 544824433 337 FDNVDAAVGA--GLQVRLFGKPEIDGTRRLGVALATGDNVDD 376
Cdd:COG0026 304 EDPGWEALLAlpGAHLHLYGKKEARPGRKMGHVTVLGDDLEE 345
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
18-322 |
1.08e-49 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 171.49 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 18 LGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELIsrEKPDFVVPEIEAIATDTLIALEQE 97
Cdd:PRK06019 8 IGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELA--EQCDVITYEFENVPAEALDALAAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 98 GqRVVPCAKAAKLTMNREGIRRLAAeELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKpvmSSS----GKGQSFIRDSST 173
Cdd:PRK06019 86 V-PVPPGPDALAIAQDRLTEKQFLD-KLGIPVAPFAVVDSAEDLEAALADLGLPAVLK---TRRggydGKGQWVIRSAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 174 LDKAWEyaqqggRAGAGRVIVEGVVKFDFEITLLTVSAVDGVHFCDPIGH-RQEDGDYRESWQPQQMSALALERAQAIAR 252
Cdd:PRK06019 161 LEAAWA------LLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVEnVHRNGILRTSIAPARISAELQAQAEEIAS 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544824433 253 KTVLALGGYGLFGVELFVCGD-EVIFSEVSPRPHDTGMVTL----ISQdlseFALHVRAFLGLPVGGIRQYGPAA 322
Cdd:PRK06019 235 RIAEELDYVGVLAVEFFVTGDgELLVNEIAPRPHNSGHWTIeacsTSQ----FEQHLRAILGLPLGTTRLLSPAV 305
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
10-365 |
2.88e-37 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 142.12 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 10 PAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLDGDALRELISRekPDFVVPEIEAIATD 89
Cdd:PLN02948 20 VSETVVGVLGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVREFAKR--CDVLTVEIEHVDVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 90 TLIALEQEGQRVVPCAKAAKLTMNREgIRRLAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPV-MSSSGKGQSFI 168
Cdd:PLN02948 98 TLEALEKQGVDVQPKSSTIRIIQDKY-AQKVHFSKHGIPLPEFMEIDDLESAEKAGDLFGYPLMLKSRrLAYDGRGNAVA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 169 RDSSTLDKAweYAQQGGRAGAgrVIVEGVVKFDFEITLLTVSAVDGVHFCDPIG---HRQEDGDYRESwqPQQMSALALE 245
Cdd:PLN02948 177 KTEEDLSSA--VAALGGFERG--LYAEKWAPFVKELAVMVARSRDGSTRCYPVVetiHKDNICHVVEA--PANVPWKVAK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 246 RAQAIARKTVLALGGYGLFGVELFVCGDE-VIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASA 324
Cdd:PLN02948 251 LATDVAEKAVGSLEGAGVFGVELFLLKDGqILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGDTSMKVPAAIM 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 544824433 325 VILPQLTSQNVTFDNVDAAVGA-----GLQVRLFGKPEIDGTRRLG 365
Cdd:PLN02948 331 YNILGEDEGEAGFRLAHQLMGRalnipGASVHWYGKPEMRKQRKMG 376
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
65-312 |
5.49e-20 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 88.39 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 65 DALRELISREKPDFVVPEIEAIATDTLIALEQEGqrvVPCAKAA-------KLTMnregirRLAAEELGLPTSSYRFAGD 137
Cdd:COG0439 7 AAAAELARETGIDAVLSESEFAVETAAELAEELG---LPGPSPEairamrdKVLM------REALAAAGVPVPGFALVDS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 138 KAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQGGRAGA--GRVIVEgvvKF--DFEITLLTVSAVD 213
Cdd:COG0439 78 PEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSpnGEVLVE---EFleGREYSVEGLVRDG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 214 GVHFCDPIGHRQEDGDYRES--WQPQQMSALALERAQAIARKTVLALG-GYGLFGVELFVCGD-EVIFSEVSPRPHDTGM 289
Cdd:COG0439 155 EVVVCSITRKHQKPPYFVELghEAPSPLPEELRAEIGELVARALRALGyRRGAFHTEFLLTPDgEPYLIEINARLGGEHI 234
|
250 260
....*....|....*....|....*..
gi 544824433 290 VTLISQ----DLseFALHVRAFLGLPV 312
Cdd:COG0439 235 PPLTELatgvDL--VREQIRLALGEPR 259
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
25-284 |
6.28e-11 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 62.65 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 25 KEVAIECQRLGVEVIAVDRyadapamhvahRSYVINMLDGDALRELISREKPDFVVPEIEAI--ATDTLIALEQEGQRVV 102
Cdd:COG0189 17 KALIEAAQRRGHEVEVIDP-----------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPfyGLALLRQLEAAGVPVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 103 PCAKAA-----KLTMNRegirrlAAEELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKA 177
Cdd:COG0189 86 NDPEAIrrardKLFTLQ------LLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 178 WEYAQQGGRagaGRVIVEGVVK----FDFEITLltvsaVDG--VHFCDPIGhrqEDGDYR------ESWQPQQMSalalE 245
Cdd:COG0189 160 LEALTELGS---EPVLVQEFIPeedgRDIRVLV-----VGGepVAAIRRIP---AEGEFRtnlargGRAEPVELT----D 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 544824433 246 RAQAIARKTVLALgGYGLFGVELFVCGDEVIFSEVSPRP 284
Cdd:COG0189 225 EERELALRAAPAL-GLDFAGVDLIEDDDGPLVLEVNVTP 262
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
14-283 |
1.33e-10 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 61.82 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 14 RVMLLGSGELGKEV-AIECQRLGVEVIAVDRYADAPAMHVAHRSYVINMLD----GDALRELISREKPDFVVPEIE---- 84
Cdd:PRK12767 3 NILVTSAGRRVQLVkALKKSLLKGRVIGADISELAPALYFADKFYVVPKVTdpnyIDRLLDICKKEKIDLLIPLIDpelp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 85 --AIATDTLialEQEGQRVVPCAKAA------KLTMNREgirrlaAEELGLPTSSYRFAGDKAAFLQA--VEEIGYPCIV 154
Cdd:PRK12767 83 llAQNRDRF---EEIGVKVLVSSKEVieicndKWLTYEF------LKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 155 KPVMSSSGKGQSFIRDSSTLDKAWEYAQQggragagrVIVEGVVKFDfEITLltvsavdGVhFCDPighrqeDGDYRESW 234
Cdd:PRK12767 154 KPRDGSASIGVFKVNDKEELEFLLEYVPN--------LIIQEFIEGQ-EYTV-------DV-LCDL------NGEVISIV 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 544824433 235 QPQQMSALALERAQAIARKT----------VLALGGYGLFGVELFVCGDEVIFSEVSPR 283
Cdd:PRK12767 211 PRKRIEVRAGETSKGVTVKDpelfklaerlAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
32-327 |
9.97e-10 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 59.55 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 32 QRLGVEVIAVDRYADAPAMHVAHRSYVINMLDG--------DALRELISREKPDFVVPEIEAIATDTLIALEQEGQRVV- 102
Cdd:COG2232 22 RRAGYRVYAVDLFADLDTRALAERWVRLDAESCgfdledlpAALLELAAADDPDGLVYGSGFENFPELLERLARRLPLLg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 103 PCAKAAKLTMNRegiRRLAA--EELGLPTSSYRFAGDKAAflqaveeigYPCIVKPVMSSSGKGqSFIRDSSTLDKAWEY 180
Cdd:COG2232 102 NPPEVVRRVKDP---LRFFAllDELGIPHPETRFEPPPDP---------GPWLVKPIGGAGGWH-IRPADSEAPPAPGRY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 181 AQQggragagrvIVEGVVkfdfeITLLTVSAVDGVHFcdpIG-HRQ---EDGD----YRESWQPQQMSALALERAQAIAR 252
Cdd:COG2232 169 FQR---------YVEGTP-----ASVLFLADGSDARV---LGfNRQligPAGErpfrYGGNIGPLALPPALAEEMRAIAE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 253 KTVLALGGYGLFGVELFVCGDEVIFSEVSPRPhdTGMVTLISQDLSE--FALHVRAFLG-LPVGGIRQYGPAASAVIL 327
Cdd:COG2232 232 ALVAALGLVGLNGVDFILDGDGPYVLEVNPRP--QASLDLYEDATGGnlFDAHLRACRGeLPEVPRPKPRRVAAKAIL 307
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
63-280 |
1.03e-09 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 58.96 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 63 DGDALRELISREKPDFVVP-------EieaiatDTLI--ALEQEGqrvVPC----AKAAKLTMNREGIRRLAAEElGLPT 129
Cdd:COG1181 41 DVEDLPAALKELKPDVVFPalhgrggE------DGTIqgLLELLG---IPYtgsgVLASALAMDKALTKRVLAAA-GLPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 130 SSYRF--AGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQGGRagagRVIVE----------GV 197
Cdd:COG1181 111 PPYVVlrRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDD----KVLVEefidgrevtvGV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 198 VKFDFEITLLTVSAVDGVHFCDpIGHRQEDGDYRESWqPQQMSALALERAQAIARKTVLALGGYGLFGVELFVCGD-EVI 276
Cdd:COG1181 187 LGNGGPRALPPIEIVPENGFYD-YEAKYTDGGTEYIC-PARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDgEPY 264
|
....
gi 544824433 277 FSEV 280
Cdd:COG1181 265 LLEV 268
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
10-161 |
1.74e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 58.79 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 10 PAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMH---VAHRSYVINMLDG-----DALRELISREKPDFVVP 81
Cdd:COG3919 3 TMRFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARsryVDEVVVVPDPGDDpeafvDALLELAERHGPDVLIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 82 eieaiATDTLIAL-----EQEGQRV-VPCAKAAKLT--MNREGIRRLAaEELGLPTSSYRFAGDKAAFLQAVEEIGYPCI 153
Cdd:COG3919 83 -----TGDEYVELlsrhrDELEEHYrLPYPDADLLDrlLDKERFYELA-EELGVPVPKTVVLDSADDLDALAEDLGFPVV 156
|
....*...
gi 544824433 154 VKPVMSSS 161
Cdd:COG3919 157 VKPADSVG 164
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
125-294 |
2.06e-07 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 51.16 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 125 LGLPTSSY-------RFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQGGRagagRVIVE-G 196
Cdd:pfam07478 5 AGLPVVPFvtftradWKLNPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDE----KVLVEeG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 197 VVKFDFEITLLTvsavDGVHFCDPIGHRQEDG---DYRESWQ--------PQQMSALALERAQAIARKTVLALGGYGLFG 265
Cdd:pfam07478 81 IEGREIECAVLG----NEDPEVSPVGEIVPSGgfyDYEAKYIddsaqivvPADLEEEQEEQIQELALKAYKALGCRGLAR 156
|
170 180 190
....*....|....*....|....*....|
gi 544824433 266 VELFVCGD-EVIFSEVSPRPhdtGMvTLIS 294
Cdd:pfam07478 157 VDFFLTEDgEIVLNEVNTIP---GF-TSIS 182
|
|
| D_ala_D_alaTIGR |
TIGR01205 |
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ... |
107-292 |
3.94e-07 |
|
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273498 [Multi-domain] Cd Length: 315 Bit Score: 51.13 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 107 AAKLTMNREGIRRLAAEeLGLPTSSY------RFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEY 180
Cdd:TIGR01205 99 ASALSMDKLLTKLLWKA-LGLPTPDYivltqnRASADELECEQVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 181 AQQGGRagagRVIVEGVVKFDfEITLltvsAVDGVHFCDPIGHRQEDG----DYRESWQ--------PQQMSALALERAQ 248
Cdd:TIGR01205 178 AFEYDE----EVLVEQFIKGR-ELEV----SILGNEEALPIIEIVPEIegfyDYEAKYLdgsteyviPAPLDEELEEKIK 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 544824433 249 AIARKTVLALGGYGLFGVELFVCGD-EVIFSEVSPRPhdtGMVTL 292
Cdd:TIGR01205 249 ELALKAYKALGCRGLARVDFFLDEEgEIYLNEINTIP---GMTAI 290
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
14-217 |
9.77e-07 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 50.40 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 14 RVMLLGSGelGKEVAIeCQRL----GVEVIAVdryadAP-----AMHVahRSYVINMLDGDALRELISREKPDFVVPEIE 84
Cdd:COG0151 2 KVLVIGSG--GREHAL-AWKLaqspRVDKLYV-----APgnagtAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 85 A-----IAtDtliALEQEGQRVV-PCAKAAKLT---------MNREGIrrlaaeelglPTSSYRFAGDKAAFLQAVEEIG 149
Cdd:COG0151 72 AplvagIV-D---AFRAAGIPVFgPSKAAAQLEgskafakefMARYGI----------PTAAYRVFTDLEEALAYLEEQG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 150 YPCIVKPVMSSSGKGqsfIRDSSTLDKAWEYAQ------QGGRAGAgRVIVEgvvkfDF----EITLLTVsaVDGVHF 217
Cdd:COG0151 138 APIVVKADGLAAGKG---VVVAETLEEALAAVDdmladgKFGDAGA-RVVIE-----EFlegeEASLFAL--TDGKTV 204
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
111-375 |
2.26e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 49.85 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 111 TMNREGIR------RLAAE--ELGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMsssGKGQSFIRDSSTLDKAWEYAQ 182
Cdd:PRK02186 96 AANTEAIRtcrdkkRLARTlrDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRM---GSGSVGVRLCASVAEAAAHCA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 183 QGGRAGAGRVIVEGVVKFDfEITLLTVSAVDGVH-------FCDPIGHRQEDG-DYreswqPQQMSALALERAQAIARKT 254
Cdd:PRK02186 173 ALRRAGTRAALVQAYVEGD-EYSVETLTVARGHQvlgitrkHLGPPPHFVEIGhDF-----PAPLSAPQRERIVRTVLRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 255 VLALG-GYGLFGVELFVCGDEVIFSEVSPRPHDtGMV-TLISQ--DLSEFALHVRAFLG---LPVGGIRQYGpaASAVIL 327
Cdd:PRK02186 247 LDAVGyAFGPAHTELRVRGDTVVIIEINPRLAG-GMIpVLLEEafGVDLLDHVIDLHLGvaaFADPTAKRYG--AIRFVL 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 544824433 328 PQLTSQNVTFDNVDAAVGAGLQVRLFG--------KPEIDGTRRLGVALATGDNVD 375
Cdd:PRK02186 324 PARSGVLRGLLFLPDDIAARPELRFHPlkqpgdalRLEGDFRDRIAAVVCAGDHRD 379
|
|
| dTDP_HR_like_SDR_e |
cd05254 |
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ... |
14-80 |
2.19e-05 |
|
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
Pssm-ID: 187564 [Multi-domain] Cd Length: 280 Bit Score: 45.70 E-value: 2.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544824433 14 RVMLLG-SGELGKEVAIECQRLGVEVIAVDRyADApamhvahRSYVINMLDGDALRELISREKPDFVV 80
Cdd:cd05254 1 KILITGaTGMLGRALVRLLKERGYEVIGTGR-SRA-------SLFKLDLTDPDAVEEAIRDYKPDVII 60
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
8-167 |
1.33e-04 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 44.22 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 8 LRPAATRVMLLGSGELGKEVAIE--------CQRL---GVEVIAVDryaDAPAM-----HVAHRSYvINMLDGDALRELI 71
Cdd:TIGR01369 2 KRTDIKKILVIGSGPIVIGQAAEfdysgsqaCKALkeeGYRVILVN---SNPATimtdpEMADKVY-IEPLTPEAVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 72 SREKPDFVVPEIE-------AIATDTLIALEQEGQRVVPC-AKAAKLTMNREGIRRlAAEELGLPTSSYRFAGDKAAFLQ 143
Cdd:TIGR01369 78 EKERPDAILPTFGgqtalnlAVELEESGVLEKYGVEVLGTpVEAIKKAEDRELFRE-AMKEIGEPVPESEIAHSVEEALA 156
|
170 180
....*....|....*....|....
gi 544824433 144 AVEEIGYPCIVKPVMSSSGKGQSF 167
Cdd:TIGR01369 157 AAKEIGYPVIVRPAFTLGGTGGGI 180
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
119-195 |
1.61e-04 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 42.29 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 119 RLAAEELGLPT--SSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQ--GGRAGAGRVIV 194
Cdd:pfam02786 6 KAAMKEAGVPTvpGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAeaPAAFGNPQVLV 85
|
.
gi 544824433 195 E 195
Cdd:pfam02786 86 E 86
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
59-170 |
2.77e-04 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 42.33 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 59 INMLDGDALRELisrEKPDFVVPEIEAI--ATDTLIALEQEGQRVVPCAKAakltMNREGIRRLAAEEL---GLPTSSYR 133
Cdd:TIGR00768 35 INLTFNEGPRAL---AELDVVIVRIVSMfrGLAVLRYLESLGVPVINSSDA----ILNAGDKFLSHQLLakaGIPLPRTG 107
|
90 100 110
....*....|....*....|....*....|....*..
gi 544824433 134 FAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRD 170
Cdd:TIGR00768 108 LAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARD 144
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
125-205 |
3.48e-04 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 42.02 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 125 LGLPTSSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQGGragaGRVIVEGVVKFDfEI 204
Cdd:PRK01372 109 AGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYD----DEVLVEKYIKGR-EL 183
|
.
gi 544824433 205 T 205
Cdd:PRK01372 184 T 184
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
19-80 |
4.93e-04 |
|
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
Pssm-ID: 396097 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 4.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544824433 19 GSGELGKEVAIECQRLGVEVIAVDR--YADAPAMHVAHRSYVINMLDGDALRELISREKPDFVV 80
Cdd:pfam01370 6 ATGFIGSHLVRRLLEKGYEVIGLDRltSASNTARLADLRFVEGDLTDRDALEKLLADVRPDAVI 69
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
107-294 |
5.68e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 41.64 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 107 AAKLTMNREGIRRLAAEeLGLPTSSY----RFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQ 182
Cdd:PRK01966 117 ASALSMDKILTKRLLAA-AGIPVAPYvvltRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 183 QGGRagagRVIVE----------GVVKFDFEITLLT-VSAVDgvHFCDpighrQE----DGDYRESwQPQQMSALALERA 247
Cdd:PRK01966 196 EYDR----KVLVEqgikgreiecAVLGNDPKASVPGeIVKPD--DFYD-----YEakylDGSAELI-IPADLSEELTEKI 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 544824433 248 QAIARKTVLALGGYGLFGVELFVCGD-EVIFSEVSPRPhdtGMvTLIS 294
Cdd:PRK01966 264 RELAIKAFKALGCSGLARVDFFLTEDgEIYLNEINTMP---GF-TPIS 307
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
119-195 |
2.05e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.51 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 119 RLAAEELGLPT--SSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQGGRA--GAGRVIV 194
Cdd:PRK12999 124 RNAAIKAGVPVipGSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAafGNDEVYL 203
|
.
gi 544824433 195 E 195
Cdd:PRK12999 204 E 204
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
142-195 |
5.51e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 38.98 E-value: 5.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 544824433 142 LQAVEEIGYPCIVKPVMSSSGKGQSF-IRDSSTLDKAWEYAQQGGRAgagrVIVE 195
Cdd:PRK14016 242 WEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD----VIVE 292
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
119-195 |
7.68e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 38.52 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544824433 119 RLAAEELGLPT--SSYRFAGDKAAFLQAVEEIGYPCIVKPVMSSSGKGQSFIRDSSTLDKAWEYAQQGGRA--GAGRVIV 194
Cdd:COG1038 123 RAAAIEAGVPVipGTEGPVDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARREAKAafGDDEVFL 202
|
.
gi 544824433 195 E 195
Cdd:COG1038 203 E 203
|
|
| |
