|
Name |
Accession |
Description |
Interval |
E-value |
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
1-391 |
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: 792.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 1 MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:COG0027 1 MTTIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 81 PEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSS 160
Cdd:COG0027 81 PEIEAIATDALVELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 161 SGKGQTFIRSAEQLAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCAPVGHRQEDGDYCESWQPQQM 239
Cdd:COG0027 161 SGKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVDGpTHFCEPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 240 SPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:COG0027 241 SEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13362027 320 PAASAVILPQLTSQNVTFDNVQNAVG-ADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQ 391
Cdd:COG0027 321 PAASAVILAEGESWAPAFDGLAEALAvPGTDLRLFGKPEAYGRRRMGVALATADDVEEAREKAREAAAKVKVV 393
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
1-392 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 787.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 1 MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:PRK09288 1 MTRLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 81 PEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSS 160
Cdd:PRK09288 81 PEIEAIATDALVELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 161 SGKGQTFIRSAEQLAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVD-GVHFCAPVGHRQEDGDYCESWQPQQM 239
Cdd:PRK09288 161 SGKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVDgGTHFCAPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 240 SPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:PRK09288 241 SPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYS 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13362027 320 PAASAVILPQLTSQNVTFDNVQNAVG-ADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQG 392
Cdd:PRK09288 321 PAASAVILAEGESANPSFDGLAEALAvPGTDVRLFGKPEIRGGRRMGVALATGEDVEEAREKAKEAASKVKVVG 394
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
14-391 |
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: 691.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 14 RVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIVPEIEAIATDMLIQ 93
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 94 LEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQ 173
Cdd:TIGR01142 81 LEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 174 LAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCAPVGHRQEDGDYCESWQPQQMSPLALERAQEIAR 252
Cdd:TIGR01142 161 IEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGnTTFCAPIGHRQIDGDYHESWQPQEMSEKALEEAQRIAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 253 KVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQLTS 332
Cdd:TIGR01142 241 RITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 333 QNVTFDNVQNAVG-ADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQ 391
Cdd:TIGR01142 321 YSPAFRGLEKALSvPNTQVRLFGKPEAYVGRRLGVALATAKSVEAARERAEEVAHAVEVR 380
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
123-294 |
1.57e-71 |
|
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: 221.36 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 123 EELQLPTSTYRFADSESLFREAVAAIGYPCIVK-PVMSSSGKGQTFIRSAEQLAQAWEYAqqggraGAGRVIVEGVVKFD 201
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEEL------GDGPVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 202 FEITLLTVSAVDG-VHFCAPVGHRQEDGDYCESWQPQQMSPLALERAQEIARKVVLALGGYGLFGVELFVCGD-EVIFSE 279
Cdd:pfam02222 75 RELSVLVVRSVDGeTAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgDLLINE 154
|
170
....*....|....*
gi 13362027 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 |
7.35e-04 |
|
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: 41.07 E-value: 7.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13362027 14 RVMLLG-SGELGKEVAIECQRLGVEVIAVDRyADApamhvahRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:cd05254 1 KILITGaTGMLGRALVRLLKERGYEVIGTGR-SRA-------SLFKLDLTDPDAVEEAIRDYKPDVII 60
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
1-391 |
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: 792.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 1 MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:COG0027 1 MTTIGTPLSPNATKVMLLGSGELGKEVAIELQRLGVEVIAVDRYANAPAMQVAHRSYVIDMLDGDALRALIEREKPDFIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 81 PEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSS 160
Cdd:COG0027 81 PEIEAIATDALVELEAEGFRVVPTARAVRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 161 SGKGQTFIRSAEQLAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCAPVGHRQEDGDYCESWQPQQM 239
Cdd:COG0027 161 SGKGQSVVRSPADIEAAWEYAQEGGRGGAGRVIVEGFVDFDYEITLLTVRAVDGpTHFCEPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 240 SPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:COG0027 241 SEAALAKAQEIAKKVTDALGGRGIFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQDLSEFALHARAILGLPVPEIRLVG 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13362027 320 PAASAVILPQLTSQNVTFDNVQNAVG-ADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQ 391
Cdd:COG0027 321 PAASAVILAEGESWAPAFDGLAEALAvPGTDLRLFGKPEAYGRRRMGVALATADDVEEAREKAREAAAKVKVV 393
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
1-392 |
0e+00 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 787.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 1 MTLLGTALRPAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:PRK09288 1 MTRLGTPLSPSATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSHVIDMLDGDALRAVIEREKPDYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 81 PEIEAIATDMLIQLEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSS 160
Cdd:PRK09288 81 PEIEAIATDALVELEKEGFNVVPTARATRLTMNREGIRRLAAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKPVMSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 161 SGKGQTFIRSAEQLAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVD-GVHFCAPVGHRQEDGDYCESWQPQQM 239
Cdd:PRK09288 161 SGKGQSVVRSPEDIEKAWEYAQEGGRGGAGRVIVEEFIDFDYEITLLTVRAVDgGTHFCAPIGHRQEDGDYRESWQPQPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 240 SPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYG 319
Cdd:PRK09288 241 SPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVSPRPHDTGMVTLISQNLSEFELHARAILGLPIPDIRLYS 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13362027 320 PAASAVILPQLTSQNVTFDNVQNAVG-ADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQG 392
Cdd:PRK09288 321 PAASAVILAEGESANPSFDGLAEALAvPGTDVRLFGKPEIRGGRRMGVALATGEDVEEAREKAKEAASKVKVVG 394
|
|
| purT |
TIGR01142 |
phosphoribosylglycinamide formyltransferase 2; This enzyme is an alternative to PurN ... |
14-391 |
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: 691.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 14 RVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIVPEIEAIATDMLIQ 93
Cdd:TIGR01142 1 RVLLLGSGELGKEVAIEAQRLGVEVIAVDRYANAPAMQVAHRSYVINMLDGDALRAVIEREKPDYIVPEIEAIATDALFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 94 LEEEGLNVVPCARATKLTMNREGIRRLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQ 173
Cdd:TIGR01142 81 LEKEGYFVVPNARATKLTMNREGIRRLAAEELGLPTSRYMFADSLDELREAVEKIGYPCVVKPVMSSSGKGQSVVRGPED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 174 LAQAWEYAQQGGRAGAGRVIVEGVVKFDFEITLLTVSAVDG-VHFCAPVGHRQEDGDYCESWQPQQMSPLALERAQEIAR 252
Cdd:TIGR01142 161 IEKAWEYAQEGARGGAGRVIVEEFIDFDYEITLLTVRHVDGnTTFCAPIGHRQIDGDYHESWQPQEMSEKALEEAQRIAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 253 KVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQLTS 332
Cdd:TIGR01142 241 RITDALGGYGLFGVELFVKGDEVIFSEVSPRPHDTGMVTLISQGLSEFALHVRAILGLPIPGIPQLGPAASAVIKAKVTG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 333 QNVTFDNVQNAVG-ADLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQVKVQ 391
Cdd:TIGR01142 321 YSPAFRGLEKALSvPNTQVRLFGKPEAYVGRRLGVALATAKSVEAARERAEEVAHAVEVR 380
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
123-294 |
1.57e-71 |
|
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: 221.36 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 123 EELQLPTSTYRFADSESLFREAVAAIGYPCIVK-PVMSSSGKGQTFIRSAEQLAQAWEYAqqggraGAGRVIVEGVVKFD 201
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKaRRGGYDGKGQYVVRSEADLPQAWEEL------GDGPVIVEEFVPFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 202 FEITLLTVSAVDG-VHFCAPVGHRQEDGDYCESWQPQQMSPLALERAQEIARKVVLALGGYGLFGVELFVCGD-EVIFSE 279
Cdd:pfam02222 75 RELSVLVVRSVDGeTAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDgDLLINE 154
|
170
....*....|....*
gi 13362027 280 VSPRPHDTGMVTLIS 294
Cdd:pfam02222 155 LAPRPHNSGHYTLDG 169
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
23-384 |
3.33e-53 |
|
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: 180.27 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 23 LGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVEleKPHYIVPEIEAIATDMLIQLEEEGlNVV 102
Cdd:COG0026 2 LGRMLALAAKRLGYRVHVLDPDPDSPAAQVADEHIVADYDDEEALREFAE--RCDVVTFEFENVPAEALEALEAEV-PVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 103 PCARATKLTMNRegIR-RLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPV-MSSSGKGQTFIRSAEQLAQAWEy 180
Cdd:COG0026 79 PGPEALEIAQDR--LLeKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRrGGYDGKGQVVIKSAADLEAAWA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 181 aqqggRAGAGRVIVEGVVKFDFEITLLTVSAVDG--VHFcaPVGH-RQEDG--DYCESwqPQQMSPLALERAQEIARKVV 255
Cdd:COG0026 156 -----ALGGGPCILEEFVPFERELSVIVARSPDGevATY--PVVEnVHRNGilDESIA--PARISEALAAEAEEIAKRIA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 256 LALGGYGLFGVELFVCGD-EVIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGGIRQYGPAASAVILPQltsqn 334
Cdd:COG0026 227 EALDYVGVLAVEFFVTKDgELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGDTELLSPAVMVNLLGD----- 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 13362027 335 VTFDNVQNAVGA--DLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHA 384
Cdd:COG0026 302 DWEDPGWEALLAlpGAHLHLYGKKEARPGRKMGHVTVLGDDLEEALERARAA 353
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
18-388 |
1.73e-49 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 171.10 E-value: 1.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 18 LGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRRVVelEKPHYIVPEIEAIATDMLIQLEEE 97
Cdd:PRK06019 8 IGGGQLGRMLALAAAPLGYKVIVLDPDPDSPAAQVADEVIVADYDDVAALRELA--EQCDVITYEFENVPAEALDALAAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 98 GlNVVPCARATKLTMNREGIRRLAAeELQLPTSTYRFADSESLFREAVAAIGYPCIVKpvmSSS----GKGQTFIRSAEQ 173
Cdd:PRK06019 86 V-PVPPGPDALAIAQDRLTEKQFLD-KLGIPVAPFAVVDSAEDLEAALADLGLPAVLK---TRRggydGKGQWVIRSAED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 174 LAQAWEyaqqggRAGAGRVIVEGVVKFDFEITLLTVSAVDGVHFCAPVGH-RQEDG--DYCESwqPQQMSPLALERAQEI 250
Cdd:PRK06019 161 LEAAWA------LLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVEnVHRNGilRTSIA--PARISAELQAQAEEI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 251 ARKVVLALGGYGLFGVELFVCGD-EVIFSEVSPRPHDTGMVTL----ISQdlseFALHVRAFLGLPVGGIRQYGPAASAV 325
Cdd:PRK06019 233 ASRIAEELDYVGVLAVEFFVTGDgELLVNEIAPRPHNSGHWTIeacsTSQ----FEQHLRAILGLPLGTTRLLSPAVMVN 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13362027 326 ILPQltsqnVTFDNVQNAVGA--DLQIRLFGKPEIDGSRRLGVALATAESVVDAIERAKHAAGQV 388
Cdd:PRK06019 309 LLGD-----DWLEPRWDALLAlpGAHLHLYGKAEARPGRKMGHVTVLGDDVEALLAKLEALAPDW 368
|
|
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
10-380 |
1.12e-36 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 140.19 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 10 PAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMHVAHRSHVINMLDGDALRrvvELEKPHYIVP-EIEAIAT 88
Cdd:PLN02948 20 VSETVVGVLGGGQLGRMLCQAASQMGIKVKVLDPLEDCPASSVAARHVVGSFDDRAAVR---EFAKRCDVLTvEIEHVDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 89 DMLIQLEEEGLNVVPCAR---------ATKLTMNREGIrrlaaeelqlPTSTYRFADSESLFREAVAAIGYPCIVKPV-M 158
Cdd:PLN02948 97 DTLEALEKQGVDVQPKSStiriiqdkyAQKVHFSKHGI----------PLPEFMEIDDLESAEKAGDLFGYPLMLKSRrL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 159 SSSGKGQTFIRSAEQLAQAweYAQQGGRAGAgrVIVEGVVKFDFEITLLTVSAVDGVHFCAPVG---HRQEDGDYCESwq 235
Cdd:PLN02948 167 AYDGRGNAVAKTEEDLSSA--VAALGGFERG--LYAEKWAPFVKELAVMVARSRDGSTRCYPVVetiHKDNICHVVEA-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 236 PQQMSPLALERAQEIARKVVLALGGYGLFGVELFVCGDE-VIFSEVSPRPHDTGMVTLISQDLSEFALHVRAFLGLPVGG 314
Cdd:PLN02948 241 PANVPWKVAKLATDVAEKAVGSLEGAGVFGVELFLLKDGqILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPLGD 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13362027 315 IRQYGPAASAVILPQLTSQNVTFDNVQNAVGADLQI-----RLFGKPEIDGSRRLGVALATAESVVDAIER 380
Cdd:PLN02948 321 TSMKVPAAIMYNILGEDEGEAGFRLAHQLMGRALNIpgasvHWYGKPEMRKQRKMGHITVVGPSAAEVEAR 391
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
119-312 |
2.09e-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: 89.93 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 119 RLAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGGRAGA--GRVIVEg 196
Cdd:COG0439 59 REALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSpnGEVLVE- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 197 vvKF--DFEITLLTVSAVDGVHFCAPVGHRQEDGDYCES--WQPQQMSPLALERAQEIARKVVLALG-GYGLFGVELFVC 271
Cdd:COG0439 138 --EFleGREYSVEGLVRDGEVVVCSITRKHQKPPYFVELghEAPSPLPEELRAEIGELVARALRALGyRRGAFHTEFLLT 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13362027 272 GD-EVIFSEVSPRPHDTGMVTLISQ----DLseFALHVRAFLGLPV 312
Cdd:COG0439 216 PDgEPYLIEINARLGGEHIPPLTELatgvDL--VREQIRLALGEPR 259
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
25-284 |
4.97e-12 |
|
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: 66.12 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 25 KEVAIECQRLGVEVIAVDRyadapamhvahRSHVINMLDGDALRRVVELEKPHYIVPEIEAI--ATDMLIQLEEEGLNVV 102
Cdd:COG0189 17 KALIEAAQRRGHEVEVIDP-----------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPfyGLALLRQLEAAGVPVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 103 PCARAT-----KLTMNRegirrlAAEELQLPTSTYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQA 177
Cdd:COG0189 86 NDPEAIrrardKLFTLQ------LLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 178 WEYAQQGGRagaGRVIVEGVVK----FDFEITLltvsaVDGVHFCA-----PVGHRQEDGDYCESWQPQQMSPlaleRAQ 248
Cdd:COG0189 160 LEALTELGS---EPVLVQEFIPeedgRDIRVLV-----VGGEPVAAirripAEGEFRTNLARGGRAEPVELTD----EER 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 13362027 249 EIARKVVLALgGYGLFGVELFVCGDEVIFSEVSPRP 284
Cdd:COG0189 228 ELALRAAPAL-GLDFAGVDLIEDDDGPLVLEVNVTP 262
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
136-294 |
3.32e-10 |
|
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: 59.25 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 136 DSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGGRagagRVIVE-GVVKFDFEITLLTvsavDG 214
Cdd:pfam07478 23 NPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDE----KVLVEeGIEGREIECAVLG----NE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 215 VHFCAPVGHRQEDG---DYCESWQP---QQMSPLAL-----ERAQEIARKVVLALGGYGLFGVELFVCGD-EVIFSEVSP 282
Cdd:pfam07478 95 DPEVSPVGEIVPSGgfyDYEAKYIDdsaQIVVPADLeeeqeEQIQELALKAYKALGCRGLARVDFFLTEDgEIVLNEVNT 174
|
170
....*....|..
gi 13362027 283 RPhdtGMvTLIS 294
Cdd:pfam07478 175 IP---GF-TSIS 182
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
32-327 |
8.95e-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: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 32 QRLGVEVIAVDRYADAPAMHVAHRSHVINMLDG--------DALRRVVELEKPHYIVP--EIEAiATDMLIQLEEEGLNV 101
Cdd:COG2232 22 RRAGYRVYAVDLFADLDTRALAERWVRLDAESCgfdledlpAALLELAAADDPDGLVYgsGFEN-FPELLERLARRLPLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 102 VPCARATKLTMNRegiRRLAA--EELQLPTSTYRFADSESlfreavaaiGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWe 179
Cdd:COG2232 101 GNPPEVVRRVKDP---LRFFAllDELGIPHPETRFEPPPD---------PGPWLVKPIGGAGGWHIRPADSEAPPAPGR- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 180 YAQQggragagrvIVEGvvkfdfeiTLLTVSAVDGVHFCAPVG-HRQ---EDGD----YCESWQPQQMSPLALERAQEIA 251
Cdd:COG2232 168 YFQR---------YVEG--------TPASVLFLADGSDARVLGfNRQligPAGErpfrYGGNIGPLALPPALAEEMRAIA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13362027 252 RKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPhdTGMVTLISQDLSE--FALHVRAFLG-LPVGGIRQYGPAASAVIL 327
Cdd:COG2232 231 EALVAALGLVGLNGVDFILDGDGPYVLEVNPRP--QASLDLYEDATGGnlFDAHLRACRGeLPEVPRPKPRRVAAKAIL 307
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
10-194 |
4.22e-09 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 57.63 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 10 PAATRVMLLGSGELGKEVAIECQRLGVEVIAVDRYADAPAMH--VAHRSHVI-NMLDG-----DALRRVVELEKPHYIVP 81
Cdd:COG3919 3 TMRFRVVVLGGDINALAVARSLGEAGVRVIVVDRDPLGPAARsrYVDEVVVVpDPGDDpeafvDALLELAERHGPDVLIP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 82 EIEAiATDMLIQLEEEgLN---VVPCARATKLT--MNREGIRRLAaEELQLPTSTYRFADSESLFREAVAAIGYPCIVKP 156
Cdd:COG3919 83 TGDE-YVELLSRHRDE-LEehyRLPYPDADLLDrlLDKERFYELA-EELGVPVPKTVVLDSADDLDALAEDLGFPVVVKP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13362027 157 VMSSS-------GKGQTF-IRSAEQLAQAWEYAqqggRAGAGRVIV 194
Cdd:COG3919 160 ADSVGydelsfpGKKKVFyVDDREELLALLRRI----AAAGYELIV 201
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
127-280 |
5.49e-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: 57.04 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 127 LPTSTYRFADSESL--FREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGGRagagRVIVE----GVvkf 200
Cdd:COG1181 108 LPTPPYVVLRRGELadLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDD----KVLVEefidGR--- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 201 dfEItllTVSAVDGVHFCA-PVG------------HRQEDGD---YCeswqPQQMSPLALERAQEIARKVVLALGGYGLF 264
Cdd:COG1181 181 --EV---TVGVLGNGGPRAlPPIeivpengfydyeAKYTDGGteyIC----PARLPEELEERIQELALKAFRALGCRGYA 251
|
170
....*....|....*..
gi 13362027 265 GVELFVCGD-EVIFSEV 280
Cdd:COG1181 252 RVDFRLDEDgEPYLLEV 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
14-283 |
9.93e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 56.43 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 14 RVMLLGSGELGKEV-AIECQRLGVEVIAVDRYADAPAMHVAHRSHVINML-DGDALRRVVEL---EKPHYIVPEIE---- 84
Cdd:PRK12767 3 NILVTSAGRRVQLVkALKKSLLKGRVIGADISELAPALYFADKFYVVPKVtDPNYIDRLLDIckkEKIDLLIPLIDpelp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 85 --AIATDMLiqlEEEG-------LNVVPCARATKLTMNregirrlAAEELQLPTS-TYRFADSESLFRE-AVAAIGYPCI 153
Cdd:PRK12767 83 llAQNRDRF---EEIGvkvlvssKEVIEICNDKWLTYE-------FLKENGIPTPkSYLPESLEDFKAAlAKGELQFPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 154 VKPVMSSSGKGQTFIRSAEQLAQAWEYAQQggragagrVIVEGVVKFDfEITLLTVSAVDGVHFCAPVGHRQE--DGdyc 231
Cdd:PRK12767 153 VKPRDGSASIGVFKVNDKEELEFLLEYVPN--------LIIQEFIEGQ-EYTVDVLCDLNGEVISIVPRKRIEvrAG--- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13362027 232 ESWQ----PQqmsplalERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPR 283
Cdd:PRK12767 221 ETSKgvtvKD-------PELFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPR 269
|
|
| 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 |
1.62e-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: 52.67 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 107 ATKLTMNREGIRRLAAEeLQLPTSTYRF-----ADSESLFREAVAA-IGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEY 180
Cdd:TIGR01205 99 ASALSMDKLLTKLLWKA-LGLPTPDYIVltqnrASADELECEQVAEpLGFPVIVKPAREGSSVGVSKVKSEEELQAALDE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 181 AQQGGRagagRVIVEGVVKFDfEITLLTVSAVDGVHFCAPVGHRQEDGDYCESWQ--------PQQMSPLALERAQEIAR 252
Cdd:TIGR01205 178 AFEYDE----EVLVEQFIKGR-ELEVSILGNEEALPIIEIVPEIEGFYDYEAKYLdgsteyviPAPLDEELEEKIKELAL 252
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13362027 253 KVVLALGGYGLFGVELFVCGD-EVIFSEVSPRPhdtGMVTL 292
Cdd:TIGR01205 253 KAYKALGCRGLARVDFFLDEEgEIYLNEINTIP---GMTAI 290
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
70-312 |
2.32e-07 |
|
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: 53.08 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 70 VVELEKPHYIVPEIEA-IATDMLIQLEEEGLNVV-PCARATKLTMNREGIRRLAaEELQLPTSTYRFADSESLFREAVAA 147
Cdd:TIGR01369 624 IIELEKPEGVIVQFGGqTPLNLAKALEEAGVPILgTSPESIDRAEDREKFSELL-DELGIPQPKWKTATSVEEAVEFASE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 148 IGYPCIVKPVMSSSGKGQTFIRSAEQLAQaweYAQQGGRAGAGRVIVegVVKFDFEITLLTVSAV-DG--VHFCAPVGHR 224
Cdd:TIGR01369 703 IGYPVLVRPSYVLGGRAMEIVYNEEELRR---YLEEAVAVSPEHPVL--IDKYLEDAVEVDVDAVsDGeeVLIPGIMEHI 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 225 QE----DGDYCESWQPQQMSPLALERAQEIARKVVLALGGYGLFGVELFVCGDEVIFSEVSPRPHDTgmVTLISQ----D 296
Cdd:TIGR01369 778 EEagvhSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRT--VPFVSKatgvP 855
|
250
....*....|....*.
gi 13362027 297 LSEFAlhVRAFLGLPV 312
Cdd:TIGR01369 856 LAKLA--VRVMLGKKL 869
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
105-381 |
1.25e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 50.62 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 105 ARATKLTMNREGI-RRLAAEELQLPTSTYRFADSESlfREAVAAIGYPCIVKPVMsssGKGQTFIRSAEQLAQAWEYAQQ 183
Cdd:PRK02186 99 TEAIRTCRDKKRLaRTLRDHGIDVPRTHALALRAVA--LDALDGLTYPVVVKPRM---GSGSVGVRLCASVAEAAAHCAA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 184 GGRAGAGRVIVEGVVKFDfEITLLTVSAVDGVH-------FCAPVGHRQEDG-DYceswqPqqmSPLALERAQEIARKVV 255
Cdd:PRK02186 174 LRRAGTRAALVQAYVEGD-EYSVETLTVARGHQvlgitrkHLGPPPHFVEIGhDF-----P---APLSAPQRERIVRTVL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 256 LALGGYGL-FG---VELFVCGDEVIFSEVSPRPHDtGMV-TLISQ--DLSEFALHVRAFLG---LPVGGIRQYGpaASAV 325
Cdd:PRK02186 245 RALDAVGYaFGpahTELRVRGDTVVIIEINPRLAG-GMIpVLLEEafGVDLLDHVIDLHLGvaaFADPTAKRYG--AIRF 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13362027 326 ILPQLTSQNVTFDNVQNAVGADLQIRLFG--------KPEIDGSRRLGVALATAESvVDAIERA 381
Cdd:PRK02186 322 VLPARSGVLRGLLFLPDDIAARPELRFHPlkqpgdalRLEGDFRDRIAAVVCAGDH-RDSVAAA 384
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
127-205 |
3.18e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 48.57 E-value: 3.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13362027 127 LPTSTYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGGragaGRVIVEGVVKFDfEIT 205
Cdd:PRK01372 111 LPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYD----DEVLVEKYIKGR-ELT 184
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
119-283 |
9.59e-05 |
|
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: 43.06 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 119 RLAAEELQLPT--STYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQ--GGRAGAGRVIV 194
Cdd:pfam02786 6 KAAMKEAGVPTvpGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAeaPAAFGNPQVLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 195 EGVVKFDFEITLLTVSavDGVHFCAPVGHRQ-----EDGDYCESWQPQQMSPLALERAQEIARKVVLALGGYGLFGVELF 269
Cdd:pfam02786 86 EKSLKGPKHIEYQVLR--DAHGNCITVCNREcsdqrRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFA 163
|
170
....*....|....*.
gi 13362027 270 V--CGDEVIFSEVSPR 283
Cdd:pfam02786 164 LdpFSGEYYFIEMNTR 179
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
110-294 |
1.36e-04 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 43.57 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 110 LTMNREGIRRLAAEeLQLPTSTY----RFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGG 185
Cdd:PRK01966 120 LSMDKILTKRLLAA-AGIPVAPYvvltRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 186 RagagRVIVE----------GVVKFDFEITLLT-VSAVDG--------VHFCApvghrQEDgdyceswQPQQMSPLALER 246
Cdd:PRK01966 199 R----KVLVEqgikgreiecAVLGNDPKASVPGeIVKPDDfydyeakyLDGSA-----ELI-------IPADLSEELTEK 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13362027 247 AQEIARKVVLALGGYGLFGVELFVCGD-EVIFSEVSPRPhdtGMvTLIS 294
Cdd:PRK01966 263 IRELAIKAFKALGCSGLARVDFFLTEDgEIYLNEINTMP---GF-TPIS 307
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
118-284 |
2.31e-04 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 41.22 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 118 RRLAAEELQLPTsTYRFADSESlfreavaaIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEY--AQQggragagrvIVE 195
Cdd:pfam02655 9 KALKNAGVPTPE-TLQAEELLR--------EEKKYVVKPRDGCGGEGVRKVENGREDEAFIENvlVQE---------FIE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 196 GVvkfdfEITLLTVSAVDGVHFCAP----VGHRQEDGDYCESWQPqqmSPLAL-ERAQEIARKVVLALGG-YGLFGVELF 269
Cdd:pfam02655 71 GE-----PLSVSLLSDGEKALPLSVnrqyIDNGGSGFVYAGNVTP---SRTELkEEIIELAEEVVECLPGlRGYVGVDLV 142
|
170
....*....|....*
gi 13362027 270 VCGDEVIFSEVSPRP 284
Cdd:pfam02655 143 LKDNEPYVIEVNPRI 157
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
8-174 |
4.14e-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: 42.68 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 8 LRPAATRVMLLGSGELGKEVAIE--------CQRL---GVEVIAVDryaDAPAM-----HVAHRSHvINMLDGDALRRVV 71
Cdd:TIGR01369 2 KRTDIKKILVIGSGPIVIGQAAEfdysgsqaCKALkeeGYRVILVN---SNPATimtdpEMADKVY-IEPLTPEAVEKII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 72 ELEKPHYIVPEIEA-IATDMLIQLEEEGL----NV----VPcARATKLTMNREGIRRlAAEELQLPTSTYRFADSESLFR 142
Cdd:TIGR01369 78 EKERPDAILPTFGGqTALNLAVELEESGVlekyGVevlgTP-VEAIKKAEDRELFRE-AMKEIGEPVPESEIAHSVEEAL 155
|
170 180 190
....*....|....*....|....*....|..
gi 13362027 143 EAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQL 174
Cdd:TIGR01369 156 AAAKEIGYPVIVRPAFTLGGTGGGIAYNREEL 187
|
|
| dTDP_HR_like_SDR_e |
cd05254 |
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ... |
14-80 |
7.35e-04 |
|
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: 41.07 E-value: 7.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13362027 14 RVMLLG-SGELGKEVAIECQRLGVEVIAVDRyADApamhvahRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:cd05254 1 KILITGaTGMLGRALVRLLKERGYEVIGTGR-SRA-------SLFKLDLTDPDAVEEAIRDYKPDVII 60
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
119-195 |
1.52e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 40.89 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 119 RLAAEELQLPT--STYRFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQAWEYAQQGGRA--GAGRVIV 194
Cdd:PRK12999 124 RNAAIKAGVPVipGSEGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAFERAKREAKAafGNDEVYL 203
|
.
gi 13362027 195 E 195
Cdd:PRK12999 204 E 204
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
65-184 |
2.33e-03 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 40.34 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 65 DALRRVVELEKPHYIVPEIEA-IATDMLIQLEEEG-----------LNVvpcaRATKLTMNREGIRRLAaEELQLPTSTY 132
Cdd:PRK12815 72 EFVKRIIAREKPDALLATLGGqTALNLAVKLHEDGileqygvellgTNI----EAIQKGEDRERFRALM-KELGEPVPES 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 13362027 133 RFADSESLFREAVAAIGYPCIVKPVMSSSGKGQTFIRSAEQLAQaweYAQQG 184
Cdd:PRK12815 147 EIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQ---LFKQG 195
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
14-217 |
3.14e-03 |
|
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: 39.23 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 14 RVMLLGSGelGKEVAIeCQRL----GVEVIAVdryadAP-----AMHVahRSHVINMLDGDALRRVVELEKPHYIVPEIE 84
Cdd:COG0151 2 KVLVIGSG--GREHAL-AWKLaqspRVDKLYV-----APgnagtAQLA--ECVDIDVTDIEALVAFAKEENIDLVVVGPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13362027 85 A-----IAtDmliQLEEEGLNVV-PCARATKLT---------MNREGIrrlaaeelqlPTSTYR-FADSESLfREAVAAI 148
Cdd:COG0151 72 AplvagIV-D---AFRAAGIPVFgPSKAAAQLEgskafakefMARYGI----------PTAAYRvFTDLEEA-LAYLEEQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13362027 149 GYPCIVKPVMSSSGKGqtfIRSAEQLAQAWEYAQ------QGGRAGAgRVIVEgvvkfDF----EITLLTVsaVDGVHF 217
Cdd:COG0151 137 GAPIVVKADGLAAGKG---VVVAETLEEALAAVDdmladgKFGDAGA-RVVIE-----EFlegeEASLFAL--TDGKTV 204
|
|
| Epimerase |
pfam01370 |
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ... |
19-80 |
3.66e-03 |
|
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: 38.43 E-value: 3.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13362027 19 GSGELGKEVAIECQRLGVEVIAVDR--YADAPAMHVAHRSHVINMLDGDALRRVVELEKPHYIV 80
Cdd:pfam01370 6 ATGFIGSHLVRRLLEKGYEVIGLDRltSASNTARLADLRFVEGDLTDRDALEKLLADVRPDAVI 69
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
143-195 |
3.70e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 39.37 E-value: 3.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 13362027 143 EAVAAIGYPCIVKPVMSSSGKGQTF-IRSAEQLAQAWEYAQQGGRAgagrVIVE 195
Cdd:PRK14016 243 EAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD----VIVE 292
|
|
| |
