|
Name |
Accession |
Description |
Interval |
E-value |
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
3-219 |
1.27e-79 |
|
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439902 [Multi-domain] Cd Length: 222 Bit Score: 238.13 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSKETPEGLRNKDALVLQSVSSLELPYQAVNPIALSE--- 79
Cdd:COG0132 2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFEEpls 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 80 -----EESSVAhsglINYPLLSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALL 154
Cdd:COG0132 82 phlaaRLEGVP----IDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736214186 155 TAQAIANDGLPLVGWVANRINPGLAHYAEIIDVLSAKLPGPLVGELPYLPRAEQRELAQYIDLSA 219
Cdd:COG0132 158 TVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLES 222
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
3-188 |
5.09e-50 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 161.58 E-value: 5.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGsketPEGLRNKDALVLQSVSSLELPYQAVNPIALSEEES 82
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTG----CPGLEDSDAELLRKLAGLLLDLELINPYRFEAPLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 83 ---SVAHSGL-INYPLLSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALLTAQA 158
Cdd:cd03109 77 phlAAELEGRdIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEA 156
|
170 180 190
....*....|....*....|....*....|
gi 1736214186 159 IANDGLPLVGWVANRINPGLAHYAEIIDVL 188
Cdd:cd03109 157 LKSRGLDVAGVVLNGIPPEPEAEADNAETL 186
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
6-172 |
1.75e-47 |
|
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 129447 [Multi-domain] Cd Length: 166 Bit Score: 154.44 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 6 FVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSKETPEglrnkDALVLQSVSSLELPYQAVNPIALSEEESSVA 85
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNS-----DALLLQNISGTALDWDEVNPYAFALPLSPHI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 86 HSGLINYPL----LSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALLTAQAIAN 161
Cdd:TIGR00347 76 AADQEGRPIdleeLSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155
|
170
....*....|.
gi 1736214186 162 DGLPLVGWVAN 172
Cdd:TIGR00347 156 TGLTLAGVILN 166
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
3-204 |
7.82e-31 |
|
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.
Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 112.35 E-value: 7.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSketpegLRNKDALVLQSVSSLELPYQAVNPIALSEEES 82
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTGL------VEDGDSELVKRLLGLDQSYEDPEPFRLSAPLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 83 SVAHSGLINYPL-LSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALLTAQAIAN 161
Cdd:pfam13500 75 PHLAARQEGVTIdLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALRQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1736214186 162 DGLPLVGWVANRINPglahyAEIIDVLSAKLPGPLVGELPYLP 204
Cdd:pfam13500 155 RGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
|
|
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-230 |
4.50e-07 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 49.77 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 1 MLKRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAkgsketpeglrnKDALVLQSVSSLelpyqavnpiaLSEE 80
Cdd:PRK05632 1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIA------------QPPLTMSEVEAL-----------LASG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 81 ESSVAHSGLI-NYpllsdglANLSEKVDHVVVEGTggwrslmnDLRPLS--EWVVQEQL------PVVMVVG----IQEG 147
Cdd:PRK05632 58 QLDELLEEIVaRY-------HALAKDCDVVLVEGL--------DPTRKHpfEFSLNAEIaknlgaEVVLVSSggndTPEE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 148 CINHALLTAQAIAND-GLPLVGWVANRINPGLAHYAEIIDVLS-----------------AKLPGPLVGELPYL-----P 204
Cdd:PRK05632 123 LAERIELAASSFGGAkNANILGVIINKLNAPVDEQGRTRPDLSeifddsskanvdpsklfASSPLPLLGVVPWSpdliaP 202
|
250 260
....*....|....*....|....*.
gi 1736214186 205 RAeqRELAQYIDLSALGGVLAVDRVV 230
Cdd:PRK05632 203 RV--IDIAKHLGATVLNEGDILTRRV 226
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
3-219 |
1.27e-79 |
|
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439902 [Multi-domain] Cd Length: 222 Bit Score: 238.13 E-value: 1.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSKETPEGLRNKDALVLQSVSSLELPYQAVNPIALSE--- 79
Cdd:COG0132 2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFEEpls 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 80 -----EESSVAhsglINYPLLSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALL 154
Cdd:COG0132 82 phlaaRLEGVP----IDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736214186 155 TAQAIANDGLPLVGWVANRINPGLAHYAEIIDVLSAKLPGPLVGELPYLPRAEQRELAQYIDLSA 219
Cdd:COG0132 158 TVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLES 222
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
3-188 |
5.09e-50 |
|
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.
Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 161.58 E-value: 5.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGsketPEGLRNKDALVLQSVSSLELPYQAVNPIALSEEES 82
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTG----CPGLEDSDAELLRKLAGLLLDLELINPYRFEAPLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 83 ---SVAHSGL-INYPLLSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALLTAQA 158
Cdd:cd03109 77 phlAAELEGRdIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEA 156
|
170 180 190
....*....|....*....|....*....|
gi 1736214186 159 IANDGLPLVGWVANRINPGLAHYAEIIDVL 188
Cdd:cd03109 157 LKSRGLDVAGVVLNGIPPEPEAEADNAETL 186
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
6-172 |
1.75e-47 |
|
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 129447 [Multi-domain] Cd Length: 166 Bit Score: 154.44 E-value: 1.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 6 FVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSKETPEglrnkDALVLQSVSSLELPYQAVNPIALSEEESSVA 85
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNS-----DALLLQNISGTALDWDEVNPYAFALPLSPHI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 86 HSGLINYPL----LSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALLTAQAIAN 161
Cdd:TIGR00347 76 AADQEGRPIdleeLSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155
|
170
....*....|.
gi 1736214186 162 DGLPLVGWVAN 172
Cdd:TIGR00347 156 TGLTLAGVILN 166
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
3-204 |
7.82e-31 |
|
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.
Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 112.35 E-value: 7.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSketpegLRNKDALVLQSVSSLELPYQAVNPIALSEEES 82
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTGL------VEDGDSELVKRLLGLDQSYEDPEPFRLSAPLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 83 SVAHSGLINYPL-LSDGLANLSEKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVVMVVGIQEGCINHALLTAQAIAN 161
Cdd:pfam13500 75 PHLAARQEGVTIdLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALRQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1736214186 162 DGLPLVGWVANRINPglahyAEIIDVLSAKLPGPLVGELPYLP 204
Cdd:pfam13500 155 RGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-211 |
1.80e-29 |
|
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.
Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 109.74 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 5 FFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAKGSKETPEGLRNKDALVLQSVSSLELPYQAVNPIALSEEESS- 83
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLKEKSDEg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 84 ---------VAHSGLINYP------LLSDGLANLSEKVDHVVVEGTGGW-RSLMNDLRPLSEWVVQEQLPVVMVVGIQE- 146
Cdd:pfam01656 81 gldlipgniDLEKFEKELLgprkeeRLREALEALKEDYDYVIIDGAPGLgELLRNALIAADYVIIPLEPEVILVEDAKRl 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736214186 147 GCINHALLTAQAIAndGLPLVGWVANRINPGLAHYAEIIDVLSAKLPGPLVGELPY---LPRAEQREL 211
Cdd:pfam01656 161 GGVIAALVGGYALL--GLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGVIPRdeaVAEAPARGL 226
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-230 |
5.31e-20 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 87.96 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 1 MLKRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVakGSKETPEGLRNKDALVLQSVSSLELPYQAVNPIALSEE 80
Cdd:COG0857 1 MMKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPI--GQSLVGGGERDEDVELIREHLGLDLPYEDASPVTLDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 81 ESSVAHSGLINypLLSDGLAN---LSEKVDHVVVEGTGGWR-SLMNDLRPLSEwvVQEQL--PVVMVVGIQ----EGCIN 150
Cdd:COG0857 79 ETLLAEGDPDE--LLERIVERyeaLAAECDVVLVEGSDPTGvGSPFELSLNAR--IAKNLgaPVLLVASGGgrtpEELVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 151 HALLTAQAIANDGLPLVGWVANRINPglAHYAEIIDVLSAKLPG---PLVGELPY-----LPRAeqRELAQYIDLSALGG 222
Cdd:COG0857 155 ALLLAADEFRGEGARVLGVIINRVPP--EKLEEVREALRPFLEGsgiPVLGVIPEnpelaAPTV--RDLAEALGAEVLNG 230
|
....*...
gi 1736214186 223 VLAVDRVV 230
Cdd:COG0857 231 GELLDRRV 238
|
|
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-230 |
4.50e-07 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 49.77 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 1 MLKRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYKPVAkgsketpeglrnKDALVLQSVSSLelpyqavnpiaLSEE 80
Cdd:PRK05632 1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIA------------QPPLTMSEVEAL-----------LASG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 81 ESSVAHSGLI-NYpllsdglANLSEKVDHVVVEGTggwrslmnDLRPLS--EWVVQEQL------PVVMVVG----IQEG 147
Cdd:PRK05632 58 QLDELLEEIVaRY-------HALAKDCDVVLVEGL--------DPTRKHpfEFSLNAEIaknlgaEVVLVSSggndTPEE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 148 CINHALLTAQAIAND-GLPLVGWVANRINPGLAHYAEIIDVLS-----------------AKLPGPLVGELPYL-----P 204
Cdd:PRK05632 123 LAERIELAASSFGGAkNANILGVIINKLNAPVDEQGRTRPDLSeifddsskanvdpsklfASSPLPLLGVVPWSpdliaP 202
|
250 260
....*....|....*....|....*.
gi 1736214186 205 RAeqRELAQYIDLSALGGVLAVDRVV 230
Cdd:PRK05632 203 RV--IDIAKHLGATVLNEGDILTRRV 226
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
3-38 |
3.37e-06 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 44.73 E-value: 3.37e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYK 38
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLID 36
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
1-38 |
1.89e-05 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 44.74 E-value: 1.89e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1736214186 1 MLKRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYK 38
Cdd:PRK01077 2 RMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFK 39
|
|
| CobB_N |
cd05388 |
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
3-38 |
8.16e-05 |
|
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.
Pssm-ID: 349773 [Multi-domain] Cd Length: 193 Bit Score: 42.20 E-value: 8.16e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1736214186 3 KRFFVTGTDTSVGKTVVSRALLQALAASGKRVAGYK 38
Cdd:cd05388 1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFK 36
|
|
| COG4028 |
COG4028 |
Predicted P-loop ATPase/GTPase [General function prediction only]; |
4-146 |
3.04e-04 |
|
Predicted P-loop ATPase/GTPase [General function prediction only];
Pssm-ID: 443206 Cd Length: 288 Bit Score: 40.78 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 4 RFFVTGTDTS-VGKTVVSRALLQALAASGKRVAGYKPVA-----------KGSKETpEGLRNKDALVLQSVSSLELPYQA 71
Cdd:COG4028 2 RLLVAGLLRVdSGKTTFSLGLLERLGEVGLDAVGFKPRAghnywydhdtlRRSLEL-GRLVGKDAYRLADASGEDRPPEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 72 VNPIAL-------SEEESSVAHSGLINYPL-------LSDGLANlsEKVDHVVVEGTGgwRSLMNDLRPlsewVVQEQLP 137
Cdd:COG4028 81 INPVHRlwrppdpEKYRNIRLYLGLLGRPDrtfvldrVTRCLNG--EEDPHYVVNATA--ERLPKSLPE----VLEELLP 152
|
....*....
gi 1736214186 138 VVMVVGIQE 146
Cdd:COG4028 153 LLDAIPVES 161
|
|
| CobQ_N |
cd05389 |
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ... |
7-116 |
9.91e-04 |
|
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid.
Pssm-ID: 349774 Cd Length: 223 Bit Score: 39.11 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736214186 7 VTGTDTSVGKTVVSRALLQALAASGKRVAGYKP--VAKGSKETPEGLRNKDALVLQSVSSLELPYQAVNPIAL---SEEE 81
Cdd:cd05389 5 VQGTASDVGKSTLVAALCRILKRRGYRVAPFKAqnMSLNSFVTKDGGEIGRAQAVQAEAAGVEPSVDMNPVLLkpkGDFK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1736214186 82 SSVAHSG--LINY-------------PLLSDGLANLSEKVDHVVVEGTGG 116
Cdd:cd05389 85 SQVIVMGkpIGDMdareyyeykgrlaPAVLESLDRLAAEYDLVVIEGAGS 134
|
|
| |
