|
Name |
Accession |
Description |
Interval |
E-value |
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
3-218 |
1.81e-85 |
|
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: 252.39 E-value: 1.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCQETSEGIRNKDALVLQASSTLPLSYEEINPITcldevF 82
Cdd:COG0132 2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYR-----F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 83 ------HAHATED---INYGVMSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHAL 153
Cdd:COG0132 77 eeplspHLAARLEgvpIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742394816 154 LTAQSIINDGLPLLGWVANRINPGLAHYAETIAALQQRIPAPLLGEIPYLPRAEQRELAHYLDIS 218
Cdd:COG0132 157 LTVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLE 221
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
3-188 |
2.71e-52 |
|
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: 166.98 E-value: 2.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCqetsEGIRNKDALVLQASSTLPLSYEEINPITcldevF 82
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGC----PGLEDSDAELLRKLAGLLLDLELINPYR-----F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 83 HAHA---------TEDINYGVMSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHAL 153
Cdd:cd03109 72 EAPLsphlaaeleGRDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 742394816 154 LTAQSIINDGLPLLGWVANRINPGLAHYAETIAAL 188
Cdd:cd03109 152 LTLEALKSRGLDVAGVVLNGIPPEPEAEADNAETL 186
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
6-172 |
8.90e-46 |
|
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: 149.43 E-value: 8.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 6 FVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCQETSEgirnkDALVLQASSTLPLSYEEINPIT----CLDEV 81
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNS-----DALLLQNISGTALDWDEVNPYAfalpLSPHI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 82 FHAHATEDINYGVMSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHALLTAQSIIN 161
Cdd:TIGR00347 76 AADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155
|
170
....*....|.
gi 742394816 162 DGLPLLGWVAN 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 |
1.51e-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: 113.89 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAarcqetSEGIRNKDALVLQASSTLPLSYEEINPItCLDEVF 82
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQ------TGLVEDGDSELVKRLLGLDQSYEDPEPF-RLSAPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 83 HAHATEDINyGV---MSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHALLTAQSI 159
Cdd:pfam13500 74 SPHLAARQE-GVtidLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 742394816 160 INDGLPLLGWVANRINPglahyAETIAALQQRIPAPLLGEIPYLP 204
Cdd:pfam13500 153 RQRGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
|
|
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-216 |
7.71e-11 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 60.94 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 1 MLKRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARcqetsegirnkdalvlqasstlPLSYEEINPITC--- 77
Cdd:PRK05632 1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP----------------------PLTMSEVEALLAsgq 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 78 LDEVFhahatEDI--NYgvmssglRDLSVKADTVVVEGSggwrvLMNDLRPY-----AEWVVQEQLPVVLVVGIK----L 146
Cdd:PRK05632 59 LDELL-----EEIvaRY-------HALAKDCDVVLVEGL-----DPTRKHPFefslnAEIAKNLGAEVVLVSSGGndtpE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 147 GCVSHALLTAQSIIND-GLPLLGWVANRINPGLAHYAETIAALQQRI-----------------PAPLLGEIPYL----- 203
Cdd:PRK05632 122 ELAERIELAASSFGGAkNANILGVIINKLNAPVDEQGRTRPDLSEIFddsskanvdpsklfassPLPLLGVVPWSpdlia 201
|
250
....*....|...
gi 742394816 204 PRAeqRELAHYLD 216
Cdd:PRK05632 202 PRV--IDIAKHLG 212
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
3-218 |
1.81e-85 |
|
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: 252.39 E-value: 1.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCQETSEGIRNKDALVLQASSTLPLSYEEINPITcldevF 82
Cdd:COG0132 2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYR-----F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 83 ------HAHATED---INYGVMSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHAL 153
Cdd:COG0132 77 eeplspHLAARLEgvpIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742394816 154 LTAQSIINDGLPLLGWVANRINPGLAHYAETIAALQQRIPAPLLGEIPYLPRAEQRELAHYLDIS 218
Cdd:COG0132 157 LTVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLE 221
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
3-188 |
2.71e-52 |
|
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: 166.98 E-value: 2.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCqetsEGIRNKDALVLQASSTLPLSYEEINPITcldevF 82
Cdd:cd03109 1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGC----PGLEDSDAELLRKLAGLLLDLELINPYR-----F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 83 HAHA---------TEDINYGVMSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHAL 153
Cdd:cd03109 72 EAPLsphlaaeleGRDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 742394816 154 LTAQSIINDGLPLLGWVANRINPGLAHYAETIAAL 188
Cdd:cd03109 152 LTLEALKSRGLDVAGVVLNGIPPEPEAEADNAETL 186
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
6-172 |
8.90e-46 |
|
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: 149.43 E-value: 8.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 6 FVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCQETSEgirnkDALVLQASSTLPLSYEEINPIT----CLDEV 81
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNS-----DALLLQNISGTALDWDEVNPYAfalpLSPHI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 82 FHAHATEDINYGVMSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHALLTAQSIIN 161
Cdd:TIGR00347 76 AADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155
|
170
....*....|.
gi 742394816 162 DGLPLLGWVAN 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 |
1.51e-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: 113.89 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAarcqetSEGIRNKDALVLQASSTLPLSYEEINPItCLDEVF 82
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQ------TGLVEDGDSELVKRLLGLDQSYEDPEPF-RLSAPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 83 HAHATEDINyGV---MSSGLRDLSVKADTVVVEGSGGWRVLMNDLRPYAEWVVQEQLPVVLVVGIKLGCVSHALLTAQSI 159
Cdd:pfam13500 74 SPHLAARQE-GVtidLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 742394816 160 INDGLPLLGWVANRINPglahyAETIAALQQRIPAPLLGEIPYLP 204
Cdd:pfam13500 153 RQRGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-211 |
1.28e-27 |
|
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: 104.74 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 5 LFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCQETSEGIRNKDALVLQASSTLPLSYEEINPITC------- 77
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLkeksdeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 78 -LDEV---FHAHATEDINYGV-----MSSGLRDLSVKADTVVVEGSGGWRVLM-NDLRPYAEWVVQEQLPVVLVVGIK-L 146
Cdd:pfam01656 81 gLDLIpgnIDLEKFEKELLGPrkeerLREALEALKEDYDYVIIDGAPGLGELLrNALIAADYVIIPLEPEVILVEDAKrL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742394816 147 GCVSHALLTAQSiiNDGLPLLGWVANRINPGLAHYAETIAALQQRIPAPLLGEIPY---LPRAEQREL 211
Cdd:pfam01656 161 GGVIAALVGGYA--LLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGVIPRdeaVAEAPARGL 226
|
|
| PtaN |
COG0857 |
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
1-216 |
5.47e-25 |
|
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 102.22 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 1 MLKRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARCQEtsEGIRNKDALVLQASSTLPLSYEEINPITcLDE 80
Cdd:COG0857 1 MMKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLVG--GGERDEDVELIREHLGLDLPYEDASPVT-LDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 81 VFHAHATEDINyGVMS---SGLRDLSVKADTVVVEGSGGWRV-LMNDLRPYAEwvVQEQL--PVVLVVGIKLG----CVS 150
Cdd:COG0857 78 VETLLAEGDPD-ELLErivERYEALAAECDVVLVEGSDPTGVgSPFELSLNAR--IAKNLgaPVLLVASGGGRtpeeLVD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 742394816 151 HALLTAQSIINDGLPLLGWVANRINPG-LAHYAETIAALQQRIPAPLLGEIPY-----LPRAeqRELAHYLD 216
Cdd:COG0857 155 ALLLAADEFRGEGARVLGVIINRVPPEkLEEVREALRPFLEGSGIPVLGVIPEnpelaAPTV--RDLAEALG 224
|
|
| PRK05632 |
PRK05632 |
phosphate acetyltransferase; Reviewed |
1-216 |
7.71e-11 |
|
phosphate acetyltransferase; Reviewed
Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 60.94 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 1 MLKRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYKPIAARcqetsegirnkdalvlqasstlPLSYEEINPITC--- 77
Cdd:PRK05632 1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQP----------------------PLTMSEVEALLAsgq 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 78 LDEVFhahatEDI--NYgvmssglRDLSVKADTVVVEGSggwrvLMNDLRPY-----AEWVVQEQLPVVLVVGIK----L 146
Cdd:PRK05632 59 LDELL-----EEIvaRY-------HALAKDCDVVLVEGL-----DPTRKHPFefslnAEIAKNLGAEVVLVSSGGndtpE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 147 GCVSHALLTAQSIIND-GLPLLGWVANRINPGLAHYAETIAALQQRI-----------------PAPLLGEIPYL----- 203
Cdd:PRK05632 122 ELAERIELAASSFGGAkNANILGVIINKLNAPVDEQGRTRPDLSEIFddsskanvdpsklfassPLPLLGVVPWSpdlia 201
|
250
....*....|...
gi 742394816 204 PRAeqRELAHYLD 216
Cdd:PRK05632 202 PRV--IDIAKHLG 212
|
|
| COG4028 |
COG4028 |
Predicted P-loop ATPase/GTPase [General function prediction only]; |
4-75 |
2.18e-08 |
|
Predicted P-loop ATPase/GTPase [General function prediction only];
Pssm-ID: 443206 Cd Length: 288 Bit Score: 53.11 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 4 RLFVTGTDT-DVGKTVVSRGLMQALAAEGRSVAGYKPIAAR--------CQETSEGIR--NKDALVLQASSTLPLSYEEI 72
Cdd:COG4028 2 RLLVAGLLRvDSGKTTFSLGLLERLGEVGLDAVGFKPRAGHnywydhdtLRRSLELGRlvGKDAYRLADASGEDRPPEII 81
|
...
gi 742394816 73 NPI 75
Cdd:COG4028 82 NPV 84
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
1-38 |
1.49e-06 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 48.21 E-value: 1.49e-06
10 20 30
....*....|....*....|....*....|....*...
gi 742394816 1 MLKRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYK 38
Cdd:PRK01077 2 RMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFK 39
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
3-38 |
1.60e-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: 45.50 E-value: 1.60e-06
10 20 30
....*....|....*....|....*....|....*.
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYK 38
Cdd:cd01983 1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLID 36
|
|
| CobB_N |
cd05388 |
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
3-211 |
4.84e-06 |
|
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: 45.67 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 3 KRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYK-------PI---AARCQETsegiRNKDalvlqassTLPLSYEEI 72
Cdd:cd05388 1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFKvgpdyidPGfheAATGRPS----RNLD--------SWMMGEDGV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394816 73 NpitcldEVFHAHATE-DINY--GVMssGLRDlsvKADTVVVEGSGGwrvlmnDLrpyAEWVvqeQLPVVLVVGIKLGCV 149
Cdd:cd05388 69 R------ELFARAAGGaDVAIieGVM--GLYD---GRDTDSDEGSTA------EL---ARLL---GAPVLLVLDCKGMAR 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742394816 150 SHALLTAQSIIND-GLPLLGWVANRINPGlAHYAETIAALQQRIPAPLLGeipYLPRAEQREL 211
Cdd:cd05388 126 SAAAIVKGYKEFDpDLNLAGVILNRVGSP-RHAELLKEAIEEYTGIPVLG---YLPRDDELTL 184
|
|
| CobB |
COG1797 |
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
2-38 |
6.17e-06 |
|
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441402 [Multi-domain] Cd Length: 459 Bit Score: 46.26 E-value: 6.17e-06
10 20 30
....*....|....*....|....*....|....*..
gi 742394816 2 LKRLFVTGTDTDVGKTVVSRGLMQALAAEGRSVAGYK 38
Cdd:COG1797 3 IPRLVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFK 39
|
|
| |
