|
Name |
Accession |
Description |
Interval |
E-value |
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
4-223 |
5.67e-101 |
|
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: 292.06 E-value: 5.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEEYPEGLRNSDALHLQEAATQNVAYEDVNPYALLLPSSP 83
Cdd:COG0132 3 GLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFEEPLSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 84 HIAAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAI 163
Cdd:COG0132 83 HLAARLEGVPIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTLLTVEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 164 RADGLNLVGWVANRINPGTEHYADIIAMLEDKLGAPKLGEIPYVPRAKSKNIGKYIDVQP 223
Cdd:COG0132 163 RARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLES 222
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
4-194 |
3.10e-69 |
|
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: 210.12 E-value: 3.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEeypeGLRNSDALHLQEAATQNVAYEDVNPYALLLPSSP 83
Cdd:cd03109 2 TLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCP----GLEDSDAELLRKLAGLLLDLELINPYRFEAPLSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 84 HIAAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAI 163
Cdd:cd03109 78 HLAAELEGRDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEAL 157
|
170 180 190
....*....|....*....|....*....|.
gi 2165457426 164 RADGLNLVGWVANRINPGTEHYADIIAMLED 194
Cdd:cd03109 158 KSRGLDVAGVVLNGIPPEPEAEADNAETLKE 188
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
6-176 |
2.88e-57 |
|
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: 179.09 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 6 FIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEEYpeglrNSDALHLQEAATQNVAYEDVNPYALLLPSSPHI 85
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKT-----NSDALLLQNISGTALDWDEVNPYAFALPLSPHI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 86 AAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAIRA 165
Cdd:TIGR00347 76 AADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155
|
170
....*....|.
gi 2165457426 166 DGLNLVGWVAN 176
Cdd:TIGR00347 156 TGLTLAGVILN 166
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
3-208 |
1.22e-38 |
|
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: 132.38 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 3 DALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGceeypeGLRNSDALHLQEAATQNVAYEDVNPYALLLPSS 82
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTG------LVEDGDSELVKRLLGLDQSYEDPEPFRLSAPLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 83 PHIAAKHDGVVVDEAVLSAKLEqhkQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEA 162
Cdd:pfam13500 75 PHLAARQEGVTIDLEKIIYELP---ADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2165457426 163 IRADGLNLVGWVANRINPgtehyADIIAMLEDKLGAPKLGEIPYVP 208
Cdd:pfam13500 152 LRQRGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
4-209 |
2.42e-06 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 47.43 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYK-------PvaagceeypeglrnsdALHlqEAATQNVAyedvnpYA 76
Cdd:PRK01077 5 ALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFKvgpdyidP----------------AYH--TAATGRPS------RN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 77 LllpssphiaakhDGVVVDEAVLSAKLEQHKQNSDIVLVEGA-----GgwrVPVSDDEYLSSWVKKE-QLPVVLTVGIK- 149
Cdd:PRK01077 61 L------------DSWMMGEELVRALFARAAQGADIAVIEGVmglfdG---AGSDPDEGSTADIAKLlGAPVVLVVDASg 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2165457426 150 ---------LGCLSHalltaeairADGLNLVGWVANRInpGTEHYADII--AMleDKLGAPKLGeipYVPR 209
Cdd:PRK01077 126 maqsaaalvLGFATF---------DPDVRIAGVILNRV--GSERHYQLLreAL--ERCGIPVLG---ALPR 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BioD |
COG0132 |
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
4-223 |
5.67e-101 |
|
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: 292.06 E-value: 5.67e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEEYPEGLRNSDALHLQEAATQNVAYEDVNPYALLLPSSP 83
Cdd:COG0132 3 GLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFEEPLSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 84 HIAAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAI 163
Cdd:COG0132 83 HLAARLEGVPIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTLLTVEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 164 RADGLNLVGWVANRINPGTEHYADIIAMLEDKLGAPKLGEIPYVPRAKSKNIGKYIDVQP 223
Cdd:COG0132 163 RARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLES 222
|
|
| DTBS |
cd03109 |
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
4-194 |
3.10e-69 |
|
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: 210.12 E-value: 3.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEeypeGLRNSDALHLQEAATQNVAYEDVNPYALLLPSSP 83
Cdd:cd03109 2 TLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCP----GLEDSDAELLRKLAGLLLDLELINPYRFEAPLSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 84 HIAAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAI 163
Cdd:cd03109 78 HLAAELEGRDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEAL 157
|
170 180 190
....*....|....*....|....*....|.
gi 2165457426 164 RADGLNLVGWVANRINPGTEHYADIIAMLED 194
Cdd:cd03109 158 KSRGLDVAGVVLNGIPPEPEAEADNAETLKE 188
|
|
| bioD |
TIGR00347 |
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ... |
6-176 |
2.88e-57 |
|
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: 179.09 E-value: 2.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 6 FIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEEYpeglrNSDALHLQEAATQNVAYEDVNPYALLLPSSPHI 85
Cdd:TIGR00347 1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKT-----NSDALLLQNISGTALDWDEVNPYAFALPLSPHI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 86 AAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAIRA 165
Cdd:TIGR00347 76 AADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155
|
170
....*....|.
gi 2165457426 166 DGLNLVGWVAN 176
Cdd:TIGR00347 156 TGLTLAGVILN 166
|
|
| AAA_26 |
pfam13500 |
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
3-208 |
1.22e-38 |
|
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: 132.38 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 3 DALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGceeypeGLRNSDALHLQEAATQNVAYEDVNPYALLLPSS 82
Cdd:pfam13500 1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTG------LVEDGDSELVKRLLGLDQSYEDPEPFRLSAPLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 83 PHIAAKHDGVVVDEAVLSAKLEqhkQNSDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEA 162
Cdd:pfam13500 75 PHLAARQEGVTIDLEKIIYELP---ADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2165457426 163 IRADGLNLVGWVANRINPgtehyADIIAMLEDKLGAPKLGEIPYVP 208
Cdd:pfam13500 152 LRQRGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
|
|
| CbiA |
pfam01656 |
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
5-215 |
1.41e-24 |
|
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: 97.03 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 5 LFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGCEEYPEGLRNSDALHLQEAATQNVAYEDVNPYAL------- 77
Cdd:pfam01656 1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLkeksdeg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 78 ---LLPSSPHI--AAKHDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWRVPVSDDEYLS-SWVKKEQLPVVLTVGIK-L 150
Cdd:pfam01656 81 gldLIPGNIDLekFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAAdYVIIPLEPEVILVEDAKrL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2165457426 151 GCLSHALLTAEAIRadGLNLVGWVANRINPGTEHYADIIAMLEDKLGAPKLGEIPY---VPRAKSKNI 215
Cdd:pfam01656 161 GGVIAALVGGYALL--GLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGVIPRdeaVAEAPARGL 226
|
|
| CobB |
COG1797 |
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
4-212 |
2.45e-07 |
|
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: 50.49 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYK--PvaagceEYpeglrnSDALHLQeAATQNVAYedvNpyaLllps 81
Cdd:COG1797 5 RLVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFKvgP------DY------IDPGYHT-LATGRPSR---N---L---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 82 sphiaakhDGVVVDEAVLSAKLEQHKQNSDIVLVEG-------AGGwrvpvsDDEYLSSW--VKKEQLPVVLTVGIK--- 149
Cdd:COG1797 62 --------DPFLMGEEGVRELFARGSAGADIAVIEGvmglydgLDG------DSGSGSTAhlAKLLGAPVVLVVDASgms 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2165457426 150 -------LGCLSHalltaeairaD-GLNLVGWVANRINPGTeHYADIIAMLEDKLGAPKLGeipYVPRAKS 212
Cdd:COG1797 128 rsaaalvLGFRAF----------DpDVRIAGVILNRVGSER-HEELLREAIEHYTGIPVLG---ALPRDEE 184
|
|
| CobB_N |
cd05388 |
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
4-205 |
1.32e-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: 47.21 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYKpvaAGceeyPEGLrnsDALHLqEAATQNVAYedvnpyALllpssp 83
Cdd:cd05388 2 RIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFK---VG----PDYI---DPGFH-EAATGRPSR------NL------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 84 hiaakhDGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGW---RVPVSDDE---YLSSWVKkeqLPVVLTVGIKLGCLSHAL 157
Cdd:cd05388 59 ------DSWMMGEDGVRELFARAAGGADVAIIEGVMGLydgRDTDSDEGstaELARLLG---APVLLVLDCKGMARSAAA 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2165457426 158 LTAEAIRAD-GLNLVGWVANRINPGtEHYADIIAMLEDKLGAPKLGEIP 205
Cdd:cd05388 130 IVKGYKEFDpDLNLAGVILNRVGSP-RHAELLKEAIEEYTGIPVLGYLP 177
|
|
| PRK01077 |
PRK01077 |
cobyrinate a,c-diamide synthase; |
4-209 |
2.42e-06 |
|
cobyrinate a,c-diamide synthase;
Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 47.43 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 4 ALFIAGTDTEVGKTVVSKAILQALAAQDLSTIGYK-------PvaagceeypeglrnsdALHlqEAATQNVAyedvnpYA 76
Cdd:PRK01077 5 ALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFKvgpdyidP----------------AYH--TAATGRPS------RN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 77 LllpssphiaakhDGVVVDEAVLSAKLEQHKQNSDIVLVEGA-----GgwrVPVSDDEYLSSWVKKE-QLPVVLTVGIK- 149
Cdd:PRK01077 61 L------------DSWMMGEELVRALFARAAQGADIAVIEGVmglfdG---AGSDPDEGSTADIAKLlGAPVVLVVDASg 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2165457426 150 ---------LGCLSHalltaeairADGLNLVGWVANRInpGTEHYADII--AMleDKLGAPKLGeipYVPR 209
Cdd:PRK01077 126 maqsaaalvLGFATF---------DPDVRIAGVILNRV--GSERHYQLLreAL--ERCGIPVLG---ALPR 180
|
|
| cobB |
TIGR00379 |
cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, ... |
7-205 |
8.05e-06 |
|
cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, the cobB (cbiA in Salmonella) protein of cobalamin biosynthesis. It is responsible for the amidation of carboxylic groups at positions A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP hydrogenolyzed for each amidation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273044 [Multi-domain] Cd Length: 449 Bit Score: 45.95 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 7 IAGTDTEVGKTVVSKAILQALAAQDLSTIGYKpvaagceeypeglrnsdalhlqeaatqnvayedVNPyALLLPSSPHIA 86
Cdd:TIGR00379 4 IAGTSSGVGKTTISTGIMKALSRRKLRVQPFK---------------------------------VGP-DYIDPMFHTQA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 87 AKH-----DGVVVDEAVLSAKLEQHKQNSDIVLVEGAGGWR---VPVSDDEYLSSWVKKEQLPVVLTVGIK-LGCLSHAL 157
Cdd:TIGR00379 50 TGRpsrnlDSFFMSEAQIQECFHRHSKGTDYSIIEGVRGLYdgiSAITDYGSTASVAKALDAPIVLVMNCQrLSRSAAAI 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2165457426 158 LTAEAIRADGLNLVGWVANRINpGTEHYADIIAMLEDKLGAPKLGEIP 205
Cdd:TIGR00379 130 VLGYRSFDPGVKLKGVILNRVG-SERHLEKLKIAVEPLRGIPILGVIP 176
|
|
| PLN02974 |
PLN02974 |
adenosylmethionine-8-amino-7-oxononanoate transaminase |
9-126 |
7.55e-04 |
|
adenosylmethionine-8-amino-7-oxononanoate transaminase
Pssm-ID: 215526 [Multi-domain] Cd Length: 817 Bit Score: 40.08 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 9 GTDTEVGKTVVSKAILQALAAQDLSTIGYKPVAAGceeYPEGlrnSDA-LHLQEAATQNVAYEDVNPYALLLPSSPHIAA 87
Cdd:PLN02974 34 GANTAVGKTLVSAGLAAAAASRRSPVLYVKPVQTG---FPDD---SDArFVFRKADSLSRRSESLFASNRTLFLSPPAAK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2165457426 88 KHDGVVVDEAVLSAKL--EQHKQNSDIVLVEGAGGWRVPVS 126
Cdd:PLN02974 108 SALGGVSSMGAHAAVNagAEAGVTSSALWCHTLFAWRRAVS 148
|
|
| COG4028 |
COG4028 |
Predicted P-loop ATPase/GTPase [General function prediction only]; |
5-83 |
8.16e-04 |
|
Predicted P-loop ATPase/GTPase [General function prediction only];
Pssm-ID: 443206 Cd Length: 288 Bit Score: 39.63 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 5 LFIAGTDT-EVGKTVVSKAILQALAAQDLSTIGYKPVAAgcEEY---PEGLRNS---------DALHLQEAATQNVAYED 71
Cdd:COG4028 3 LLVAGLLRvDSGKTTFSLGLLERLGEVGLDAVGFKPRAG--HNYwydHDTLRRSlelgrlvgkDAYRLADASGEDRPPEI 80
|
90
....*....|...
gi 2165457426 72 VNPYALLL-PSSP 83
Cdd:COG4028 81 INPVHRLWrPPDP 93
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
5-177 |
2.94e-03 |
|
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: 36.25 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 5 LFIAGTDTEVGKTVVSKAILQALAAQdlstiGYKPVAAGCEeypeglrnsdalhlqeaatqnvayedvnpyalllpssph 84
Cdd:cd01983 3 IAVTGGKGGVGKTTLAAALAVALAAK-----GYKVLLIDLD--------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2165457426 85 iaakhdgvvvdeavlsakleqhkqnsDIVLVEGAGGWRVPVSDDEYLSSWVKKEQLPVVLTVGIKLGCLSHALLTAEAIR 164
Cdd:cd01983 39 --------------------------DYVLIDGGGGLETGLLLGTIVALLALKKADEVIVVVDPELGSLLEAVKLLLALL 92
|
170
....*....|....*
gi 2165457426 165 AD--GLNLVGWVANR 177
Cdd:cd01983 93 LLgiGIRPDGIVLNK 107
|
|
| |
