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Conserved domains on  [gi|446841972|ref|WP_000919228|]
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MULTISPECIES: dethiobiotin synthase [Escherichia]

Protein Classification

ATP-dependent dethiobiotin synthetase BioD( domain architecture ID 10000625)

ATP-dependent dethiobiotin synthetase BioD catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring

EC:  6.3.3.3
Gene Symbol:  bioD
Gene Ontology:  GO:0004141|GO:0009102|GO:0005524
PubMed:  9211290|11322938

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 3-218 3.96e-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: 236.59  E-value: 3.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEGLRNKDALVLQSVSTIELPYEAVNPIAL----- 77
Cdd:COG0132    2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFeepls 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972  78 ----SEEESsvahsCPINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHAL 153
Cdd:COG0132   82 phlaARLEG-----VPIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446841972 154 LTAQAIANDGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPYLPRAEQRELGQYIRLS 218
Cdd:COG0132  157 LTVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLE 221
 
Name Accession Description Interval E-value
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 3-218 3.96e-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: 236.59  E-value: 3.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEGLRNKDALVLQSVSTIELPYEAVNPIAL----- 77
Cdd:COG0132    2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFeepls 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972  78 ----SEEESsvahsCPINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHAL 153
Cdd:COG0132   82 phlaARLEG-----VPIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446841972 154 LTAQAIANDGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPYLPRAEQRELGQYIRLS 218
Cdd:COG0132  157 LTVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLE 221
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 3-190 4.32e-49

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: 159.27  E-value: 4.32e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGsketPEGLRNKDALVLQSVSTIELPYEAVNPIALSEEES 82
Cdd:cd03109    1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTG----CPGLEDSDAELLRKLAGLLLDLELINPYRFEAPLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972  83 ---SVAHSC-PINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQA 158
Cdd:cd03109   77 phlAAELEGrDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446841972 159 IANDGLPLIGWVANRINPGLAHYAEIIDVLGK 190
Cdd:cd03109  157 LKSRGLDVAGVVLNGIPPEPEAEADNAETLKE 188
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
 6-172 7.02e-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: 150.20  E-value: 7.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972    6 FITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEglrnkDALVLQSVSTIELPYEAVNPIALSEEES--- 82
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNS-----DALLLQNISGTALDWDEVNPYAFALPLSphi 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   83 -SVAHSCPINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQAIAN 161
Cdd:TIGR00347  76 aADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155

                         170
                  ....*....|.
gi 446841972  162 DGLPLIGWVAN 172
Cdd:TIGR00347 156 TGLTLAGVILN 166
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-211 2.26e-30

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: 112.05  E-value: 2.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972    5 FFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEGLRNKDALVLQSVSTIELPYEAVNPIALSE---EE 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLKEksdEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   82 SSVAHSCPINY-------------TLISNGLANLTDKVDHVVVEGTGGW-RSLMNDLRPLSEWVVQEQLPVLMVVGIQE- 146
Cdd:pfam01656  81 GLDLIPGNIDLekfekellgprkeERLREALEALKEDYDYVIIDGAPGLgELLRNALIAADYVIIPLEPEVILVEDAKRl 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446841972  147 GCINHALLTAQAIAndGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPY---LPRAEQREL 211
Cdd:pfam01656 161 GGVIAALVGGYALL--GLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGVIPRdeaVAEAPARGL 226
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
1-38 4.23e-06

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 46.66  E-value: 4.23e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446841972   1 MLKRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYK 38
Cdd:PRK01077   2 RMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFK 39
 
Name Accession Description Interval E-value
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 3-218 3.96e-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: 236.59  E-value: 3.96e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEGLRNKDALVLQSVSTIELPYEAVNPIAL----- 77
Cdd:COG0132    2 KGLFVTGTDTDVGKTVVTAALAAALRAAGLRVGYYKPVQTGCEETDGGLRNGDAELLRRLSGLPLSYELVNPYRFeepls 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972  78 ----SEEESsvahsCPINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHAL 153
Cdd:COG0132   82 phlaARLEG-----VPIDLDKILAALRALAARYDLVLVEGAGGLLVPLTEDLTLADLAKALGLPVILVVRARLGTINHTL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446841972 154 LTAQAIANDGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPYLPRAEQRELGQYIRLS 218
Cdd:COG0132  157 LTVEALRARGLPLAGIVLNGVPPPDLAERDNLETLERLTGAPVLGVLPYLADLDPEALAAYLDLE 221
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 3-190 4.32e-49

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: 159.27  E-value: 4.32e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGsketPEGLRNKDALVLQSVSTIELPYEAVNPIALSEEES 82
Cdd:cd03109    1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTG----CPGLEDSDAELLRKLAGLLLDLELINPYRFEAPLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972  83 ---SVAHSC-PINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQA 158
Cdd:cd03109   77 phlAAELEGrDIDLEEIVRALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGTINHTLLTLEA 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446841972 159 IANDGLPLIGWVANRINPGLAHYAEIIDVLGK 190
Cdd:cd03109  157 LKSRGLDVAGVVLNGIPPEPEAEADNAETLKE 188
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
 6-172 7.02e-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: 150.20  E-value: 7.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972    6 FITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEglrnkDALVLQSVSTIELPYEAVNPIALSEEES--- 82
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKPVQTGIEKTNS-----DALLLQNISGTALDWDEVNPYAFALPLSphi 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   83 -SVAHSCPINYTLISNGLANLTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQAIAN 161
Cdd:TIGR00347  76 aADQEGRPIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLGTINHTLLTVEHARQ 155

                         170
                  ....*....|.
gi 446841972  162 DGLPLIGWVAN 172
Cdd:TIGR00347 156 TGLTLAGVILN 166
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 5-211 2.26e-30

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: 112.05  E-value: 2.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972    5 FFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEGLRNKDALVLQSVSTIELPYEAVNPIALSE---EE 81
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPILLKEksdEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   82 SSVAHSCPINY-------------TLISNGLANLTDKVDHVVVEGTGGW-RSLMNDLRPLSEWVVQEQLPVLMVVGIQE- 146
Cdd:pfam01656  81 GLDLIPGNIDLekfekellgprkeERLREALEALKEDYDYVIIDGAPGLgELLRNALIAADYVIIPLEPEVILVEDAKRl 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446841972  147 GCINHALLTAQAIAndGLPLIGWVANRINPGLAHYAEIIDVLGKKLPAPLIGELPY---LPRAEQREL 211
Cdd:pfam01656 161 GGVIAALVGGYALL--GLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVLGVIPRdeaVAEAPARGL 226
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 3-204 1.08e-28

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: 106.96  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972    3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSketpegLRNKDALVLQSVSTIELPYEAVNPIALSEEES 82
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQTGL------VEDGDSELVKRLLGLDQSYEDPEPFRLSAPLS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   83 SVAHSCPINYTLISNGLAN-LTDKVDHVVVEGTGGWRSLMNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQAIAN 161
Cdd:pfam13500  75 PHLAARQEGVTIDLEKIIYeLPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLGTINHTLLTLEALRQ 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 446841972  162 DGLPLIGWVANRINPglahyAEIIDVLGKKLPAPLIGELPYLP 204
Cdd:pfam13500 155 RGIPVLGVILNGVPN-----PENVRTIFAFGGVPVLGAVPYLP 192
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
1-204 2.60e-20

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 89.12  E-value: 2.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   1 MLKRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVakGSKETPEGLRNKDALVLQSVSTIELPYEAVNPIALSEE 80
Cdd:COG0857    1 MMKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPI--GQSLVGGGERDEDVELIREHLGLDLPYEDASPVTLDEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972  81 ESSVAHSCPINY--TLISNgLANLTDKVDHVVVEGTGGWR-SLMNDLRPLSEwvVQEQL--PVLMVVGIQ----EGCINH 151
Cdd:COG0857   79 ETLLAEGDPDELleRIVER-YEALAAECDVVLVEGSDPTGvGSPFELSLNAR--IAKNLgaPVLLVASGGgrtpEELVDA 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446841972 152 ALLTAQAIANDGLPLIGWVANRINPglAHYAEIIDVLGKKL---PAPLIGELPYLP 204
Cdd:COG0857  156 LLLAADEFRGEGARVLGVIINRVPP--EKLEEVREALRPFLegsGIPVLGVIPENP 209
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
1-38 4.23e-06

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 46.66  E-value: 4.23e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446841972   1 MLKRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYK 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 1.95e-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: 43.74  E-value: 1.95e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYK 38
Cdd:cd05388    1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFK 36
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 3-38 3.19e-05

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: 41.65  E-value: 3.19e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446841972   3 KRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYK 38
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLID 36
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
 1-41 1.13e-04

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 42.83  E-value: 1.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446841972   1 MLKRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVA 41
Cdd:PRK05632   1 MSRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIA 41
COG4028 COG4028
Predicted P-loop ATPase/GTPase [General function prediction only];
4-77 1.35e-04

Predicted P-loop ATPase/GTPase [General function prediction only];


Pssm-ID: 443206  Cd Length: 288  Bit Score: 41.94  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446841972   4 RFFITGTDTS-VGKTVVSRALLQALASQGKTVAGYKPVA-----------KGSKEtpEG-LRNKDALVLQSVSTIELPYE 70
Cdd:COG4028    2 RLLVAGLLRVdSGKTTFSLGLLERLGEVGLDAVGFKPRAghnywydhdtlRRSLE--LGrLVGKDAYRLADASGEDRPPE 79


                 ....*..
gi 446841972  71 AVNPIAL 77
Cdd:COG4028   80 IINPVHR 86
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
 5-43 3.25e-03

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 38.16  E-value: 3.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446841972   5 FFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKG 43
Cdd:PLN02974  30 FAVWGANTAVGKTLVSAGLAAAAASRRSPVLYVKPVQTG 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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