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Conserved domains on  [gi|1519644004|gb|RPG16084|]
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MAG: hypothetical protein CBD67_000080 [Opitutales bacterium TMED207]

Protein Classification

phosphotransacetylase family protein( domain architecture ID 11436704)

phosphotransacetylase family protein containing the BioD-like N-terminal domain of phosphotransacetylase (containing a DRTGG domain), similar to Archaeoglobus fulgidus protein Af1212

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
10-372 5.75e-93

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


:

Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 292.50  E-value: 5.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVdiNGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDF 89
Cdd:COG0857     2 MKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLV--GGGERDEDVELIREHLGLDLPYEDASPVTLDEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  90 TKDYLDDSKSIYPKIVNRlcrsFDRAAYEKDYIIIEGTGHAGVGSVFDLS-NAEVAKMLNAKAIIIASGGIGRP---IDE 165
Cdd:COG0857    80 TLLAEGDPDELLERIVER----YEALAAECDVVLVEGSDPTGVGSPFELSlNARIAKNLGAPVLLVASGGGRTPeelVDA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 166 IALNQALFEKAGVDIIGVIINKVQTDKLDFIKHYCGQALEKMNLKLLGIIPENAKLSEPSLSQIFHEIKGECLNtTDNIQ 245
Cdd:COG0857   156 LLLAADEFRGEGARVLGVIINRVPPEKLEEVREALRPFLEGSGIPVLGVIPENPELAAPTVRDLAEALGAEVLN-GGELL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 246 SKKIKKVVIAAKTGLSTIDDIEDGTLIVSSGDREDIIQPCIKSNKASM--LSGIILTNAIKPNDATLADIQASE--IPFI 321
Cdd:COG0857   235 DRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTpsIAGLILTGGLPPDPAVLRLAEGLGqtLPIL 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 322 LSKDSSYSVISRMNKMNIKTQPHDVDKISIIKEILKSNIDLKEIEEAFKLS 372
Cdd:COG0857   315 SVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWLLSRLGLP 365
 
Name Accession Description Interval E-value
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
10-372 5.75e-93

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


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 292.50  E-value: 5.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVdiNGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDF 89
Cdd:COG0857     2 MKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLV--GGGERDEDVELIREHLGLDLPYEDASPVTLDEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  90 TKDYLDDSKSIYPKIVNRlcrsFDRAAYEKDYIIIEGTGHAGVGSVFDLS-NAEVAKMLNAKAIIIASGGIGRP---IDE 165
Cdd:COG0857    80 TLLAEGDPDELLERIVER----YEALAAECDVVLVEGSDPTGVGSPFELSlNARIAKNLGAPVLLVASGGGRTPeelVDA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 166 IALNQALFEKAGVDIIGVIINKVQTDKLDFIKHYCGQALEKMNLKLLGIIPENAKLSEPSLSQIFHEIKGECLNtTDNIQ 245
Cdd:COG0857   156 LLLAADEFRGEGARVLGVIINRVPPEKLEEVREALRPFLEGSGIPVLGVIPENPELAAPTVRDLAEALGAEVLN-GGELL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 246 SKKIKKVVIAAKTGLSTIDDIEDGTLIVSSGDREDIIQPCIKSNKASM--LSGIILTNAIKPNDATLADIQASE--IPFI 321
Cdd:COG0857   235 DRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTpsIAGLILTGGLPPDPAVLRLAEGLGqtLPIL 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 322 LSKDSSYSVISRMNKMNIKTQPHDVDKISIIKEILKSNIDLKEIEEAFKLS 372
Cdd:COG0857   315 SVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWLLSRLGLP 365
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
 10-367 5.25e-42

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 155.70  E-value: 5.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVD-------INGEKIDEdsflltetfdvsvpiqAMSp 82
Cdd:PRK05632    2 SRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQPPLTmsevealLASGQLDE----------------LLE- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  83 ivvdkdftkdylddsksiypKIVNRlcrsFDRAAYEKDYIIIEGTGHAGVGSV-FDLsNAEVAKMLNAKAIIIASGGiGR 161
Cdd:PRK05632   65 --------------------EIVAR----YHALAKDCDVVLVEGLDPTRKHPFeFSL-NAEIAKNLGAEVVLVSSGG-ND 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 162 PIDEIA----LNQALFEKA-GVDIIGVIINKVQ----------------TDKLDFIKHYCGQALEKMNLKLLGIIPENAK 220
Cdd:PRK05632  119 TPEELAerieLAASSFGGAkNANILGVIINKLNapvdeqgrtrpdlseiFDDSSKANVDPSKLFASSPLPLLGVVPWSPD 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 221 LSEPSLSQIFHEIKGECLNTTDnIQSKKIKKVVIAAKTGLSTIDDIEDGTLIVSSGDREDIIQPCIKSNKASM-LSGIIL 299
Cdd:PRK05632  199 LIAPRVIDIAKHLGATVLNEGD-ILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPpIAGLLL 277

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 300 TNAIKPNDATLADIQ---ASEIPFILSKDSSYSVISRMNKMNIKTQPHDVDKISIIKEILKSNIDLKEIEE 367
Cdd:PRK05632  278 TGGYEPDPRIAKLCEgafETGLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDTDELLE 348
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 11-225 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: 118.13  E-value: 1.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  11 KRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQrfvdinGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDFt 90
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQT------GLVEDGDSELVKRLLGLDQSYEDPEPFRLSAPL- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  91 kdylddSKSIYPKIVNR---LCRSFDRAAYEKDYIIIEGTGHAGVGSVFDLSNAEVAKMLNAKAIIIASGGIGrPIDEIA 167
Cdd:pfam13500  74 ------SPHLAARQEGVtidLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLG-TINHTL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1519644004 168 LNQALFEKAGVDIIGVIINKVQT-DKLDFIKHYCGqalekmnLKLLGIIPENAKLSEPS 225
Cdd:pfam13500 147 LTLEALRQRGIPVLGVILNGVPNpENVRTIFAFGG-------VPVLGAVPYLPDLTAPT 198
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 11-199 1.61e-25

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: 101.49  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  11 KRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVDingeKIDEDSFLLTETFDVSVPI---------QAMS 81
Cdd:cd03109     1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCPG----LEDSDAELLRKLAGLLLDLelinpyrfeAPLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  82 PIVVDKDFTKDYLDDsksiypKIVnrlcRSFDRAAYEKDYIIIEGTGHAGVGSVFDLSNAEVAKMLNAKAIIIASGGIGR 161
Cdd:cd03109    77 PHLAAELEGRDIDLE------EIV----RALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGT 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1519644004 162 PIDEIALNQALfEKAGVDIIGVIINKVQT------DKLDFIKHY 199
Cdd:cd03109   147 INHTLLTLEAL-KSRGLDVAGVVLNGIPPepeaeaDNAETLKEL 189
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
 14-186 2.97e-09

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: 55.44  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  14 FIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPvgqrfVDINGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDfTKDY 93
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKP-----VQTGIEKTNSDALLLQNISGTALDWDEVNPYAFALP-LSPH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  94 L---DDSKSIYPKIVNRLCRSFDRAAyekDYIIIEGTGHAGVGSVFDLSNAEVAKMLNAKAIIIASGGIGrpideiALNQ 170
Cdd:TIGR00347  75 IaadQEGRPIDLEELSKHLRTLEQKY---DFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLG------TINH 145

                         170       180
                  ....*....|....*....|.
gi 1519644004 171 ALF-----EKAGVDIIGVIIN 186
Cdd:TIGR00347 146 TLLtvehaRQTGLTLAGVILN 166
 
Name Accession Description Interval E-value
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
10-372 5.75e-93

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


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 292.50  E-value: 5.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVdiNGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDF 89
Cdd:COG0857     2 MKSIYIASTEPGSGKTSVALGLARALQRKGLRVGYFKPIGQSLV--GGGERDEDVELIREHLGLDLPYEDASPVTLDEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  90 TKDYLDDSKSIYPKIVNRlcrsFDRAAYEKDYIIIEGTGHAGVGSVFDLS-NAEVAKMLNAKAIIIASGGIGRP---IDE 165
Cdd:COG0857    80 TLLAEGDPDELLERIVER----YEALAAECDVVLVEGSDPTGVGSPFELSlNARIAKNLGAPVLLVASGGGRTPeelVDA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 166 IALNQALFEKAGVDIIGVIINKVQTDKLDFIKHYCGQALEKMNLKLLGIIPENAKLSEPSLSQIFHEIKGECLNtTDNIQ 245
Cdd:COG0857   156 LLLAADEFRGEGARVLGVIINRVPPEKLEEVREALRPFLEGSGIPVLGVIPENPELAAPTVRDLAEALGAEVLN-GGELL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 246 SKKIKKVVIAAKTGLSTIDDIEDGTLIVSSGDREDIIQPCIKSNKASM--LSGIILTNAIKPNDATLADIQASE--IPFI 321
Cdd:COG0857   235 DRRVESVVVGAMSVPNALERLREGALVITPGDRSDILLAALLAALSGTpsIAGLILTGGLPPDPAVLRLAEGLGqtLPIL 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 322 LSKDSSYSVISRMNKMNIKTQPHDVDKISIIKEILKSNIDLKEIEEAFKLS 372
Cdd:COG0857   315 SVELDTYTTAERLERVRGRIRADDPRKIELALELFAEHVDVDWLLSRLGLP 365
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
 10-367 5.25e-42

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 155.70  E-value: 5.25e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVD-------INGEKIDEdsflltetfdvsvpiqAMSp 82
Cdd:PRK05632    2 SRSIYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFKPIAQPPLTmsevealLASGQLDE----------------LLE- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  83 ivvdkdftkdylddsksiypKIVNRlcrsFDRAAYEKDYIIIEGTGHAGVGSV-FDLsNAEVAKMLNAKAIIIASGGiGR 161
Cdd:PRK05632   65 --------------------EIVAR----YHALAKDCDVVLVEGLDPTRKHPFeFSL-NAEIAKNLGAEVVLVSSGG-ND 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 162 PIDEIA----LNQALFEKA-GVDIIGVIINKVQ----------------TDKLDFIKHYCGQALEKMNLKLLGIIPENAK 220
Cdd:PRK05632  119 TPEELAerieLAASSFGGAkNANILGVIINKLNapvdeqgrtrpdlseiFDDSSKANVDPSKLFASSPLPLLGVVPWSPD 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 221 LSEPSLSQIFHEIKGECLNTTDnIQSKKIKKVVIAAKTGLSTIDDIEDGTLIVSSGDREDIIQPCIKSNKASM-LSGIIL 299
Cdd:PRK05632  199 LIAPRVIDIAKHLGATVLNEGD-ILTRRVKSVTVCARSIPNMLEHLKPGSLVVTPGDRSDVILAALLAAMNGPpIAGLLL 277

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 300 TNAIKPNDATLADIQ---ASEIPFILSKDSSYSVISRMNKMNIKTQPHDVDKISIIKEILKSNIDLKEIEE 367
Cdd:PRK05632  278 TGGYEPDPRIAKLCEgafETGLPVLSVDTNTYQTALRLQSFNGEVPVDDHERIETVLELVASHVDTDELLE 348
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 11-225 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: 118.13  E-value: 1.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  11 KRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQrfvdinGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDFt 90
Cdd:pfam13500   1 RTLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKPVQT------GLVEDGDSELVKRLLGLDQSYEDPEPFRLSAPL- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  91 kdylddSKSIYPKIVNR---LCRSFDRAAYEKDYIIIEGTGHAGVGSVFDLSNAEVAKMLNAKAIIIASGGIGrPIDEIA 167
Cdd:pfam13500  74 ------SPHLAARQEGVtidLEKIIYELPADADPVVVEGAGGLLVPINEDLLNADIAANLGLPVILVARGGLG-TINHTL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1519644004 168 LNQALFEKAGVDIIGVIINKVQT-DKLDFIKHYCGqalekmnLKLLGIIPENAKLSEPS 225
Cdd:pfam13500 147 LTLEALRQRGIPVLGVILNGVPNpENVRTIFAFGG-------VPVLGAVPYLPDLTAPT 198
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 11-199 1.61e-25

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: 101.49  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  11 KRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPVGQRFVDingeKIDEDSFLLTETFDVSVPI---------QAMS 81
Cdd:cd03109     1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKPVQTGCPG----LEDSDAELLRKLAGLLLDLelinpyrfeAPLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  82 PIVVDKDFTKDYLDDsksiypKIVnrlcRSFDRAAYEKDYIIIEGTGHAGVGSVFDLSNAEVAKMLNAKAIIIASGGIGR 161
Cdd:cd03109    77 PHLAAELEGRDIDLE------EIV----RALEELAKSYDVVLVEGAGGLLVPLTEGYLNADLARALGLPVILVARGGLGT 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1519644004 162 PIDEIALNQALfEKAGVDIIGVIINKVQT------DKLDFIKHY 199
Cdd:cd03109   147 INHTLLTLEAL-KSRGLDVAGVVLNGIPPepeaeaDNAETLKEL 189
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 10-231 5.41e-18

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: 81.74  E-value: 5.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATrmnD---GKTTTSLGLYSALSDGKKKIGYIKPV--GqrFVDINGEKIDEDSFLLTETFDVSVPI------- 77
Cdd:COG0132     1 MKGLFVTGT---DtdvGKTVVTAALAAALRAAGLRVGYYKPVqtG--CEETDGGLRNGDAELLRRLSGLPLSYelvnpyr 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  78 --QAMSP--------IVVDkdftkdylddsksiypkiVNRLCRSFDRAAYEKDYIIIEgtghaGVGSVF-----DLSNAE 142
Cdd:COG0132    76 feEPLSPhlaarlegVPID------------------LDKILAALRALAARYDLVLVE-----GAGGLLvplteDLTLAD 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 143 VAKMLNAKAIIIASGGIGrpideiALNQAL-----FEKAGVDIIGVIINKVQTDK------LDFIKHYCGqalekmnLKL 211
Cdd:COG0132   133 LAKALGLPVILVVRARLG------TINHTLltveaLRARGLPLAGIVLNGVPPPDlaerdnLETLERLTG-------APV 199

                         250       260
                  ....*....|....*....|
gi 1519644004 212 LGIIPENAKLSEPSLSQIFH 231
Cdd:COG0132   200 LGVLPYLADLDPEALAAYLD 219
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 13-223 1.62e-16

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: 77.77  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  13 IFIAATRMNDGKTTTSLGLYSALSDGKKKI------------------GYIKPVGQRFVDINGEKIDEDSFLLTETFDVS 74
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVllidldpqsnnssvegleGDIAPALQALAEGLKGRVNLDPILLKEKSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  75 VPIQAMSPIVVDKdFTKDYLDDSKSiypkivNRLCRSFDRAAYEKDYIIIEGTGHAGVGSVFDL-SNAEVAKMLNAKAII 153
Cdd:pfam01656  81 GLDLIPGNIDLEK-FEKELLGPRKE------ERLREALEALKEDYDYVIIDGAPGLGELLRNALiAADYVIIPLEPEVIL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 154 IAS-GGIGRPIDEIALNQALFekaGVDIIGVIINKVQTDKLdFIKHYCGQALEKMNLKLLGIIPENAKLSE 223
Cdd:pfam01656 154 VEDaKRLGGVIAALVGGYALL---GLKIIGVVLNKVDGDNH-GKLLKEALEELLRGLPVLGVIPRDEAVAE 220
DRTGG pfam07085
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ...
 228-337 8.60e-15

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).


Pssm-ID: 429285 [Multi-domain]  Cd Length: 105  Bit Score: 69.45  E-value: 8.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 228 QIFHEIKGECLNTtDNIQSKKIKKVVIAAKTGLSTIDDIEDGTLIVSSGDREDIIQPCIKSNkasmLSGIILTNAIKPND 307
Cdd:pfam07085   1 DIARILGAEVLNG-GDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITPGDREDIQLAALEAG----IAGLILTGGFEPSP 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1519644004 308 ATLADIQASEIPFILSKDSSYSVISRMNKM 337
Cdd:pfam07085  76 EVLKLAEELGLPVLSTPYDTFTTASRINRA 105
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
10-225 3.97e-13

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 70.16  E-value: 3.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSD-GKK----KIG--YIKP-----VGQRFVdINgekidEDSFLLTEtfdvsvpi 77
Cdd:PRK01077    3 MPALVIAAPASGSGKTTVTLGLMRALRRrGLRvqpfKVGpdYIDPayhtaATGRPS-RN-----LDSWMMGE-------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  78 qamspivvdkdftkdylddsksiypkivNRLCRSFDRAAYEKDYIIIEGT-----GHAGVGSVFdlSNAEVAKMLNAKAI 152
Cdd:PRK01077   69 ----------------------------ELVRALFARAAQGADIAVIEGVmglfdGAGSDPDEG--STADIAKLLGAPVV 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519644004 153 -IIASGGIGRPIDEIALNQALFEKaGVDIIGVIINKVQTDkldfiKHY--CGQALEKMNLKLLGIIPENAKLSEPS 225
Cdd:PRK01077  119 lVVDASGMAQSAAALVLGFATFDP-DVRIAGVILNRVGSE-----RHYqlLREALERCGIPVLGALPRDAALALPE 188
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
 10-225 1.07e-12

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: 68.98  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  10 TKRIFIAATRMNDGKTTTSLGLYSALSD-GKK----KIG--YIKP-----VGQRFVdINgekidEDSFLLTEtfdvsvpi 77
Cdd:COG1797     3 IPRLVIAAPHSGSGKTTVTLGLLAALRRrGLKvqpfKVGpdYIDPgyhtlATGRPS-RN-----LDPFLMGE-------- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  78 qamspivvdkdftkdylddsksiypkivNRLCRSFDRAAYEKDYIIIEGT-----GHAGVGSVFdlSNAEVAKMLNAKAI 152
Cdd:COG1797    69 ----------------------------EGVRELFARGSAGADIAVIEGVmglydGLDGDSGSG--STAHLAKLLGAPVV 118

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519644004 153 -IIASGGIGRPIDEIALNQALFEKaGVDIIGVIINKVQTDkldfiKHY--CGQALEKM-NLKLLGIIPENAKLSEPS 225
Cdd:COG1797   119 lVVDASGMSRSAAALVLGFRAFDP-DVRIAGVILNRVGSE-----RHEelLREAIEHYtGIPVLGALPRDEELELPS 189
CobB_N cd05388
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ...
 11-225 1.10e-12

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: 66.09  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  11 KRIFIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKpVGQRFVD------ING-EKIDEDSFLLTEtfdvsvpiqamspi 83
Cdd:cd05388     1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFK-VGPDYIDpgfheaATGrPSRNLDSWMMGE-------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  84 vvdkdftkdylDDSKSIypkivnrlcrsFDRAAYEKDYIIIEGT-----GHAGVGSvfDLSNAEVAKMLNAKAII-IASG 157
Cdd:cd05388    66 -----------DGVREL-----------FARAAGGADVAIIEGVmglydGRDTDSD--EGSTAELARLLGAPVLLvLDCK 121

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 158 GIGRPIDEIALNQALFEKaGVDIIGVIINKVQTDkldfiKHY--CGQALEKM-NLKLLGIIPENAKLSEPS 225
Cdd:cd05388   122 GMARSAAAIVKGYKEFDP-DLNLAGVILNRVGSP-----RHAelLKEAIEEYtGIPVLGYLPRDDELTLPE 186
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
 14-186 2.97e-09

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: 55.44  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  14 FIAATRMNDGKTTTSLGLYSALSDGKKKIGYIKPvgqrfVDINGEKIDEDSFLLTETFDVSVPIQAMSPIVVDKDfTKDY 93
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKKAGYSVGYYKP-----VQTGIEKTNSDALLLQNISGTALDWDEVNPYAFALP-LSPH 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  94 L---DDSKSIYPKIVNRLCRSFDRAAyekDYIIIEGTGHAGVGSVFDLSNAEVAKMLNAKAIIIASGGIGrpideiALNQ 170
Cdd:TIGR00347  75 IaadQEGRPIDLEELSKHLRTLEQKY---DFVLVEGAGGLCVPITEEYTTADLIKLLQLPVILVVRVKLG------TINH 145

                         170       180
                  ....*....|....*....|.
gi 1519644004 171 ALF-----EKAGVDIIGVIIN 186
Cdd:TIGR00347 146 TLLtvehaRQTGLTLAGVILN 166
PRK06278 PRK06278
cobyrinic acid a,c-diamide synthase; Validated
 120-214 8.16e-05

cobyrinic acid a,c-diamide synthase; Validated


Pssm-ID: 180505 [Multi-domain]  Cd Length: 476  Bit Score: 44.26  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 120 DYIIIEGTGHAGVGSVFDL---SNAEVAKMLNAKAIIIAS---GGIGRPIDEIALNQALFEKAGVDIIGVIINKVQTDKL 193
Cdd:PRK06278  319 DYYIIEGVMGAFTGALNKKnpySGAEIAKALGFPVYIVSScskSGIEGAFVESMAYYSLLKKMGVKVEGIILNKVYNMEI 398

                          90       100
                  ....*....|....*....|..
gi 1519644004 194 -DFIKHYcgqaLEKMNLKLLGI 214
Cdd:PRK06278  399 fEKVKKI----AENSNINLIGV 416
CobQ_N cd05389
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ...
 91-216 3.57e-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: 41.42  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004  91 KDYLDDSKSIYPKIvnrlCRSFDRAAYEKDYIIIEGTG-------HAGvgsvfDLSNAEVAKMLNAKAIIIAS---GGIG 160
Cdd:cd05389   100 REYYEYKGRLAPAV----LESLDRLAAEYDLVVIEGAGspaeinlRDR-----DIVNMGMARAADAPVILVADidrGGVF 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519644004 161 RPI-DEIALnqaLFEKAGVDIIGVIINKVQTDKLDF---IKhycgqALEKM-NLKLLGIIP 216
Cdd:cd05389   171 ASLyGTLAL---LPEEERKLVKGVVINKFRGDRSLLepgIE-----MLEERtGVPVLGVLP 223
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
210-335 4.70e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 42.13  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 210 KLLGII--------------PENAKLSEPSLSQIFHEIKGECLNTTDNiQSKKIKKVVIAAKTGLSTIDDIEDGTLIVSs 275
Cdd:PRK14869  110 KLLGLVslsdlaraymdildPEILSKSPTSLENIIRTLDGEVLVGAEE-DKVEEGKVVVAAMAPESLLERIEEGDIVIV- 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519644004 276 GDREDIIQPCIKSnKASMLsgiILTNAIKPNDATLADIQASEIPFILSKDSSYSVISRMN 335
Cdd:PRK14869  188 GDREDIQLAAIEA-GVRLL---IITGGAPVSEDVLELAKENGVTVISTPYDTFTTARLIN 243
 
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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