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Conserved domains on  [gi|1121717800|ref|WP_073924093|]
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MULTISPECIES: menaquinone biosynthetic enzyme MqnA/MqnD family protein [Streptomycetaceae]

Protein Classification

menaquinone biosynthetic enzyme MqnA/MqnD family protein( domain architecture ID 10003665)

menaquinone biosynthetic enzyme MqnA/MqnD family protein similar to Campylobacter jejuni MqnA which catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
17-290 5.62e-119

Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


:

Pssm-ID: 441036  Cd Length: 268  Bit Score: 342.20  E-value: 5.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  17 RPRVGHIQFLNCLPLYWGLARTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMS 96
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARHADDYLILPDLSISADGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  97 CVIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEREGVRPEYFSSPPDLDAMLAHADAAVLIGDPALRASLEQapsQG 176
Cdd:COG1427    81 VLLFSRVPLEELDGKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADAALLIGDRALRAAARG---RF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 LAVHDLGEMWREWTGLPFVFAVWAARRDFLESRPeaVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFtEA 256
Cdd:COG1427   158 PYVYDLGEEWKELTGLPFVFAVWAVRRDAAEANP--VAELHEALLEAKERGLAHLDEIAEEAARRLGLPPELLEDYL-RN 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1121717800 257 LDYSLGERQLAGIAEFARRVSHDSGFAPDVAVRL 290
Cdd:COG1427   235 LRYDLGEEERKGLRLFYEYAAELGLLPEVPELRF 268
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
17-290 5.62e-119

Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441036  Cd Length: 268  Bit Score: 342.20  E-value: 5.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  17 RPRVGHIQFLNCLPLYWGLARTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMS 96
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARHADDYLILPDLSISADGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  97 CVIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEREGVRPEYFSSPPDLDAMLAHADAAVLIGDPALRASLEQapsQG 176
Cdd:COG1427    81 VLLFSRVPLEELDGKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADAALLIGDRALRAAARG---RF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 LAVHDLGEMWREWTGLPFVFAVWAARRDFLESRPeaVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFtEA 256
Cdd:COG1427   158 PYVYDLGEEWKELTGLPFVFAVWAVRRDAAEANP--VAELHEALLEAKERGLAHLDEIAEEAARRLGLPPELLEDYL-RN 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1121717800 257 LDYSLGERQLAGIAEFARRVSHDSGFAPDVAVRL 290
Cdd:COG1427   235 LRYDLGEEERKGLRLFYEYAAELGLLPEVPELRF 268
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
17-275 1.21e-111

The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein fold; This group includes the SCO4506 protein from Streptomyces coelicolor and related hypothetical proteins. SCO4506 is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. SCO4506 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270352  Cd Length: 256  Bit Score: 323.35  E-value: 1.21e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  17 RPRVGHIQFLNCLPLYWGLARTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMS 96
Cdd:cd13634     1 MLRVGRISYLNTLPLFYGLEKGKVPPGFELVLGVPSELNRMLLEGELDVGLVSSIEYARNADDYLILPDLSISSDGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  97 CVIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEREGVRPEYFSSPPDLDAMLAHADAAVLIGDPALRASLEQapsQG 176
Cdd:cd13634    81 VLLFSKVPLEELEGKRVALTTESATSVALLKILLEEFYGLEPEYVPAPPDLDEMLADADAALLIGDDALRARASG---RG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 LAVHDLGEMWREWTGLPFVFAVWAARRDFLEsRPEAVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFTEa 256
Cdd:cd13634   158 PYVYDLGEEWKELTGLPFVFAVWAVRRDAAE-RPEELAELVQALLESKRYGLANLEEIIAEAAERLGLSEEFLRDYFTN- 235
                         250
                  ....*....|....*....
gi 1121717800 257 LDYSLGERQLAGIAEFARR 275
Cdd:cd13634   236 LRYDLGEEELEGLELFYRY 254
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
18-275 2.78e-82

Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone biosynthesis. One which catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to futalosine. These enzymes comprise two domains with alpha/beta structures, a large domain and a small domain. A pocket between the two domains may form the active site, a conserved histidine located within this pocket could be the catalytic base.


Pssm-ID: 426881  Cd Length: 252  Bit Score: 248.62  E-value: 2.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  18 PRVGHIQFLNCLPLYWGLArTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMSC 97
Cdd:pfam02621   1 LRVGHSPYPNDLPLFYALV-HDEGLDFEIVLGDPETLNRMLLEGELDVSAISSAAYARNADDYVLLPDLSGSALGRVYSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  98 VIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEReGVRPEYFSSPPDL-DAMLAHADAAVLIGDPALRASLEQAPsqg 176
Cdd:pfam02621  80 LLVSRVPELDGDGKRVALPGESTTSVLLLRLLLPER-YGKPRYVPMPDEImAAVLEGEDAGLLIGDSALTYAERGLK--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 lAVHDLGEMWREWTGLPFVFAVWAARRDFLEsrpEAVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFTEa 256
Cdd:pfam02621 156 -KVLDLGEWWKELTGLPMPFGLWVVRRDLAL---ETAKELEEALRASKEYALAHPDEIAEYAAEHAQEMEEFLRLYVNE- 230
                         250
                  ....*....|....*....
gi 1121717800 257 LDYSLGERQLAGIAEFARR 275
Cdd:pfam02621 231 LSYDLGEEGRAGLEEFYER 249
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
58-240 2.51e-07

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 50.82  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  58 LVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMSCVIVSKVP---LADLDGRKVALgsTSRTSVRLAQLLLEERE 134
Cdd:TIGR01728  46 LGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSDNKATAIVVIKGSPirtVADLKGKRIAV--PKGGSGHDLLLRALLKA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 135 GVRPE----YFSSPPDLDAMLAHADA-AVLIGDPALRASLEQAPSQGLAvhDLGEMW-REWTGLpFVfavwaARRDFLES 208
Cdd:TIGR01728 124 GLSGDdvtiLYLGPSDARAAFAAGQVdAWAIWEPWGSALVEEGGARVLA--NGEGIGlPGQPGF-LV-----VRREFAEA 195
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1121717800 209 RPEAVAAVHRAFLESRDLSLAEAGQVAEQAAR 240
Cdd:TIGR01728 196 HPEQVQRVLKVLVKARKWAEENPEESAKILAK 227
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
17-290 5.62e-119

Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441036  Cd Length: 268  Bit Score: 342.20  E-value: 5.62e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  17 RPRVGHIQFLNCLPLYWGLARTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMS 96
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGGLLPDVELVKGVPSQLNRMLAEGELDVGLISSIEYARHADDYLILPDLSISADGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  97 CVIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEREGVRPEYFSSPPDLDAMLAHADAAVLIGDPALRASLEQapsQG 176
Cdd:COG1427    81 VLLFSRVPLEELDGKTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADAALLIGDRALRAAARG---RF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 LAVHDLGEMWREWTGLPFVFAVWAARRDFLESRPeaVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFtEA 256
Cdd:COG1427   158 PYVYDLGEEWKELTGLPFVFAVWAVRRDAAEANP--VAELHEALLEAKERGLAHLDEIAEEAARRLGLPPELLEDYL-RN 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1121717800 257 LDYSLGERQLAGIAEFARRVSHDSGFAPDVAVRL 290
Cdd:COG1427   235 LRYDLGEEERKGLRLFYEYAAELGLLPEVPELRF 268
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
17-275 1.21e-111

The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein fold; This group includes the SCO4506 protein from Streptomyces coelicolor and related hypothetical proteins. SCO4506 is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. SCO4506 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270352  Cd Length: 256  Bit Score: 323.35  E-value: 1.21e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  17 RPRVGHIQFLNCLPLYWGLARTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMS 96
Cdd:cd13634     1 MLRVGRISYLNTLPLFYGLEKGKVPPGFELVLGVPSELNRMLLEGELDVGLVSSIEYARNADDYLILPDLSISSDGPVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  97 CVIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEREGVRPEYFSSPPDLDAMLAHADAAVLIGDPALRASLEQapsQG 176
Cdd:cd13634    81 VLLFSKVPLEELEGKRVALTTESATSVALLKILLEEFYGLEPEYVPAPPDLDEMLADADAALLIGDDALRARASG---RG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 LAVHDLGEMWREWTGLPFVFAVWAARRDFLEsRPEAVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFTEa 256
Cdd:cd13634   158 PYVYDLGEEWKELTGLPFVFAVWAVRRDAAE-RPEELAELVQALLESKRYGLANLEEIIAEAAERLGLSEEFLRDYFTN- 235
                         250
                  ....*....|....*....
gi 1121717800 257 LDYSLGERQLAGIAEFARR 275
Cdd:cd13634   236 LRYDLGEEELEGLELFYRY 254
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
18-275 2.78e-82

Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone biosynthesis. One which catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate, and one which may be involved in the conversion of chorismate to futalosine. These enzymes comprise two domains with alpha/beta structures, a large domain and a small domain. A pocket between the two domains may form the active site, a conserved histidine located within this pocket could be the catalytic base.


Pssm-ID: 426881  Cd Length: 252  Bit Score: 248.62  E-value: 2.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  18 PRVGHIQFLNCLPLYWGLArTGNLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMSC 97
Cdd:pfam02621   1 LRVGHSPYPNDLPLFYALV-HDEGLDFEIVLGDPETLNRMLLEGELDVSAISSAAYARNADDYVLLPDLSGSALGRVYSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  98 VIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEEReGVRPEYFSSPPDL-DAMLAHADAAVLIGDPALRASLEQAPsqg 176
Cdd:pfam02621  80 LLVSRVPELDGDGKRVALPGESTTSVLLLRLLLPER-YGKPRYVPMPDEImAAVLEGEDAGLLIGDSALTYAERGLK--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 177 lAVHDLGEMWREWTGLPFVFAVWAARRDFLEsrpEAVAAVHRAFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFTEa 256
Cdd:pfam02621 156 -KVLDLGEWWKELTGLPMPFGLWVVRRDLAL---ETAKELEEALRASKEYALAHPDEIAEYAAEHAQEMEEFLRLYVNE- 230
                         250
                  ....*....|....*....
gi 1121717800 257 LDYSLGERQLAGIAEFARR 275
Cdd:pfam02621 231 LSYDLGEEGRAGLEEFYER 249
PBP2_MqnD_like cd13534
Menaquinone biosynthetic enzyme and related hypothetical proteins; the type 2 ...
17-276 4.73e-62

Menaquinone biosynthetic enzyme and related hypothetical proteins; the type 2 periplasmic-binding protein fold; This family represents MqnD, an enzyme within the alternative menaquinone biosynthetic pathway, and related conserved hypothetical proteins. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. The members include Ttha1568, MqnD from Thermus thermophiles HB8, and the conserved hypothetical proteins SCO4506 from Streptomyces coelicolor, Af1704 from Archaeoglobus DSM 4304, Dr0370 from Deinococcus radiodurans, and Ca3427 from candida albicans. They all have significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270252 [Multi-domain]  Cd Length: 261  Bit Score: 197.26  E-value: 4.73e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  17 RPRVGHIQFLNCLPLYWGLARTG---NLLDLDLTKDTPEKLSDLLVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGp 93
Cdd:cd13534     1 TIRVGHSPDADDLFLFYALKHGWvkeTDLIFENVKEDVETLNELALKNELDVSAISFAAYPKIADDYVILPTGAVFGDG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  94 vMSCVIVSKVPLADLDGRKVALGSTSRTSVRLAQLLLEerEGVRPEYFSSPPDLDAML-AHADAAVLIGDpalrASLEQA 172
Cdd:cd13534    80 -YGPVLVAKSPLDDKQGKRVAVSGRNTTAYLLLKLLAP--QYFRPIVVRFDDIEDAVLeGEVDAGVLIHE----SILMTY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 173 PSQGLAVH-DLGEMWREWTGLPFVFAVWAARRDFLEsrpEAVAAVHRAFLESRDLSLA---EAGQVAEQAARWEEFDAAL 248
Cdd:cd13534   153 PRYGLKVVrDLWDLWKESTNLPLPLGVVAIRRDLGE---DLIRAFKEAVLLSKAYALAhpdEAIEYMLQEAREIRLDEEV 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1121717800 249 LERYF-TEALDYS--LGERQLAGIAEFARRV 276
Cdd:cd13534   230 LKKYLkTYVNEYSnrTGEDQDRAVDKLFELA 260
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
7-275 5.99e-14

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 70.80  E-value: 5.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800   7 SAPATPAVPVRPRVGHIQFLNCLPLYWGLARtGNL----LDLDLTK-DTPEKLSDLLVAGSLDIG--------------- 66
Cdd:COG0715    13 SAAAAAAEKVTLRLGWLPNTDHAPLYVAKEK-GYFkkegLDVELVEfAGGAAALEALAAGQADFGvagappalaarakga 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  67 PITCV--EYLRHADELVVLPDIAVGSdgpvmscvivskvpLADLDGRKVALGSTSrTSVRLAQLLLEE----REGVRPEY 140
Cdd:COG0715    92 PVKAVaaLSQSGGNALVVRKDSGIKS--------------LADLKGKKVAVPGGS-TSHYLLRALLAKagldPKDVEIVN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 141 FSSPPDLDAMLAHADAAVLIGDPalraSLEQAPSQGLA--VHDLGEMWREWTGlpfvfAVWAARRDFLESRPEAVAAVHR 218
Cdd:COG0715   157 LPPPDAVAALLAGQVDAAVVWEP----FESQAEKKGGGrvLADSADLVPGYPG-----DVLVASEDFLEENPEAVKAFLR 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121717800 219 AFLESRDLSLAEAGQVAEQAARWEEFDAALLERYFTEALDYSLG-----ERQLAGIAEFARR 275
Cdd:COG0715   228 ALLKAWAWAAANPDEAAAILAKATGLDPEVLAAALEGDLRLDPPlgapdPARLQRVADFLVE 289
MqnD COG2107
1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) [Coenzyme ...
52-286 1.00e-08

1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and metabolism]; 1,4-dihydroxy-6-naphtoate synthase (menaquinone biosynthesis, futalosine pathway) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441710  Cd Length: 276  Bit Score: 55.15  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  52 EKLSDLLVAGSLDIGPITCVEYLRHADELVVLPD-IAVGSD-GPVmscvIVSKVP--LADLDGRKVALGSTSRTSVRLAQ 127
Cdd:COG2107    41 ETLNRRALKGELDVTAISFHAYPYIADDYALLRSgASLGRGyGPL----VVAKKPmsLEELKGKRIAVPGRYTTAYLLLR 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 128 LLLEERegVRPEY--FSSPPDldAMLA-HADAAVLIGDpaLRASLEQapsQGLAVH-DLGEMWREWTGLPFVFAVWAARR 203
Cdd:COG2107   117 LALPKA--FEVVEmpFDEIMP--AVLSgEVDAGLIIHE--GQLTYAE---YGLVKVlDLGEWWEEETGLPLPLGGNVIRR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 204 DFlesRPEAVAAVHRAFLESRDLSLA---EAGQVAEQAARweEFDAALLERY-------FTealdYSLGERQLAGIAEFA 273
Cdd:COG2107   188 DL---GEEVARKIEEALRKSIKYALAhpdEALEYAMKYAR--ELDEEVIDKFigmyvneYT----VDLGEEGRRAVRTLL 258
                         250
                  ....*....|...
gi 1121717800 274 RRvSHDSGFAPDV 286
Cdd:COG2107   259 ER-AYEKGLIPKP 270
SsuA_fam TIGR01728
ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this ...
58-240 2.51e-07

ABC transporter, substrate-binding protein, aliphatic sulfonates family; Members of this family are substrate-binding periplasmic proteins of ABC transporters. This subfamily includes SsuA, a member of a transporter operon needed to obtain sulfur from aliphatic sulfonates. Related proteins outside the scope of this model include taurine (NH2-CH2-CH2-S03H) binding proteins, the probable sulfate ester binding protein AtsR, and the probable aromatic sulfonate binding protein AsfC. All these families make sulfur available when Cys and sulfate levels are low. Please note that phylogenetic analysis by neighbor-joining suggests that a number of sequences belonging to this family have been excluded because of scoring lower than taurine-binding proteins. [Transport and binding proteins, Other]


Pssm-ID: 130789 [Multi-domain]  Cd Length: 288  Bit Score: 50.82  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  58 LVAGSLDIGPITCVEYLRHADELVVLPDIAVGSDGPVMSCVIVSKVP---LADLDGRKVALgsTSRTSVRLAQLLLEERE 134
Cdd:TIGR01728  46 LGAGSLDFGYIGPGPALFAYAAGADIKAVGLVSDNKATAIVVIKGSPirtVADLKGKRIAV--PKGGSGHDLLLRALLKA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 135 GVRPE----YFSSPPDLDAMLAHADA-AVLIGDPALRASLEQAPSQGLAvhDLGEMW-REWTGLpFVfavwaARRDFLES 208
Cdd:TIGR01728 124 GLSGDdvtiLYLGPSDARAAFAAGQVdAWAIWEPWGSALVEEGGARVLA--NGEGIGlPGQPGF-LV-----VRREFAEA 195
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1121717800 209 RPEAVAAVHRAFLESRDLSLAEAGQVAEQAAR 240
Cdd:TIGR01728 196 HPEQVQRVLKVLVKARKWAEENPEESAKILAK 227
Phosphonate-bd pfam12974
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ...
56-252 1.40e-06

ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake.


Pssm-ID: 432911 [Multi-domain]  Cd Length: 243  Bit Score: 48.41  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  56 DLLVAGSLDI---GPITCVEYLRHADELVVLpdIAVGSDG-PVMSCVIVSKV-----PLADLDGRKVALGSTSRTSVRLA 126
Cdd:pfam12974  44 EALRAGQVDIayfGPLAYVQAVDRAGAEPLA--TPVEPDGsAGYRSVIIVRKdspiqSLEDLKGKTVAFGDPSSTSGYLV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 127 QL-LLEEREGVRPEYFSSPPDLD----AMLA----HADAAVlIGDPALRASLEQAPSQGLAVHDLgemwreWTGLPFVFA 197
Cdd:pfam12974 122 PLaLLFAEAGLDPEDDFKPVFSGshdaVALAvlngDADAGA-VNSEVLERLVAEGPIDRDQLRVI------AESPPIPND 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1121717800 198 VWAARRDFlesRPEAVAAVHRAFLesrDLSLAEAGQVAEQAARWEEFDAALLERY 252
Cdd:pfam12974 195 PLVARPDL---PPELKEKIRDALL---ALDETPEGRKVLEALGIDGFVPADDSDY 243
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
56-223 4.51e-06

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 46.51  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  56 DLLVAGSLDIG------PITcveyLRHADELVVLpdIAVGSDGPVMSCVIVSKVP----LADLDGRKVALGSTSRTSVRL 125
Cdd:cd01008    46 EALAAGSLDFGtggdtpALL----AAAGGVPVVL--IAALSRSPNGNGIVVRKDSgitsLADLKGKKIAVTKGTTGHFLL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 126 AQLLleEREGVRPEYFS----SPPDLDAMLA--HADAAVlIGDPALraSLEQAPSQGLAVHDLGEMWREWTGlpfvfaVW 199
Cdd:cd01008   120 LKAL--AKAGLSVDDVElvnlGPADAAAALAsgDVDAWV-TWEPFL--SLAEKGGDARIIVDGGGLPYTDPS------VL 188
                         170       180
                  ....*....|....*....|....
gi 1121717800 200 AARRDFLESRPEAVAAVHRAFLES 223
Cdd:cd01008   189 VARRDFVEENPEAVKALLKALVEA 212
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
19-223 1.25e-05

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 45.26  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  19 RVGHIQFLNCLPLYWGLAR---TGNLLDLDLTKDT--PEkLSDLLVAGSLDIG------PITcVEYLRHADELVVLpdiA 87
Cdd:cd13553     3 RIGYLPITDHAPLLVAKEKgffEKEGLDVELVKFPswAD-LRDALAAGELDAAhvlapmPAA-ATYGKGAPIKVVA---G 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  88 VGSDGpvmSCVIVSKVP----LADLDGRKVA---LGSTSRTSVR--LAQllleerEGVRPE-----YFSSPPDLDAMLAH 153
Cdd:cd13553    78 LHRNG---SAIVVSKDSgiksVADLKGKTIAvpfPGSTHDVLLRywLAA------AGLDPGkdveiVVLPPPDMVAALAA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121717800 154 AD-AAVLIGDPalraSLEQAPSQGLA--VHDLGEMWREwtglpFVFAVWAARRDFLESRPEAVAAVHRAFLES 223
Cdd:cd13553   149 GQiDAYCVGEP----WNARAVAEGVGrvLADSGDIWPG-----HPCCVLVVREDFLEENPEAVQALLKALVEA 212
PBP2_Af1704 cd13636
The conserved hypothetical protein Af1704 exhibits the type 2 periplasmic-binding protein fold; ...
52-252 3.92e-05

The conserved hypothetical protein Af1704 exhibits the type 2 periplasmic-binding protein fold; This group includes the Af1704 protein from from Archaeoglobus fulgidus DSM 4304, which is an ortholog of Ttha1568 (MqnD) from Thermus thermophilies HB8. MqnD is an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Af1704 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270354  Cd Length: 259  Bit Score: 44.13  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  52 EKLSDLLVAGSLDIGPITCVEYLRHADELVVLPdiaVGSD-----GPVmscvIVSK--VPLADLDGRKVALGSTSRTSVR 124
Cdd:cd13636    39 ETLNREALEGELDVTAISAHAYAYVADKYALLS---SGASmgdgyGPM----VVAKeeLTPEELKGKRIAVPGTLTTAYL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 125 LAQLLLEEREgvrpeYFSSPPD--LDAMLA-HADAAVLIGDPALRASLEqapsqGLAVH-DLGEMWREWTGLPFVFAVWA 200
Cdd:cd13636   112 LLRLYLPKFE-----VVVVPFDeiPDAVLSgEVDAGLIIHEGQLTYERE-----GLKKVvDLGEWWKERTGLPLPLGGNV 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1121717800 201 ARRDFlesRPEAVAAVHRAFLESRDLSLA---EAGQVAEQAARWEefDAALLERY 252
Cdd:cd13636   182 IRKDL---GEEVIREIARLLRESIQYALAhreEALEYAMQFARGL--DRELADRF 231
PBP2_Ttha1568_Mqnd cd13635
A menaquinone biosynthetic enzyme exhibits the type 2 periplasmic-binding protein fold; This ...
52-236 1.56e-04

A menaquinone biosynthetic enzyme exhibits the type 2 periplasmic-binding protein fold; This group includes Ttha1568 (MqnD) from Thermus thermophilies HB8, an enzyme within an alternative menaquinone biosynthetic pathway that catalyzes the conversion of cyclic de-hypoxanthine futalosine to 1,4-dihydroxy-6-naphthoate. Menaquinone (MK; vitamin K) is an essential lipid-soluble carrier that shuttles electrons between membrane-bound protein complexes in the electron transport chain. Ttha1568 has significant structural homology with the members of type 2 periplasmic-binding fold protein superfamily. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270353  Cd Length: 260  Bit Score: 42.50  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  52 EKLSDLLVAGSLDIGPITCVEYLRHADELVVLPdiaVGSD-----GPVmscvIVSK--VPLADLDGRKVALGSTSRTSVR 124
Cdd:cd13635    39 ETLNRLALEGRLDVTKLSFAALPHLLDDYALLR---SGGAlgrgcGPL----LVARkpDSIEDLRGKRIAIPGENTTAHL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 125 LAQLLLEEREGVRPEYFSSPpdLDAMLA-HADAAVLIGDPALrasleQAPSQGL-AVHDLGEMWREWTGLPFVFAVWAAR 202
Cdd:cd13635   112 LLRLFYPDDFELVPMRFDEI--MPAVLRgEVDAGVIIHEGRF-----TYQDYGLhKLLDLGEWWEEETGLPIPLGGIVIR 184
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1121717800 203 RDFLesrPEAVAAVHRAFLESRDLSLAEAGQVAE 236
Cdd:cd13635   185 RDLG---AALARAIEEAIRRSLEYARAHPEAARP 215
PBP2_SsuA cd13557
Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic ...
86-265 1.64e-04

Substrate binding domain of sulfonate binding protein, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes the sulfonate binding domains SsuA found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270275  Cd Length: 275  Bit Score: 42.28  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  86 IAVGSDGPVMScvivskvpLADLDGRKVALGSTSRTSVRLAQLLleEREG-----VRPEYFSSPpdlDAMLAHADAAV-- 158
Cdd:cd13557    87 ILVPKDSPIKT--------VADLKGKKIAFQKGSSAHYLLVKAL--EKAGltlddIEPVYLSPA---DARAAFEQGQVda 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 159 -LIGDPALRASLEQAPSQGLAVHdlgemwrewTGLPFVFAVWAARRDFLESRPEAVAAVHRAFLESRDLSLAEAGQVAEQ 237
Cdd:cd13557   154 wAIWDPYLAAAELTGGARVLADG---------EGLVNNRSFYLAARDFAKDNPEAIQIVLEELNKAGEWANTNRDEAAKL 224
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1121717800 238 AARWEEFDAALLE------RYFTEALDYSLGERQ 265
Cdd:cd13557   225 LAESLGIDAVVLElavarrTYGIIPIDDEIIAAQ 258
PBP2_DszB cd13554
Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 ...
39-225 3.61e-04

Substrate binding domain of 2'-hydroxybiphenyl-2-sulfinate desulfinase, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes DszB, which converts 2'-hydroxybiphenyl-2-sulfinate to 2-hydroxybiphenyl and sulfinate at the rate-limiting step of the microbial dibenzothiophene desulfurization pathway. The overall fold of DszB is highly similar to those of periplasmic substrate-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The DszB protein belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270272 [Multi-domain]  Cd Length: 246  Bit Score: 41.34  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  39 GNLLDLDLTKDTPEKLSDLL--------VAGSLDIGPITCvEYLRHADELVVL---------PDIAVGSDGPVMSCvivs 101
Cdd:cd13554    25 AAGIDLEVVAGTPTGTVDFTydqgipadVVFSGAIPPLLA-EGLRAPGRTRLIgitpldlgrQGLFVRADSPITSA---- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 102 kvplADLDGRKVAL--GSTSRTSVRLAQLLLEEREGVRPEYFssppDLDAMLAHADAAVLIGDPALRAS----LEQAPSQ 175
Cdd:cd13554   100 ----ADLEGKRIGMsaGAIRGSWLARALLHNLEIGGLDVEIV----PIDSPGRGQAAALDSGDIDALASwlpwATTLQAT 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1121717800 176 GlAVHDLGEMwrEWTGLPFVFAVWAARRDFLESRPEAVAAVHRAFLESRD 225
Cdd:cd13554   172 G-GARPLVDL--GLVEGNSYYSTWTVRSDFIEQNPEAVKALVEALVRAGD 218
PBP2_SsuA_like_3 cd13559
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
86-246 3.91e-04

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270277  Cd Length: 258  Bit Score: 41.25  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  86 IAVGSDGPVMScvivskvpLADLDGRKVA--LGSTSRTSV--RLAQLLLEEREGVR-----PEYFSSPPDLDAMLAHADA 156
Cdd:cd13559   105 IVVPKDSPVNS--------LDDLKGKTVSvpFGSSAHGMLlrALDRAGLNPDTDVTiinqaPEVGGSALQANKIDAHADF 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 157 AVLigdpalrASLeqAPSQGLA--VHDLGEmwrewTGLPFvFAVWAARRDFLESRPEAVAAVHRAFLESRDLSLAEAGQV 234
Cdd:cd13559   177 VPF-------PEL--FPHRGIArkLYDGSQ-----TKVPT-FHGIVVDRDFAEKHPEVVVAYLRALIEAHRLIREEPEAY 241
                         170
                  ....*....|..
gi 1121717800 235 AEQAARWEEFDA 246
Cdd:cd13559   242 SELIEKVTGIEA 253
PBP2_taurine cd13560
Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This ...
59-215 1.02e-03

Taurine-binding periplasmic protein; the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270278 [Multi-domain]  Cd Length: 218  Bit Score: 39.60  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  59 VAGSLDIGPITCVEYLRHADELVVLPDIAVGSdgpvmscvivskvpLADLDGRKVA--LGSTSRTSVrLAQLlleEREGV 136
Cdd:cd13560    64 IAAGLPIEVIWIADVIGDAEALVVRKGSGIKS--------------LKDLAGKKVAvpFGSTAHYSL-LAAL---KHAGV 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 137 RPE----YFSSPPDLDAMLAHADA-AVLIGDPALRasleQAPSQGLAVHDLGEMwREWtGLPfVFAVWAARRDFLESRPE 211
Cdd:cd13560   126 DPGkvkiLDMQPPEIVAAWQRGDIdAAYVWEPALS----QLKKNGKVLLSSKDL-AKK-GIL-TFDVWVVRKDFAEKYPD 198

                  ....
gi 1121717800 212 AVAA 215
Cdd:cd13560   199 VVAA 202
PBP2_SsuA_like_4 cd13561
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
58-222 2.08e-03

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270279 [Multi-domain]  Cd Length: 212  Bit Score: 38.51  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800  58 LVAGSLDIGPITCVEYLRHADELVVLpdIAVGSDGPVMSCVIVSKVP----LADLDGRKVAL--GSTSRTSVRL----AQ 127
Cdd:cd13561    47 LGSGSLDVGYTGPVAFNLPASGQAKV--VLINNLENATASLIVRADSgiasIADLKGKKIGTpsGTTADVALDLalrkAG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121717800 128 LLLEEREGVR---PEYFSsppdldAMLAHADAAVLIGDPALRASLEQAPsqGLAVHDLGEMWREWTGLPfvfAVWAARRD 204
Cdd:cd13561   125 LSEKDVQIVNmdpAEIVT------AFTSGSVDAAALWAPNTATIKEKVP--GAVELADNSDFGPDAAVP---GAWVARNK 193
                         170
                  ....*....|....*...
gi 1121717800 205 FLESRPEAVAAVHRAFLE 222
Cdd:cd13561   194 YAEENPEELKKFLAALAE 211
 
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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