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Conserved domains on  [gi|540365742|gb|AGV09599|]
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hypothetical protein G157_02395 [Campylobacter coli CVM N29710]

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 super family cl42777
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
4-222 4.73e-41

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


The actual alignment was detected with superfamily member COG1427:

Pssm-ID: 441036  Cd Length: 268  Bit Score: 140.74  E-value: 4.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   4 GKIDYINLLPLHIYLKKYPLPNGFkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKRVLS 80
Cdd:COG1427    5 GAVSYLNTLPLYYGLERGGLLPDV----ELVKGVPSQLNRMLAEGELDVGLISSIEYARhaDDYLILpDLSISADGPVGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  81 VLVEKNTPNAK--------DPSSATSNALAKVLKQE-----------------------GRVIIGDKALKLYLQDPSRY- 128
Cdd:COG1427   81 VLLFSRVPLEEldgktvalTSESRTSVALLKILLAEyygvrpeyvpgppdleamlegadAALLIGDRALRAAARGRFPYv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742 129 TDLCTKWHEKTGLPFVFArFSCVQKKALYKQILKKFPKTKIKIPYY-------ILQNYAKTRDLDIKDIRYYLDEIIYHk 201
Cdd:COG1427  161 YDLGEEWKELTGLPFVFA-VWAVRRDAAEANPVAELHEALLEAKERglahldeIAEEAARRLGLPPELLEDYLRNLRYD- 238
                        250       260
                 ....*....|....*....|.
gi 540365742 202 ISTKEKAALKRFIKACKALNL 222
Cdd:COG1427  239 LGEEERKGLRLFYEYAAELGL 259
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
4-222 4.73e-41

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: 140.74  E-value: 4.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   4 GKIDYINLLPLHIYLKKYPLPNGFkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKRVLS 80
Cdd:COG1427    5 GAVSYLNTLPLYYGLERGGLLPDV----ELVKGVPSQLNRMLAEGELDVGLISSIEYARhaDDYLILpDLSISADGPVGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  81 VLVEKNTPNAK--------DPSSATSNALAKVLKQE-----------------------GRVIIGDKALKLYLQDPSRY- 128
Cdd:COG1427   81 VLLFSRVPLEEldgktvalTSESRTSVALLKILLAEyygvrpeyvpgppdleamlegadAALLIGDRALRAAARGRFPYv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742 129 TDLCTKWHEKTGLPFVFArFSCVQKKALYKQILKKFPKTKIKIPYY-------ILQNYAKTRDLDIKDIRYYLDEIIYHk 201
Cdd:COG1427  161 YDLGEEWKELTGLPFVFA-VWAVRRDAAEANPVAELHEALLEAKERglahldeIAEEAARRLGLPPELLEDYLRNLRYD- 238
                        250       260
                 ....*....|....*....|.
gi 540365742 202 ISTKEKAALKRFIKACKALNL 222
Cdd:COG1427  239 LGEEERKGLRLFYEYAAELGL 259
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
1-213 6.69e-40

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: 137.30  E-value: 6.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   1 MIFGKIDYINLLPLHIYLKKYPLPNGFkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKR 77
Cdd:cd13634    2 LRVGRISYLNTLPLFYGLEKGKVPPGF----ELVLGVPSELNRMLLEGELDVGLVSSIEYARnaDDYLILpDLSISSDGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  78 VLSVLVEKNTPNAK--------DPSSATSNALAKVL-----------------------KQEGRVIIGDKALKLYLQDPS 126
Cdd:cd13634   78 VGSVLLFSKVPLEElegkrvalTTESATSVALLKILleefyglepeyvpappdldemlaDADAALLIGDDALRARASGRG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742 127 RY-TDLCTKWHEKTGLPFVFA----RFSCVQKKALYKQILKKFPKTK---IKIPYYILQNYAKTRDLDIKDIRYYLDEII 198
Cdd:cd13634  158 PYvYDLGEEWKELTGLPFVFAvwavRRDAAERPEELAELVQALLESKrygLANLEEIIAEAAERLGLSEEFLRDYFTNLR 237
                        250
                 ....*....|....*
gi 540365742 199 YHkISTKEKAALKRF 213
Cdd:cd13634  238 YD-LGEEELEGLELF 251
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
4-219 3.44e-20

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: 85.68  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742    4 GKIDYINLLPLHIYLKKYPLPNGfkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKRVLS 80
Cdd:pfam02621   4 GHSPYPNDLPLFYALVHDEGLDF-----EIVLGDPETLNRMLLEGELDVSAISSAAYARnaDDYVLLpDLSGSALGRVYS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   81 VLVEKNTPN--------AKDPSSATSNALAKVL--------------------KQEGR---VIIGDKALKLYLQDPSRYT 129
Cdd:pfam02621  79 PLLVSRVPEldgdgkrvALPGESTTSVLLLRLLlperygkpryvpmpdeimaaVLEGEdagLLIGDSALTYAERGLKKVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  130 DLCTKWHEKTGLPFVFARFscVQKKALYKQILKKFPKTKIKIPYYILQNY-------AKTRDLDIKDIRYYLDEIIYHkI 202
Cdd:pfam02621 159 DLGEWWKELTGLPMPFGLW--VVRRDLALETAKELEEALRASKEYALAHPdeiaeyaAEHAQEMEEFLRLYVNELSYD-L 235
                         250
                  ....*....|....*..
gi 540365742  203 STKEKAALKRFIKACKA 219
Cdd:pfam02621 236 GEEGRAGLEEFYERAAE 252
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
4-222 4.73e-41

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: 140.74  E-value: 4.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   4 GKIDYINLLPLHIYLKKYPLPNGFkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKRVLS 80
Cdd:COG1427    5 GAVSYLNTLPLYYGLERGGLLPDV----ELVKGVPSQLNRMLAEGELDVGLISSIEYARhaDDYLILpDLSISADGPVGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  81 VLVEKNTPNAK--------DPSSATSNALAKVLKQE-----------------------GRVIIGDKALKLYLQDPSRY- 128
Cdd:COG1427   81 VLLFSRVPLEEldgktvalTSESRTSVALLKILLAEyygvrpeyvpgppdleamlegadAALLIGDRALRAAARGRFPYv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742 129 TDLCTKWHEKTGLPFVFArFSCVQKKALYKQILKKFPKTKIKIPYY-------ILQNYAKTRDLDIKDIRYYLDEIIYHk 201
Cdd:COG1427  161 YDLGEEWKELTGLPFVFA-VWAVRRDAAEANPVAELHEALLEAKERglahldeIAEEAARRLGLPPELLEDYLRNLRYD- 238
                        250       260
                 ....*....|....*....|.
gi 540365742 202 ISTKEKAALKRFIKACKALNL 222
Cdd:COG1427  239 LGEEERKGLRLFYEYAAELGL 259
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
1-213 6.69e-40

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: 137.30  E-value: 6.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   1 MIFGKIDYINLLPLHIYLKKYPLPNGFkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKR 77
Cdd:cd13634    2 LRVGRISYLNTLPLFYGLEKGKVPPGF----ELVLGVPSELNRMLLEGELDVGLVSSIEYARnaDDYLILpDLSISSDGP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  78 VLSVLVEKNTPNAK--------DPSSATSNALAKVL-----------------------KQEGRVIIGDKALKLYLQDPS 126
Cdd:cd13634   78 VGSVLLFSKVPLEElegkrvalTTESATSVALLKILleefyglepeyvpappdldemlaDADAALLIGDDALRARASGRG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742 127 RY-TDLCTKWHEKTGLPFVFA----RFSCVQKKALYKQILKKFPKTK---IKIPYYILQNYAKTRDLDIKDIRYYLDEII 198
Cdd:cd13634  158 PYvYDLGEEWKELTGLPFVFAvwavRRDAAERPEELAELVQALLESKrygLANLEEIIAEAAERLGLSEEFLRDYFTNLR 237
                        250
                 ....*....|....*
gi 540365742 199 YHkISTKEKAALKRF 213
Cdd:cd13634  238 YD-LGEEELEGLELF 251
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
4-219 3.44e-20

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: 85.68  E-value: 3.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742    4 GKIDYINLLPLHIYLKKYPLPNGfkasmEHKKGVPSKLNKDLFYRRIDAAIVSSIESAR--KKYKNL-DLGICANKRVLS 80
Cdd:pfam02621   4 GHSPYPNDLPLFYALVHDEGLDF-----EIVLGDPETLNRMLLEGELDVSAISSAAYARnaDDYVLLpDLSGSALGRVYS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742   81 VLVEKNTPN--------AKDPSSATSNALAKVL--------------------KQEGR---VIIGDKALKLYLQDPSRYT 129
Cdd:pfam02621  79 PLLVSRVPEldgdgkrvALPGESTTSVLLLRLLlperygkpryvpmpdeimaaVLEGEdagLLIGDSALTYAERGLKKVL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540365742  130 DLCTKWHEKTGLPFVFARFscVQKKALYKQILKKFPKTKIKIPYYILQNY-------AKTRDLDIKDIRYYLDEIIYHkI 202
Cdd:pfam02621 159 DLGEWWKELTGLPMPFGLW--VVRRDLALETAKELEEALRASKEYALAHPdeiaeyaAEHAQEMEEFLRLYVNELSYD-L 235
                         250
                  ....*....|....*..
gi 540365742  203 STKEKAALKRFIKACKA 219
Cdd:pfam02621 236 GEEGRAGLEEFYERAAE 252
 
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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