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Conserved domains on  [gi|1483497858|gb|AYD46593|]
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hypothetical protein D6B99_02555 [Arachidicoccus soli]

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 ...
3-250 8.08e-90

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: 266.32  E-value: 8.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   3 KIRVAAVSYLNTKPLLYGIKRDKtLMEQMDLIEDYPAKIGQMLVDDDVDMGLIP-VAYIPQMREWHIYSDYCIGSVGPVE 81
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGG-LLPDVELVKGVPSQLNRMLAEGELDVGLISsIEYARHADDYLILPDLSISADGPVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  82 TVCLFSDVPVEKIE--KVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNSTNSkK 159
Cdd:COG1427    80 SVLLFSRVPLEELDgkTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADAALLIGDRALRAAARGRF-P 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 160 YIYDLAEEWTNFTGLPFLMAAWIANKELPES-----FVERFNAANKVGLDDLDAVIDEN----PYPAYDLHQYFtRDISF 230
Cdd:COG1427   159 YVYDLGEEWKELTGLPFVFAVWAVRRDAAEAnpvaeLHEALLEAKERGLAHLDEIAEEAarrlGLPPELLEDYL-RNLRY 237
                         250       260
                  ....*....|....*....|
gi 1483497858 231 NVDEKKLKAMDLFLKLMKEL 250
Cdd:COG1427   238 DLGEEERKGLRLFYEYAAEL 257
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
3-250 8.08e-90

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: 266.32  E-value: 8.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   3 KIRVAAVSYLNTKPLLYGIKRDKtLMEQMDLIEDYPAKIGQMLVDDDVDMGLIP-VAYIPQMREWHIYSDYCIGSVGPVE 81
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGG-LLPDVELVKGVPSQLNRMLAEGELDVGLISsIEYARHADDYLILPDLSISADGPVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  82 TVCLFSDVPVEKIE--KVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNSTNSkK 159
Cdd:COG1427    80 SVLLFSRVPLEELDgkTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADAALLIGDRALRAAARGRF-P 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 160 YIYDLAEEWTNFTGLPFLMAAWIANKELPES-----FVERFNAANKVGLDDLDAVIDEN----PYPAYDLHQYFtRDISF 230
Cdd:COG1427   159 YVYDLGEEWKELTGLPFVFAVWAVRRDAAEAnpvaeLHEALLEAKERGLAHLDEIAEEAarrlGLPPELLEDYL-RNLRY 237
                         250       260
                  ....*....|....*....|
gi 1483497858 231 NVDEKKLKAMDLFLKLMKEL 250
Cdd:COG1427   238 DLGEEERKGLRLFYEYAAEL 257
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
3-248 1.46e-72

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: 222.04  E-value: 1.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   3 KIRVAAVSYLNTKPLLYGIKRDKtLMEQMDLIEDYPAKIGQMLVDDDVDMGLIP-VAYIPQMREWHIYSDYCIGSVGPVE 81
Cdd:cd13634     1 MLRVGRISYLNTLPLFYGLEKGK-VPPGFELVLGVPSELNRMLLEGELDVGLVSsIEYARNADDYLILPDLSISSDGPVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  82 TVCLFSDVPVE--KIEKVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNStNSKK 159
Cdd:cd13634    80 SVLLFSKVPLEelEGKRVALTTESATSVALLKILLEEFYGLEPEYVPAPPDLDEMLADADAALLIGDDALRARAS-GRGP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 160 YIYDLAEEWTNFTGLPFLMAAWIANKELPES------FVERFNAANKVGLDDLDAVIDE----NPYPAYDLHQYFTRdIS 229
Cdd:cd13634   159 YVYDLGEEWKELTGLPFVFAVWAVRRDAAERpeelaeLVQALLESKRYGLANLEEIIAEaaerLGLSEEFLRDYFTN-LR 237
                         250
                  ....*....|....*....
gi 1483497858 230 FNVDEKKLKAMDLFLKLMK 248
Cdd:cd13634   238 YDLGEEELEGLELFYRYAA 256
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
4-249 5.52e-42

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: 143.46  E-value: 5.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   4 IRVAAVSYLNTKPLLYGIKRDKTLMEqmDLIEDYPAKIGQMLVDDDVDMGLIPV-AYIPQMREWHIYSDYCIGSVGPVET 82
Cdd:pfam02621   1 LRVGHSPYPNDLPLFYALVHDEGLDF--EIVLGDPETLNRMLLEGELDVSAISSaAYARNADDYVLLPDLSGSALGRVYS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  83 VCLFSDVPV--EKIEKVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNSTNskKY 160
Cdd:pfam02621  79 PLLVSRVPEldGDGKRVALPGESTTSVLLLRLLLPERYGKPRYVPMPDEIMAAVLEGEDAGLLIGDSALTYAERGL--KK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 161 IYDLAEEWTNFTGLPFLMAAWIANKELPES----FVERFNAANKVGLDDLDAVIDE----NPYPAYDLHQYFtRDISFNV 232
Cdd:pfam02621 157 VLDLGEWWKELTGLPMPFGLWVVRRDLALEtakeLEEALRASKEYALAHPDEIAEYaaehAQEMEEFLRLYV-NELSYDL 235
                         250
                  ....*....|....*..
gi 1483497858 233 DEKKLKAMDLFLKLMKE 249
Cdd:pfam02621 236 GEEGRAGLEEFYERAAE 252
 
Name Accession Description Interval E-value
MqnA COG1427
Chorismate dehydratase (menaquinone biosynthesis, futalosine pathway) [Coenzyme transport and ...
3-250 8.08e-90

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: 266.32  E-value: 8.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   3 KIRVAAVSYLNTKPLLYGIKRDKtLMEQMDLIEDYPAKIGQMLVDDDVDMGLIP-VAYIPQMREWHIYSDYCIGSVGPVE 81
Cdd:COG1427     1 KLRIGAVSYLNTLPLYYGLERGG-LLPDVELVKGVPSQLNRMLAEGELDVGLISsIEYARHADDYLILPDLSISADGPVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  82 TVCLFSDVPVEKIE--KVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNSTNSkK 159
Cdd:COG1427    80 SVLLFSRVPLEELDgkTVALTSESRTSVALLKILLAEYYGVRPEYVPGPPDLEAMLEGADAALLIGDRALRAAARGRF-P 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 160 YIYDLAEEWTNFTGLPFLMAAWIANKELPES-----FVERFNAANKVGLDDLDAVIDEN----PYPAYDLHQYFtRDISF 230
Cdd:COG1427   159 YVYDLGEEWKELTGLPFVFAVWAVRRDAAEAnpvaeLHEALLEAKERGLAHLDEIAEEAarrlGLPPELLEDYL-RNLRY 237
                         250       260
                  ....*....|....*....|
gi 1483497858 231 NVDEKKLKAMDLFLKLMKEL 250
Cdd:COG1427   238 DLGEEERKGLRLFYEYAAEL 257
PBP2_Sco4506 cd13634
The conserved hypothetical protein SCO4506 exhibits the type 2 periplasmic-binidng protein ...
3-248 1.46e-72

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: 222.04  E-value: 1.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   3 KIRVAAVSYLNTKPLLYGIKRDKtLMEQMDLIEDYPAKIGQMLVDDDVDMGLIP-VAYIPQMREWHIYSDYCIGSVGPVE 81
Cdd:cd13634     1 MLRVGRISYLNTLPLFYGLEKGK-VPPGFELVLGVPSELNRMLLEGELDVGLVSsIEYARNADDYLILPDLSISSDGPVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  82 TVCLFSDVPVE--KIEKVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNStNSKK 159
Cdd:cd13634    80 SVLLFSKVPLEelEGKRVALTTESATSVALLKILLEEFYGLEPEYVPAPPDLDEMLADADAALLIGDDALRARAS-GRGP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 160 YIYDLAEEWTNFTGLPFLMAAWIANKELPES------FVERFNAANKVGLDDLDAVIDE----NPYPAYDLHQYFTRdIS 229
Cdd:cd13634   159 YVYDLGEEWKELTGLPFVFAVWAVRRDAAERpeelaeLVQALLESKRYGLANLEEIIAEaaerLGLSEEFLRDYFTN-LR 237
                         250
                  ....*....|....*....
gi 1483497858 230 FNVDEKKLKAMDLFLKLMK 248
Cdd:cd13634   238 YDLGEEELEGLELFYRYAA 256
VitK2_biosynth pfam02621
Menaquinone biosynthesis; This family includes two enzymes which are involved in menaquinone ...
4-249 5.52e-42

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: 143.46  E-value: 5.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   4 IRVAAVSYLNTKPLLYGIKRDKTLMEqmDLIEDYPAKIGQMLVDDDVDMGLIPV-AYIPQMREWHIYSDYCIGSVGPVET 82
Cdd:pfam02621   1 LRVGHSPYPNDLPLFYALVHDEGLDF--EIVLGDPETLNRMLLEGELDVSAISSaAYARNADDYVLLPDLSGSALGRVYS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  83 VCLFSDVPV--EKIEKVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEIGGTTAGVIIGDRVFEQKNSTNskKY 160
Cdd:pfam02621  79 PLLVSRVPEldGDGKRVALPGESTTSVLLLRLLLPERYGKPRYVPMPDEIMAAVLEGEDAGLLIGDSALTYAERGL--KK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 161 IYDLAEEWTNFTGLPFLMAAWIANKELPES----FVERFNAANKVGLDDLDAVIDE----NPYPAYDLHQYFtRDISFNV 232
Cdd:pfam02621 157 VLDLGEWWKELTGLPMPFGLWVVRRDLALEtakeLEEALRASKEYALAHPDEIAEYaaehAQEMEEFLRLYV-NELSYDL 235
                         250
                  ....*....|....*..
gi 1483497858 233 DEKKLKAMDLFLKLMKE 249
Cdd:pfam02621 236 GEEGRAGLEEFYERAAE 252
PBP2_MqnD_like cd13534
Menaquinone biosynthetic enzyme and related hypothetical proteins; the type 2 ...
3-248 4.26e-09

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: 55.50  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858   3 KIRVAAVSYLNTKPLLYGIKRDK---TLMEQMDLIEDyPAKIGQMLVDDDVDMGLIPVAYIPQMRE-WHIYSDycIGSVG 78
Cdd:cd13534     1 TIRVGHSPDADDLFLFYALKHGWvkeTDLIFENVKED-VETLNELALKNELDVSAISFAAYPKIADdYVILPT--GAVFG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858  79 PVETVCLFSDVPVEKIE--KVLLDYQSFSSVNLCKVLLKNYWEKDVIFEKASENYISEiGGTTAGVIIGDRVFEQ--KNS 154
Cdd:cd13534    78 DGYGPVLVAKSPLDDKQgkRVAVSGRNTTAYLLLKLLAPQYFRPIVVRFDDIEDAVLE-GEVDAGVLIHESILMTypRYG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1483497858 155 TNSKKYIYDLAEEWTNftgLPFLMAAWIANKELPE----SFVERFNAANKVGLDDLDAVI-------DENPYPAYDLHQY 223
Cdd:cd13534   157 LKVVRDLWDLWKESTN---LPLPLGVVAIRRDLGEdlirAFKEAVLLSKAYALAHPDEAIeymlqeaREIRLDEEVLKKY 233
                         250       260
                  ....*....|....*....|....*...
gi 1483497858 224 FTRDI---SFNVDEKKLKAMDLFLKLMK 248
Cdd:cd13534   234 LKTYVneySNRTGEDQDRAVDKLFELAE 261
 
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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