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Conserved domains on  [gi|115312127|sp|Q5V5R9|]
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RecName: Full=2-phospho-L-lactate transferase

Protein Classification

CofD/YvcK family protein( domain architecture ID 1837)

CofD/YvcK family protein similar to Bacillus subtilis gluconeogenesis factor YvcK, which is essential for growth on intermediates of the Krebs cycle and the pentose phosphate pathway and may play a role in carbon metabolism, and related to CofD, a 2-phospho-L-lactate transferase involved in F420 biosynthesis

PubMed:  16272399

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CofD_YvcK super family cl00425
Family of CofD-like proteins and proteins related to YvcK; CofD is a 2-phospho-L-lactate ...
2-322 1.27e-121

Family of CofD-like proteins and proteins related to YvcK; CofD is a 2-phospho-L-lactate transferase that catalyzes the last step in the biosynthesis of coenzyme F(420)-0 (F(420) without polyglutamate) by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (F0). F420 is a hydride carrier, important for energy metabolism of methanogenic archaea, as well as for the biosynthesis of other natural products, like tetracycline in Streptomyces. F420 and some of its precursors are also utilized as cofactors for enzymes, like DNA photolyase in Mycobacterium tuberculosis. YvcK from Bacillus subtilis is a member of a family of mostly uncharacterized proteins and has been proposed to play a role in carbon metabolism, since its function is essential for growth on intermediates of the Krebs cycle and pentose phosphate pathway. Both families appear to have a conserved phosphate binding site, but have different substrate binding residues conserved within each family.


The actual alignment was detected with superfamily member cd07186:

Pssm-ID: 444899  Cd Length: 303  Bit Score: 351.51  E-value: 1.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   2 VTFLAGGTGTPKLLAGADDVFSPAATTVVANTGDDIELGGHLVCPDLDTVLFLDGEVLDRETWWGIADDTAETHTELTRL 81
Cdd:cd07186    1 IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDTFNTLEALERL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  82 adaagldggprylpddaqtagrdiarwrrfsGVAEFMHIGDRDRAVHVTRTSLLDEGRSLTAVTRTLADAFGLERTLLPM 161
Cdd:cd07186   81 -------------------------------GGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 162 SDDPVASIIHTPSGPMHFQEWWVGRNGEPPVEDVEFRGAERASATDAVLTAL--DDTVVIGPSNPVTSLGPMLAIDDIQR 239
Cdd:cd07186  130 SDDRVETRVVTDEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIedADLVIIGPSNPVTSIGPILALPGIRE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 240 ALHETT--VVAVSPFIEDTVFSGPAADLMAGVGLEPSTAGVAEAY-PFADSFVLDEEDST------PLDVPVVRTDTTLN 310
Cdd:cd07186  210 ALRDKKapVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYgDLLDGFVIDEADRAladaieALGIEVSRTDTLMT 289
                        330
                 ....*....|..
gi 115312127 311 DAADAERVNRAV 322
Cdd:cd07186  290 DEEDKIRLAREV 301
 
Name Accession Description Interval E-value
CofD_like cd07186
LPPG:FO 2-phospho-L-lactate transferase; important in F420 biosynthesis; CofD is a ...
2-322 1.27e-121

LPPG:FO 2-phospho-L-lactate transferase; important in F420 biosynthesis; CofD is a 2-phospho-L-lactate transferase that catalyzes the last step in the biosynthesis of coenzyme F(420)-0 (F(420) without polyglutamate) by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (F0). F420 is a hydride carrier, important for energy metabolism of methanogenic archaea, as well as for the biosynthesis of other natural products, like tetracycline in Streptomyces. F420 and some of its precursors are also utilized as cofactors for enzymes, like DNA photolyase in Mycobacterium tuberculosis.


Pssm-ID: 132872  Cd Length: 303  Bit Score: 351.51  E-value: 1.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   2 VTFLAGGTGTPKLLAGADDVFSPAATTVVANTGDDIELGGHLVCPDLDTVLFLDGEVLDRETWWGIADDTAETHTELTRL 81
Cdd:cd07186    1 IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDTFNTLEALERL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  82 adaagldggprylpddaqtagrdiarwrrfsGVAEFMHIGDRDRAVHVTRTSLLDEGRSLTAVTRTLADAFGLERTLLPM 161
Cdd:cd07186   81 -------------------------------GGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 162 SDDPVASIIHTPSGPMHFQEWWVGRNGEPPVEDVEFRGAERASATDAVLTAL--DDTVVIGPSNPVTSLGPMLAIDDIQR 239
Cdd:cd07186  130 SDDRVETRVVTDEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIedADLVIIGPSNPVTSIGPILALPGIRE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 240 ALHETT--VVAVSPFIEDTVFSGPAADLMAGVGLEPSTAGVAEAY-PFADSFVLDEEDST------PLDVPVVRTDTTLN 310
Cdd:cd07186  210 ALRDKKapVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYgDLLDGFVIDEADRAladaieALGIEVSRTDTLMT 289
                        330
                 ....*....|..
gi 115312127 311 DAADAERVNRAV 322
Cdd:cd07186  290 DEEDKIRLAREV 301
F420_cofD TIGR01819
2-phospho-L-lactate transferase; This model represents LPPG:Fo 2-phospho-L-lactate transferase, ...
3-322 5.40e-117

2-phospho-L-lactate transferase; This model represents LPPG:Fo 2-phospho-L-lactate transferase, which catalyses the fourth step in the biosynthesis of coenzyme F420, a flavin derivative found in methanogens, the Mycobacteria, and several other lineages. This enzyme is characterized so far in Methanococcus jannaschii but appears restricted to F420-containing species and is predicted to carry out the same function in these other species. The clade represented by this model is one of two major divisions of proteins in pfam01933. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 130878  Cd Length: 297  Bit Score: 339.80  E-value: 5.40e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127    3 TFLAGGTGTPKLLAGADDVFSPAATTVVANTGDDIELGGHLVCPDLDTVLFLDGEVLDRETWWGIADDTAETHTELTRLa 82
Cdd:TIGR01819   1 TVLSGGTGTPKLLQGLKEVLPDAELTVVVNTGEDVWVSGLLVCPDLDTVLYTLGGGIDRERWWGIADDTFHTHERLKEL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   83 daagldggprylpddaqtagrdiarwrrfsGVAEFMHIGDRDRAVHVTRTSLLDEGRSLTAVTRTLADAFGLERTLLPMS 162
Cdd:TIGR01819  80 ------------------------------GVPEGLRLGDRDRATHIVRTQMLRAGHSLSEVTEALCDAFGIKARLLPMT 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  163 DDPVASIIHTPSGPMHFQEWWVGRNGEPPVEDVEFRGAERASATDAVLTAL--DDTVVIGPSNPVTSLGPMLAIDDIQRA 240
Cdd:TIGR01819 130 DDEVSTYVETDEGAMHFQEFWVRRRGEPPVEDVDFRGAEKASIAPKVLEAIrkEDNILIGPSNPITSIGPILSLPGIREA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  241 LHETTVVAVSPFIEDTVFSGPAADLMAGVGLEPSTAGVAEAYP-FADSFVLDEEDSTPLD---VPVVRTDTTLNDAADAE 316
Cdd:TIGR01819 210 LRDKKVVAVSPIVGNAPVSGPAGKLMAAVGVEVSAAGVAEHYGdFLDVFVVDEVDKADEDrfgCHVRRTDTLMTTLEDTA 289

                  ....*.
gi 115312127  317 RVNRAV 322
Cdd:TIGR01819 290 RLARAV 295
CofD COG0391
Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family ...
1-323 1.18e-44

Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440160  Cd Length: 314  Bit Score: 154.91  E-value: 1.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   1 MVTFLAGGTGTPKLLAGADDVfsPAATTVVANTGDDIELGGHL------VCP-DLDTVLFLdgevldretwwgIADDTae 73
Cdd:COG0391    8 KVVAIGGGTGLSTLLRGLKRY--TANLTAIVTVADDGGSSGRLrrelgvLPPgDLRNCLAA------------LADDE-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  74 thTELTRLADAagldggprylpddaqtagrdiarwrRFSGvaefmhigDRDRAVHVTRTSLLDEG----RSLTAVTRTLA 149
Cdd:COG0391   72 --PLLSRLFQY-------------------------RFSG--------GGDLAGHSLGNLLLAALteitGDFVEAIDLLS 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 150 DAFGLERTLLPMSDDPVASIIHTPSGPMHFQEWWVGRNGEpPVEDVEFRgAERASATDAVLTALD--DTVVIGPSNPVTS 227
Cdd:COG0391  117 KLLGVRGRVLPMTLDPVDLVAELEDGRIVRGESAIAKAGG-RIERVFLE-PEDAPATPEALEAIEeaDLIVLGPGSLYTS 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 228 LGPMLAIDDIQRALHET--TVVAVSPFIEdtvFSGPAadlmAGVGLEPSTAGVAEAYP--FADSFVLD------------ 291
Cdd:COG0391  195 IIPNLLVPGIAEALRETkaPKVYVCNLMT---QPGET----DGYSAADHVRALERHLGgpFIDAVLVNnapvpdellery 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 115312127 292 -EEDSTP----------LDVPVVRTDTTLNDAA---DAERVNRAVE 323
Cdd:COG0391  268 aEEGAEPveldrerleeLGVRVVRADLLDEDGPvrhDPEKLARALL 313
CofD pfam01933
2-phospho-L-lactate transferase CofD; This entry contains 2-phospho-L-lactate transferase ...
2-270 2.16e-38

2-phospho-L-lactate transferase CofD; This entry contains 2-phospho-L-lactate transferase (CofD), phosphoenolpyruvate transferase and related sequences. CofD catalyzes the fourth step in the biosynthesis of coenzyme F420, which is the transfer of the 2-phospholactate moiety from lactyl (2)diphospho-(5') guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of the L-lactyl phosphodiester of 7,8-didemethyl- 8-hydroxy-5-deazariboflavin (F420-0) and GMP. F420 is a flavin derivative found in methanogens, Mycobacteria, and several other lineages. This enzyme is characterized so far in Methanocaldococcus jannaschii (Methanococcus jannaschii) but appears restricted to F420-containing species and is predicted to carry out the same function in these other species. CofD monomer contains 12 beta- strands, seven of them form a Rossmann fold, and 13 alpha-helices.


Pssm-ID: 426519  Cd Length: 249  Bit Score: 136.42  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127    2 VTFLAGGTGTPKLLAGADDVfsPAATTVVANTGDDIELGG-------HLVCPDLDTVLFldgEVLDRETWwgiaddtaet 74
Cdd:pfam01933   1 IVVIGGGTGLSRLLRGLKRY--TANLTAIVTVADDGGSSGrlrrelgLLPPGDIRNCLV---ALADTEPL---------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   75 HTELTRLadaagldggprylpddaqtagrdiarwrRFsgvaefmhIGDRDRAVHVTRTSLLDEGR----SLTAVTRTLAD 150
Cdd:pfam01933  66 MEELFQY----------------------------RF--------LGDGDLAGHSLGNLFLAALTeitgDFSEAIEALSK 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  151 AFGLERTLLPMSDDPVASIIHTPSGPMHFQEWWVG--RNGEPPVEDVeFRGAERASATDAVLTAL--DDTVVIGPSNPVT 226
Cdd:pfam01933 110 VLAVRGRVLPMTDDPVELHAELEDGTIVHGESWIPeaRKAKPPIKRV-FLGPEDAKALPEVLEAIeeADLIVLGPGSLYT 188
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115312127  227 SLGPMLAIDDIQRALHETT--VVAVSPFI------EDTVFSGPAADLMAGVG 270
Cdd:pfam01933 189 SIIPNLLVPGIREALRESKapKVYVSNIMtqpgetDGYTVSDHAKAIMRHLG 240
 
Name Accession Description Interval E-value
CofD_like cd07186
LPPG:FO 2-phospho-L-lactate transferase; important in F420 biosynthesis; CofD is a ...
2-322 1.27e-121

LPPG:FO 2-phospho-L-lactate transferase; important in F420 biosynthesis; CofD is a 2-phospho-L-lactate transferase that catalyzes the last step in the biosynthesis of coenzyme F(420)-0 (F(420) without polyglutamate) by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (F0). F420 is a hydride carrier, important for energy metabolism of methanogenic archaea, as well as for the biosynthesis of other natural products, like tetracycline in Streptomyces. F420 and some of its precursors are also utilized as cofactors for enzymes, like DNA photolyase in Mycobacterium tuberculosis.


Pssm-ID: 132872  Cd Length: 303  Bit Score: 351.51  E-value: 1.27e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   2 VTFLAGGTGTPKLLAGADDVFSPAATTVVANTGDDIELGGHLVCPDLDTVLFLDGEVLDRETWWGIADDTAETHTELTRL 81
Cdd:cd07186    1 IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDTFNTLEALERL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  82 adaagldggprylpddaqtagrdiarwrrfsGVAEFMHIGDRDRAVHVTRTSLLDEGRSLTAVTRTLADAFGLERTLLPM 161
Cdd:cd07186   81 -------------------------------GGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 162 SDDPVASIIHTPSGPMHFQEWWVGRNGEPPVEDVEFRGAERASATDAVLTAL--DDTVVIGPSNPVTSLGPMLAIDDIQR 239
Cdd:cd07186  130 SDDRVETRVVTDEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIedADLVIIGPSNPVTSIGPILALPGIRE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 240 ALHETT--VVAVSPFIEDTVFSGPAADLMAGVGLEPSTAGVAEAY-PFADSFVLDEEDST------PLDVPVVRTDTTLN 310
Cdd:cd07186  210 ALRDKKapVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYgDLLDGFVIDEADRAladaieALGIEVSRTDTLMT 289
                        330
                 ....*....|..
gi 115312127 311 DAADAERVNRAV 322
Cdd:cd07186  290 DEEDKIRLAREV 301
F420_cofD TIGR01819
2-phospho-L-lactate transferase; This model represents LPPG:Fo 2-phospho-L-lactate transferase, ...
3-322 5.40e-117

2-phospho-L-lactate transferase; This model represents LPPG:Fo 2-phospho-L-lactate transferase, which catalyses the fourth step in the biosynthesis of coenzyme F420, a flavin derivative found in methanogens, the Mycobacteria, and several other lineages. This enzyme is characterized so far in Methanococcus jannaschii but appears restricted to F420-containing species and is predicted to carry out the same function in these other species. The clade represented by this model is one of two major divisions of proteins in pfam01933. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 130878  Cd Length: 297  Bit Score: 339.80  E-value: 5.40e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127    3 TFLAGGTGTPKLLAGADDVFSPAATTVVANTGDDIELGGHLVCPDLDTVLFLDGEVLDRETWWGIADDTAETHTELTRLa 82
Cdd:TIGR01819   1 TVLSGGTGTPKLLQGLKEVLPDAELTVVVNTGEDVWVSGLLVCPDLDTVLYTLGGGIDRERWWGIADDTFHTHERLKEL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   83 daagldggprylpddaqtagrdiarwrrfsGVAEFMHIGDRDRAVHVTRTSLLDEGRSLTAVTRTLADAFGLERTLLPMS 162
Cdd:TIGR01819  80 ------------------------------GVPEGLRLGDRDRATHIVRTQMLRAGHSLSEVTEALCDAFGIKARLLPMT 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  163 DDPVASIIHTPSGPMHFQEWWVGRNGEPPVEDVEFRGAERASATDAVLTAL--DDTVVIGPSNPVTSLGPMLAIDDIQRA 240
Cdd:TIGR01819 130 DDEVSTYVETDEGAMHFQEFWVRRRGEPPVEDVDFRGAEKASIAPKVLEAIrkEDNILIGPSNPITSIGPILSLPGIREA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  241 LHETTVVAVSPFIEDTVFSGPAADLMAGVGLEPSTAGVAEAYP-FADSFVLDEEDSTPLD---VPVVRTDTTLNDAADAE 316
Cdd:TIGR01819 210 LRDKKVVAVSPIVGNAPVSGPAGKLMAAVGVEVSAAGVAEHYGdFLDVFVVDEVDKADEDrfgCHVRRTDTLMTTLEDTA 289

                  ....*.
gi 115312127  317 RVNRAV 322
Cdd:TIGR01819 290 RLARAV 295
CofD COG0391
Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family ...
1-323 1.18e-44

Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family [Carbohydrate transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440160  Cd Length: 314  Bit Score: 154.91  E-value: 1.18e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   1 MVTFLAGGTGTPKLLAGADDVfsPAATTVVANTGDDIELGGHL------VCP-DLDTVLFLdgevldretwwgIADDTae 73
Cdd:COG0391    8 KVVAIGGGTGLSTLLRGLKRY--TANLTAIVTVADDGGSSGRLrrelgvLPPgDLRNCLAA------------LADDE-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  74 thTELTRLADAagldggprylpddaqtagrdiarwrRFSGvaefmhigDRDRAVHVTRTSLLDEG----RSLTAVTRTLA 149
Cdd:COG0391   72 --PLLSRLFQY-------------------------RFSG--------GGDLAGHSLGNLLLAALteitGDFVEAIDLLS 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 150 DAFGLERTLLPMSDDPVASIIHTPSGPMHFQEWWVGRNGEpPVEDVEFRgAERASATDAVLTALD--DTVVIGPSNPVTS 227
Cdd:COG0391  117 KLLGVRGRVLPMTLDPVDLVAELEDGRIVRGESAIAKAGG-RIERVFLE-PEDAPATPEALEAIEeaDLIVLGPGSLYTS 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 228 LGPMLAIDDIQRALHET--TVVAVSPFIEdtvFSGPAadlmAGVGLEPSTAGVAEAYP--FADSFVLD------------ 291
Cdd:COG0391  195 IIPNLLVPGIAEALRETkaPKVYVCNLMT---QPGET----DGYSAADHVRALERHLGgpFIDAVLVNnapvpdellery 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 115312127 292 -EEDSTP----------LDVPVVRTDTTLNDAA---DAERVNRAVE 323
Cdd:COG0391  268 aEEGAEPveldrerleeLGVRVVRADLLDEDGPvrhDPEKLARALL 313
CofD pfam01933
2-phospho-L-lactate transferase CofD; This entry contains 2-phospho-L-lactate transferase ...
2-270 2.16e-38

2-phospho-L-lactate transferase CofD; This entry contains 2-phospho-L-lactate transferase (CofD), phosphoenolpyruvate transferase and related sequences. CofD catalyzes the fourth step in the biosynthesis of coenzyme F420, which is the transfer of the 2-phospholactate moiety from lactyl (2)diphospho-(5') guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of the L-lactyl phosphodiester of 7,8-didemethyl- 8-hydroxy-5-deazariboflavin (F420-0) and GMP. F420 is a flavin derivative found in methanogens, Mycobacteria, and several other lineages. This enzyme is characterized so far in Methanocaldococcus jannaschii (Methanococcus jannaschii) but appears restricted to F420-containing species and is predicted to carry out the same function in these other species. CofD monomer contains 12 beta- strands, seven of them form a Rossmann fold, and 13 alpha-helices.


Pssm-ID: 426519  Cd Length: 249  Bit Score: 136.42  E-value: 2.16e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127    2 VTFLAGGTGTPKLLAGADDVfsPAATTVVANTGDDIELGG-------HLVCPDLDTVLFldgEVLDRETWwgiaddtaet 74
Cdd:pfam01933   1 IVVIGGGTGLSRLLRGLKRY--TANLTAIVTVADDGGSSGrlrrelgLLPPGDIRNCLV---ALADTEPL---------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   75 HTELTRLadaagldggprylpddaqtagrdiarwrRFsgvaefmhIGDRDRAVHVTRTSLLDEGR----SLTAVTRTLAD 150
Cdd:pfam01933  66 MEELFQY----------------------------RF--------LGDGDLAGHSLGNLFLAALTeitgDFSEAIEALSK 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  151 AFGLERTLLPMSDDPVASIIHTPSGPMHFQEWWVG--RNGEPPVEDVeFRGAERASATDAVLTAL--DDTVVIGPSNPVT 226
Cdd:pfam01933 110 VLAVRGRVLPMTDDPVELHAELEDGTIVHGESWIPeaRKAKPPIKRV-FLGPEDAKALPEVLEAIeeADLIVLGPGSLYT 188
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115312127  227 SLGPMLAIDDIQRALHETT--VVAVSPFI------EDTVFSGPAADLMAGVG 270
Cdd:pfam01933 189 SIIPNLLVPGIREALRESKapKVYVSNIMtqpgetDGYTVSDHAKAIMRHLG 240
CofD_YvcK cd07044
Family of CofD-like proteins and proteins related to YvcK; CofD is a 2-phospho-L-lactate ...
2-294 9.26e-29

Family of CofD-like proteins and proteins related to YvcK; CofD is a 2-phospho-L-lactate transferase that catalyzes the last step in the biosynthesis of coenzyme F(420)-0 (F(420) without polyglutamate) by transferring the lactyl phosphate moiety of lactyl(2)diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin ribitol (F0). F420 is a hydride carrier, important for energy metabolism of methanogenic archaea, as well as for the biosynthesis of other natural products, like tetracycline in Streptomyces. F420 and some of its precursors are also utilized as cofactors for enzymes, like DNA photolyase in Mycobacterium tuberculosis. YvcK from Bacillus subtilis is a member of a family of mostly uncharacterized proteins and has been proposed to play a role in carbon metabolism, since its function is essential for growth on intermediates of the Krebs cycle and pentose phosphate pathway. Both families appear to have a conserved phosphate binding site, but have different substrate binding residues conserved within each family.


Pssm-ID: 132871  Cd Length: 309  Bit Score: 112.68  E-value: 9.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127   2 VTFLAGGTGTPKLLAGADDVfsPAATTVVANTGDDIELGGHL-------VCPDLDTVLFLDGEVLDRETWWGIaddtaet 74
Cdd:cd07044    1 VVVFGGGTGLPVLLRGLKEF--PVEITAIVTVADDGGSSGELrn*qdipPPGDLRNVLVALSDQEDRLEQLFQ------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127  75 hteltrladaagldggprylpddaqtagrdiarWRRFSGVAEFMHIGDRDRAVHVTRTSLLDEGRSltavTRTLADAFGL 154
Cdd:cd07044   72 ---------------------------------YRKEEGINEGLGHSLGNLAIAG*TSITGDFTDA----IVELSKVFNI 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115312127 155 ERTLLPMSDDPVAS-IIHTPSGPMHFQEWWVgrNGEPPVEDVEFRGAERASATDAVLTALD--DTVVIGPSNPVTSLGPM 231
Cdd:cd07044  115 KGNILPSSDDPVSLhAE*EDGTIVHGESFIP--KGEKKIDRVFLTPVDEASPSREVLEAIEkaDNIVIGPGSLYTSILPN 192
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115312127 232 LAIDDIQRALHETT--VVAVSPfiedtVFSGPAADlmagvgLEPSTAGVAEAY------PFADSFVLDEED 294
Cdd:cd07044  193 ISVPGIREALKKT*akKVYVSN-----I*TQPGET------DEYTSSDHAEALqrhlgrPFIDVVLVDEED 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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