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Conserved domains on  [gi|503817269|ref|WP_014051263|]
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2-phospho-L-lactate transferase [Halolamina sp.]

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 6.95e-116

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: 338.03  E-value: 6.95e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   2 VTFLAGGTGTPKLLSGESPVFARDAVTVVGNTGDDVELGGLLVSPDLDTVLFDGGGVLDRETWWGIAGDSHETDDELFAL 81
Cdd:cd07186    1 IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDTFNTLEALERL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  82 adaagletgprylddaaqtsgrdivrwrrfsGVGEFMTIGDRDRAVHITRTSLLDEGHTLTEATRTLADAFDLEIDLLPM 161
Cdd:cd07186   81 -------------------------------GGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 162 SDDPVATIIHTPDGAMHFQEYWVANRAAPRVEDVEFRGASRAQPTAAVHAAL--SEPVVVGPSNPVTSVGPIRALPAVDR 239
Cdd:cd07186  130 SDDRVETRVVTDEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIedADLVIIGPSNPVTSIGPILALPGIRE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 240 ALHQT--PVVAVSPFLEDEPFSGPVAELMAGVDREPSTAGVANTYA-FADAFVLDSQDET------TLDRPVVRTDTNID 310
Cdd:cd07186  210 ALRDKkaPVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYGdLLDGFVIDEADRAladaieALGIEVSRTDTLMT 289
                        330
                 ....*....|..
gi 503817269 311 EPEDAERVARAC 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 6.95e-116

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: 338.03  E-value: 6.95e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   2 VTFLAGGTGTPKLLSGESPVFARDAVTVVGNTGDDVELGGLLVSPDLDTVLFDGGGVLDRETWWGIAGDSHETDDELFAL 81
Cdd:cd07186    1 IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDTFNTLEALERL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  82 adaagletgprylddaaqtsgrdivrwrrfsGVGEFMTIGDRDRAVHITRTSLLDEGHTLTEATRTLADAFDLEIDLLPM 161
Cdd:cd07186   81 -------------------------------GGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 162 SDDPVATIIHTPDGAMHFQEYWVANRAAPRVEDVEFRGASRAQPTAAVHAAL--SEPVVVGPSNPVTSVGPIRALPAVDR 239
Cdd:cd07186  130 SDDRVETRVVTDEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIedADLVIIGPSNPVTSIGPILALPGIRE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 240 ALHQT--PVVAVSPFLEDEPFSGPVAELMAGVDREPSTAGVANTYA-FADAFVLDSQDET------TLDRPVVRTDTNID 310
Cdd:cd07186  210 ALRDKkaPVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYGdLLDGFVIDEADRAladaieALGIEVSRTDTLMT 289
                        330
                 ....*....|..
gi 503817269 311 EPEDAERVARAC 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 1.19e-110

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: 324.77  E-value: 1.19e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269    3 TFLAGGTGTPKLLSGESPVFARDAVTVVGNTGDDVELGGLLVSPDLDTVLFDGGGVLDRETWWGIAGDSHETDDELFALa 82
Cdd:TIGR01819   1 TVLSGGTGTPKLLQGLKEVLPDAELTVVVNTGEDVWVSGLLVCPDLDTVLYTLGGGIDRERWWGIADDTFHTHERLKEL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   83 daagletgprylddaaqtsgrdivrwrrfsGVGEFMTIGDRDRAVHITRTSLLDEGHTLTEATRTLADAFDLEIDLLPMS 162
Cdd:TIGR01819  80 ------------------------------GVPEGLRLGDRDRATHIVRTQMLRAGHSLSEVTEALCDAFGIKARLLPMT 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  163 DDPVATIIHTPDGAMHFQEYWVANRAAPRVEDVEFRGASRAQPTAAVHAAL--SEPVVVGPSNPVTSVGPIRALPAVDRA 240
Cdd:TIGR01819 130 DDEVSTYVETDEGAMHFQEFWVRRRGEPPVEDVDFRGAEKASIAPKVLEAIrkEDNILIGPSNPITSIGPILSLPGIREA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  241 LHQTPVVAVSPFLEDEPFSGPVAELMAGVDREPSTAGVANTYA-FADAFVLDSQDETTLDR---PVVRTDTNIDEPEDAE 316
Cdd:TIGR01819 210 LRDKKVVAVSPIVGNAPVSGPAGKLMAAVGVEVSAAGVAEHYGdFLDVFVVDEVDKADEDRfgcHVRRTDTLMTTLEDTA 289

                  ....*.
gi 503817269  317 RVARAC 322
Cdd:TIGR01819 290 RLARAV 295
CofD COG0391
Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family ...
1-322 3.21e-39

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: 141.43  E-value: 3.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   1 MVTFLAGGTGTPKLLSGESPVFARdaVTVVGNTGDDVELGGLL------VSP-DLDTVLFdgggvldretwwgiagdshe 73
Cdd:COG0391    8 KVVAIGGGTGLSTLLRGLKRYTAN--LTAIVTVADDGGSSGRLrrelgvLPPgDLRNCLA-------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  74 tddelfALADaagletGPRYLDDAAQtsgrdivrwRRFSGVGefmtigdrDRAVHITRTSLLDEG----HTLTEATRTLA 149
Cdd:COG0391   66 ------ALAD------DEPLLSRLFQ---------YRFSGGG--------DLAGHSLGNLLLAALteitGDFVEAIDLLS 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 150 DAFDLEIDLLPMSDDPVATIIHTPDGAMHFQEYWVANRAApRVEDVEFRgASRAQPTAAVHAALSE--PVVVGPSNPVTS 227
Cdd:COG0391  117 KLLGVRGRVLPMTLDPVDLVAELEDGRIVRGESAIAKAGG-RIERVFLE-PEDAPATPEALEAIEEadLIVLGPGSLYTS 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 228 VGPIRALPAVDRALHQT--PVVAVSPFLedePFSGPVaelmAGVDREPSTAGVANTY--AFADAFVLDSQ--DETTLDR- 300
Cdd:COG0391  195 IIPNLLVPGIAEALRETkaPKVYVCNLM---TQPGET----DGYSAADHVRALERHLggPFIDAVLVNNApvPDELLERy 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 503817269 301 --------------------PVVRTD-TNIDEPE--DAERVARAC 322
Cdd:COG0391  268 aeegaepveldrerleelgvRVVRADlLDEDGPVrhDPEKLARAL 312
CofD pfam01933
2-phospho-L-lactate transferase CofD; This entry contains 2-phospho-L-lactate transferase ...
2-267 3.90e-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: 136.80  E-value: 3.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269    2 VTFLAGGTGTPKLLSGESPVFARdaVTVVGNTGDDVELGG-------LLVSPDLDTVLFdggGVLDRETWWgiagdshet 74
Cdd:pfam01933   1 IVVIGGGTGLSRLLRGLKRYTAN--LTAIVTVADDGGSSGrlrrelgLLPPGDIRNCLV---ALADTEPLM--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   75 dDELFALadaagletgprylddaaqtsgrdivrwrRFsgvgefmtIGDRDRAVHITRTSLL----DEGHTLTEATRTLAD 150
Cdd:pfam01933  67 -EELFQY----------------------------RF--------LGDGDLAGHSLGNLFLaaltEITGDFSEAIEALSK 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  151 AFDLEIDLLPMSDDPVATIIHTPDGAMHFQEYWV--ANRAAPRVEDVeFRGASRAQPTAAVHAALSEP--VVVGPSNPVT 226
Cdd:pfam01933 110 VLAVRGRVLPMTDDPVELHAELEDGTIVHGESWIpeARKAKPPIKRV-FLGPEDAKALPEVLEAIEEAdlIVLGPGSLYT 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 503817269  227 SVGPIRALPAVDRALHQT--PVVAVSPFL------EDEPFSGPVAELMA 267
Cdd:pfam01933 189 SIIPNLLVPGIREALRESkaPKVYVSNIMtqpgetDGYTVSDHAKAIMR 237
 
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 6.95e-116

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: 338.03  E-value: 6.95e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   2 VTFLAGGTGTPKLLSGESPVFARDAVTVVGNTGDDVELGGLLVSPDLDTVLFDGGGVLDRETWWGIAGDSHETDDELFAL 81
Cdd:cd07186    1 IVVLSGGTGGAKLLRGLKRVLDPEELTVVVNTGDDFWLSGLYVSPDLDTVLYTLAGLIDRETGWGIEGDTFNTLEALERL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  82 adaagletgprylddaaqtsgrdivrwrrfsGVGEFMTIGDRDRAVHITRTSLLDEGHTLTEATRTLADAFDLEIDLLPM 161
Cdd:cd07186   81 -------------------------------GGEEWFRLGDRDRATHILRTEMLREGKSLSEVTAELAERLGIKARILPM 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 162 SDDPVATIIHTPDGAMHFQEYWVANRAAPRVEDVEFRGASRAQPTAAVHAAL--SEPVVVGPSNPVTSVGPIRALPAVDR 239
Cdd:cd07186  130 SDDRVETRVVTDEGDLHFQEYWVRRRGEPEVRDVRFVGAEEARPAPEVLEAIedADLVIIGPSNPVTSIGPILALPGIRE 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 240 ALHQT--PVVAVSPFLEDEPFSGPVAELMAGVDREPSTAGVANTYA-FADAFVLDSQDET------TLDRPVVRTDTNID 310
Cdd:cd07186  210 ALRDKkaPVVAVSPIIGGKAVSGPAAKLMAALGFEPSAAGVAEIYGdLLDGFVIDEADRAladaieALGIEVSRTDTLMT 289
                        330
                 ....*....|..
gi 503817269 311 EPEDAERVARAC 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 1.19e-110

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: 324.77  E-value: 1.19e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269    3 TFLAGGTGTPKLLSGESPVFARDAVTVVGNTGDDVELGGLLVSPDLDTVLFDGGGVLDRETWWGIAGDSHETDDELFALa 82
Cdd:TIGR01819   1 TVLSGGTGTPKLLQGLKEVLPDAELTVVVNTGEDVWVSGLLVCPDLDTVLYTLGGGIDRERWWGIADDTFHTHERLKEL- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   83 daagletgprylddaaqtsgrdivrwrrfsGVGEFMTIGDRDRAVHITRTSLLDEGHTLTEATRTLADAFDLEIDLLPMS 162
Cdd:TIGR01819  80 ------------------------------GVPEGLRLGDRDRATHIVRTQMLRAGHSLSEVTEALCDAFGIKARLLPMT 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  163 DDPVATIIHTPDGAMHFQEYWVANRAAPRVEDVEFRGASRAQPTAAVHAAL--SEPVVVGPSNPVTSVGPIRALPAVDRA 240
Cdd:TIGR01819 130 DDEVSTYVETDEGAMHFQEFWVRRRGEPPVEDVDFRGAEKASIAPKVLEAIrkEDNILIGPSNPITSIGPILSLPGIREA 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  241 LHQTPVVAVSPFLEDEPFSGPVAELMAGVDREPSTAGVANTYA-FADAFVLDSQDETTLDR---PVVRTDTNIDEPEDAE 316
Cdd:TIGR01819 210 LRDKKVVAVSPIVGNAPVSGPAGKLMAAVGVEVSAAGVAEHYGdFLDVFVVDEVDKADEDRfgcHVRRTDTLMTTLEDTA 289

                  ....*.
gi 503817269  317 RVARAC 322
Cdd:TIGR01819 290 RLARAV 295
CofD COG0391
Archaeal 2-phospho-L-lactate transferase/Bacterial gluconeogenesis factor, CofD/UPF0052 family ...
1-322 3.21e-39

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: 141.43  E-value: 3.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   1 MVTFLAGGTGTPKLLSGESPVFARdaVTVVGNTGDDVELGGLL------VSP-DLDTVLFdgggvldretwwgiagdshe 73
Cdd:COG0391    8 KVVAIGGGTGLSTLLRGLKRYTAN--LTAIVTVADDGGSSGRLrrelgvLPPgDLRNCLA-------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  74 tddelfALADaagletGPRYLDDAAQtsgrdivrwRRFSGVGefmtigdrDRAVHITRTSLLDEG----HTLTEATRTLA 149
Cdd:COG0391   66 ------ALAD------DEPLLSRLFQ---------YRFSGGG--------DLAGHSLGNLLLAALteitGDFVEAIDLLS 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 150 DAFDLEIDLLPMSDDPVATIIHTPDGAMHFQEYWVANRAApRVEDVEFRgASRAQPTAAVHAALSE--PVVVGPSNPVTS 227
Cdd:COG0391  117 KLLGVRGRVLPMTLDPVDLVAELEDGRIVRGESAIAKAGG-RIERVFLE-PEDAPATPEALEAIEEadLIVLGPGSLYTS 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 228 VGPIRALPAVDRALHQT--PVVAVSPFLedePFSGPVaelmAGVDREPSTAGVANTY--AFADAFVLDSQ--DETTLDR- 300
Cdd:COG0391  195 IIPNLLVPGIAEALRETkaPKVYVCNLM---TQPGET----DGYSAADHVRALERHLggPFIDAVLVNNApvPDELLERy 267
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 503817269 301 --------------------PVVRTD-TNIDEPE--DAERVARAC 322
Cdd:COG0391  268 aeegaepveldrerleelgvRVVRADlLDEDGPVrhDPEKLARAL 312
CofD pfam01933
2-phospho-L-lactate transferase CofD; This entry contains 2-phospho-L-lactate transferase ...
2-267 3.90e-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: 136.80  E-value: 3.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269    2 VTFLAGGTGTPKLLSGESPVFARdaVTVVGNTGDDVELGG-------LLVSPDLDTVLFdggGVLDRETWWgiagdshet 74
Cdd:pfam01933   1 IVVIGGGTGLSRLLRGLKRYTAN--LTAIVTVADDGGSSGrlrrelgLLPPGDIRNCLV---ALADTEPLM--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   75 dDELFALadaagletgprylddaaqtsgrdivrwrRFsgvgefmtIGDRDRAVHITRTSLL----DEGHTLTEATRTLAD 150
Cdd:pfam01933  67 -EELFQY----------------------------RF--------LGDGDLAGHSLGNLFLaaltEITGDFSEAIEALSK 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  151 AFDLEIDLLPMSDDPVATIIHTPDGAMHFQEYWV--ANRAAPRVEDVeFRGASRAQPTAAVHAALSEP--VVVGPSNPVT 226
Cdd:pfam01933 110 VLAVRGRVLPMTDDPVELHAELEDGTIVHGESWIpeARKAKPPIKRV-FLGPEDAKALPEVLEAIEEAdlIVLGPGSLYT 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 503817269  227 SVGPIRALPAVDRALHQT--PVVAVSPFL------EDEPFSGPVAELMA 267
Cdd:pfam01933 189 SIIPNLLVPGIREALRESkaPKVYVSNIMtqpgetDGYTVSDHAKAIMR 237
CofD_YvcK cd07044
Family of CofD-like proteins and proteins related to YvcK; CofD is a 2-phospho-L-lactate ...
2-251 2.00e-27

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: 109.59  E-value: 2.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269   2 VTFLAGGTGTPKLLSG--ESPVFARDAVTVV---GNTGDDVELGGLLVSPDLDTVLFDGGGVLDRETWWGIagdshetdd 76
Cdd:cd07044    1 VVVFGGGTGLPVLLRGlkEFPVEITAIVTVAddgGSSGELRN*QDIPPPGDLRNVLVALSDQEDRLEQLFQ--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269  77 elfaladaagletgprylddaaqtsgrdivrWRRFSGVGEFMTIGDRDRAVHITRTSLLDEGHtlteATRTLADAFDLEI 156
Cdd:cd07044   72 -------------------------------YRKEEGINEGLGHSLGNLAIAG*TSITGDFTD----AIVELSKVFNIKG 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503817269 157 DLLPMSDDPVATIIHTPDGAM-HFQEYWVanRAAPRVEDVEFRGASRAQPTAAVHAAL--SEPVVVGPSNPVTSVGPIRA 233
Cdd:cd07044  117 NILPSSDDPVSLHAE*EDGTIvHGESFIP--KGEKKIDRVFLTPVDEASPSREVLEAIekADNIVIGPGSLYTSILPNIS 194
                        250       260
                 ....*....|....*....|
gi 503817269 234 LPAVDRALHQT--PVVAVSP 251
Cdd:cd07044  195 VPGIREALKKT*aKKVYVSN 214
 
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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