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Conserved domains on  [gi|499329406|ref|WP_011019898|]
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formylmethanofuran dehydrogenase subunit C [Methanopyrus kandleri]

Protein Classification

similar to tungsten-containing formylmethanofuran dehydrogenase 2 subunit C( domain architecture ID 10022140)

protein similar to tungsten-containing formylmethanofuran dehydrogenase 2 subunit C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
one_C_dehyd_C TIGR03122
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ...
4-258 5.60e-124

formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.


:

Pssm-ID: 274439 [Multi-domain]  Cd Length: 257  Bit Score: 353.18  E-value: 5.60e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406    4 VVLTPKGEPDVPLEAEVICPDEFAGKSEGEIEALKIYEGNSTVELGEYFDVEGDagDSPGDTRIVIEGDVPWVKLIGYRM 83
Cdd:TIGR03122   1 LTLTPKKEPSVPLEADPILPDNLAGKSAEEIEALELWYGNKTVPLGDLFDVEGD--GKPDETRLVIDGDMSRVKRIGENM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406   84 SAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGDEIG 163
Cdd:TIGR03122  79 SAGEIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYVGSAYRGEWRGMSGGKIIVEGNAGDYLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  164 EWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCGRAEDILPSFRYEGLKEDPV------EEATG 237
Cdd:TIGR03122 159 ERMRGGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDELLPTFKFEGLHELPFllksafTQAIG 238
                         250       260
                  ....*....|....*....|.
gi 499329406  238 TFHLFTGDYANGPKveGELYL 258
Cdd:TIGR03122 239 TFHKFTGDYANKGK--GELYI 257
 
Name Accession Description Interval E-value
one_C_dehyd_C TIGR03122
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ...
4-258 5.60e-124

formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.


Pssm-ID: 274439 [Multi-domain]  Cd Length: 257  Bit Score: 353.18  E-value: 5.60e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406    4 VVLTPKGEPDVPLEAEVICPDEFAGKSEGEIEALKIYEGNSTVELGEYFDVEGDagDSPGDTRIVIEGDVPWVKLIGYRM 83
Cdd:TIGR03122   1 LTLTPKKEPSVPLEADPILPDNLAGKSAEEIEALELWYGNKTVPLGDLFDVEGD--GKPDETRLVIDGDMSRVKRIGENM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406   84 SAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGDEIG 163
Cdd:TIGR03122  79 SAGEIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYVGSAYRGEWRGMSGGKIIVEGNAGDYLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  164 EWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCGRAEDILPSFRYEGLKEDPV------EEATG 237
Cdd:TIGR03122 159 ERMRGGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDELLPTFKFEGLHELPFllksafTQAIG 238
                         250       260
                  ....*....|....*....|.
gi 499329406  238 TFHLFTGDYANGPKveGELYL 258
Cdd:TIGR03122 239 TFHKFTGDYANKGK--GELYI 257
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
1-258 8.50e-121

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 345.26  E-value: 8.50e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406   1 MKEVVLTPKGEPDVPLEAEVICPDEFAGKSEGEIEALKIYEGNSTVELGEYFDVEGDagdsPGDTRIVIEGDVPWVKLIG 80
Cdd:COG2218    1 MSTLTLTLKAEPELRLEASGITPDALAGKSAAEIAALPVWEGNRKVPLGDLFDVEGD----DGDTKIVIEGDLSRVKRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  81 YRMSAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGD 160
Cdd:COG2218   77 AGMTAGEIIVEGDVGMYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEINGNAGDFLGAAYRGDWRGMSGGTIIVKGNAGD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406 161 EIGEWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCGRAEDILPSFRYEGLKEDPV-------- 232
Cdd:COG2218  157 RLGDRMRRGTIIIEGDAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPEELLPTFVDCGTHELVFlrllakap 236
                        250       260
                 ....*....|....*....|....*...
gi 499329406 233 --EEATGTFHLFTGDYANGPKveGELYL 258
Cdd:COG2218  237 faELDGRRFRRYAGDLAVKGK--GELLV 262
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
45-246 3.90e-97

FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.


Pssm-ID: 238480 [Multi-domain]  Cd Length: 203  Bit Score: 283.09  E-value: 3.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  45 TVELGEYFDVEGDAGDspGDTRIVIEGDVPWVKLIGYRMSAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGG 124
Cdd:cd00980    1 RVPLGDFFEVSGDGAD--ADTKLVIEGDVPRLKRIGARMTAGEIVVEGDVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406 125 EITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGDEIGEWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQM 204
Cdd:cd00980   79 EITIKGNAGDYVGSAYRGDWRGMSGGTITIEGNAGDRLGERMRRGEILIKGDAGIFAGIRMNGGTIIVRGDAGAHPGYEM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 499329406 205 EGGTVVVCGRAEDILPSFRYEGLKEDPV---EEATGTFHLFTGDY 246
Cdd:cd00980  159 KRGTIVIGGEIEELLPTFKEEGTEEDVFvsgEELSGTFYKFTGDL 203
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
102-207 3.37e-12

GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran dehydrogenase subunit c (FwdC) and molybdenum formylmethanofuran dehydrogenase subunit c (FmdC). A repeated G-XX-G-XXX-G motif is seen in the alignment.


Pssm-ID: 460231 [Multi-domain]  Cd Length: 190  Bit Score: 63.59  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  102 MKGGKLIVEGDADDWLGREMKGGEITVHGNAgnyvGSTYRGEWR---------GMSGGRILVKGDAGDEIGEWMSDGKII 172
Cdd:pfam01493  49 PKGLTLELEGDANDYVGKGLSGGKIIIYPPA----ESTFKAEENiiigntclyGATGGELFINGRAGERFAVRNSGATAV 124
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499329406  173 VEGdAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGG 207
Cdd:pfam01493 125 VEG-VGDHGCEYMTGGRVVVLGKTGRNFGAGMSGG 158
 
Name Accession Description Interval E-value
one_C_dehyd_C TIGR03122
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ...
4-258 5.60e-124

formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.


Pssm-ID: 274439 [Multi-domain]  Cd Length: 257  Bit Score: 353.18  E-value: 5.60e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406    4 VVLTPKGEPDVPLEAEVICPDEFAGKSEGEIEALKIYEGNSTVELGEYFDVEGDagDSPGDTRIVIEGDVPWVKLIGYRM 83
Cdd:TIGR03122   1 LTLTPKKEPSVPLEADPILPDNLAGKSAEEIEALELWYGNKTVPLGDLFDVEGD--GKPDETRLVIDGDMSRVKRIGENM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406   84 SAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGDEIG 163
Cdd:TIGR03122  79 SAGEIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYVGSAYRGEWRGMSGGKIIVEGNAGDYLG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  164 EWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCGRAEDILPSFRYEGLKEDPV------EEATG 237
Cdd:TIGR03122 159 ERMRGGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDELLPTFKFEGLHELPFllksafTQAIG 238
                         250       260
                  ....*....|....*....|.
gi 499329406  238 TFHLFTGDYANGPKveGELYL 258
Cdd:TIGR03122 239 TFHKFTGDYANKGK--GELYI 257
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
1-258 8.50e-121

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 345.26  E-value: 8.50e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406   1 MKEVVLTPKGEPDVPLEAEVICPDEFAGKSEGEIEALKIYEGNSTVELGEYFDVEGDagdsPGDTRIVIEGDVPWVKLIG 80
Cdd:COG2218    1 MSTLTLTLKAEPELRLEASGITPDALAGKSAAEIAALPVWEGNRKVPLGDLFDVEGD----DGDTKIVIEGDLSRVKRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  81 YRMSAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGD 160
Cdd:COG2218   77 AGMTAGEIIVEGDVGMYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEINGNAGDFLGAAYRGDWRGMSGGTIIVKGNAGD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406 161 EIGEWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCGRAEDILPSFRYEGLKEDPV-------- 232
Cdd:COG2218  157 RLGDRMRRGTIIIEGDAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPEELLPTFVDCGTHELVFlrllakap 236
                        250       260
                 ....*....|....*....|....*...
gi 499329406 233 --EEATGTFHLFTGDYANGPKveGELYL 258
Cdd:COG2218  237 faELDGRRFRRYAGDLAVKGK--GELLV 262
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
45-246 3.90e-97

FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.


Pssm-ID: 238480 [Multi-domain]  Cd Length: 203  Bit Score: 283.09  E-value: 3.90e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  45 TVELGEYFDVEGDAGDspGDTRIVIEGDVPWVKLIGYRMSAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGG 124
Cdd:cd00980    1 RVPLGDFFEVSGDGAD--ADTKLVIEGDVPRLKRIGARMTAGEIVVEGDVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406 125 EITVHGNAGNYVGSTYRGEWRGMSGGRILVKGDAGDEIGEWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQM 204
Cdd:cd00980   79 EITIKGNAGDYVGSAYRGDWRGMSGGTITIEGNAGDRLGERMRRGEILIKGDAGIFAGIRMNGGTIIVRGDAGAHPGYEM 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 499329406 205 EGGTVVVCGRAEDILPSFRYEGLKEDPV---EEATGTFHLFTGDY 246
Cdd:cd00980  159 KRGTIVIGGEIEELLPTFKEEGTEEDVFvsgEELSGTFYKFTGDL 203
GXGXG cd00504
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ...
76-213 1.23e-45

GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS), in subunit C of tungsten formylmethanofuran dehydrogenase (FwdC) and in subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC). It is also found in a primarily archeal group of proteins predicted to encode part of the large subunit of GltS. It is characterized by a repeated GXXGXXXG motif. GltS is a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites occur in other domains within the protein or or encoded by separate genes, and are not present in the domain in this CD. FwdC and FmdC are reversible ion pumps that catalyze the formylation and deformylation of methanofuran in hyperthermophiles and bacteria. They require the presence of either tungstun (FwdC) or molybdenum (FmdC). The specific function of this domain also remains unidentified in the formylmethanofuran dehydrogenases.


Pssm-ID: 238281 [Multi-domain]  Cd Length: 149  Bit Score: 150.03  E-value: 1.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  76 VKLIGYRMSAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYRGEWRGMSGGRILVK 155
Cdd:cd00504   12 GKRPGLPEDTVEIIINGSAGQSFGAFMAGGTITVEGNANDYVGKGMSGGEIVIHPPAGDENGIAGNVALYGATGGKIFVR 91
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499329406 156 GDAGDEIGEWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCG 213
Cdd:cd00504   92 GNAGERFGVRMSGGTIVVEGVGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
arch_gltB cd00981
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ...
62-196 4.78e-17

Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.


Pssm-ID: 238481 [Multi-domain]  Cd Length: 232  Bit Score: 77.72  E-value: 4.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  62 PGDTRIVIEGdVPWVKLiGYRMSAGEILVKGDVGRHAGAEMKGGKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTYR 141
Cdd:cd00981   44 PGNVRINIYG-VPGNDL-GAFMSGPTIIVYGNAQDDVGNTMNDGKIVIHGSAGDVLGYAMRGGKIFIRGNAGYRVGIHMK 121
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499329406 142 GEWRgmSGGRILVKGDAGDEIGEWMSDGKIIVEG------DAGIMIGIHMQGGTIIVRGDV 196
Cdd:cd00981  122 EYKD--KVPVLVIGGTAGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIYIRGKV 180
arch_gltB cd00981
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ...
96-226 4.58e-14

Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.


Pssm-ID: 238481 [Multi-domain]  Cd Length: 232  Bit Score: 69.64  E-value: 4.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  96 RHAGAEMKG-GKLIVEGDADDWLGREMKGGEITVHGNAGNYVGSTyrgewrgMSGGRILVKGDAGDEIGEWMSDGKIIVE 174
Cdd:cd00981   37 RYIGDGLPGnVRINIYGVPGNDLGAFMSGPTIIVYGNAQDDVGNT-------MNDGKIVIHGSAGDVLGYAMRGGKIFIR 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499329406 175 GDAGIMIGIHMQ-----GGTIIVRGDVGVRPGAQMEGGTVVVCGRAEDILPSFRYEG 226
Cdd:cd00981  110 GNAGYRVGIHMKeykdkVPVLVIGGTAGDFLGEYMAGGVIIVLGLGTDEEPVGRYIG 166
arch_gltB cd00981
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ...
51-157 1.35e-12

Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.


Pssm-ID: 238481 [Multi-domain]  Cd Length: 232  Bit Score: 65.40  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  51 YFDVEGDAGDSPGDTRIVIEGDVPWVklIGYRMSAGEILVKGDVGRHAGAEMKGGK-----LIVEGDADDWLGREMKGGE 125
Cdd:cd00981   71 YGNAQDDVGNTMNDGKIVIHGSAGDV--LGYAMRGGKIFIRGNAGYRVGIHMKEYKdkvpvLVIGGTAGDFLGEYMAGGV 148
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 499329406 126 ITVHGN------AGNYVGStyrgewrGMSGGRILVKGD 157
Cdd:cd00981  149 IIVLGLgtdeepVGRYIGT-------GMHGGVIYIRGK 179
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
102-207 3.37e-12

GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran dehydrogenase subunit c (FwdC) and molybdenum formylmethanofuran dehydrogenase subunit c (FmdC). A repeated G-XX-G-XXX-G motif is seen in the alignment.


Pssm-ID: 460231 [Multi-domain]  Cd Length: 190  Bit Score: 63.59  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  102 MKGGKLIVEGDADDWLGREMKGGEITVHGNAgnyvGSTYRGEWR---------GMSGGRILVKGDAGDEIGEWMSDGKII 172
Cdd:pfam01493  49 PKGLTLELEGDANDYVGKGLSGGKIIIYPPA----ESTFKAEENiiigntclyGATGGELFINGRAGERFAVRNSGATAV 124
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499329406  173 VEGdAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGG 207
Cdd:pfam01493 125 VEG-VGDHGCEYMTGGRVVVLGKTGRNFGAGMSGG 158
gltB_C cd00982
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ...
102-211 7.90e-08

gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS). GltS encodes a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites appear to occur in other domains within the protein, and not the domain in this CD. This particular domain has no known function, but it likely has a structural role as it interacts with the amidotransferase and FMN-binding domains of gltS.


Pssm-ID: 238482 [Multi-domain]  Cd Length: 251  Bit Score: 51.76  E-value: 7.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406 102 MKGGKLIVEGDADDWLGREMKGGEITV----------HGN--AGNYVGstYrgewrGMSGGRILVKGDAGDEIGEWMSDG 169
Cdd:cd00982   72 AKGVTLELEGDANDYVGKGLSGGRIVVrppkdatfkpEENiiIGNVCL--Y-----GATSGEAFIRGRAGERFAVRNSGA 144
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499329406 170 KIIVEGdagimIGIH----MQGGTIIVRGDVGVRPGAQMEGGTVVV 211
Cdd:cd00982  145 TAVVEG-----VGDHgceyMTGGTVVVLGKTGRNFAAGMSGGVAYV 185
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
121-214 8.99e-08

GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran dehydrogenase subunit c (FwdC) and molybdenum formylmethanofuran dehydrogenase subunit c (FmdC). A repeated G-XX-G-XXX-G motif is seen in the alignment.


Pssm-ID: 460231 [Multi-domain]  Cd Length: 190  Bit Score: 50.88  E-value: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406  121 MKGGEITVHGNAGNYVGstyrgewRGMSGGRILVKGDA------------GDEIGEWMSDGKIIVEGDAGIMIGIHMQGG 188
Cdd:pfam01493  49 PKGLTLELEGDANDYVG-------KGLSGGKIIIYPPAestfkaeeniiiGNTCLYGATGGELFINGRAGERFAVRNSGA 121
                          90       100
                  ....*....|....*....|....*.
gi 499329406  189 TIIVRGdVGVRPGAQMEGGTVVVCGR 214
Cdd:pfam01493 122 TAVVEG-VGDHGCEYMTGGRVVVLGK 146
GXGXG cd00504
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ...
156-217 1.02e-04

GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS), in subunit C of tungsten formylmethanofuran dehydrogenase (FwdC) and in subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC). It is also found in a primarily archeal group of proteins predicted to encode part of the large subunit of GltS. It is characterized by a repeated GXXGXXXG motif. GltS is a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites occur in other domains within the protein or or encoded by separate genes, and are not present in the domain in this CD. FwdC and FmdC are reversible ion pumps that catalyze the formylation and deformylation of methanofuran in hyperthermophiles and bacteria. They require the presence of either tungstun (FwdC) or molybdenum (FmdC). The specific function of this domain also remains unidentified in the formylmethanofuran dehydrogenases.


Pssm-ID: 238281 [Multi-domain]  Cd Length: 149  Bit Score: 41.40  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499329406 156 GDAGDEIGEWMSDGKIIVEGDAGIMIGIHMQGGTIIVRGDVGVRPGAQMEGGTVVVCGRAED 217
Cdd:cd00504    9 RYIGKRPGLPEDTVEIIINGSAGQSFGAFMAGGTITVEGNANDYVGKGMSGGEIVIHPPAGD 70
gltB_C cd00982
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ...
121-214 4.59e-03

gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate synthase (GltS). GltS encodes a complex iron-sulfur flavoprotein that catalyzes the synthesis of L-glutamate from L-glutamine and 2-oxoglutarate. It requires the transfer of ammonia and electrons among three distinct active centers that carry out L-Gln hydrolysis, conversion of 2-oxoglutarate into L-Glu, and electron uptake from a donor. These catalytic sites appear to occur in other domains within the protein, and not the domain in this CD. This particular domain has no known function, but it likely has a structural role as it interacts with the amidotransferase and FMN-binding domains of gltS.


Pssm-ID: 238482 [Multi-domain]  Cd Length: 251  Bit Score: 37.51  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499329406 121 MKGGEITVHGNAGNYVGstyrgewRGMSGGRILVK--GDAGDEIGEWM----------SDGKIIVEGDAGIMIGIHMQGG 188
Cdd:cd00982   72 AKGVTLELEGDANDYVG-------KGLSGGRIVVRppKDATFKPEENIiignvclygaTSGEAFIRGRAGERFAVRNSGA 144
                         90       100
                 ....*....|....*....|....*.
gi 499329406 189 TIIVRGdVGVRPGAQMEGGTVVVCGR 214
Cdd:cd00982  145 TAVVEG-VGDHGCEYMTGGTVVVLGK 169
 
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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