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Conserved domains on  [gi|1549476545|gb|RVI01103|]
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protein glxC [Sinorhizobium meliloti]

Protein Classification

GXGXG domain-containing protein( domain architecture ID 10087701)

GXGXG domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GXGXG cd00504
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ...
 32-169 6.73e-33

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: 116.13  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  32 VANPRGSHAVAV---GIDGPVVVDVNGSVGYYCAGMNDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAG-------A 101
Cdd:cd00504     2 AVGTRGSRYIGKrpgLPEDTVEIIINGSAGQSFGAFMAGGTITVEGNANDYVGKGMSGGEIVIHPPAGDENGiagnvalY 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1549476545 102 TGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGDSLYEAKLFVRG 169
Cdd:cd00504    82 GATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
 
Name Accession Description Interval E-value
GXGXG cd00504
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ...
 32-169 6.73e-33

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: 116.13  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  32 VANPRGSHAVAV---GIDGPVVVDVNGSVGYYCAGMNDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAG-------A 101
Cdd:cd00504     2 AVGTRGSRYIGKrpgLPEDTVEIIINGSAGQSFGAFMAGGTITVEGNANDYVGKGMSGGEIVIHPPAGDENGiagnvalY 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1549476545 102 TGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGDSLYEAKLFVRG 169
Cdd:cd00504    82 GATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
51-138 9.04e-18

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 79.47  E-value: 9.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  51 VDVNGSVGYYCA--------GMNdGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISM 122
Cdd:COG2218   122 IEINGNAGDFLGaayrgdwrGMS-GGTIIVKGNAGDRLGDRMRRGTIIIEGDAGDFAGSRMIAGTIIVKGNAGRRPGYGM 200

                          90
                  ....*....|....*.
gi 1549476545 123 KGIDIVVHGNIGHMSA 138
Cdd:COG2218   201 KRGTIVVAGKPEELLP 216
one_C_dehyd_C TIGR03122
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ...
 51-182 2.38e-16

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: 75.45  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  51 VDVNGSVGYYC-AGMNdGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGR-------GGLLVIKGNAASRCGISM 122
Cdd:TIGR03122  83 IVVEGDVGMHVgAEMK-GGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYVGSAYRgewrgmsGGKIIVEGNAGDYLGERM 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1549476545 123 KGIDIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGDSLYEAKLFVRGTVKSLGA---DCIEKE 182
Cdd:TIGR03122 162 RGGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDELLPtfkFEGLHE 224
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
 10-157 5.78e-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: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  10 PLREFNRSLHNIqqgsndLSYEVANPRGSHAVAvgiDGPVVVDVNGSVGY-YCAGMNDGGTVTVHGSAGPGVAENMMSGK 88
Cdd:pfam01493   2 EIRNTDRSVGTI------LSGEIAKRYGEDGLP---DDTITIKFNGSAGQsFGAFLPKGLTLELEGDANDYVGKGLSGGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  89 VVIEGDA-SQYA-------------GATGrgGLLVIKGNAASRCGISMKGIDIVVHGNIGHMSAFM-GqsGHLVVLGDAG 153
Cdd:pfam01493  73 IIIYPPAeSTFKaeeniiigntclyGATG--GELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMtG--GRVVVLGKTG 148


                  ....
gi 1549476545 154 DALG 157
Cdd:pfam01493 149 RNFG 152
 
Name Accession Description Interval E-value
GXGXG cd00504
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ...
 32-169 6.73e-33

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: 116.13  E-value: 6.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  32 VANPRGSHAVAV---GIDGPVVVDVNGSVGYYCAGMNDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAG-------A 101
Cdd:cd00504     2 AVGTRGSRYIGKrpgLPEDTVEIIINGSAGQSFGAFMAGGTITVEGNANDYVGKGMSGGEIVIHPPAGDENGiagnvalY 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1549476545 102 TGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGDSLYEAKLFVRG 169
Cdd:cd00504    82 GATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
arch_gltB cd00981
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ...
 31-196 4.63e-19

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: 82.35  E-value: 4.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  31 EVANPRGSHAVAVGIDGPVVVDVNGSVGYYCAGMNDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVI 110
Cdd:cd00981    29 VLDNVLGQRYIGDGLPGNVRINIYGVPGNDLGAFMSGPTIIVYGNAQDDVGNTMNDGKIVIHGSAGDVLGYAMRGGKIFI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545 111 KGNAASRCGISMKGID-----IVVHGNIGhmsAFMGQ---SGHLVVLG------DAGDALGDSLYEAKLFVRGTVKS--L 174
Cdd:cd00981   109 RGNAGYRVGIHMKEYKdkvpvLVIGGTAG---DFLGEymaGGVIIVLGlgtdeePVGRYIGTGMHGGVIYIRGKVERskL 185

                         170       180
                  ....*....|....*....|..
gi 1549476545 175 GADCIEKEMRPEHLQKLAELLE 196
Cdd:cd00981   186 GKEVPKFELTEEDLEFIEKYIE 207
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
51-138 9.04e-18

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 79.47  E-value: 9.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  51 VDVNGSVGYYCA--------GMNdGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISM 122
Cdd:COG2218   122 IEINGNAGDFLGaayrgdwrGMS-GGTIIVKGNAGDRLGDRMRRGTIIIEGDAGDFAGSRMIAGTIIVKGNAGRRPGYGM 200

                          90
                  ....*....|....*.
gi 1549476545 123 KGIDIVVHGNIGHMSA 138
Cdd:COG2218   201 KRGTIVVAGKPEELLP 216
one_C_dehyd_C TIGR03122
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ...
 51-182 2.38e-16

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: 75.45  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  51 VDVNGSVGYYC-AGMNdGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGR-------GGLLVIKGNAASRCGISM 122
Cdd:TIGR03122  83 IVVEGDVGMHVgAEMK-GGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYVGSAYRgewrgmsGGKIIVEGNAGDYLGERM 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1549476545 123 KGIDIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGDSLYEAKLFVRGTVKSLGA---DCIEKE 182
Cdd:TIGR03122 162 RGGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDELLPtfkFEGLHE 224
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
62-157 2.54e-16

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 75.62  E-value: 2.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  62 AGMnDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGIS-------MKGIDIVVHGNIG 134
Cdd:COG2218    77 AGM-TAGEIIVEGDVGMYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEINGNAGDFLGAAyrgdwrgMSGGTIIVKGNAG 155

                          90       100
                  ....*....|....*....|....*...
gi 1549476545 135 -----HMSAfmgqsGHLVVLGDAGDALG 157
Cdd:COG2218   156 drlgdRMRR-----GTIIIEGDAGDFAG 178
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 53-172 1.85e-15

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: 72.00  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  53 VNGSVGYYCAGMNDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGR-------GGLLVIKGNAASRCGISMKGI 125
Cdd:cd00980    44 VEGDVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGGEITIKGNAGDYVGSAYRgdwrgmsGGTITIEGNAGDRLGERMRRG 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1549476545 126 DIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGdslYEAKlfvRGTVK 172
Cdd:cd00980   124 EILIKGDAGIFAGIRMNGGTIIVRGDAGAHPG---YEMK---RGTIV 164
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 53-156 5.70e-15

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: 70.84  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  53 VNGSVGYYCAGMNDGGTVTVHGSAG-------PGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISMKGI 125
Cdd:cd00980    63 VEGNAGSWAGCEMKGGEITIKGNAGdyvgsayRGDWRGMSGGTITIEGNAGDRLGERMRRGEILIKGDAGIFAGIRMNGG 142

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1549476545 126 DIVVHGNIGHMSAFMGQSGHLVVLGDAGDAL 156
Cdd:cd00980   143 TIIVRGDAGAHPGYEMKRGTIVIGGEIEELL 173
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
53-150 6.90e-15

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 71.38  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  53 VNGSVGYYCA-GMNdGGTVTVHGSAG-------PGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISMKG 124
Cdd:COG2218   105 VNGNAGSFAGaEMK-GGEIEINGNAGdflgaayRGDWRGMSGGTIIVKGNAGDRLGDRMRRGTIIIEGDAGDFAGSRMIA 183

                          90       100
                  ....*....|....*....|....*.
gi 1549476545 125 IDIVVHGNIGHMSAFMGQSGHLVVLG 150
Cdd:COG2218   184 GTIIVKGNAGRRPGYGMKRGTIVVAG 209
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 62-171 8.41e-14

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: 67.37  E-value: 8.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  62 AGMNDGGTVtVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGIS-------MKGIDIVVHGNIG 134
Cdd:cd00980    35 ARMTAGEIV-VEGDVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGGEITIKGNAGDYVGSAyrgdwrgMSGGTITIEGNAG 113

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1549476545 135 HMSAFMGQSGHLVVLGDAGDALGDSLYEAKLFVRGTV 171
Cdd:cd00980   114 DRLGERMRRGEILIKGDAGIFAGIRMNGGTIIVRGDA 150
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 51-137 1.53e-13

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: 66.99  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  51 VDVNGSVGYY--CA------GMnDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISM 122
Cdd:cd00980    80 ITIKGNAGDYvgSAyrgdwrGM-SGGTITIEGNAGDRLGERMRRGEILIKGDAGIFAGIRMNGGTIIVRGDAGAHPGYEM 158

                          90
                  ....*....|....*
gi 1549476545 123 KGIDIVVHGNIGHMS 137
Cdd:cd00980   159 KRGTIVIGGEIEELL 173
FwdC COG2218
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
79-158 3.53e-13

Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];


Pssm-ID: 441820 [Multi-domain]  Cd Length: 264  Bit Score: 66.76  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  79 GVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHM--SAFMG-----QSGHLVVLGD 151
Cdd:COG2218    74 RIGAGMTAGEIIVEGDVGMYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEINGNAGDFlgAAYRGdwrgmSGGTIIVKGN 153


                  ....*..
gi 1549476545 152 AGDALGD 158
Cdd:COG2218   154 AGDRLGD 160
one_C_dehyd_C TIGR03122
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ...
 79-172 4.62e-13

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: 66.21  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  79 GVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHM--SAFMGQS-----GHLVVLGD 151
Cdd:TIGR03122  73 RIGENMSAGEIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKGGEIIIKGNAGDYvgSAYRGEWrgmsgGKIIVEGN 152

                          90       100
                  ....*....|....*....|.
gi 1549476545 152 AGDALGDSLYEAKLFVRGTVK 172
Cdd:TIGR03122 153 AGDYLGERMRGGEILIKGNAG 173
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 80-176 2.93e-12

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: 63.14  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  80 VAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHM--SAFMGQS-----GHLVVLGDA 152
Cdd:cd00980    33 IGARMTAGEIVVEGDVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGGEITIKGNAGDYvgSAYRGDWrgmsgGTITIEGNA 112

                          90       100
                  ....*....|....*....|....
gi 1549476545 153 GDALGDSLYEAKLFVRGTVKSLGA 176
Cdd:cd00980   113 GDRLGERMRRGEILIKGDAGIFAG 136
GXGXG pfam01493
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ...
 10-157 5.78e-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: 5.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  10 PLREFNRSLHNIqqgsndLSYEVANPRGSHAVAvgiDGPVVVDVNGSVGY-YCAGMNDGGTVTVHGSAGPGVAENMMSGK 88
Cdd:pfam01493   2 EIRNTDRSVGTI------LSGEIAKRYGEDGLP---DDTITIKFNGSAGQsFGAFLPKGLTLELEGDANDYVGKGLSGGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1549476545  89 VVIEGDA-SQYA-------------GATGrgGLLVIKGNAASRCGISMKGIDIVVHGNIGHMSAFM-GqsGHLVVLGDAG 153
Cdd:pfam01493  73 IIIYPPAeSTFKaeeniiigntclyGATG--GELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMtG--GRVVVLGKTG 148


                  ....
gi 1549476545 154 DALG 157
Cdd:pfam01493 149 RNFG 152
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 88-161 9.07e-08

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: 50.81  E-value: 9.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1549476545  88 KVVIEGDAS--QYAGATGRGGLLVIKGNAASRCGISMKGIDIVVHGNIGHMSAFMGQSGHLVVLGDAGDALGDSLY 161
Cdd:cd00980    20 KLVIEGDVPrlKRIGARMTAGEIVVEGDVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGGEITIKGNAGDYVGSAYR 95
FwdC/FmdC cd00980
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ...
 44-116 1.45e-04

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: 41.57  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1549476545  44 GIDGPVVVdVNGSVGYYCAGMNDGGTVTVHGSAGPGVAENMMSGKVVIEGDASQYAGATGRGGLLVIKGNAAS 116
Cdd:cd00980   100 GMSGGTIT-IEGNAGDRLGERMRRGEILIKGDAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIGGEIEE 171
NAD_bind_1_Glu_DH cd01076
NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is ...
 100-148 1.55e-03

NAD(P) binding domain of glutamate dehydrogenase, subgroup 1; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. Glutamate DH is a multidomain enzyme that catalyzes the reaction from glutamate to 2-oxyoglutarate and ammonia in the presence of NAD or NADP. It is present in all organisms. Enzymes involved in ammonia assimilation are typically NADP+-dependent, while those involved in glutamate catabolism are generally NAD+-dependent. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha -beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133445 [Multi-domain]  Cd Length: 227  Bit Score: 38.67  E-value: 1.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1549476545 100 GATGRGGLLVIKgNAASRCGISMKGIDIVVH--GNIGHMSA-FMGQSGHLVV 148
Cdd:cd01076     8 EATGRGVAYATR-EALKKLGIGLAGARVAIQgfGNVGSHAArFLHEAGAKVV 58
 
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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