|
Name |
Accession |
Description |
Interval |
E-value |
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
1-369 |
0e+00 |
|
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439840 [Multi-domain] Cd Length: 1508 Bit Score: 628.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 1 CPVGVATQNEELRKRFVGRSEYLINFFKFLAQEIRETLAEIGVRKLDDVIGRADMLEVKPQHATHKTTHLDFSRILYMPA 80
Cdd:COG0070 1138 CPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPD 1217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 81 ECRTNAIINVTEQQHDIAHVLDRQLISRSFPAIESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTFRG 160
Cdd:COG0070 1218 VPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTG 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 161 SAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCVRN 240
Cdd:COG0070 1298 SAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRN 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 241 SGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDFDYFCNMEMVELSLIEDMADNRELYRLIGN 320
Cdd:COG0070 1378 SGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEE 1457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2559663843 321 HYKHTHSQLAGRMLDNWHEYVGQFIKVIPFEYKKVLHDEKLAKLQQKIA 369
Cdd:COG0070 1458 HVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDA 1506
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
101-349 |
4.02e-163 |
|
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: 456.60 E-value: 4.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 101 LDRQLISRSFPA-IESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTFRGSAGQSFGAFLAHGISFRLE 179
Cdd:cd00982 1 LDDKLIADAEPAlIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 180 GDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCVRNSGAIAVVEGVGDHCCEYMT 259
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 260 GGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDFDYFCNMEMVELSLIEDMADNRELYRLIGNHYKHTHSQLAGRMLDNWHE 339
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWEA 240
|
250
....*....|
gi 2559663843 340 YVGQFIKVIP 349
Cdd:cd00982 241 YLKKFVKVIP 250
|
|
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
1-349 |
7.79e-143 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 440.47 E-value: 7.79e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 1 CPVGVATQNEELRKR-FVGRSEYLINFFKFLAQEIRETLAEIGVRKLDDVIGRADMLEVKPQHaTHKTTHLDFSRILYMP 79
Cdd:PRK11750 1116 CATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGE-TAKQQKLDLSPLLETA 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 80 A----ECRT-NAIINVTEQQHDIAHVLDRQLIsrsfPAIESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTI 154
Cdd:PRK11750 1195 EppagKALYcTEERNPPFDKGLLNEQMLQQAK----PAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPI 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 155 LCTFRGSAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGE 234
Cdd:PRK11750 1271 KLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGE 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 235 RFCVRNSGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDFDYFCNMEMVELSLIEDMADNRE- 313
Cdd:PRK11750 1351 RFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILRVEDLEIHREh 1430
|
330 340 350
....*....|....*....|....*....|....*.
gi 2559663843 314 LYRLIGNHYKHTHSQLAGRMLDNWHEYVGQFIKVIP 349
Cdd:PRK11750 1431 LRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
123-310 |
1.97e-130 |
|
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: 371.36 E-value: 1.97e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 123 FPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTFRGSAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKG 202
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 203 SQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCVRNSGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVA 282
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180
....*....|....*....|....*...
gi 2559663843 283 YVWNPNGDFDYFCNMEMVELSLIEDMAD 310
Cdd:pfam01493 161 YVLDEDGDFPEKLNKEMVELERVTDEDE 188
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
179-287 |
2.25e-08 |
|
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: 54.65 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 179 EGDANDYVGKGLSGGKIVIVPPKGSqFVPQDN-----IIAGNTLLY----------GATSGEVYING----RVGERFCvr 239
Cdd:TIGR03122 86 EGDVGMHVGAEMKGGKIVVNGNADS-WAGCEMkggeiIIKGNAGDYvgsayrgewrGMSGGKIIVEGnagdYLGERMR-- 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2559663843 240 nSGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNP 287
Cdd:TIGR03122 163 -GGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGK 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
1-369 |
0e+00 |
|
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439840 [Multi-domain] Cd Length: 1508 Bit Score: 628.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 1 CPVGVATQNEELRKRFVGRSEYLINFFKFLAQEIRETLAEIGVRKLDDVIGRADMLEVKPQHATHKTTHLDFSRILYMPA 80
Cdd:COG0070 1138 CPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPD 1217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 81 ECRTNAIINVTEQQHDIAHVLDRQLISRSFPAIESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTFRG 160
Cdd:COG0070 1218 VPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTG 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 161 SAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCVRN 240
Cdd:COG0070 1298 SAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRN 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 241 SGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDFDYFCNMEMVELSLIEDMADNRELYRLIGN 320
Cdd:COG0070 1378 SGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEE 1457
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2559663843 321 HYKHTHSQLAGRMLDNWHEYVGQFIKVIPFEYKKVLHDEKLAKLQQKIA 369
Cdd:COG0070 1458 HVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDA 1506
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
101-349 |
4.02e-163 |
|
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: 456.60 E-value: 4.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 101 LDRQLISRSFPA-IESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTFRGSAGQSFGAFLAHGISFRLE 179
Cdd:cd00982 1 LDDKLIADAEPAlIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 180 GDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCVRNSGAIAVVEGVGDHCCEYMT 259
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 260 GGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDFDYFCNMEMVELSLIEDMADNRELYRLIGNHYKHTHSQLAGRMLDNWHE 339
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWEA 240
|
250
....*....|
gi 2559663843 340 YVGQFIKVIP 349
Cdd:cd00982 241 YLKKFVKVIP 250
|
|
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
1-349 |
7.79e-143 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 440.47 E-value: 7.79e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 1 CPVGVATQNEELRKR-FVGRSEYLINFFKFLAQEIRETLAEIGVRKLDDVIGRADMLEVKPQHaTHKTTHLDFSRILYMP 79
Cdd:PRK11750 1116 CATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGE-TAKQQKLDLSPLLETA 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 80 A----ECRT-NAIINVTEQQHDIAHVLDRQLIsrsfPAIESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTI 154
Cdd:PRK11750 1195 EppagKALYcTEERNPPFDKGLLNEQMLQQAK----PAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPI 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 155 LCTFRGSAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGE 234
Cdd:PRK11750 1271 KLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGE 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 235 RFCVRNSGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDFDYFCNMEMVELSLIEDMADNRE- 313
Cdd:PRK11750 1351 RFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILRVEDLEIHREh 1430
|
330 340 350
....*....|....*....|....*....|....*.
gi 2559663843 314 LYRLIGNHYKHTHSQLAGRMLDNWHEYVGQFIKVIP 349
Cdd:PRK11750 1431 LRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
123-310 |
1.97e-130 |
|
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: 371.36 E-value: 1.97e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 123 FPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTFRGSAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKG 202
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 203 SQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCVRNSGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVA 282
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180
....*....|....*....|....*...
gi 2559663843 283 YVWNPNGDFDYFCNMEMVELSLIEDMAD 310
Cdd:pfam01493 161 YVLDEDGDFPEKLNKEMVELERVTDEDE 188
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
1-239 |
1.66e-81 |
|
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439839 Cd Length: 728 Bit Score: 263.26 E-value: 1.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 1 CPVGVATQNEELRKRFV--GRSEYLINFFKFLAQEIRETLAEIGVRKLDDVIGRADMLEVKPqHATHKTTHLDFSRILYM 78
Cdd:COG0069 489 CPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVREILAALGVRSPDELIGRHDLLRVRD-GEHWKAKGLDLSPLLYK 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 79 PAECRTNAIINVTEQQHDIAHVLDRQLISRSFPAIESGMPVELDFPIANTDRSVGAMLSGVVAKKYGNDGLPDNTILCTF 158
Cdd:COG0069 568 PELPEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLITNIRNNNRRVGGMLSGEIAKRYGGAGLPDDTIILGF 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 159 RGSAGQSFGAFLAHGISFRLEGDANDYVGKGLSGGKIVIVPPKGSQFVPQDNIIAGNTLLYGATSGEVYINGRVGERFCV 238
Cdd:COG0069 648 AGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAV 727
|
.
gi 2559663843 239 R 239
Cdd:COG0069 728 R 728
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
130-285 |
8.07e-70 |
|
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: 215.51 E-value: 8.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 130 RSVGAMLSGVVAKKygnDGLPDNTILCTFRGSAGQSFGAFLaHGISFRLEGDANDYVGKGLSGGKIVIVPPKGsqfvpQD 209
Cdd:cd00504 1 RAVGTRGSRYIGKR---PGLPEDTVEIIINGSAGQSFGAFM-AGGTITVEGNANDYVGKGMSGGEIVIHPPAG-----DE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2559663843 210 NIIAGNTLLYGATSGEVYINGRVGERFCVRNSGAIAVVEGVGD-HCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVW 285
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVR 148
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
136-284 |
4.11e-13 |
|
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: 68.09 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 136 LSGVVAKKYGNDGLPDNTILcTFRGSAGQSFGAFLAhGISFRLEGDANDYVGKGLSGGKIVIvppKGSqfvpqdniiAGN 215
Cdd:cd00981 30 LDNVLGQRYIGDGLPGNVRI-NIYGVPGNDLGAFMS-GPTIIVYGNAQDDVGNTMNDGKIVI---HGS---------AGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 216 TLLYGATSGEVYINGRVGERFCV-----RNSGAIAVVEG-VGDHCCEYMTGGRTVVLG------STGRNFAAGMSGGVAY 283
Cdd:cd00981 96 VLGYAMRGGKIFIRGNAGYRVGIhmkeyKDKVPVLVIGGtAGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIY 175
|
.
gi 2559663843 284 V 284
Cdd:cd00981 176 I 176
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
1-56 |
7.30e-13 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 69.11 E-value: 7.30e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2559663843 1 CPVGVATQNEELRKR--FVGRSEYLINFFKFLAQEIRETLAEIGVRKLDDvIGRADML 56
Cdd:cd02808 334 CPVGVATQDPELRRRldVEGKAERVANYLKSLAEELRELAAALGKRSLEL-LGRSDLL 390
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
159-287 |
7.48e-12 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 64.83 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 159 RGSAGQSFGAFLAHGiSFRLEGDANDYVGKGLSGGKIVIvppKGSqfvpqdniiAGNTL-------LYGATSGEVYINGR 231
Cdd:COG2218 87 EGDVGMYLGAGMKGG-KITVNGNAGSFAGAEMKGGEIEI---NGN---------AGDFLgaayrgdWRGMSGGTIIVKGN 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2559663843 232 VGERFCVRNSGAIAVVEG-VGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNP 287
Cdd:COG2218 154 AGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGK 210
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
1-44 |
1.65e-11 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 65.05 E-value: 1.65e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2559663843 1 CPVGVATQNEELRKR--FVGRSEYLINFFKFLAQEIRETLAEIGVR 44
Cdd:pfam01645 322 CPVGVATQDPELRKRldFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
179-287 |
2.25e-08 |
|
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: 54.65 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 179 EGDANDYVGKGLSGGKIVIVPPKGSqFVPQDN-----IIAGNTLLY----------GATSGEVYING----RVGERFCvr 239
Cdd:TIGR03122 86 EGDVGMHVGAEMKGGKIVVNGNADS-WAGCEMkggeiIIKGNAGDYvgsayrgewrGMSGGKIIVEGnagdYLGERMR-- 162
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2559663843 240 nSGAIAVVEGVGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNP 287
Cdd:TIGR03122 163 -GGEILIKGNAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGK 209
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
177-300 |
5.90e-08 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 53.27 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 177 RLEGDAN--DYVGKGLSGGKIVIvppKGSqfvpqdniiAGNTLLYGATSGEVYINGRVGeRFCVRN-SGAIAVVEG-VGD 252
Cdd:COG2218 64 VIEGDLSrvKRIGAGMTAGEIIV---EGD---------VGMYLGAGMKGGKITVNGNAG-SFAGAEmKGGEIEINGnAGD 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2559663843 253 HC-CEY------MTGGRTVVLGSTGRNFAAGMSGGVAYVwnpNGDFDYFCNMEMV 300
Cdd:COG2218 131 FLgAAYrgdwrgMSGGTIIVKGNAGDRLGDRMRRGTIII---EGDAGDFAGSRMI 182
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
160-280 |
9.25e-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: 51.97 E-value: 9.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559663843 160 GSAGQSFGAFLAHGiSFRLEGDANDYVGKGLSGGKIVIvppKGSqfvpqdniiAGNTL---LYGA----TSGEVYINGRV 232
Cdd:cd00980 46 GDVGMYVGAGMKGG-KLVVEGNAGSWAGCEMKGGEITI---KGN---------AGDYVgsaYRGDwrgmSGGTITIEGNA 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2559663843 233 GERFCVRNSGAIAVVEG-VGDHCCEYMTGGRTVVLGSTGRNFAAGMSGG 280
Cdd:cd00980 113 GDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRG 161
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
231-291 |
4.03e-03 |
|
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: 38.10 E-value: 4.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2559663843 231 RVGERFcvrNSGAIaVVEG-VGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVWNPNGDF 291
Cdd:cd00980 32 RIGARM---TAGEI-VVEGdVGMYVGAGMKGGKLVVEGNAGSWAGCEMKGGEITIKGNAGDY 89
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
231-295 |
6.17e-03 |
|
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: 38.09 E-value: 6.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2559663843 231 RVGERFcvrNSGAIaVVEG-VGDHCCEYMTGGRTVVLGSTGRNFAAGMSGGVAYVwnpNGDFDYFC 295
Cdd:TIGR03122 73 RIGENM---SAGEI-VVEGdVGMHVGAEMKGGKIVVNGNADSWAGCEMKGGEIII---KGNAGDYV 131
|
|
| |
