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Conserved domains on  [gi|505393189|ref|WP_015580291|]
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MULTISPECIES: FMN-binding glutamate synthase family protein [Streptomyces]

Protein Classification

FMN-binding glutamate synthase family protein( domain architecture ID 10120226)

FMN-binding glutamate synthase family protein similar to the FMN-binding domain of glutamate synthase large subunit, GltS, which 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

CATH:  3.20.20.70
EC:  1.4.-.-
Gene Ontology:  GO:0006537|GO:0016638|GO:0015930
SCOP:  3000014

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GltB2 super family cl43016
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
22-467 3.40e-166

Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis


The actual alignment was detected with superfamily member COG0069:

Pssm-ID: 439839  Cd Length: 728  Bit Score: 487.45  E-value: 3.40e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  22 LVQKKHALLRNFPVVGHARYLLERIGPELRQYVVTSNDEERPFSRDQRSWIYASAKEENNYFGFGTDndVEHVQGHAYVk 101
Cdd:COG0069  121 LTQHRHAILRNLPVGGRYRYRFESIGPEIRQYFFESDGEEHPFNRETRSLLYQAAKNEEDYKPFGTL--VDYQPGYEWT- 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 102 qrtfagrlpdLRDAQAPLPSAK--VLGGPRgrAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEGGLSP 179
Cdd:COG0069  198 ----------LRSLFPFKADRPpiPIGEPV--EPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESP 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 180 YHL--NGGELVLQIGTSYFGCRNEDGTfNLDklksvvasgPVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGK 257
Cdd:COG0069  266 YHLgdGGGDAIKQIASGRFGVRDEDGE-YLP---------NAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGV 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 258 DCASPSRHTAFHDVDSMLDFVELLATET-GLPVGIKSAIGEMGFWEELATLMERGDRGVDFVTIDGGEGGTGAAPLIFAD 336
Cdd:COG0069  336 DLISPPPHHDIYSIEDLAQLIFDLRELNpGAPVGVKLVSGAGVGTIAACKGVAKTGAYADFITIDGGEGGTGAAPLESIK 415
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 337 SVSLPFRMGFSRVYSVFAERGLTDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIAT 416
Cdd:COG0069  416 HAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVAT 495
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505393189 417 QDPWLTRGIDAPSKAIRAAMYLRTLRRELLRVSGAVGVAHPSLITATDIDI 467
Cdd:COG0069  496 QDPELRKGFVVEGKPERVVNYFRFTAEEVREILAALGVRSPDELIGRHDLL 546
 
Name Accession Description Interval E-value
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
22-467 3.40e-166

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: 487.45  E-value: 3.40e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  22 LVQKKHALLRNFPVVGHARYLLERIGPELRQYVVTSNDEERPFSRDQRSWIYASAKEENNYFGFGTDndVEHVQGHAYVk 101
Cdd:COG0069  121 LTQHRHAILRNLPVGGRYRYRFESIGPEIRQYFFESDGEEHPFNRETRSLLYQAAKNEEDYKPFGTL--VDYQPGYEWT- 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 102 qrtfagrlpdLRDAQAPLPSAK--VLGGPRgrAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEGGLSP 179
Cdd:COG0069  198 ----------LRSLFPFKADRPpiPIGEPV--EPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESP 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 180 YHL--NGGELVLQIGTSYFGCRNEDGTfNLDklksvvasgPVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGK 257
Cdd:COG0069  266 YHLgdGGGDAIKQIASGRFGVRDEDGE-YLP---------NAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGV 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 258 DCASPSRHTAFHDVDSMLDFVELLATET-GLPVGIKSAIGEMGFWEELATLMERGDRGVDFVTIDGGEGGTGAAPLIFAD 336
Cdd:COG0069  336 DLISPPPHHDIYSIEDLAQLIFDLRELNpGAPVGVKLVSGAGVGTIAACKGVAKTGAYADFITIDGGEGGTGAAPLESIK 415
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 337 SVSLPFRMGFSRVYSVFAERGLTDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIAT 416
Cdd:COG0069  416 HAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVAT 495
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505393189 417 QDPWLTRGIDAPSKAIRAAMYLRTLRRELLRVSGAVGVAHPSLITATDIDI 467
Cdd:COG0069  496 QDPELRKGFVVEGKPERVVNYFRFTAEEVREILAALGVRSPDELIGRHDLL 546
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
41-468 8.71e-137

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: 400.38  E-value: 8.71e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  41 YLLERIGPELRQYVVtsndeerpFSRDQRSWIYASAKEENNyFGFGTDNDVEhvqghayvKQRTFAGRLPDLRDaqaPLP 120
Cdd:cd02808    1 YLLEIERLEEIQYFV--------FNRAERYGVYNRAGNSRG-RPFGTLRDLL--------EFGAQLAKHPLEPD---EEV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 121 SAKVLGGPRgRAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEGGLSPYHLNGGE-LVLQIGTSYFGCR 199
Cdd:cd02808   61 DDRVTIGPN-AEKPLKLDSPFNISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREGGGdIIKQVASGRFGVR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 200 NEDGTFnldklksvvasgpVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGKDCASPSRHTAFHDVDSMLDFVE 279
Cdd:cd02808  140 PEYLNK-------------ADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIE 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 280 LLATETGL-PVGIKSAIGEMgfWEELATLMERGdrGVDFVTIDGGEGGTGAAPLIFADSVSLPFRMGFSRVYSVFAERGL 358
Cdd:cd02808  207 DLREATGGkPIGVKLVAGHG--EGDIAAGVAAA--GADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGL 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 359 TDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIATQDPWLTRGIDAPSKAIRAAMYL 438
Cdd:cd02808  283 RDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCPVGVATQDPELRRRLDVEGKAERVANYL 362
                        410       420       430
                 ....*....|....*....|....*....|
gi 505393189 439 RTLRRELLRVSGAVGVAHPSLITATDIDIL 468
Cdd:cd02808  363 KSLAEELRELAAALGKRSLELLGRSDLLAL 392
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
99-437 3.71e-79

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: 251.48  E-value: 3.71e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189   99 YVKQRTFAGRLPDL---RDAQAPLPSAKVlggprgrAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEG 175
Cdd:pfam01645  29 PLNERVPIGALRDLlefDFAEDPIPLEEV-------EPALEIKTRFCTGAMSYGALSEEAHEALAKAMNRLGTKSNTGEG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  176 GLSPYHLNGGE--LVLQIGTSYFGCRNEdgtfNLDKlksvvasgpVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGI 253
Cdd:pfam01645 102 GEDPERLKYADniAIKQVASGRFGVTPE----YLNN---------ADAIEIKIAQGAKPGEGGHLPGEKVSPEIARIRGS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  254 PAGKDCASPSRHTAFHDVDSMLDFVELLATETG-LPVGIK--SAIGEmgfwEELATLMERGdrGVDFVTIDGGEGGTGAA 330
Cdd:pfam01645 169 PPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPkAPISVKlvSGHGV----GTIAAGVAKA--GADIILIDGYDGGTGAS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  331 PLIFADSVSLPFRMGFSRVYSVFAERGLTDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDAC 410
Cdd:pfam01645 243 PKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCRVCHTNTC 322
                         330       340
                  ....*....|....*....|....*..
gi 505393189  411 PTGIATQDPWLTRGIDAPSKAIRAAMY 437
Cdd:pfam01645 323 PVGVATQDPELRKRLDFEGAPERVVNY 349
gltB PRK11750
glutamate synthase subunit alpha; Provisional
145-418 1.04e-20

glutamate synthase subunit alpha; Provisional


Pssm-ID: 236968 [Multi-domain]  Cd Length: 1485  Bit Score: 96.10  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  145 AMSFGSLSGAAVTALnkgaALA----GTMHNTGEGGLSP--YHLNGGELVLQIGTSYFGcrnedgtfnldklksVVASGP 218
Cdd:PRK11750  865 AMSIGALSPEAHEAL----AIAmnrlGGRSNSGEGGEDParYGTEKVSKIKQVASGRFG---------------VTPAYL 925
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  219 VKA--IEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGKDCASPSRHtafHDVDSMLDFVEL---------------- 280
Cdd:PRK11750  926 VNAevLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPH---HDIYSIEDLAQLifdlkqvnpkalvsvk 1002
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  281 LATETGlpVGIksaigemgfweeLATlmergdrGV-----DFVTIDGGEGGTGAAPLI---FADSvslPFRMGFSRVYSV 352
Cdd:PRK11750 1003 LVSEPG--VGT------------IAT-------GVakayaDLITISGYDGGTGASPLTsvkYAGS---PWELGLAETHQA 1058
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505393189  353 FAERGLTDDITFIGSG--KLGLpeNAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIATQD 418
Cdd:PRK11750 1059 LVANGLRHKIRLQVDGglKTGL--DVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQD 1124
 
Name Accession Description Interval E-value
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
22-467 3.40e-166

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: 487.45  E-value: 3.40e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  22 LVQKKHALLRNFPVVGHARYLLERIGPELRQYVVTSNDEERPFSRDQRSWIYASAKEENNYFGFGTDndVEHVQGHAYVk 101
Cdd:COG0069  121 LTQHRHAILRNLPVGGRYRYRFESIGPEIRQYFFESDGEEHPFNRETRSLLYQAAKNEEDYKPFGTL--VDYQPGYEWT- 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 102 qrtfagrlpdLRDAQAPLPSAK--VLGGPRgrAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEGGLSP 179
Cdd:COG0069  198 ----------LRSLFPFKADRPpiPIGEPV--EPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESP 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 180 YHL--NGGELVLQIGTSYFGCRNEDGTfNLDklksvvasgPVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGK 257
Cdd:COG0069  266 YHLgdGGGDAIKQIASGRFGVRDEDGE-YLP---------NAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGV 335
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 258 DCASPSRHTAFHDVDSMLDFVELLATET-GLPVGIKSAIGEMGFWEELATLMERGDRGVDFVTIDGGEGGTGAAPLIFAD 336
Cdd:COG0069  336 DLISPPPHHDIYSIEDLAQLIFDLRELNpGAPVGVKLVSGAGVGTIAACKGVAKTGAYADFITIDGGEGGTGAAPLESIK 415
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 337 SVSLPFRMGFSRVYSVFAERGLTDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIAT 416
Cdd:COG0069  416 HAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVAT 495
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505393189 417 QDPWLTRGIDAPSKAIRAAMYLRTLRRELLRVSGAVGVAHPSLITATDIDI 467
Cdd:COG0069  496 QDPELRKGFVVEGKPERVVNYFRFTAEEVREILAALGVRSPDELIGRHDLL 546
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
41-468 8.71e-137

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: 400.38  E-value: 8.71e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  41 YLLERIGPELRQYVVtsndeerpFSRDQRSWIYASAKEENNyFGFGTDNDVEhvqghayvKQRTFAGRLPDLRDaqaPLP 120
Cdd:cd02808    1 YLLEIERLEEIQYFV--------FNRAERYGVYNRAGNSRG-RPFGTLRDLL--------EFGAQLAKHPLEPD---EEV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 121 SAKVLGGPRgRAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEGGLSPYHLNGGE-LVLQIGTSYFGCR 199
Cdd:cd02808   61 DDRVTIGPN-AEKPLKLDSPFNISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREGGGdIIKQVASGRFGVR 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 200 NEDGTFnldklksvvasgpVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGKDCASPSRHTAFHDVDSMLDFVE 279
Cdd:cd02808  140 PEYLNK-------------ADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIE 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 280 LLATETGL-PVGIKSAIGEMgfWEELATLMERGdrGVDFVTIDGGEGGTGAAPLIFADSVSLPFRMGFSRVYSVFAERGL 358
Cdd:cd02808  207 DLREATGGkPIGVKLVAGHG--EGDIAAGVAAA--GADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGL 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 359 TDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIATQDPWLTRGIDAPSKAIRAAMYL 438
Cdd:cd02808  283 RDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCPVGVATQDPELRRRLDVEGKAERVANYL 362
                        410       420       430
                 ....*....|....*....|....*....|
gi 505393189 439 RTLRRELLRVSGAVGVAHPSLITATDIDIL 468
Cdd:cd02808  363 KSLAEELRELAAALGKRSLELLGRSDLLAL 392
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
99-437 3.71e-79

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: 251.48  E-value: 3.71e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189   99 YVKQRTFAGRLPDL---RDAQAPLPSAKVlggprgrAKAFRPASVVNISAMSFGSLSGAAVTALNKGAALAGTMHNTGEG 175
Cdd:pfam01645  29 PLNERVPIGALRDLlefDFAEDPIPLEEV-------EPALEIKTRFCTGAMSYGALSEEAHEALAKAMNRLGTKSNTGEG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  176 GLSPYHLNGGE--LVLQIGTSYFGCRNEdgtfNLDKlksvvasgpVKAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGI 253
Cdd:pfam01645 102 GEDPERLKYADniAIKQVASGRFGVTPE----YLNN---------ADAIEIKIAQGAKPGEGGHLPGEKVSPEIARIRGS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  254 PAGKDCASPSRHTAFHDVDSMLDFVELLATETG-LPVGIK--SAIGEmgfwEELATLMERGdrGVDFVTIDGGEGGTGAA 330
Cdd:pfam01645 169 PPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPkAPISVKlvSGHGV----GTIAAGVAKA--GADIILIDGYDGGTGAS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  331 PLIFADSVSLPFRMGFSRVYSVFAERGLTDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDAC 410
Cdd:pfam01645 243 PKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCRVCHTNTC 322
                         330       340
                  ....*....|....*....|....*..
gi 505393189  411 PTGIATQDPWLTRGIDAPSKAIRAAMY 437
Cdd:pfam01645 323 PVGVATQDPELRKRLDFEGAPERVVNY 349
gltB PRK11750
glutamate synthase subunit alpha; Provisional
145-418 1.04e-20

glutamate synthase subunit alpha; Provisional


Pssm-ID: 236968 [Multi-domain]  Cd Length: 1485  Bit Score: 96.10  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  145 AMSFGSLSGAAVTALnkgaALA----GTMHNTGEGGLSP--YHLNGGELVLQIGTSYFGcrnedgtfnldklksVVASGP 218
Cdd:PRK11750  865 AMSIGALSPEAHEAL----AIAmnrlGGRSNSGEGGEDParYGTEKVSKIKQVASGRFG---------------VTPAYL 925
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  219 VKA--IEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGKDCASPSRHtafHDVDSMLDFVEL---------------- 280
Cdd:PRK11750  926 VNAevLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPH---HDIYSIEDLAQLifdlkqvnpkalvsvk 1002
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  281 LATETGlpVGIksaigemgfweeLATlmergdrGV-----DFVTIDGGEGGTGAAPLI---FADSvslPFRMGFSRVYSV 352
Cdd:PRK11750 1003 LVSEPG--VGT------------IAT-------GVakayaDLITISGYDGGTGASPLTsvkYAGS---PWELGLAETHQA 1058
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505393189  353 FAERGLTDDITFIGSG--KLGLpeNAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIATQD 418
Cdd:PRK11750 1059 LVANGLRHKIRLQVDGglKTGL--DVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQD 1124
GltB3 COG0070
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ...
71-419 3.10e-11

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: 66.08  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189   71 WIYASAKEENNYFGFGTDNDVEHVQGHAYVKQRTFAGRLPDLRDAQAPLPSAKVLGGPRGRAK----AFRPASVVNISAM 146
Cdd:COG0070   804 GRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEevepEEEIVKRFATGAM 883
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  147 SFGSLSGAAVTALNKGAALAGTMHNTGEGGlspyhlnggelvlqiGTSYFGCRNEDGTFNLDKLKSVVASGPV------- 219
Cdd:COG0070   884 SGGSSSSEAHEELAIAMNRIGGKSNGGGGG---------------EEEGREDPLRNGDSRRSAIKQVASGRFGvtseylv 948
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  220 --KAIEIKLSQGAKPGLGGMLPGVKVTDEIAGIRGIPAGKDCASPSRHtafHDVDSMLDFVEL----------------L 281
Cdd:COG0070   949 naDEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPH---HDIYSIEDLAQLifdlknanpaarisvkL 1025
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189  282 ATETGlpVGIKSAigemgfweelatlmergdrGV-----DFVTIDGGEGGTGAAPLIfadSVS---LPFRMGFSRVYSVF 353
Cdd:COG0070  1026 VSEVG--VGTIAA-------------------GVakaaaDVILISGHDGGTGASPLS---SIKhagLPWELGLAETQQTL 1081
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505393189  354 AERGLTDDITFIGSGKLGLPENAVVAFALGVDMVNVGREAMLSIGCIQAQKCHTDACPTGIATQDP 419
Cdd:COG0070  1082 VLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQDP 1147
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
291-391 2.92e-03

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 39.11  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505393189 291 IKSAIGEMGFWEELATLMERGDR-----GVDFVTIDGGEGGTGAAPLIFADSVSLPFRMGFSRvysvfaergltddITFI 365
Cdd:cd04722  108 LREAVPDVKVVVKLSPTGELAAAaaeeaGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSK-------------VPVI 174
                         90       100
                 ....*....|....*....|....*.
gi 505393189 366 GSGKLGLPENAVVAFALGVDMVNVGR 391
Cdd:cd04722  175 AGGGINDPEDAAEALALGADGVIVGS 200
 
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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