|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
1-1460 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1758.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPDNkLAVGQVFLPR 80
Cdd:PRK11750 15 CGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLAKN-YAVGMVFLNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 81 ISLDAQeACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAVK 160
Cdd:PRK11750 94 DPELAA-AARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERRLFIARRRIEKRLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 161 GEqiNDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGN 240
Cdd:PRK11750 173 DD--KDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLAHNGEINTITGN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 241 VNWMKAHETRMEHPAFgTHMQDLKPVIGVGLSDSGSLDTVFEVMV-------RAGRtapmvkmMLVPQALTSSQTTPDNH 313
Cdd:PRK11750 251 RQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLaggmdlfRAMR-------LLVPPAWQNNPDMDPDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 314 KALIQYcNSV-MEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIA 392
Cdd:PRK11750 323 RAFYEF-NSMhMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 393 VDLQSGKLYRDRELKDHLATLKPWDKWV-QNTTHLDELVKTASLKGEPSDMDKAELRRRQQAFGLTMEDMELILHPMVED 471
Cdd:PRK11750 402 IDTRTGRILHSAEIDNDLKSRHPYKEWLeKNVRRLVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRVLAEN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 472 GKEAIGSMGDDSPIAVLSDKYRGLHHFFRQNFSQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVLT 551
Cdd:PRK11750 482 GQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPVLS 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 552 TAEFRAMR--DYMGDTAAEIDATF-PVDGGpeaLRDALRRIRQETEDAVRGGATHVILTDEAMGPARAAIPAILATGAVH 628
Cdd:PRK11750 562 YSDFKQLTtlDEEHYRADTLDLNYdPEETG---LEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVGAVQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 629 THLIRSNLRTFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFgSMPLEKGMANYKKAIDDGLLKIM 708
Cdd:PRK11750 639 HRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEI-LKDYRQVMLNYRKGINKGLYKIM 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 709 SKMGISVISSYRGGGNFEAIGLSRALVAEHFPAMVSRISGIGLNGIQKKVLEQHATAYNEEVvALPVGGFYRFRKSGDRH 788
Cdd:PRK11750 718 SKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARK-PIDQGGLLKYVHGGEYH 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 789 GWEGGVIHTLQQAVTNDSYTTFKKYSEQVNKRPPMQLRDLLELRSTKAPVPVDEVESITAIRKRFITPGMSMGALSPEAH 868
Cdd:PRK11750 797 AYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAH 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 869 GTLNVAMNRIGAKSDSGEGGEDPARFrpdknGDNWNSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFK 948
Cdd:PRK11750 877 EALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDK 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 949 VTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISGNSG 1028
Cdd:PRK11750 952 VNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDG 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1029 GTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMVRQC 1108
Cdd:PRK11750 1032 GTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRIC 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1109 HSNTCPVGVCVQDDKLRQK-FVGTPEKVVNLFTFLAEEVREILAGLGFRSLNEVIGRTDLLHQVSRGAEHLDDLDLNPRL 1187
Cdd:PRK11750 1112 HLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPLL 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1188 AQVDPGEN-ARYCTLQgRNEVPDT--LDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGMFGLQPGHI 1264
Cdd:PRK11750 1192 ETAEPPAGkALYCTEE-RNPPFDKglLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPI 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1265 TIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGE 1344
Cdd:PRK11750 1271 KLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGE 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1345 RFAVRNSGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLYINDESVIFQRIE-VGHYESQ 1423
Cdd:PRK11750 1351 RFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILRVEdLEIHREH 1430
|
1450 1460 1470
....*....|....*....|....*....|....*..
2VDC_D 1424 LKHLIEEHVTETQSRFAAEILNDWAREVTKFWQVVPK 1460
Cdd:PRK11750 1431 LRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPK 1467
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
1-1469 |
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: 1289.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPDNKLAVGQVFLPR 80
Cdd:COG0070 27 LGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 81 ISLDAQEACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAVk 160
Cdd:COG0070 107 AVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFR- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 161 geqinDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGN 240
Cdd:COG0070 186 -----RRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 241 VNWMKAHETRMEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVPQALTSSQTTPDNHKALIQYC 320
Cdd:COG0070 261 NNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 321 NSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGKL 400
Cdd:COG0070 341 AADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 401 YRDRELKDHLATLKPWDKWVQNTTHLDELVKTASLKG---EPSDMDKAELRRRQQAFGLTMEDMELILHPMVEDGKEAIG 477
Cdd:COG0070 421 LDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELlllEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 478 SMGDDSPIAVLSDKYRGLHHFFRQNFSQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVLTTAEFRA 557
Cdd:COG0070 501 AAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 558 MRDYMGDTAAEIDatFPVDGGPEALRDALRRIRQETEDAVRGGATHVILTDEAMGPARAAIPAILATGAVHTHLIRSNLR 637
Cdd:COG0070 581 LLLLGDATTLAAA--LEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHHLLRALGR 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 638 TFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAIDDGLLKIMSKMGISVIS 717
Cdd:COG0070 659 VLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISS 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 718 SYRGGGNFEAIGLSRALVA---EHFPAMVSRISGIGLNGIQKKVLEQHATAYNEEVVALPVGGFYRFRKSGDRHGWEGGV 794
Cdd:COG0070 739 SSGGGIIEGAGGGLGLLLElggTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYH 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 795 IHTLQQAVTNDSYTTFKKYSEQVNKRPPMQLRDLLELR-STKAPVPVDEVESITAIRKRFITPGMSMGALSPEAHGTLNV 873
Cdd:COG0070 819 HLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLfLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAI 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 874 AMNRIGAKSDSGEGGEDPARFRPDKNGDNWNSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFKVTEMI 953
Cdd:COG0070 899 AMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWI 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 954 ARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISGNSGGTGAS 1033
Cdd:COG0070 979 ARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGAS 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1034 PQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMVRQCHSNTC 1113
Cdd:COG0070 1059 PLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTC 1138
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1114 PVGVCVQDDKLRQKFVGTPEKVVNLFTFLAEEVREILAGLGFRSLNEVIGRTDLLhQVSRGAEH--LDDLDLNPRLAQVD 1191
Cdd:COG0070 1139 PVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLL-LVRRAVDHwkAKGLDLSPLLYKPD 1217
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1192 PGEN-ARYCTLQGRNEVPDTLDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGMFGLQPGHITIRLRG 1270
Cdd:COG0070 1218 VPADvPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTG 1297
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1271 TAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVRN 1350
Cdd:COG0070 1298 SAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRN 1377
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1351 SGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLYINDESVIFQRIEVGHYESQLKHLIEE 1430
Cdd:COG0070 1378 SGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEE 1457
|
1450 1460 1470
....*....|....*....|....*....|....*....
2VDC_D 1431 HVTETQSRFAAEILNDWAREVTKFWQVVPKEMLNRLEVP 1469
Cdd:COG0070 1458 HVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAI 1496
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
1-414 |
0e+00 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 688.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPD-NKLAVGQVFLP 79
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEaGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 80 RiSLDAQEACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAV 159
Cdd:cd00713 81 R-DEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 160 KgEQINDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKG 239
Cdd:cd00713 160 R-AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 240 NVNWMKAHETRMEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVPQALTSSQTTPDNHKALIQY 319
Cdd:cd00713 239 NRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 320 CNSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGK 399
Cdd:cd00713 319 HSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGR 398
|
410
....*....|....*
2VDC_D 400 LYRDRELKDHLATLK 414
Cdd:cd00713 399 ILDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
788-1156 |
0e+00 |
|
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: 610.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 788 HGWEGGVIHTLQQAVTNDSYTTFKKYSEQVNKR-PPMQLRDLLELRSTKAPVPVDEVESITAIRKRFITPGMSMGALSPE 866
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERvPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 867 AHGTLNVAMNRIGAKSDSGEGGEDPARFRPDKNGdnwnsAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPG 946
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-----AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 947 FKVTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISGN 1026
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1027 SGGTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMVR 1106
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2VDC_D 1107 QCHSNTCPVGVCVQDDKLR--QKFVGTPEKVVNLFTFLAEEVREILAGLGFR 1156
Cdd:pfam01645 316 VCHTNTCPVGVATQDPELRkrLDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1285-1395 |
5.03e-07 |
|
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: 52.72 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1285 KLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKN----TIIGNTVLY----------GATAGKLFAAGQAGERFAVRN 1350
Cdd:TIGR03122 82 EIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKggeiIIKGNAGDYvgsayrgewrGMSGGKIIVEGNAGDYLGERM 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
2VDC_D 1351 SGATVVVEG-CGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVY 1395
Cdd:TIGR03122 162 RGGEILIKGnAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVG 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
1-1460 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1758.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPDNkLAVGQVFLPR 80
Cdd:PRK11750 15 CGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLAKN-YAVGMVFLNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 81 ISLDAQeACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAVK 160
Cdd:PRK11750 94 DPELAA-AARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERRLFIARRRIEKRLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 161 GEqiNDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGN 240
Cdd:PRK11750 173 DD--KDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLAHNGEINTITGN 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 241 VNWMKAHETRMEHPAFgTHMQDLKPVIGVGLSDSGSLDTVFEVMV-------RAGRtapmvkmMLVPQALTSSQTTPDNH 313
Cdd:PRK11750 251 RQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLaggmdlfRAMR-------LLVPPAWQNNPDMDPDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 314 KALIQYcNSV-MEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIA 392
Cdd:PRK11750 323 RAFYEF-NSMhMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 393 VDLQSGKLYRDRELKDHLATLKPWDKWV-QNTTHLDELVKTASLKGEPSDMDKAELRRRQQAFGLTMEDMELILHPMVED 471
Cdd:PRK11750 402 IDTRTGRILHSAEIDNDLKSRHPYKEWLeKNVRRLVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRVLAEN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 472 GKEAIGSMGDDSPIAVLSDKYRGLHHFFRQNFSQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVLT 551
Cdd:PRK11750 482 GQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPVLS 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 552 TAEFRAMR--DYMGDTAAEIDATF-PVDGGpeaLRDALRRIRQETEDAVRGGATHVILTDEAMGPARAAIPAILATGAVH 628
Cdd:PRK11750 562 YSDFKQLTtlDEEHYRADTLDLNYdPEETG---LEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVGAVQ 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 629 THLIRSNLRTFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFgSMPLEKGMANYKKAIDDGLLKIM 708
Cdd:PRK11750 639 HRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEI-LKDYRQVMLNYRKGINKGLYKIM 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 709 SKMGISVISSYRGGGNFEAIGLSRALVAEHFPAMVSRISGIGLNGIQKKVLEQHATAYNEEVvALPVGGFYRFRKSGDRH 788
Cdd:PRK11750 718 SKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARK-PIDQGGLLKYVHGGEYH 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 789 GWEGGVIHTLQQAVTNDSYTTFKKYSEQVNKRPPMQLRDLLELRSTKAPVPVDEVESITAIRKRFITPGMSMGALSPEAH 868
Cdd:PRK11750 797 AYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAH 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 869 GTLNVAMNRIGAKSDSGEGGEDPARFrpdknGDNWNSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFK 948
Cdd:PRK11750 877 EALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDK 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 949 VTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISGNSG 1028
Cdd:PRK11750 952 VNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDG 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1029 GTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMVRQC 1108
Cdd:PRK11750 1032 GTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRIC 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1109 HSNTCPVGVCVQDDKLRQK-FVGTPEKVVNLFTFLAEEVREILAGLGFRSLNEVIGRTDLLHQVSRGAEHLDDLDLNPRL 1187
Cdd:PRK11750 1112 HLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPLL 1191
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1188 AQVDPGEN-ARYCTLQgRNEVPDT--LDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGMFGLQPGHI 1264
Cdd:PRK11750 1192 ETAEPPAGkALYCTEE-RNPPFDKglLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPI 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1265 TIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGE 1344
Cdd:PRK11750 1271 KLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGE 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1345 RFAVRNSGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLYINDESVIFQRIE-VGHYESQ 1423
Cdd:PRK11750 1351 RFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILRVEdLEIHREH 1430
|
1450 1460 1470
....*....|....*....|....*....|....*..
2VDC_D 1424 LKHLIEEHVTETQSRFAAEILNDWAREVTKFWQVVPK 1460
Cdd:PRK11750 1431 LRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPK 1467
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
1-1469 |
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: 1289.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPDNKLAVGQVFLPR 80
Cdd:COG0070 27 LGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 81 ISLDAQEACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAVk 160
Cdd:COG0070 107 AVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFR- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 161 geqinDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGN 240
Cdd:COG0070 186 -----RRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 241 VNWMKAHETRMEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVPQALTSSQTTPDNHKALIQYC 320
Cdd:COG0070 261 NNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 321 NSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGKL 400
Cdd:COG0070 341 AADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 401 YRDRELKDHLATLKPWDKWVQNTTHLDELVKTASLKG---EPSDMDKAELRRRQQAFGLTMEDMELILHPMVEDGKEAIG 477
Cdd:COG0070 421 LDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELlllEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 478 SMGDDSPIAVLSDKYRGLHHFFRQNFSQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVLTTAEFRA 557
Cdd:COG0070 501 AAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 558 MRDYMGDTAAEIDatFPVDGGPEALRDALRRIRQETEDAVRGGATHVILTDEAMGPARAAIPAILATGAVHTHLIRSNLR 637
Cdd:COG0070 581 LLLLGDATTLAAA--LEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHHLLRALGR 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 638 TFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAIDDGLLKIMSKMGISVIS 717
Cdd:COG0070 659 VLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISS 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 718 SYRGGGNFEAIGLSRALVA---EHFPAMVSRISGIGLNGIQKKVLEQHATAYNEEVVALPVGGFYRFRKSGDRHGWEGGV 794
Cdd:COG0070 739 SSGGGIIEGAGGGLGLLLElggTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYH 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 795 IHTLQQAVTNDSYTTFKKYSEQVNKRPPMQLRDLLELR-STKAPVPVDEVESITAIRKRFITPGMSMGALSPEAHGTLNV 873
Cdd:COG0070 819 HLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLfLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAI 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 874 AMNRIGAKSDSGEGGEDPARFRPDKNGDNWNSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFKVTEMI 953
Cdd:COG0070 899 AMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWI 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 954 ARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISGNSGGTGAS 1033
Cdd:COG0070 979 ARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGAS 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1034 PQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMVRQCHSNTC 1113
Cdd:COG0070 1059 PLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTC 1138
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1114 PVGVCVQDDKLRQKFVGTPEKVVNLFTFLAEEVREILAGLGFRSLNEVIGRTDLLhQVSRGAEH--LDDLDLNPRLAQVD 1191
Cdd:COG0070 1139 PVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLL-LVRRAVDHwkAKGLDLSPLLYKPD 1217
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1192 PGEN-ARYCTLQGRNEVPDTLDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGMFGLQPGHITIRLRG 1270
Cdd:COG0070 1218 VPADvPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTG 1297
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1271 TAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVRN 1350
Cdd:COG0070 1298 SAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRN 1377
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1351 SGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLYINDESVIFQRIEVGHYESQLKHLIEE 1430
Cdd:COG0070 1378 SGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEE 1457
|
1450 1460 1470
....*....|....*....|....*....|....*....
2VDC_D 1431 HVTETQSRFAAEILNDWAREVTKFWQVVPKEMLNRLEVP 1469
Cdd:COG0070 1458 HVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAI 1496
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
1-1471 |
0e+00 |
|
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439837 [Multi-domain] Cd Length: 1520 Bit Score: 1176.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPD-NKLAVGQVFLP 79
Cdd:COG0067 23 CGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIELPEpGEYAVGMVFLP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 80 RiSLDAQEACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAV 159
Cdd:COG0067 103 Q-DEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFERKLYVARKRIEKAI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 160 KGEQIN--DFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTV 237
Cdd:COG0067 182 RALGLDdeDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQPFRYLAHNGEINTL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 238 KGNVNWMKAHETRMEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVPQALTSSQTTPDNHKALI 317
Cdd:COG0067 262 RGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMMLIPEAWENNPDMDPERRAFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 318 QYCNSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQS 397
Cdd:COG0067 342 EYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGRLQPGKMLLVDLEE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 398 GKLYRDRELKDHLATLKPWDKWV-QNTTHLDELVKTASLKGEPSDmdkaELRRRQQAFGLTMEDMELILHPMVEDGKEAI 476
Cdd:COG0067 422 GRIIDDEEIKAELAAAHPYGEWLkENRIRLEDLPEPEEEPAPDDD----LLLRRQQAFGYTEEEELLLLLPMAAGGEEEG 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 477 GSMGDDSPIAVLSDKYRGLHHFFRQNFSQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQT-RLLQLESPVLTTAEF 555
Cdd:COG0067 498 GSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEARrRLLLLPPPLLNELLL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 556 RAMRDYMGDTAAEIDATFPVDGGPEALRDALRRIRQETEDAVRGGATHVILTDEAMGPARAAIPAILATGAVHTHLIRSN 635
Cdd:COG0067 578 LLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDAAPAPLAAAAAAHHHHLHL 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 636 LRTFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAIDDGLLKIMSKMGISV 715
Cdd:COG0067 658 LRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAAAAKKKKKKKKGKLKKKKMSGI 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 716 ISSYRGGGNFEAIGLSRALVAEHFPAMVSRISGIGLNGIQKKVLEQHATAYNEEVVALPVGGFYRFRKSGDRHGWEGGVI 795
Cdd:COG0067 738 ISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLLGLGGGGGGEYGRRREGE 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 796 HTLQQAVTNDSYTTFKKYSEQVNKRPPMQLRDLLELRSTK----------APVPVDEVESITAIRKRFITPGMSMGALSP 865
Cdd:COG0067 818 LHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLllllfeeeeeEEEPEEEEEEEESSAIAAASSAAASAAASA 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 866 EAHGTLNVAMNRIGAKSDSGEGGEDPARFRPDKNGdnwnSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLP 945
Cdd:COG0067 898 AAAAAAAGAGGGGGGGGGGGGGGGEGRRASGGSGS----SSSASVAAAGGGVVVGAGAAAAEGGGGGGGGGGGGGGGGGG 973
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 946 GFKVTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISG 1025
Cdd:COG0067 974 GGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAAAAAAAAAAAAVGSSG 1053
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1026 NSGGTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMV 1105
Cdd:COG0067 1054 GGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGALGGGAAALVVVGCGVA 1133
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1106 RQCHSNTCPVGVCVQDDKLRQKFVGTPEKVVNLFTFLAEEVREILAGLGFRslnevIGRTDLLHQVSRGAEHLDDLDLNP 1185
Cdd:COG0067 1134 MCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELL-----RLLEEGLGVVELLLLLLLLLLLAK 1208
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1186 RLAQVDPGENARYCTLQGRNEVPDTLDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGM-------FG 1258
Cdd:COG0067 1209 LLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGGGGGGgggggggGG 1288
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1259 LQPGHITIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFA 1338
Cdd:COG0067 1289 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGAG 1368
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1339 AGQAGERFAVRNSGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDdslplyinDESVIFQRIEVG 1418
Cdd:COG0067 1369 GGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLD--------LDVVLDEEEEEE 1440
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|...
2VDC_D 1419 HYESQLKHLIEEHVTETQSRFAAEILNDWAREVTKFWQVVPKEMLNRLEVPVH 1471
Cdd:COG0067 1441 LEELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLL 1493
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
623-1349 |
0e+00 |
|
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: 926.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 623 ATGAVHTHLIRSNLRTFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAIDD 702
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 703 GLLKIMSKMGISVISSYRGGGNFEAIGLSRALVAehfpamvsrisgIGLngiqKKVLEQHATAYNEEvvaLPVGGFYRFR 782
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELVD------------IGI----ADVLTQHRHAILRN---LPVGGRYRYR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 783 KS--------------GDRHGWEGGVIHTLQQAVTNDSytTFKKYSEQVNKRP--PMQLRDLLELRSTKAPVPVDE-VES 845
Cdd:COG0069 142 FEsigpeirqyffesdGEEHPFNRETRSLLYQAAKNEE--DYKPFGTLVDYQPgyEWTLRSLFPFKADRPPIPIGEpVEP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 846 ITAIRKRFITPGMSMGALSPEAHGTLNVAMNRIGAKSDSGEGGEDPARFrpdknGDNWNSAIKQVASGRFGVT---AEYL 922
Cdd:COG0069 220 PYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRdedGEYL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 923 NQCRELEIKVAQGAKPGEGGQLPGFKVTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVS 1002
Cdd:COG0069 295 PNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVGVKLVS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1003 RSGIGTIAA--GVAK--ANADIILISGNSGGTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRD 1078
Cdd:COG0069 375 GAGVGTIAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1079 IVIAAMLGAEEFGIGTASLIAMGCIMVRQCHSNTCPVGVCVQDDKLRQKFV--GTPEKVVNLFTFLAEEVREILAGLGFR 1156
Cdd:COG0069 455 VAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVREILAALGVR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1157 SLNEVIGRTDLLHQVSRGAEHLDDLDLNPRLAQVDPGEN-ARYCTLQGRNEVPDTLDARIVADARPLFEEGEKMQLAYNA 1235
Cdd:COG0069 535 SPDELIGRHDLLRVRDGEHWKAKGLDLSPLLYKPELPEGvPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLITNI 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1236 RNTQRAIGTRLSSMVTRKFGMFGLQPGHITIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPL 1315
Cdd:COG0069 615 RNNNRRVGGMLSGEIAKRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPPGASF 694
|
730 740 750
....*....|....*....|....*....|....
2VDC_D 1316 ETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVR 1349
Cdd:COG0069 695 FPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
1-414 |
0e+00 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 688.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPD-NKLAVGQVFLP 79
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEaGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 80 RiSLDAQEACRCIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAV 159
Cdd:cd00713 81 R-DEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 160 KgEQINDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKG 239
Cdd:cd00713 160 R-AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 240 NVNWMKAHETRMEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVPQALTSSQTTPDNHKALIQY 319
Cdd:cd00713 239 NRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 320 CNSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGK 399
Cdd:cd00713 319 HSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGR 398
|
410
....*....|....*
2VDC_D 400 LYRDRELKDHLATLK 414
Cdd:cd00713 399 ILDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
788-1156 |
0e+00 |
|
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: 610.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 788 HGWEGGVIHTLQQAVTNDSYTTFKKYSEQVNKR-PPMQLRDLLELRSTKAPVPVDEVESITAIRKRFITPGMSMGALSPE 866
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERvPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 867 AHGTLNVAMNRIGAKSDSGEGGEDPARFRPDKNGdnwnsAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPG 946
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-----AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 947 FKVTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKANADIILISGN 1026
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1027 SGGTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIMVR 1106
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
2VDC_D 1107 QCHSNTCPVGVCVQDDKLR--QKFVGTPEKVVNLFTFLAEEVREILAGLGFR 1156
Cdd:pfam01645 316 VCHTNTCPVGVATQDPELRkrLDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
1-419 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 572.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1 CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAVPQKFFKDHVKVIGHRAPDN-KLAVGQVFLP 79
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAgQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 80 RISLDAQEACRcIVETEILAFGYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYIIRRRIEKAV 159
Cdd:pfam00310 81 QDEAKRAEAKK-IFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 160 KGEQIN-DFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVK 238
Cdd:pfam00310 160 GVEGGDkDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 239 GNVNWMKAHETRMEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVPQALTSSQTTPDNHKALIQ 318
Cdd:pfam00310 240 GNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 319 YCNSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSG 398
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
2VDC_D 399 KLYRDRELKDHLATLKPWDKW 419
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
795-1170 |
1.32e-167 |
|
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: 508.23 E-value: 1.32e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 795 IHTLQQAVTN--DSYTTFKKYSEQVN--KRPPMQLRDLLELRSTKAPVPVDE-------------VESITAIRKRFITPG 857
Cdd:cd02808 5 IERLEEIQYFvfNRAERYGVYNRAGNsrGRPFGTLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPFNISA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 858 MSMGALSPEAHGTLNVAMNRIGAKSDSGEGGEDPARFRpdkngdNWNSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAK 937
Cdd:cd02808 85 MSFGALSKEAKEALAIGAALAGTASNTGEGGELPEERE------GGGDIIKQVASGRFGVRPEYLNKADAIEIKIGQGAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 938 PGEGGQLPGFKVTEMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGTIAAGVAKAN 1017
Cdd:cd02808 159 PGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVAAAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1018 ADIILISGNSGGTGASPQTSIKFAGLPWEMGLSEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASL 1097
Cdd:cd02808 239 ADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAAL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2VDC_D 1098 IAMGCIMVRQCHSNTCPVGVCVQDDKL--RQKFVGTPEKVVNLFTFLAEEVREILAGLGFRSLNEvIGRTDLLHQ 1170
Cdd:cd02808 319 IALGCIQARKCHTNTCPVGVATQDPELrrRLDVEGKAERVANYLKSLAEELRELAAALGKRSLEL-LGRSDLLAL 392
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
449-731 |
2.28e-148 |
|
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino terminal amidotransferase domain with the FMN-binding domain and has an alpha / beta overall topology. This domain appears to be a rudimentary form of the FMN-binding TIM barrel according to SCOP.
Pssm-ID: 461469 [Multi-domain] Cd Length: 281 Bit Score: 452.61 E-value: 2.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 449 RRQQAFGLTMEDMELILHPMVEDGKEAIGSMGDDSPIAVLSDKYRGLHHFFRQNFSQVTNPPIDSLRERRVMSLKTRLGN 528
Cdd:pfam04898 1 RRQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 529 LGNILDEDETQTRLLQLESPVLTTAEFRAMR--DYMGDTAAEIDATFPvdggpeALRDALRRIRQETEDAVRGGATHVIL 606
Cdd:pfam04898 81 EGNLLEETPEHCRRLELPSPILTNEELEKLRslKGPGFKVATLDITFD------GLEAALERLCEEAEEAVRDGANILIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 607 TDEAMGPARAAIPAILATGAVHTHLIRSNLRTFTSLNVRTAEGLDTHYFAVLIGVGATTVNAYLAQEAIAERHRRG--LF 684
Cdd:pfam04898 155 SDRGVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGkgKL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
2VDC_D 685 GSMPLEKGMANYKKAIDDGLLKIMSKMGISVISSYRGGGNFEAIGLS 731
Cdd:pfam04898 235 TDEDLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1211-1460 |
1.82e-138 |
|
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: 425.02 E-value: 1.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1211 LDARIVADARP-LFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGMFGLQPGHITIRLRGTAGQSLGAFAVQGIKLEVM 1289
Cdd:cd00982 1 LDDKLIADAEPaLIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1290 GDANDYVGKGLSGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVRNSGATVVVEGCGSNGCEYMT 1369
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1370 GGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLYINDESVIFQRIEVGHYESQLKHLIEEHVTETQSRFAAEILNDWAR 1449
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWEA 240
|
250
....*....|.
2VDC_D 1450 EVTKFWQVVPK 1460
Cdd:cd00982 241 YLKKFVKVIPR 251
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1233-1416 |
2.02e-102 |
|
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: 324.37 E-value: 2.02e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1233 YNARNTQRAIGTRLSSMVTRKFGMFGLQPGHITIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTS 1312
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1313 SPLETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVRNSGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMA 1392
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180
....*....|....*....|....
2VDC_D 1393 YVYDLDDSLPLYINDESVIFQRIE 1416
Cdd:pfam01493 161 YVLDEDGDFPEKLNKEMVELERVT 184
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1240-1396 |
2.63e-59 |
|
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: 200.49 E-value: 2.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1240 RAIGTRLSSMVTRKFGmfgLQPGHITIRLRGTAGQSLGAFAVqGIKLEVMGDANDYVGKGLSGGTIVVRPTtssplETNK 1319
Cdd:cd00504 1 RAVGTRGSRYIGKRPG---LPEDTVEIIINGSAGQSFGAFMA-GGTITVEGNANDYVGKGMSGGEIVIHPP-----AGDE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2VDC_D 1320 NTIIGNTVLYGATAGKLFAAGQAGERFAVRNSGATVVVEG-CGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYD 1396
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGvGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
191-391 |
4.13e-31 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 122.56 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 191 FYPDLLDERFESDFAIYHQRYSTNTFPTWPLAQPFR------MLAHNGEINTVKGNVNWMKAhetrmehpafgthmqdlK 264
Cdd:cd00352 57 VALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEA-----------------R 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 265 PVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLvpqaltssqttpdnhkaliqycnsvmEPWDGPAALAMTDG--RWVV 342
Cdd:cd00352 120 GYRFEGESDSEVILHLLERLGREGGLFEAVEDAL--------------------------KRLDGPFAFALWDGkpDRLF 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
2VDC_D 343 GGMDRNGLRPMRYTITTDGLIIGGSETGMvkIDETQVIEKGRLGPGEMI 391
Cdd:cd00352 174 AARDRFGIRPLYYGITKDGGLVFASEPKA--LLALPFKGVRRLPPGELL 220
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1258-1402 |
6.65e-14 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1258 GLQPGHITIRlrGTAGQSLGAFAVQGiKLEVMGDANDYVGKGLSGGTIVVRpttsspletnkntiiGNT------VLYGA 1331
Cdd:COG2218 78 GMTAGEIIVE--GDVGMYLGAGMKGG-KITVNGNAGSFAGAEMKGGEIEIN---------------GNAgdflgaAYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1332 TAG----KLFAAGQAGERFAVRNSGATVVVEG-----CGSNgceyMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLP 1402
Cdd:COG2218 140 WRGmsggTIIVKGNAGDRLGDRMRRGTIIIEGdagdfAGSR----MIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPEELL 215
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1266-1395 |
2.11e-09 |
|
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: 58.90 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1266 IRLRGTAGQSLGaFAVQGIKLEVMGDANDYVGKGLSGGTIVVrpttssplETNKNTIIGNTV---LYGATAGKLFAAGQA 1342
Cdd:cd00980 42 IVVEGDVGMYVG-AGMKGGKLVVEGNAGSWAGCEMKGGEITI--------KGNAGDYVGSAYrgdWRGMSGGTITIEGNA 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
2VDC_D 1343 GERFAVRNSGATVVVEG-----CGSNgceyMTGGTAVILGRVGDNFAAGMTGGMAYVY 1395
Cdd:cd00980 113 GDRLGERMRRGEILIKGdagifAGIR----MNGGTIIVRGDAGAHPGYEMKRGTIVIG 166
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1239-1394 |
8.76e-09 |
|
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: 57.69 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1239 QRAIGTRLssmvtrkfgmfglqPGHITIRLRGTAGQSLGAFaVQGIKLEVMGDANDYVGKGLSGGTIVVrpttsspletn 1318
Cdd:cd00981 36 QRYIGDGL--------------PGNVRINIYGVPGNDLGAF-MSGPTIIVYGNAQDDVGNTMNDGKIVI----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1319 kNTIIGNTVLYGATAGKLFAAGQAGERFAVR----NSGATVVVEGcGSNG---CEYMTGGTAVILG------RVGDNFAA 1385
Cdd:cd00981 90 -HGSAGDVLGYAMRGGKIFIRGNAGYRVGIHmkeyKDKVPVLVIG-GTAGdflGEYMAGGVIIVLGlgtdeePVGRYIGT 167
|
....*....
2VDC_D 1386 GMTGGMAYV 1394
Cdd:cd00981 168 GMHGGVIYI 176
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
970-1094 |
1.70e-07 |
|
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: 53.36 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 970 PHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRSGIGtiAAGVAKANADIILIsGNSGGTGASPQTSikfaglpwemgl 1049
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKLSPTGELA--AAAAEEAGVDEVGL-GNGGGGGGGRDAV------------ 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
2VDC_D 1050 SEVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGT 1094
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1285-1395 |
5.03e-07 |
|
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: 52.72 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1285 KLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKN----TIIGNTVLY----------GATAGKLFAAGQAGERFAVRN 1350
Cdd:TIGR03122 82 EIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEMKggeiIIKGNAGDYvgsayrgewrGMSGGKIIVEGNAGDYLGERM 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
2VDC_D 1351 SGATVVVEG-CGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVY 1395
Cdd:TIGR03122 162 RGGEILIKGnAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVG 207
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1254-1381 |
6.61e-07 |
|
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: 51.58 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 1254 FGMFGlqpGHITIRlrGTAGQSLGAFAVQGIkLEVMGDANDYVG-------KGLSGGTIVVRPTTsspletnkntiiGNT 1326
Cdd:cd00980 54 AGMKG---GKLVVE--GNAGSWAGCEMKGGE-ITIKGNAGDYVGsayrgdwRGMSGGTITIEGNA------------GDR 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
2VDC_D 1327 VLYGATAGKLFAAGQAGERFAVRNSGATVVVEG-CGSNGCEYMTGGTAVILGRVGD 1381
Cdd:cd00980 116 LGERMRRGEILIKGDAGIFAGIRMNGGTIIVRGdAGAHPGYEMKRGTIVIGGEIEE 171
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
164-391 |
2.48e-06 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 50.73 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 164 INDFYICSLSARSIIYKGMFLAEQLTTFYpDLldERFESDFAIYHQRYSTNTFPTWPLAQPFRM----LAHNGEINTVKG 239
Cdd:cd01907 42 DPDAFVYSSGKDMEVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2VDC_D 240 NVNWMkahetRMEHPAFGTHmqdlkpvigvglSDSGSLDTVFEVMVRAGRtapmVKMMLVPQALTSSQTTPDNHKALIQ- 318
Cdd:cd01907 119 NREYL-----ERFGYKFETE------------TDTEVIAYYLDLLLRKGG----LPLEYYKHIIRMPEEERELLLALRLt 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2VDC_D 319 YCNSVMepwDGPAALAMTDGRWVVGGMDRNGLRPMrYTITTDGLIIGGSEtgMVKIDETQVIEKGR---LGPGEMI 391
Cdd:cd01907 178 YRLADL---DGPFTIIVGTPDGFIVIRDRIKLRPA-VVAETDDYVAIASE--ECAIREIPDRDNAKvwePRPGEYV 247
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1340-1396 |
6.69e-04 |
|
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: 43.06 E-value: 6.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
2VDC_D 1340 GQAGERFAVRNSGATVVVEGCGSNGC-EYMTGGTAVILGRVGDNFAAGMTGGMAYVYD 1396
Cdd:cd00981 53 GVPGNDLGAFMSGPTIIVYGNAQDDVgNTMNDGKIVIHGSAGDVLGYAMRGGKIFIRG 110
|
|
| |
