|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
1-1482 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 2973.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1 MTAGLYRPDDFRDNCGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRtAVQTEQAVT 80
Cdd:PRK11750 1 MHMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFR-AVAEEAGWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 81 LPEDYAVAQIFLSADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTT-LSKEQVAVT 159
Cdd:PRK11750 80 LAKNYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAgWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 160 LFLLRRKIEKALVHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLA 239
Cdd:PRK11750 160 LFIARRRIEKRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 240 HNGEINTIEGNRNWTEARRNKFVSDRLPDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMD 319
Cdd:PRK11750 240 HNGEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDMD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 320 PDVKAFYEYNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQI 399
Cdd:PRK11750 320 PDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 400 IAVDTETGQLLNNEAIENELKSAHPYKQWLRDGAARIESTLGGAENDL---LLSKVQLPIYQKMFQVSFEEREQVLRPLA 476
Cdd:PRK11750 400 LVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVgsrELDDDTLKSYQKQFQYSFEELDQVIRVLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 477 DSGNEATGSMGDDTPMAVLSQKQRGLYDYFRQKFAQVTNPPIDPLREAIVMSLESCLGAEKNVFEQSPAHAERIVLNSPI 556
Cdd:PRK11750 480 ENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 557 LSAYKFNALLQVERVGYSSISLDLCYDPEQKNLQQAVQNLCQQAVAAAKQGHTLIVLSDRQLTPQRLPIHSLMATGAVHH 636
Cdd:PRK11750 560 LSYSDFKQLTTLDEEHYRADTLDLNYDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVGAVQH 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 637 CLIKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILGDPIQIHRNYRKGVNKGLLKILSK 716
Cdd:PRK11750 640 RLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYKIMSK 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 717 MGIATIASYRGAQLFEAVGLAEDVVDLCFCGVASRIKGAGFSDLERDQLALAKNAWLSRKPMEQGGLLKYVHGQEYHAFN 796
Cdd:PRK11750 720 MGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARKPIDQGGLLKYVHGGEYHAYN 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 797 PDVVCQLQAAVQAGDYKLWKIYADSVNTRPVATLRDLLGFSKNINPIDIADVEPIENILPRFDSAGMSLGALSPEAHEAL 876
Cdd:PRK11750 800 PDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAHEAL 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 877 AMAMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNTLIARL 956
Cdd:PRK11750 880 AIAMNRLGGRSNSGEGGEDPARYGTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARL 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 957 RYAVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTAASPLA 1036
Cdd:PRK11750 960 RYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLT 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1037 SIRYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLNNCATG 1116
Cdd:PRK11750 1040 SVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATG 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1117 VATQNDYLRDKHFIGTVEMVMHFFKFIAEETREWLAVLGVRSLEDLIGRTDLLVQLEGQTDKHKNLDYSAILYKDAEFAE 1196
Cdd:PRK11750 1120 VATQDEKLRKNHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPLLETAEPPAG 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1197 QAEFCQVSNNQPFDKGLTAEAILAATQQAIVNKTGGEFTFTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLSGTGG 1276
Cdd:PRK11750 1200 KALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPIKLRFTGTAG 1279
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1277 QSFGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEGVQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVRNSGC 1356
Cdd:PRK11750 1280 QSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGA 1359
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1357 HAVIEGAGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFAYVLDEDRSFVDKYNSELVQIQRlnVESMEAYRHHLRSNIRE 1436
Cdd:PRK11750 1360 IAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILR--VEDLEIHREHLRGLITE 1437
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*.
gi 648552595 1437 FVDETGSEWGQYILDNFVDYIGKFWMVSPKAASLDALLASTKQRPE 1482
Cdd:PRK11750 1438 HVEETGSEWGEEILANFDDYLRKFWLVKPKAADVKALLGHRSRSAA 1483
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
3-1482 |
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: 1337.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 3 AGLYRPDDFRDNCGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRTAVQtEQAVTLP 82
Cdd:COG0070 25 DGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAG-LAAGLLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 83 EDYAVAQIFLSADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTTLSKE-QVAVTLF 161
Cdd:COG0070 104 LAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRrRRRRRRE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 162 LLRRKIEKALVHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLAHN 241
Cdd:COG0070 184 FRRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNNNNN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 242 GEINTIEGNRNWTEARRNKFVSDRLPDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMDPD 321
Cdd:COG0070 264 NNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAAAAD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 322 VKAFYEYNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQIIA 401
Cdd:COG0070 344 LYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGLLDD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 402 VDT---ETGQLLNNEAIENELKSAHPYKQWLRDGAARIESTLGGAENDLLLSKVQLPIYQKMFQVSFEEREQVLRPLADS 478
Cdd:COG0070 424 EEEdaeELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAAAAA 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 479 GNEATGSMGDDTPMAVLSQKQRGLYDYFRQKFAQVTNPPIDPLREAIVMSLESCLGAEKNVFEQSPAHAERIVLNSPILS 558
Cdd:COG0070 504 LDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLLLLL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 559 AYKFNALLQVERVGYSSISLDLCYDPEQKNLQQAVQNLCQQAVAAAKQGHTLIVLSDRQLTPQRLPIHSLMATGAVHHCL 638
Cdd:COG0070 584 LGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHHLLRALGRVLVLL 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 639 IKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILGDPIQIHRNYRKGVNKGLLKILSKMG 718
Cdd:COG0070 664 VEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSSGGG 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 719 IATIASYRGAQLFEAVGLAEDVVDLCFCGVASRIKGAGFSDLERDQLALAKNAWLSRKPMEQGGLLKYVHGQEYHAFNPD 798
Cdd:COG0070 744 IIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQ 823
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 799 VVCQLQAAVQAGDYKLWKIYADSVNTRPVATLRDLLGFSKNINPIDIADVEPIENILPRFDSAGMSLGALSPEAHEALAM 878
Cdd:COG0070 824 LAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAMNRI 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 879 AMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNTLIARLRY 958
Cdd:COG0070 904 GGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRH 983
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 959 AVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTAASPLASI 1038
Cdd:COG0070 984 STPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPLSSI 1063
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1039 RYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLNNCATGVA 1118
Cdd:COG0070 1064 KHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVA 1143
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1119 TQNDYLRDKHFIGTVEMVMHFFKFIAEETREWLAVLGVRSLEDLIGRTDLLVQLEGQTDKHKNLDYSAILYKDAEFAEQA 1198
Cdd:COG0070 1144 TQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPDVPADVP 1223
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1199 EFCQVSNNQPFDKGLtAEAILAATQQAIVNKTGGEFTFTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLSGTGGQS 1278
Cdd:COG0070 1224 RYCTEEQNHGLEGAL-DRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTGSAGQS 1302
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1279 FGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEGVQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVRNSGCHA 1358
Cdd:COG0070 1303 FGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATA 1382
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1359 VIEGAGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFAYVLDEDRSFVDKYNSELVQIQRLNVesmEAYRHHLRSNIREFV 1438
Cdd:COG0070 1383 VVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDE---EEDEEELRELIEEHV 1459
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 648552595 1439 DETGSEWGQYILDNFVDYIGKFWMVSPKAASLDALLASTKQRPE 1482
Cdd:COG0070 1460 EYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAG 1503
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
15-428 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 665.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 15 CGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRtAVQTEQAVTLPE--DYAVAQIFL 92
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFR-KEAKELGIELPEagQYAVGMVFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 93 SADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTT-LSKEQVAVTLFLLRRKIEKAL 171
Cdd:pfam00310 80 PQDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAgKSEDDFERKLYVARKRIEKEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 172 V---HDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLAHNGEINTIE 248
Cdd:pfam00310 160 GvegGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 249 GNRNWTEARRNKFVSDRLP-DLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMDPDVKAFYE 327
Cdd:pfam00310 240 GNRNWMRAREALLKSELFGdDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 328 YNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQIIAVDTETG 407
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 648552595 408 QLLNNEAIENELKSAHPYKQW 428
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
15-423 |
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: 623.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 15 CGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRTAV-QTEQAVTLPEDYAVAQIFLS 93
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELaEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 94 ADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTT-LSKEQVAVTLFLLRRKIEKAL- 171
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSgDDGEAFERKLYLLRKRIEKAIr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 172 VHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLAHNGEINTIEGNR 251
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 252 NWTEARRNKFVSDRL-PDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMDPDVKAFYEYNS 330
Cdd:cd00713 241 NWMRAREGLLKSPLFgEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 331 MHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQIIAVDTETGQLL 410
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|...
gi 648552595 411 NNEAIENELKSAH 423
Cdd:cd00713 401 DDEEIKDQLAKRH 413
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1293-1393 |
2.26e-06 |
|
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: 50.80 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1293 GDANDYVGKGMAGGKIVlrppegvqfssqdtpIMGNTCLYGA---TGGKLFASGRAGERF--AVRN-----SGCHAVIEG 1362
Cdd:TIGR03122 87 GDVGMHVGAEMKGGKIV---------------VNGNADSWAGcemKGGEIIIKGNAGDYVgsAYRGewrgmSGGKIIVEG 151
|
90 100 110
....*....|....*....|....*....|..
gi 648552595 1363 -AGDHCCEYMTGGNVTVIGSTGVNFGAGMTGG 1393
Cdd:TIGR03122 152 nAGDYLGERMRGGEILIKGNAGIFAGIHMNGG 183
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
1-1482 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 2973.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1 MTAGLYRPDDFRDNCGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRtAVQTEQAVT 80
Cdd:PRK11750 1 MHMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFR-AVAEEAGWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 81 LPEDYAVAQIFLSADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTT-LSKEQVAVT 159
Cdd:PRK11750 80 LAKNYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAgWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 160 LFLLRRKIEKALVHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLA 239
Cdd:PRK11750 160 LFIARRRIEKRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 240 HNGEINTIEGNRNWTEARRNKFVSDRLPDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMD 319
Cdd:PRK11750 240 HNGEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDMD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 320 PDVKAFYEYNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQI 399
Cdd:PRK11750 320 PDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 400 IAVDTETGQLLNNEAIENELKSAHPYKQWLRDGAARIESTLGGAENDL---LLSKVQLPIYQKMFQVSFEEREQVLRPLA 476
Cdd:PRK11750 400 LVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVgsrELDDDTLKSYQKQFQYSFEELDQVIRVLA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 477 DSGNEATGSMGDDTPMAVLSQKQRGLYDYFRQKFAQVTNPPIDPLREAIVMSLESCLGAEKNVFEQSPAHAERIVLNSPI 556
Cdd:PRK11750 480 ENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 557 LSAYKFNALLQVERVGYSSISLDLCYDPEQKNLQQAVQNLCQQAVAAAKQGHTLIVLSDRQLTPQRLPIHSLMATGAVHH 636
Cdd:PRK11750 560 LSYSDFKQLTTLDEEHYRADTLDLNYDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVGAVQH 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 637 CLIKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILGDPIQIHRNYRKGVNKGLLKILSK 716
Cdd:PRK11750 640 RLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYKIMSK 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 717 MGIATIASYRGAQLFEAVGLAEDVVDLCFCGVASRIKGAGFSDLERDQLALAKNAWLSRKPMEQGGLLKYVHGQEYHAFN 796
Cdd:PRK11750 720 MGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARKPIDQGGLLKYVHGGEYHAYN 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 797 PDVVCQLQAAVQAGDYKLWKIYADSVNTRPVATLRDLLGFSKNINPIDIADVEPIENILPRFDSAGMSLGALSPEAHEAL 876
Cdd:PRK11750 800 PDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAHEAL 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 877 AMAMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNTLIARL 956
Cdd:PRK11750 880 AIAMNRLGGRSNSGEGGEDPARYGTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARL 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 957 RYAVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTAASPLA 1036
Cdd:PRK11750 960 RYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLT 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1037 SIRYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLNNCATG 1116
Cdd:PRK11750 1040 SVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATG 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1117 VATQNDYLRDKHFIGTVEMVMHFFKFIAEETREWLAVLGVRSLEDLIGRTDLLVQLEGQTDKHKNLDYSAILYKDAEFAE 1196
Cdd:PRK11750 1120 VATQDEKLRKNHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPLLETAEPPAG 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1197 QAEFCQVSNNQPFDKGLTAEAILAATQQAIVNKTGGEFTFTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLSGTGG 1276
Cdd:PRK11750 1200 KALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPIKLRFTGTAG 1279
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1277 QSFGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEGVQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVRNSGC 1356
Cdd:PRK11750 1280 QSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGA 1359
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1357 HAVIEGAGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFAYVLDEDRSFVDKYNSELVQIQRlnVESMEAYRHHLRSNIRE 1436
Cdd:PRK11750 1360 IAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILR--VEDLEIHREHLRGLITE 1437
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*.
gi 648552595 1437 FVDETGSEWGQYILDNFVDYIGKFWMVSPKAASLDALLASTKQRPE 1482
Cdd:PRK11750 1438 HVEETGSEWGEEILANFDDYLRKFWLVKPKAADVKALLGHRSRSAA 1483
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
3-1482 |
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: 1337.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 3 AGLYRPDDFRDNCGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRTAVQtEQAVTLP 82
Cdd:COG0070 25 DGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAG-LAAGLLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 83 EDYAVAQIFLSADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTTLSKE-QVAVTLF 161
Cdd:COG0070 104 LAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRrRRRRRRE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 162 LLRRKIEKALVHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLAHN 241
Cdd:COG0070 184 FRRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNNNNN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 242 GEINTIEGNRNWTEARRNKFVSDRLPDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMDPD 321
Cdd:COG0070 264 NNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAAAAD 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 322 VKAFYEYNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQIIA 401
Cdd:COG0070 344 LYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGLLDD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 402 VDT---ETGQLLNNEAIENELKSAHPYKQWLRDGAARIESTLGGAENDLLLSKVQLPIYQKMFQVSFEEREQVLRPLADS 478
Cdd:COG0070 424 EEEdaeELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAAAAA 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 479 GNEATGSMGDDTPMAVLSQKQRGLYDYFRQKFAQVTNPPIDPLREAIVMSLESCLGAEKNVFEQSPAHAERIVLNSPILS 558
Cdd:COG0070 504 LDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLLLLL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 559 AYKFNALLQVERVGYSSISLDLCYDPEQKNLQQAVQNLCQQAVAAAKQGHTLIVLSDRQLTPQRLPIHSLMATGAVHHCL 638
Cdd:COG0070 584 LGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHHLLRALGRVLVLL 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 639 IKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILGDPIQIHRNYRKGVNKGLLKILSKMG 718
Cdd:COG0070 664 VEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSSGGG 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 719 IATIASYRGAQLFEAVGLAEDVVDLCFCGVASRIKGAGFSDLERDQLALAKNAWLSRKPMEQGGLLKYVHGQEYHAFNPD 798
Cdd:COG0070 744 IIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQ 823
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 799 VVCQLQAAVQAGDYKLWKIYADSVNTRPVATLRDLLGFSKNINPIDIADVEPIENILPRFDSAGMSLGALSPEAHEALAM 878
Cdd:COG0070 824 LAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAMNRI 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 879 AMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNTLIARLRY 958
Cdd:COG0070 904 GGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRH 983
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 959 AVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTAASPLASI 1038
Cdd:COG0070 984 STPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPLSSI 1063
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1039 RYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLNNCATGVA 1118
Cdd:COG0070 1064 KHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVA 1143
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1119 TQNDYLRDKHFIGTVEMVMHFFKFIAEETREWLAVLGVRSLEDLIGRTDLLVQLEGQTDKHKNLDYSAILYKDAEFAEQA 1198
Cdd:COG0070 1144 TQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPDVPADVP 1223
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1199 EFCQVSNNQPFDKGLtAEAILAATQQAIVNKTGGEFTFTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLSGTGGQS 1278
Cdd:COG0070 1224 RYCTEEQNHGLEGAL-DRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTGSAGQS 1302
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1279 FGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEGVQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVRNSGCHA 1358
Cdd:COG0070 1303 FGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATA 1382
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1359 VIEGAGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFAYVLDEDRSFVDKYNSELVQIQRLNVesmEAYRHHLRSNIREFV 1438
Cdd:COG0070 1383 VVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDE---EEDEEELRELIEEHV 1459
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 648552595 1439 DETGSEWGQYILDNFVDYIGKFWMVSPKAASLDALLASTKQRPE 1482
Cdd:COG0070 1460 EYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAG 1503
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
2-1482 |
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: 1180.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 2 TAGLYRPDDFRDNCGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRtAVQTEQAVTL 81
Cdd:COG0067 10 AQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFR-AEAAELGIEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 82 PE--DYAVAQIFLSADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVT-TLSKEQVAV 158
Cdd:COG0067 89 PEpgEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPdGLDGDAFER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 159 TLFLLRRKIEKAL----VHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQP 234
Cdd:COG0067 169 KLYVARKRIEKAIralgLDDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 235 FRLLAHNGEINTIEGNRNWTEARRNKFVSDRL-PDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQ 313
Cdd:COG0067 249 FRYLAHNGEINTLRGNRNWMRAREALLASPLFgDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMMLIPEAWE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 314 NMDRMDPDVKAFYEYNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGR 393
Cdd:COG0067 329 NNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 394 VGPGQIIAVDTETGQLLNNEAIENELKSAHPYKQWLRDGAARIESTLGGAENDLLLSKVQLPIYQKMFQVSFEEREQVLr 473
Cdd:COG0067 409 LQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDLLLRRQQAFGYTEEEELLLLL- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 474 PLADSGNEATGSMGDDTPMAVLSQKQRGLYDYFRQKFAQVTNPPIDPLREAIVMSLES-CLGAEKNVFEQSPAHAERIVL 552
Cdd:COG0067 488 PMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTtGGGGNNLLLEEEEARRRLLLL 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 553 NSPILSAYKFNALLQVERVGYSSISLDLCYDPEQKNLQQAVQNLCQQAVAAAKQGHTLIVLSDRQLTPQRLPIHSLMATG 632
Cdd:COG0067 568 PPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDAAPAPLAAA 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 633 AVHHCLIKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILGDPIQIHRNYRKGVNKGLLK 712
Cdd:COG0067 648 AAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAAAAKKKKKKKKG 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 713 ILSKMGIATIASYRGAQLFEAVGLAEDVVDLCFCGVASRIKGAGFSDLERDQLALAKNAWLSRKPMEQGGLLKYVHGQEY 792
Cdd:COG0067 728 KLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLLGLGGGGG 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 793 HAFNPDVVCQLQAAVQAGDYKLWKIYADSVNTRPVATLRDLLGFSKNINPIDIADVEPIENILPRFDSAGMSLGALSPEA 872
Cdd:COG0067 808 GEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEEEEEESSAIAAAS 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 873 HEALAMAMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNTL 952
Cdd:COG0067 888 SAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRRASGGSGSSSSASVAAAGGGVVVGAGAAAAEGGGGGGGGGGGG 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 953 IARLRYAVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTAA 1032
Cdd:COG0067 968 GGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAAAAAAAAAAA 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1033 SPLASIRYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLNN 1112
Cdd:COG0067 1048 AVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGALGGGAAALVV 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1113 CATGVATQNDYLRDKHFIGTVEMVMHFFKFIAEETREWLAVLGVRSLEDLIGRTDLLVQLEGQTDKHKNLDYSAILYKDA 1192
Cdd:COG0067 1128 VGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLGVVELLLLLLLLLLLA 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1193 EFAEQAEFCQVSNNQPFDKGLTAEAILAATQQAIVNKTGGEFTFTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLS 1272
Cdd:COG0067 1208 KLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGGGGGGGGGGGGGG 1287
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1273 GTGGQSFGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEGVQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVR 1352
Cdd:COG0067 1288 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGA 1367
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1353 NSGCHAVIEGAGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFAYVLDEDRSFVDKYNSELVQIQRLNVESMEAYRHHLRS 1432
Cdd:COG0067 1368 GGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDEEEEEELEELLLL 1447
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|
gi 648552595 1433 NIREFVDETGSEWGQYILDNFVDYIGKFWMVSPKAASLDALLASTKQRPE 1482
Cdd:COG0067 1448 LEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAA 1497
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
629-1352 |
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: 954.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 629 MATGAVHHCLIKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILGDPIQIHRNYRKGVNK 708
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 709 GLLKILSKMGIATIASYRGAQLFEAVGLAEDVVDLcfcGVAsrikgagfsdlerDQLALAKNAWlsRKPMEQGGLLKYVH 788
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDI---GIA-------------DVLTQHRHAI--LRNLPVGGRYRYRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 789 --------------GQEYHAFNPDVVCQLQAAVQAGDykLWKIYADSVNTRP--VATLRDLLGFSKNINPIDI-ADVEPI 851
Cdd:COG0069 143 esigpeirqyffesDGEEHPFNRETRSLLYQAAKNEE--DYKPFGTLVDYQPgyEWTLRSLFPFKADRPPIPIgEPVEPP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 852 ENILPRFDSAGMSLGALSPEAHEALAMAMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVT---PHYLVNAEVL 928
Cdd:COG0069 221 YSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHLGDGGGDAIKQIASGRFGVRdedGEYLPNAKMI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 929 QIKIAQGAKPGEGGQLPGGKVNTLIARLRYAVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGT 1008
Cdd:COG0069 301 EIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVGVKLVSGAGVGT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1009 IAA--GVAK--AYADLITISGYDGGTAASPLASIRYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAI 1084
Cdd:COG0069 381 IAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1085 LGAESFGFGTTPMVALGCKFLRICHLNNCATGVATQNDYLRdKHFI--GTVEMVMHFFKFIAEETREWLAVLGVRSLEDL 1162
Cdd:COG0069 461 LGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELR-KGFVveGKPERVVNYFRFTAEEVREILAALGVRSPDEL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1163 IGRTDLLVQLEGQTDKHKNLDYSAILYKDAEFAEQAEFCQVSNNQPFDKGLTAEAILAATQQAIVNKTGGEFTFTINNCD 1242
Cdd:COG0069 540 IGRHDLLRVRDGEHWKAKGLDLSPLLYKPELPEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLITNIRNNNR 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1243 RSIGARLSGEIARHHGNSGMSDnPITLKLSGTGGQSFGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEGVQFSSQD 1322
Cdd:COG0069 620 RVGGMLSGEIAKRYGGAGLPDD-TIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPPGASFFPEE 698
|
730 740 750
....*....|....*....|....*....|
gi 648552595 1323 TPIMGNTCLYGATGGKLFASGRAGERFAVR 1352
Cdd:COG0069 699 NIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
15-428 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 665.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 15 CGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRtAVQTEQAVTLPE--DYAVAQIFL 92
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFR-KEAKELGIELPEagQYAVGMVFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 93 SADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTT-LSKEQVAVTLFLLRRKIEKAL 171
Cdd:pfam00310 80 PQDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAgKSEDDFERKLYVARKRIEKEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 172 V---HDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLAHNGEINTIE 248
Cdd:pfam00310 160 GvegGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 249 GNRNWTEARRNKFVSDRLP-DLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMDPDVKAFYE 327
Cdd:pfam00310 240 GNRNWMRAREALLKSELFGdDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 328 YNSMHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQIIAVDTETG 407
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 648552595 408 QLLNNEAIENELKSAHPYKQW 428
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
15-423 |
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: 623.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 15 CGFGLIAHMQGEPSHELLTTAITSLTCMTHRGGIAADGKTGDGCGLLMKKPDSFLRTAV-QTEQAVTLPEDYAVAQIFLS 93
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELaEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 94 ADPMLASASKNTIAELVAQQQLSLVAWRDVPVDKSVCGEIALSSMPTIMQCFIDVTT-LSKEQVAVTLFLLRRKIEKAL- 171
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSgDDGEAFERKLYLLRKRIEKAIr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 172 VHDEAFYICSLSSAVISYKGLVMPVDLAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFRLLAHNGEINTIEGNR 251
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 252 NWTEARRNKFVSDRL-PDLESIMPLVNKSGSDSSSLDNMLELLVAGGMSLFRAARLLVPPAWQNMDRMDPDVKAFYEYNS 330
Cdd:cd00713 241 NWMRAREGLLKSPLFgEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 331 MHMESWDGPAGIVLTDGRYAVCMLDRNGLRPARYIITKNGFITLASEVGTYPYQPEDIVEKGRVGPGQIIAVDTETGQLL 410
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|...
gi 648552595 411 NNEAIENELKSAH 423
Cdd:cd00713 401 DDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
793-1157 |
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: 546.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 793 HAFNPDVVCQLQAAVQAGDYKLWKIYADSVNTR-PVATLRDLLGFSKNINPIDIADVEPIENILPRFDSAGMSLGALSPE 871
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERvPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 872 AHEALAMAMNRLGGRSNSGEGGEDPARYGTERNSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNT 951
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYADNIAIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPGEKVSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 952 LIARLRYAVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTA 1031
Cdd:pfam01645 161 EIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGYDGGTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1032 ASPLASIRYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLN 1111
Cdd:pfam01645 241 ASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCRVCHTN 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 648552595 1112 NCATGVATQNDYLRD-KHFIGTVEMVMHFFKFIAEETREWLAVLGVR 1157
Cdd:pfam01645 321 TCPVGVATQDPELRKrLDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
810-1169 |
6.73e-160 |
|
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: 488.20 E-value: 6.73e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 810 GDYKLWKIYADSVNTR--PVATLRDLLGFSKNINPIDIAD-------------VEPIENILPRFDSAGMSLGALSPEAHE 874
Cdd:cd02808 17 NRAERYGVYNRAGNSRgrPFGTLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPFNISAMSFGALSKEAKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 875 ALAMAMNRLGGRSNSGEGGEDPARYGTERnSKIKQIASGRFGVTPHYLVNAEVLQIKIAQGAKPGEGGQLPGGKVNTLIA 954
Cdd:cd02808 97 ALAIGAALAGTASNTGEGGELPEEREGGG-DIIKQVASGRFGVRPEYLNKADAIEIKIGQGAKPGEGGHLPGEKVTEEIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 955 RLRYAVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPTALVSVKLVSEPGVGTIAAGVAKAYADLITISGYDGGTAASP 1034
Cdd:cd02808 176 KIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTGAAP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1035 LASIRYAGSPWELGLAETQQTLRANGLRGLVRVQTDGGLKTGLDVVKAAILGAESFGFGTTPMVALGCKFLRICHLNNCA 1114
Cdd:cd02808 256 LTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCP 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 648552595 1115 TGVATQNDYLRD-KHFIGTVEMVMHFFKFIAEETREWLAVLGVRSLEdLIGRTDLL 1169
Cdd:cd02808 336 VGVATQDPELRRrLDVEGKAERVANYLKSLAEELRELAAALGKRSLE-LLGRSDLL 390
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
457-737 |
2.02e-147 |
|
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: 450.29 E-value: 2.02e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 457 YQKMFQVSFEEREQVLRPLADSGNEATGSMGDDTPMAVLSQKQRGLYDYFRQKFAQVTNPPIDPLREAIVMSLESCLGAE 536
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 537 KNVFEQSPAHAERIVLNSPILSAYKFNALLQVERVGYSSISLDLCYDPeqknLQQAVQNLCQQAVAAAKQGHTLIVLSDR 616
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITFDG----LEAALERLCEEAEEAVRDGANILILSDR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 617 QLTPQRLPIHSLMATGAVHHCLIKAGLRCDSNIIVETGSARDSHQIACLIGFGATLVYPYMAYSVLDDLLASGEILG--- 693
Cdd:pfam04898 158 GVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGKGKLtde 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 648552595 694 DPIQIHRNYRKGVNKGLLKILSKMGIATIASYRGAQLFEAVGLA 737
Cdd:pfam04898 238 DLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1218-1466 |
4.01e-125 |
|
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: 389.19 E-value: 4.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1218 ILAATQQAIVNKTGGEFTFTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLSGTGGQSFGVWNAGGLHLYLTGDAND 1297
Cdd:cd00982 6 IADAEPALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELEGDAND 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1298 YVGKGMAGGKIVLRPPEGVQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVRNSGCHAVIEGAGDHCCEYMTGGNVT 1377
Cdd:cd00982 86 YVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGTVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1378 VIGSTGVNFGAGMTGGFAYVLDEDRSFVDKYNSELVQIQRLNvesMEAYRHHLRSNIREFVDETGSEWGQYILDNFVDYI 1457
Cdd:cd00982 166 VLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLE---DAEDEEQLKELIEEHVEYTGSEKAKEILANWEAYL 242
|
....*....
gi 648552595 1458 GKFWMVSPK 1466
Cdd:cd00982 243 KKFVKVIPR 251
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1236-1425 |
3.04e-106 |
|
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: 335.15 E-value: 3.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1236 FTINNCDRSIGARLSGEIARHHGNSGMSDNPITLKLSGTGGQSFGVWNAGGLHLYLTGDANDYVGKGMAGGKIVLRPPEG 1315
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1316 VQFSSQDTPIMGNTCLYGATGGKLFASGRAGERFAVRNSGCHAVIEGAGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFA 1395
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180 190
....*....|....*....|....*....|
gi 648552595 1396 YVLDEDRSFVDKYNSELVQIQRLNVESMEA 1425
Cdd:pfam01493 161 YVLDEDGDFPEKLNKEMVELERVTDEDEEA 190
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1243-1399 |
3.66e-58 |
|
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: 197.41 E-value: 3.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1243 RSIGARLSGEIARHHGNSgmsDNPITLKLSGTGGQSFGVWNAGGlHLYLTGDANDYVGKGMAGGKIVLRPPEGvqfssQD 1322
Cdd:cd00504 1 RAVGTRGSRYIGKRPGLP---EDTVEIIINGSAGQSFGAFMAGG-TITVEGNANDYVGKGMSGGEIVIHPPAG-----DE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648552595 1323 TPIMGNTCLYGATGGKLFASGRAGERFAVRNSGCHAVIEG-AGDHCCEYMTGGNVTVIGSTGVNFGAGMTGGFAYVLD 1399
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGvGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
198-400 |
7.10e-30 |
|
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: 118.71 E-value: 7.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 198 LAKFYLDLANPALETAICVFHQRFSTNTLPRWPLAQPFR------LLAHNGEINTIEGNRNWTEARRNKFVSDrlpdles 271
Cdd:cd00352 54 VSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEARGYRFEGE------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 272 implvnksgSDSSSLDNMLELLVAGGMsLFRAARLLVPPawqnmdrmdpdvkafyeynsmhmesWDGPAGIVLTDG--RY 349
Cdd:cd00352 127 ---------SDSEVILHLLERLGREGG-LFEAVEDALKR-------------------------LDGPFAFALWDGkpDR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 648552595 350 AVCMLDRNGLRPARYIITKNGFITLASEVGTYPyqPEDIVEKGRVGPGQII 400
Cdd:cd00352 172 LFAARDRFGIRPLYYGITKDGGLVFASEPKALL--ALPFKGVRRLPPGELL 220
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1227-1406 |
4.12e-12 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 68.30 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1227 VNKTGGEFTFTINN----CDRsIGARLS-GEIaRHHGNSGMSdnpitlklsgtggqsFGVWNAGGlHLYLTGDANDYVGK 1301
Cdd:COG2218 54 VEGDDGDTKIVIEGdlsrVKR-IGAGMTaGEI-IVEGDVGMY---------------LGAGMKGG-KITVNGNAGSFAGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1302 GMAGGKIVlrppegvqfssqdtpIMGNT------CLYGA----TGGKLFASGRAGERFAVRNSGCHAVIEG-AGDHCCEY 1370
Cdd:COG2218 116 EMKGGEIE---------------INGNAgdflgaAYRGDwrgmSGGTIIVKGNAGDRLGDRMRRGTIIIEGdAGDFAGSR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 648552595 1371 MTGGNVTVIGSTGVNFGAGMTGGFAYVLDEDR----SFVD 1406
Cdd:COG2218 181 MIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPEellpTFVD 220
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1232-1440 |
3.41e-11 |
|
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.
Pssm-ID: 238481 [Multi-domain] Cd Length: 232 Bit Score: 65.01 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1232 GEFTFTINNC--DRSIGARLSGEIarhhgnsgmsdnpiTLKLSGTGGQSFGVWNAGGLhLYLTGDANDYVGKGMAGGKIV 1309
Cdd:cd00981 24 GADEIVLDNVlgQRYIGDGLPGNV--------------RINIYGVPGNDLGAFMSGPT-IIVYGNAQDDVGNTMNDGKIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1310 lrppegVQFSSqdtpimGNTCLYGATGGKLFASGRAGERFAV-----RNSGCHAVIEG-AGDHCCEYMTGGNVTVIG--- 1380
Cdd:cd00981 89 ------IHGSA------GDVLGYAMRGGKIFIRGNAGYRVGIhmkeyKDKVPVLVIGGtAGDFLGEYMAGGVIIVLGlgt 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648552595 1381 ---STGVNFGAGMTGGFAYVldedRSFVDKYN-SELVQIQRLNVESMEAYRHHLRSNIREFVDE 1440
Cdd:cd00981 157 deePVGRYIGTGMHGGVIYI----RGKVERSKlGKEVPKFELTEEDLEFIEKYIEEFCKEFGYD 216
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1260-1393 |
5.61e-10 |
|
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: 60.83 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1260 SGMSDNPITLKlsGTGGQSFGVWNAGGlHLYLTGDANDYVGKGMAGGKIVlrppegvqfssqdtpIMGNT-----CLY-- 1332
Cdd:cd00980 35 ARMTAGEIVVE--GDVGMYVGAGMKGG-KLVVEGNAGSWAGCEMKGGEIT---------------IKGNAgdyvgSAYrg 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648552595 1333 ---GATGGKLFASGRAGERFAVRNSGCHAVIEG-AGDHCCEYMTGGNVTVIGSTGVNFGAGMTGG 1393
Cdd:cd00980 97 dwrGMSGGTITIEGNAGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRG 161
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
178-378 |
1.19e-08 |
|
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: 57.66 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 178 YICSLSSAVISYKGLVMPVDLAKFYlDLanPALETAICVFHQRFSTNTLPRWPLAQPFRL----LAHNGEINTIEGNRNW 253
Cdd:cd01907 46 FVYSSGKDMEVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGSNREY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 254 TEARRNKFvsdrlpdlesimplvnKSGSDSSSLDNMLELLVA-GGMSLFRAARLLVPPAWQnmDRMDPDVKafYEYNSMH 332
Cdd:cd01907 123 LERFGYKF----------------ETETDTEVIAYYLDLLLRkGGLPLEYYKHIIRMPEEE--RELLLALR--LTYRLAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 648552595 333 MeswDGP-AGIVLTDGRYAVCMlDRNGLRPArYIITKNGFITLASEV 378
Cdd:cd01907 183 L---DGPfTIIVGTPDGFIVIR-DRIKLRPA-VVAETDDYVAIASEE 224
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1293-1393 |
2.26e-06 |
|
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: 50.80 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1293 GDANDYVGKGMAGGKIVlrppegvqfssqdtpIMGNTCLYGA---TGGKLFASGRAGERF--AVRN-----SGCHAVIEG 1362
Cdd:TIGR03122 87 GDVGMHVGAEMKGGKIV---------------VNGNADSWAGcemKGGEIIIKGNAGDYVgsAYRGewrgmSGGKIIVEG 151
|
90 100 110
....*....|....*....|....*....|..
gi 648552595 1363 -AGDHCCEYMTGGNVTVIGSTGVNFGAGMTGG 1393
Cdd:TIGR03122 152 nAGDYLGERMRGGEILIKGNAGIFAGIHMNGG 183
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
891-1094 |
2.60e-05 |
|
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: 46.81 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 891 EGGEDPARYGTerNSKIKQIASGRFGVtPHYLVNAEVLQIKIAQGAKPGeggqlPGGKVNTLIARLRYAVPGVTLIsppP 970
Cdd:cd04722 23 EAGADAIIVGT--RSSDPEEAETDDKE-VLKEVAAETDLPLGVQLAIND-----AAAAVDIAAAAARAAGADGVEI---H 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 971 HHDIYSIEDLAQLIFDLKQVNPTALVSVKLVsePGVGTIAAGVAKAYADLITISGYDGGTAASPLASIryAGSPWELGLA 1050
Cdd:cd04722 92 GAVGYLAREDLELIRELREAVPDVKVVVKLS--PTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPI--ADLLLILAKR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 648552595 1051 ETQQTlranglrglvrVQTDGGLKTGLDVVKAAILGAESFGFGT 1094
Cdd:cd04722 168 GSKVP-----------VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1297-1397 |
1.05e-04 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 45.03 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648552595 1297 DYVGKGMAGGKIVlrppegvqfssqdtpIMGNTCLY---GATGGKLFASGRAGERFAVRNSGCHAVIEG-AGDHC-CEY- 1370
Cdd:cd00980 31 KRIGARMTAGEIV---------------VEGDVGMYvgaGMKGGKLVVEGNAGSWAGCEMKGGEITIKGnAGDYVgSAYr 95
|
90 100 110
....*....|....*....|....*....|..
gi 648552595 1371 -----MTGGNVTVIGSTGVNFGAGMTGGFAYV 1397
Cdd:cd00980 96 gdwrgMSGGTITIEGNAGDRLGERMRRGEILI 127
|
|
| |
