|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
30-1512 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 3296.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 30 HDMLYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRLA 109
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 110 KNYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLF 189
Cdd:PRK11750 82 KNYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERRLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 190 IARRRIEKRLEADKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHN 269
Cdd:PRK11750 162 IARRRIEKRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLAHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 270 GEINTITGNRQWARARTYKFQTPLIPDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPE 349
Cdd:PRK11750 242 GEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDMDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 350 LRAFFDFNSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMV 429
Cdd:PRK11750 322 LRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 430 IDTRSGRILHSAETDDDLKSRHPYKEWMEKNVRRLVPFEDLPDEEVGSRELDDDTLASYQKQFNYSAEELDSVIRVLGEN 509
Cdd:PRK11750 402 IDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRVLAEN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 510 GQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGREMNVFCEAEGQAHRLSFKSPILL 589
Cdd:PRK11750 482 GQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPVLS 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 590 YSDFKQLTTMKEEHYRADTLDITFDVTKTTLEATVKELCDKAEKMVRSGTVLLVLSDRNIAKDRLPVPAPMAVGAIQTRL 669
Cdd:PRK11750 562 YSDFKQLTTLDEEHYRADTLDLNYDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVGAVQHRL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 670 VDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGINKGLYKIMSKMG 749
Cdd:PRK11750 642 VDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYKIMSKMG 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 750 ISTIASYRCSKLFEAVGLHNDVVGLCFQGAVSRIGGASFEDFQQDLLNLSKRAWLARKPISQGGLLKYVHGGEYHAYNPD 829
Cdd:PRK11750 722 ISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARKPIDQGGLLKYVHGGEYHAYNPD 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 830 VVRTLQQAVQSGEYSDYQEYAKLVNERPATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSPEAHEALAE 909
Cdd:PRK11750 802 VVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAHEALAI 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 910 AMNSIGGNSNSGEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTPYIAKLRY 989
Cdd:PRK11750 882 AMNRLGGRSNSGEGGEDPARYGTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRY 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 990 SVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADLITIAGYDGGTGASPLSSV 1069
Cdd:PRK11750 962 SVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLTSV 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1070 KYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVA 1149
Cdd:PRK11750 1042 KYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVA 1121
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1150 TQDDKLRKNHYHGLPFKVTNYFEFIARETRELMAQLGVTRLVDLIGRTDLLKELDGFTAKQQKLALSKLLETAEPHPGKA 1229
Cdd:PRK11750 1122 TQDEKLRKNHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPLLETAEPPAGKA 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1230 LYCTET-NPPFDNGLLNAQLLQQAKPFVDERQSKTFWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFNGTAGQS 1308
Cdd:PRK11750 1202 LYCTEErNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPIKLRFTGTAGQS 1281
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1309 FGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVRNSGAIT 1388
Cdd:PRK11750 1282 FGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIA 1361
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1389 VVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEVLSVDDLAIHEEHLRGLITEHVQH 1468
Cdd:PRK11750 1362 VVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILRVEDLEIHREHLRGLITEHVEE 1441
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 1398297727 1469 TGSQRGEEILANWSTFATKFALVKPKSSDVKALLGHRSRSAAEL 1512
Cdd:PRK11750 1442 TGSEWGEEILANFDDYLRKFWLVKPKAADVKALLGHRSRSAAEL 1485
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
27-1511 |
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: 1363.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 27 GEVHDMLYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGW 106
Cdd:COG0070 21 GAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 107 RLAKNYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMER 186
Cdd:COG0070 101 LLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 187 RLFIARRRIEKRLEADKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYL 266
Cdd:COG0070 181 RREFRRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 267 AHNGEINTITGNRQWARARTYKFQTPLIPDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDM 346
Cdd:COG0070 261 NNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 347 DPELRAFFDFNSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGE 426
Cdd:COG0070 341 AADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 427 LMVIDTRSGRILHSAETDDDLKSRHPYKEWMEKNVRRLVPFEDLPDEEVGSRELDDDTLASYQKQFNYSAEELDSVIRVL 506
Cdd:COG0070 421 LDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 507 GENGQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGREMNVFCEAEGQAHRLSFKSP 586
Cdd:COG0070 501 AAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 587 ILLYSDFKQLTTMKEEHYRADTLDITFDVTKTTLEATVKELCDKAEKMVRSGTVLLVLSDRNIAKDRLPVPAPMAVGAIQ 666
Cdd:COG0070 581 LLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHHLLRALGRVL 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 667 TRLVDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGINKGLYKIMS 746
Cdd:COG0070 661 VLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSS 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 747 KMGISTIASYRCSKLFEAVGLHNDVVGLCFQGAVSRIGGASFEDFQQDLLNLSKRAWLARKPISQGGLLKYVHGGEYHAY 826
Cdd:COG0070 741 GGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYHHL 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 827 NPDVVRTLQQAVQSGEYSDYQEYAKLVNERPATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSPEAHEA 906
Cdd:COG0070 821 LQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAM 900
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 907 LAEAMNSIGGNSNSGEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTPYIAK 986
Cdd:COG0070 901 NRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIAR 980
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 987 LRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADLITIAGYDGGTGASPL 1066
Cdd:COG0070 981 LRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPL 1060
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1067 SSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCAT 1146
Cdd:COG0070 1061 SSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPV 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1147 GVATQDDKLRKNHYHGLPFKVtNYFEFIARETRELMAQLGVTRLVDLIGRTDLLKE-LDGFTAKQQKLALSKLLETAEPH 1225
Cdd:COG0070 1141 GVATQDPELRKRFFGGPEHVV-NFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVrRAVDHWKAKGLDLSPLLYKPDVP 1219
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1226 PGKALYCTEtnpPFDNGL---LNAQLLQQAKPFVDERQSKTFWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFN 1302
Cdd:COG0070 1220 ADVPRYCTE---EQNHGLegaLDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFT 1296
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1303 GTAGQSFGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVR 1382
Cdd:COG0070 1297 GSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVR 1376
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1383 NSGAITVVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEVLSVDDlAIHEEHLRGLI 1462
Cdd:COG0070 1377 NSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDE-EEDEEELRELI 1455
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*....
gi 1398297727 1463 TEHVQHTGSQRGEEILANWSTFATKFALVKPKSSDVKALLGHRSRSAAE 1511
Cdd:COG0070 1456 EEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGL 1504
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
43-456 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 740.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 43 CGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRLAK--NYAVGMLFLN 120
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEagQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 121 KDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFIARRRIEKRL- 199
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 200 --EADKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHNGEINTITG 277
Cdd:pfam00310 161 veGGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 278 NRQWARARTYKFQTPLIP-DLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPELRAFFDF 356
Cdd:pfam00310 241 NRNWMRAREALLKSELFGdDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 357 NSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMVIDTRSGR 436
Cdd:pfam00310 321 HSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEGR 400
|
410 420
....*....|....*....|
gi 1398297727 437 ILHSAETDDDLKSRHPYKEW 456
Cdd:pfam00310 401 IIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
43-451 |
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: 664.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 43 CGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRL--AKNYAVGMLFLN 120
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELpeAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 121 KDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFIARRRIEKRLE 200
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 201 A-DKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHNGEINTITGNR 279
Cdd:cd00713 161 AaDEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 280 QWARARTYKFQTPLI-PDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPELRAFFDFNS 358
Cdd:cd00713 241 NWMRAREGLLKSPLFgEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 359 MHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMVIDTRSGRIL 438
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|...
gi 1398297727 439 HSAETDDDLKSRH 451
Cdd:cd00713 401 DDEEIKDQLAKRH 413
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1318-1423 |
1.42e-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: 51.57 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1318 ELYLTGDANDYVGKGMAGGLIAIRPPVGS----AFRSHEASIIGNT-----CLY-----GATGGRLYAAGRAGERFGVRN 1383
Cdd:TIGR03122 82 EIVVEGDVGMHVGAEMKGGKIVVNGNADSwagcEMKGGEIIIKGNAgdyvgSAYrgewrGMSGGKIIVEGNAGDYLGERM 161
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1398297727 1384 SGAITVVEG-IGDNGCEYMTGGIVCILGKTGVNFGAGMTGG 1423
Cdd:TIGR03122 162 RGGEILIKGnAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRG 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
30-1512 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 3296.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 30 HDMLYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRLA 109
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 110 KNYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLF 189
Cdd:PRK11750 82 KNYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERRLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 190 IARRRIEKRLEADKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHN 269
Cdd:PRK11750 162 IARRRIEKRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLAHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 270 GEINTITGNRQWARARTYKFQTPLIPDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPE 349
Cdd:PRK11750 242 GEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDMDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 350 LRAFFDFNSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMV 429
Cdd:PRK11750 322 LRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 430 IDTRSGRILHSAETDDDLKSRHPYKEWMEKNVRRLVPFEDLPDEEVGSRELDDDTLASYQKQFNYSAEELDSVIRVLGEN 509
Cdd:PRK11750 402 IDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRVLAEN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 510 GQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGREMNVFCEAEGQAHRLSFKSPILL 589
Cdd:PRK11750 482 GQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKSPVLS 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 590 YSDFKQLTTMKEEHYRADTLDITFDVTKTTLEATVKELCDKAEKMVRSGTVLLVLSDRNIAKDRLPVPAPMAVGAIQTRL 669
Cdd:PRK11750 562 YSDFKQLTTLDEEHYRADTLDLNYDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVGAVQHRL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 670 VDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGINKGLYKIMSKMG 749
Cdd:PRK11750 642 VDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYKIMSKMG 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 750 ISTIASYRCSKLFEAVGLHNDVVGLCFQGAVSRIGGASFEDFQQDLLNLSKRAWLARKPISQGGLLKYVHGGEYHAYNPD 829
Cdd:PRK11750 722 ISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARKPIDQGGLLKYVHGGEYHAYNPD 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 830 VVRTLQQAVQSGEYSDYQEYAKLVNERPATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSPEAHEALAE 909
Cdd:PRK11750 802 VVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAHEALAI 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 910 AMNSIGGNSNSGEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTPYIAKLRY 989
Cdd:PRK11750 882 AMNRLGGRSNSGEGGEDPARYGTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRY 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 990 SVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADLITIAGYDGGTGASPLSSV 1069
Cdd:PRK11750 962 SVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLTSV 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1070 KYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVA 1149
Cdd:PRK11750 1042 KYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVA 1121
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1150 TQDDKLRKNHYHGLPFKVTNYFEFIARETRELMAQLGVTRLVDLIGRTDLLKELDGFTAKQQKLALSKLLETAEPHPGKA 1229
Cdd:PRK11750 1122 TQDEKLRKNHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETAKQQKLDLSPLLETAEPPAGKA 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1230 LYCTET-NPPFDNGLLNAQLLQQAKPFVDERQSKTFWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFNGTAGQS 1308
Cdd:PRK11750 1202 LYCTEErNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAPIKLRFTGTAGQS 1281
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1309 FGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVRNSGAIT 1388
Cdd:PRK11750 1282 FGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIA 1361
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1389 VVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEVLSVDDLAIHEEHLRGLITEHVQH 1468
Cdd:PRK11750 1362 VVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILRVEDLEIHREHLRGLITEHVEE 1441
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 1398297727 1469 TGSQRGEEILANWSTFATKFALVKPKSSDVKALLGHRSRSAAEL 1512
Cdd:PRK11750 1442 TGSEWGEEILANFDDYLRKFWLVKPKAADVKALLGHRSRSAAEL 1485
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
27-1511 |
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: 1363.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 27 GEVHDMLYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGW 106
Cdd:COG0070 21 GAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 107 RLAKNYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMER 186
Cdd:COG0070 101 LLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 187 RLFIARRRIEKRLEADKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYL 266
Cdd:COG0070 181 RREFRRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 267 AHNGEINTITGNRQWARARTYKFQTPLIPDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDM 346
Cdd:COG0070 261 NNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 347 DPELRAFFDFNSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGE 426
Cdd:COG0070 341 AADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 427 LMVIDTRSGRILHSAETDDDLKSRHPYKEWMEKNVRRLVPFEDLPDEEVGSRELDDDTLASYQKQFNYSAEELDSVIRVL 506
Cdd:COG0070 421 LDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 507 GENGQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGREMNVFCEAEGQAHRLSFKSP 586
Cdd:COG0070 501 AAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLL 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 587 ILLYSDFKQLTTMKEEHYRADTLDITFDVTKTTLEATVKELCDKAEKMVRSGTVLLVLSDRNIAKDRLPVPAPMAVGAIQ 666
Cdd:COG0070 581 LLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHHLLRALGRVL 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 667 TRLVDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGINKGLYKIMS 746
Cdd:COG0070 661 VLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSS 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 747 KMGISTIASYRCSKLFEAVGLHNDVVGLCFQGAVSRIGGASFEDFQQDLLNLSKRAWLARKPISQGGLLKYVHGGEYHAY 826
Cdd:COG0070 741 GGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGGGGRGGGGEGHHGGHYHHL 820
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 827 NPDVVRTLQQAVQSGEYSDYQEYAKLVNERPATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSPEAHEA 906
Cdd:COG0070 821 LQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAM 900
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 907 LAEAMNSIGGNSNSGEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTPYIAK 986
Cdd:COG0070 901 NRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIAR 980
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 987 LRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADLITIAGYDGGTGASPL 1066
Cdd:COG0070 981 LRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPL 1060
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1067 SSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCAT 1146
Cdd:COG0070 1061 SSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPV 1140
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1147 GVATQDDKLRKNHYHGLPFKVtNYFEFIARETRELMAQLGVTRLVDLIGRTDLLKE-LDGFTAKQQKLALSKLLETAEPH 1225
Cdd:COG0070 1141 GVATQDPELRKRFFGGPEHVV-NFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVrRAVDHWKAKGLDLSPLLYKPDVP 1219
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1226 PGKALYCTEtnpPFDNGL---LNAQLLQQAKPFVDERQSKTFWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFN 1302
Cdd:COG0070 1220 ADVPRYCTE---EQNHGLegaLDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFT 1296
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1303 GTAGQSFGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVR 1382
Cdd:COG0070 1297 GSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVR 1376
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1383 NSGAITVVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEVLSVDDlAIHEEHLRGLI 1462
Cdd:COG0070 1377 NSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDE-EEDEEELRELI 1455
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*....
gi 1398297727 1463 TEHVQHTGSQRGEEILANWSTFATKFALVKPKSSDVKALLGHRSRSAAE 1511
Cdd:COG0070 1456 EEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGL 1504
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
33-1517 |
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: 1215.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 33 LYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRL--AK 110
Cdd:COG0067 13 LYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIELpePG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 111 NYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFI 190
Cdd:COG0067 93 EYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFERKLYV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 191 ARRRIEKRLEA----DKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYL 266
Cdd:COG0067 173 ARKRIEKAIRAlgldDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQPFRYL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 267 AHNGEINTITGNRQWARARTYKFQTPLI-PDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPD 345
Cdd:COG0067 253 AHNGEINTLRGNRNWMRAREALLASPLFgDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMMLIPEAWENNPD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 346 MDPELRAFFDFNSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPG 425
Cdd:COG0067 333 MDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGRLQPG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 426 ELMVIDTRSGRILHSAETDDDLKSRHPYKEWMEKNVRRLvpfEDLPDEEVgSRELDDDTLASYQKQFNYSAEELDSVIRV 505
Cdd:COG0067 413 KMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRL---EDLPEPEE-EPAPDDDLLLRRQQAFGYTEEEELLLLLP 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 506 LGENGQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGREMNVFCEAEGQAH-RLSFK 584
Cdd:COG0067 489 MAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEARRrLLLLP 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 585 SPILLYSDFKQLTTMKEEHYRADTLDITFDVTKTTLEATVKELCDKAEKMVRSGTVLLVLSDRNIAKDRLPVPAPMAVGA 664
Cdd:COG0067 569 PPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDAAPAPLAAAA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 665 IQTRLVDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGIN---KGL 741
Cdd:COG0067 649 AAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAAAAKKKKkkkKGK 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 742 YKIMSKMGISTIASYRCSKLFEAVGLHNDVVGLCFQGAVSRIGGASFEDFQQDLLNLSKRAWLARKPISQGGLLKYVHGG 821
Cdd:COG0067 729 LKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLLGLGGGGGG 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 822 EYHAYNPDVVRTLQQAVQSGEYSDYQEYAKLVNERPATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSP 901
Cdd:COG0067 809 EYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEEEEEESSAIAAASS 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 902 EAHEALAEAMNSIGGNSNS----------GEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGE 971
Cdd:COG0067 889 AAASAAASAAAAAAAAGAGggggggggggGGGGEGRRASGGSGSSSSASVAAAGGGVVVGAGAAAAEGGGGGGGGGGGGG 968
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 972 GGQLPGDKVTPYIAKLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADL 1051
Cdd:COG0067 969 GGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAAAAAAAAAAAA 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1052 ITIAGYDGGTGASPLSSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVAL 1131
Cdd:COG0067 1049 VGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGALGGGAAALVVV 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1132 GCKYLRICHLNNCATGVATQDDKLRKNHYHGLPFKVTNYFEFIARETRELMAQLGVTRLVDLIGRTDLLKELDGFTAKQQ 1211
Cdd:COG0067 1129 GCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLGVVELLLLLLLLLLLAK 1208
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1212 KLALSKLLETAEPHPGKALYCTETNPPFDNGLLNAQLLQQAKPFVDERQSKTFWFDIRNTDRSVGASLSGYIAQTHGDQG 1291
Cdd:COG0067 1209 LLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGGGGGGGGGGGGGGG 1288
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1292 LAADPIKAYFNGTAGQSFGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYA 1371
Cdd:COG0067 1289 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGAG 1368
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1372 AGRAGERFGVRNSGAITVVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEvlsvddl 1451
Cdd:COG0067 1369 GGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDEEEEEEL------- 1441
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398297727 1452 aiHEEHLRGLITEHVQHTGSQRGEEILANWSTFATKFALVKPKSSDVKALLGHRSRSAAELRVQAQ 1517
Cdd:COG0067 1442 --EELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAA 1505
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
660-1382 |
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: 907.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 660 MAVGAIQTRLVDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGINK 739
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 740 GLYKIMSKMGISTIASYRCSKLFEAVGLHNDVVGLcfqgavsriggasfedFQQDLLNLSKRAWlaRKPISQGGLLKYVH 819
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDI----------------GIADVLTQHRHAI--LRNLPVGGRYRYRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 820 --------------GGEYHAYNPDVVRTLQQAVQSGEysDYQEYAKLVNERPAT--TLRDLLAITPGENAVNI-ADVEPA 882
Cdd:COG0069 143 esigpeirqyffesDGEEHPFNRETRSLLYQAAKNEE--DYKPFGTLVDYQPGYewTLRSLFPFKADRPPIPIgEPVEPP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 883 SELFKRFDTAAMSIGALSPEAHEALAEAMN-----------SIggnsnsgeggeDPARYGTNKVSRIKQVASGRFGVT-- 949
Cdd:COG0069 221 YSIVSRFNISAMSFGALSAEAHEALAIGMNriggksntgegGE-----------SPYHLGDGGGDAIKQIASGRFGVRde 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 950 -PAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTPYIAKLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMIS 1028
Cdd:COG0069 290 dGEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1029 VKLVSEPGVGTIA--TGVAK--AYADLITIAGYDGGTGASPLSSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGL 1104
Cdd:COG0069 370 VKLVSGAGVGTIAacKGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1105 KTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQDDKLRKN-HYHGLPFKVTNYFEFIARETRELMA 1183
Cdd:COG0069 450 KTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGfVVEGKPERVVNYFRFTAEEVREILA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1184 QLGVTRLVDLIGRTDLLKELDGFTAKQQKLALSKLLETAEPHPGKALYCTETNPPFDNGLLNAQLLQQAKPFVDERQSKT 1263
Cdd:COG0069 530 ALGVRSPDELIGRHDLLRVRDGEHWKAKGLDLSPLLYKPELPEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVV 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1264 FWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFNGTAGQSFGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPP 1343
Cdd:COG0069 610 LITNIRNNNRRVGGMLSGEIAKRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPP 689
|
730 740 750
....*....|....*....|....*....|....*....
gi 1398297727 1344 VGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVR 1382
Cdd:COG0069 690 PGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
43-456 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 740.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 43 CGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRLAK--NYAVGMLFLN 120
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEagQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 121 KDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFIARRRIEKRL- 199
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 200 --EADKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHNGEINTITG 277
Cdd:pfam00310 161 veGGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 278 NRQWARARTYKFQTPLIP-DLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPELRAFFDF 356
Cdd:pfam00310 241 NRNWMRAREALLKSELFGdDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 357 NSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMVIDTRSGR 436
Cdd:pfam00310 321 HSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEGR 400
|
410 420
....*....|....*....|
gi 1398297727 437 ILHSAETDDDLKSRHPYKEW 456
Cdd:pfam00310 401 IIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
43-451 |
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: 664.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 43 CGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRL--AKNYAVGMLFLN 120
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELpeAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 121 KDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFIARRRIEKRLE 200
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 201 A-DKDFYVCSLSNLVNIYKGLCMPADLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHNGEINTITGNR 279
Cdd:cd00713 161 AaDEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 280 QWARARTYKFQTPLI-PDLHDAAPFVNEIGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPELRAFFDFNS 358
Cdd:cd00713 241 NWMRAREGLLKSPLFgEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 359 MHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMVIDTRSGRIL 438
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|...
gi 1398297727 439 HSAETDDDLKSRH 451
Cdd:cd00713 401 DDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
824-1188 |
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: 583.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 824 HAYNPDVVRTLQQAVQSGEYSDYQEYAKLVNER-PATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSPE 902
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERvPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 903 AHEALAEAMNSIGGNSNSGEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTP 982
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYADNIAIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPGEKVSP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 983 YIAKLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADLITIAGYDGGTG 1062
Cdd:pfam01645 161 EIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGYDGGTG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1063 ASPLSSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLN 1142
Cdd:pfam01645 241 ASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCRVCHTN 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1398297727 1143 NCATGVATQDDKLRK-NHYHGLPFKVTNYFEFIARETRELMAQLGVT 1188
Cdd:pfam01645 321 TCPVGVATQDPELRKrLDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
827-1201 |
2.98e-153 |
|
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: 471.26 E-value: 2.98e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 827 NPDVVRTLQQAV--QSGEYSDYQEY--AKLVNERPATTLRDLLAIT-------PGENAVNIADV------EPASELFKRF 889
Cdd:cd02808 1 YLLEIERLEEIQyfVFNRAERYGVYnrAGNSRGRPFGTLRDLLEFGaqlakhpLEPDEEVDDRVtigpnaEKPLKLDSPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 890 DTAAMSIGALSPEAHEALAEAMNSIGGNSNSGEGGEDPARYGTNKvSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKP 969
Cdd:cd02808 81 NISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREGGG-DIIKQVASGRFGVRPEYLNKADAIEIKIGQGAKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 970 GEGGQLPGDKVTPYIAKLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYA 1049
Cdd:cd02808 160 GEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVAAAGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1050 DLITIAGYDGGTGASPLSSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMV 1129
Cdd:cd02808 240 DFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALI 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398297727 1130 ALGCKYLRICHLNNCATGVATQDDKLRK-NHYHGLPFKVTNYFEFIARETRELMAQLGVTRLvDLIGRTDLLK 1201
Cdd:cd02808 320 ALGCIQARKCHTNTCPVGVATQDPELRRrLDVEGKAERVANYLKSLAEELRELAAALGKRSL-ELLGRSDLLA 391
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
488-768 |
5.63e-145 |
|
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: 444.52 E-value: 5.63e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 488 YQKQFNYSAEELDSVIRVLGENGQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGRE 567
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 568 MNVFCEAEGQAHRLSFKSPILLYSDFKQLTTMKEEHYRADTLDITFDVtkttLEATVKELCDKAEKMVRSGTVLLVLSDR 647
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITFDG----LEAALERLCEEAEEAVRDGANILILSDR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 648 NIAKDRLPVPAPMAVGAIQTRLVDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAI---AK 724
Cdd:pfam04898 158 GVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGKGkltDE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1398297727 725 DYRTVMLNYRNGINKGLYKIMSKMGISTIASYRCSKLFEAVGLH 768
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 ... |
1244-1494 |
8.16e-144 |
|
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: 440.04 E-value: 8.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1244 LNAQLLQQAKPFVDERQSK-TFWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFNGTAGQSFGVWNAGGVELYLT 1322
Cdd:cd00982 1 LDDKLIADAEPALIENGEPvTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1323 GDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVRNSGAITVVEGIGDNGCEYMT 1402
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1403 GGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEVLSVDDlAIHEEHLRGLITEHVQHTGSQRGEEILANWS 1482
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLED-AEDEEQLKELIEEHVEYTGSEKAKEILANWE 239
|
250
....*....|..
gi 1398297727 1483 TFATKFALVKPK 1494
Cdd:cd00982 240 AYLKKFVKVIPR 251
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1266-1450 |
1.43e-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: 336.31 E-value: 1.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1266 FDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFNGTAGQSFGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVG 1345
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1346 SAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVRNSGAITVVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFA 1425
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180
....*....|....*....|....*
gi 1398297727 1426 YVLDESGDFRKRVNPELVEVLSVDD 1450
Cdd:pfam01493 161 YVLDEDGDFPEKLNKEMVELERVTD 185
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1273-1429 |
1.19e-63 |
|
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: 212.81 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1273 RSVGASLSGYIAQthgDQGLAADPIKAYFNGTAGQSFGVWNAGGvELYLTGDANDYVGKGMAGGLIAIRPPVGsafrsHE 1352
Cdd:cd00504 1 RAVGTRGSRYIGK---RPGLPEDTVEIIINGSAGQSFGAFMAGG-TITVEGNANDYVGKGMSGGEIVIHPPAG-----DE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398297727 1353 ASIIGNTCLYGATGGRLYAAGRAGERFGVRNSGAITVVEGIGDN-GCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLD 1429
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDDfGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
229-428 |
2.16e-29 |
|
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: 117.55 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 229 FYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFR------YLAHNGEINTITGNRQWARARTYKFQTplipdlhdaap 302
Cdd:cd00352 57 VALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEARGYRFEG----------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 303 fvneiGSDSSSMDNMLELLLAGGMDIIRAMRLLvppawqnnpdmdpelraffdfnsmhmEPWDGPAGIVMSDGR----FA 378
Cdd:cd00352 126 -----ESDSEVILHLLERLGREGGLFEAVEDAL--------------------------KRLDGPFAFALWDGKpdrlFA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398297727 379 ACnlDRNGLRPARYVITKDKLITCASEVGIWDyqPDEVVEKGRVGPGELM 428
Cdd:cd00352 175 AR--DRFGIRPLYYGITKDGGLVFASEPKALL--ALPFKGVRRLPPGELL 220
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1302-1466 |
4.14e-12 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 66.99 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1302 NGTAGQSFGVWNAGGvELYLTGDANDYVGKGMAGGLIAIRPP----VGSAFRsheasiiGNTClyGATGGRLYAAGRAGE 1377
Cdd:cd00980 45 EGDVGMYVGAGMKGG-KLVVEGNAGSWAGCEMKGGEITIKGNagdyVGSAYR-------GDWR--GMSGGTITIEGNAGD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1378 RFGVRNSGAITVVEG-IGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRkrvnPELVEVLSVDDLAIHEE 1456
Cdd:cd00980 115 RLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIGGEIEELL----PTFKEEGTEEDVFVSGE 190
|
170
....*....|
gi 1398297727 1457 HLRGLITEHV 1466
Cdd:cd00980 191 ELSGTFYKFT 200
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
202-417 |
5.04e-11 |
|
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: 64.60 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 202 DKDFYVCSLSNLVNIYKGLCMPADLPRFYlDLADLrlESAICLFHQRFSTNTVPRWPLAQPFRY----LAHNGEINTITG 277
Cdd:cd01907 42 DPDAFVYSSGKDMEVFKGVGYPEDIARRY-DLEEY--KGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 278 NRQWARARTYKFqtplipdlhdaapfvnEIGSDSSSMDNMLELLLA-GGMDIIRAMRLLVPPawQNNPDMDPELRAFFDF 356
Cdd:cd01907 119 NREYLERFGYKF----------------ETETDTEVIAYYLDLLLRkGGLPLEYYKHIIRMP--EEERELLLALRLTYRL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398297727 357 NSMhmepwDGPAGIVM--SDGRFAACnlDRNGLRPArYVITKDKLITCASEV------------GIWDYQPDEVV 417
Cdd:cd01907 181 ADL-----DGPFTIIVgtPDGFIVIR--DRIKLRPA-VVAETDDYVAIASEEcaireipdrdnaKVWEPRPGEYV 247
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1318-1423 |
1.33e-09 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 60.59 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1318 ELYLTGDANDYVGKGMAGGLIAIR----PPVGSAFRSHEASIIGNT------CLYGA----TGGRLYAAGRAGERFGVRN 1383
Cdd:COG2218 83 EIIVEGDVGMYLGAGMKGGKITVNgnagSFAGAEMKGGEIEINGNAgdflgaAYRGDwrgmSGGTIIVKGNAGDRLGDRM 162
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1398297727 1384 SGAITVVEGIGDNGCEY-MTGGIVCILGKTGVNFGAGMTGG 1423
Cdd:COG2218 163 RRGTIIIEGDAGDFAGSrMIAGTIIVKGNAGRRPGYGMKRG 203
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1302-1495 |
4.36e-07 |
|
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: 52.69 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1302 NGTAGQSFGVWNAGGV------------------ELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASiigntclYG 1363
Cdd:cd00981 52 YGVPGNDLGAFMSGPTiivygnaqddvgntmndgKIVIHGSAGDVLGYAMRGGKIFIRGNAGYRVGIHMKE-------YK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1364 ATGGRLYAAGRAGERFGvrnsgaitvvegigdngcEYMTGGIVCILGK------TGVNFGAGMTGGFAYVldesgdfRKR 1437
Cdd:cd00981 125 DKVPVLVIGGTAGDFLG------------------EYMAGGVIIVLGLgtdeepVGRYIGTGMHGGVIYI-------RGK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1438 VNPEL--VEVLSVDDLAIHEEHLRGLITEHVQHTGSQRgEEILanwstfATKFALVKPKS 1495
Cdd:cd00981 180 VERSKlgKEVPKFELTEEDLEFIEKYIEEFCKEFGYDK-AEIL------DEEFTKLKPKS 232
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1318-1423 |
1.42e-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: 51.57 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1318 ELYLTGDANDYVGKGMAGGLIAIRPPVGS----AFRSHEASIIGNT-----CLY-----GATGGRLYAAGRAGERFGVRN 1383
Cdd:TIGR03122 82 EIVVEGDVGMHVGAEMKGGKIVVNGNADSwagcEMKGGEIIIKGNAgdyvgSAYrgewrGMSGGKIIVEGNAGDYLGERM 161
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1398297727 1384 SGAITVVEG-IGDNGCEYMTGGIVCILGKTGVNFGAGMTGG 1423
Cdd:TIGR03122 162 RGGEILIKGnAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRG 202
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1302-1434 |
2.84e-06 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1302 NGTAGQSFGVWNAGGvELYLTGDANDYVGKGMAGGLIAIRppvgsafrsheasiiGNTclygatgGRLYAAGRAGERFGv 1381
Cdd:COG2218 87 EGDVGMYLGAGMKGG-KITVNGNAGSFAGAEMKGGEIEIN---------------GNA-------GDFLGAAYRGDWRG- 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1398297727 1382 rnsgaitvvegigdngceyMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDF 1434
Cdd:COG2218 143 -------------------MSGGTIIVKGNAGDRLGDRMRRGTIIIEGDAGDF 176
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
1001-1125 |
4.35e-04 |
|
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: 43.34 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1001 PHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVsePGVGTIATGVAKAYADLITIAGYDGGTGASPLSSvkyagcpwelgl 1080
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKLS--PTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVP------------ 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1398297727 1081 vETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGT 1125
Cdd:cd04722 157 -IADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1314-1434 |
5.39e-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: 43.11 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398297727 1314 AGGVELYLTGDAN--DYVGKGMAGGLIAIRppvGSAfrsheasiiGNTCLYGATGGRLYAAGRAGERFGVRNSGAITVVE 1391
Cdd:cd00980 16 DADTKLVIEGDVPrlKRIGARMTAGEIVVE---GDV---------GMYVGAGMKGGKLVVEGNAGSWAGCEMKGGEITIK 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1398297727 1392 G-IGDN-GCEY------MTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDF 1434
Cdd:cd00980 84 GnAGDYvGSAYrgdwrgMSGGTITIEGNAGDRLGERMRRGEILIKGDAGIF 134
|
|
| |
