|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
15-1501 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1667.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 15 KQGLYDPEFERDSCGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLP 94
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 95 EkgNYAVGNIFLPQKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSkkaDV-GPAALDCKPNIEQIFIKSKKDVDQNYF 173
Cdd:PRK11750 82 K--NYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNP---SVlGEIALSSLPRIEQVFVNAPAGWRERDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 174 ERKLYLVRKIFTKKLRQESNlsqalmFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWD 253
Cdd:PRK11750 157 ERRLFIARRRIEKRLADDKD------FYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 254 RAQPCRYMCHNGEINTLKGNMNLMQSRQGKADSDLYKNkINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIP 333
Cdd:PRK11750 231 LAQPFRYLAHNGEINTITGNRQWARARAYKFQTPLIPD-LQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 334 EAWQNDKNMSKVKKDFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVL 413
Cdd:PRK11750 310 PAWQNNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 414 RKGRLQPGKMFLIDFEKGKLISDEEIKKEVANQHPYGDW---NANQIIELDDLPERSKTYVVPD---LISKMKAFGYTTE 487
Cdd:PRK11750 390 EKGRVGPGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWlekNVRRLVPFEELPDEQVGSRELDddtLKSYQKQFQYSFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 488 TLEFMLLPLVTELRDPLGSMGNDAALACLSDKPRMIYDYFKQLFAQITNPPIDSIREEIIMSLECLIGPEGNLLSTDETN 567
Cdd:PRK11750 470 ELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGH 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 568 VRRLRLEHPILSNQELEKIRSIKTKGYKSKTIDITYKkgLGKKGLTKALDKICKESLKAIDDGYSFIILSDKSITSDKLA 647
Cdd:PRK11750 550 AHRVIFKSPVLSYSDFKQLTTLDEEHYRADTLDLNYD--PEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 648 LSTLLACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALedenLNNAFDLVK 727
Cdd:PRK11750 628 IPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEI----LKDYRQVML 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 728 AYKKGVAKGMLKVMAKMGISTLQSYKGAQIFEAVGLSDEIIEKSFPGTPSRVQGVTFEILSEEMERRHLMGFpenseNNV 807
Cdd:PRK11750 704 NYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAW-----LAR 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 808 ASLPNPGDFHWRNGGDSHMWDPKSISALQIAARNNDESAYWNFSNHANEETTknSTLRGLMKFKFSKNPIPLDKVEPEKE 887
Cdd:PRK11750 779 KPIDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPV--ATLRDLLALKPADNPIPLDEVEPAEE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 888 IVKRFATGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRFkpledGSSKRSAIKQVASGRFGVTMWYLTNADEL 967
Cdd:PRK11750 857 LFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVL 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 968 QIKIAQGAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGT 1047
Cdd:PRK11750 932 QIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGT 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1048 IAAGVVKAKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAE 1127
Cdd:PRK11750 1012 IATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAE 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1128 EFGFSTAPLVTLGCIMMRKCHLNTCPVGIATQDKELRKK-FKGSPENVVNYLFMVAKELRMIMANLGITKLDNLIGRVDL 1206
Cdd:PRK11750 1092 SFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDL 1171
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1207 LE-MDKAIDhwKRDGLDLSKILSPAEIIyKDTEVFNTQKQNHNLEK-SLDIKLLKKIKTHIKTKKKIIIDSKIGNTNRVF 1284
Cdd:PRK11750 1172 LEeLEGETA--KQQKLDLSPLLETAEPP-AGKALYCTEERNPPFDKgLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSV 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1285 GTIISNEVAKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFVPNENII 1364
Cdd:PRK11750 1249 GARLSGEIARRHGNQGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAI 1328
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1365 LGNVALYGATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFK 1444
Cdd:PRK11750 1329 IGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFV 1408
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 297170345 1445 KNCNMSTFDLEKMVIKEDKEE-LKTLISNHFKYTKSDVAEKILSNWVKELSNFKKVMP 1501
Cdd:PRK11750 1409 DRVNHELVEILRVEDLEIHREhLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
17-1508 |
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: 1371.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 17 GLYDPEFERDSCGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLPEK 96
Cdd:COG0070 16 GGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 97 GNYAVGNIFLPQKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDskKADVGPAALDCKPNIEQIFIKSKKDVDQNYFERK 176
Cdd:COG0070 96 GLAAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVL--LALGVRAAALARREAELSELAARRRLRLRRLALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 177 LYLVRKIFTKKLRqesnlsqalmFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQ 256
Cdd:COG0070 174 RRRRRRRRREFRR----------RSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 257 PCRYMCHNGEINTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIPEAW 336
Cdd:COG0070 244 APRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 337 QNDKNMSKVKKDFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVLRKG 416
Cdd:COG0070 324 PAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 417 RLQPGKMFLIDFEKGKLISDEEIKKEVANQHPYGDWNANQIIELDDLPERSKTYVVPDLISKMKAFGYTTETLEFMLLPL 496
Cdd:COG0070 404 RELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 497 VTELR---DPLGSMGNDAALACLSDKPRMIYDYFKQLFAQITNPPIDSIREEIIMSLECLIGPEGNLLSTDETNVRRLRL 573
Cdd:COG0070 484 LAEALeeeEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 574 EHPILSNQELEKIRSIKTKGYKSKTIDITYKKGLGKKGLTKALDKICKESLKAIDD-GYSFIILSDKSITSDKLALSTLL 652
Cdd:COG0070 564 LLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAaVAAILAASIRDSALLLALLPALL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 653 ACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALEDENLnnafDLVKAYKKG 732
Cdd:COG0070 644 ALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLL----EAAAYKAKA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 733 VAKGMLKVMAKMGISTLQSYKGAQIFEAVGLSDEIIEKSFPGTPSRVQGVTFEILSEEMERRHLMGFPENSENNVASLPN 812
Cdd:COG0070 720 ALKAGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGG 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 813 PGDFHWRNGGDSHMWDPKSISALQIAARNNDESAYWNFSNhANEETTKNSTLRGLMKFKFSKNPIPLDKVEPEKEIVKRF 892
Cdd:COG0070 800 GGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAY-EDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRF 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 893 ATGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRFKPLEDGSSKRSAIKQVASGRFGVTMWYLTNADELQIKIA 972
Cdd:COG0070 879 ATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMA 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 973 QGAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGTIAAGV 1052
Cdd:COG0070 959 QGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGV 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1053 VKAKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAEEFGFS 1132
Cdd:COG0070 1039 AKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFA 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1133 TAPLVTLGCIMMRKCHLNTCPVGIATQDKELRKKFKGSPENVVNYLFMVAKELRMIMANLGITKLDNLIGRVDLLEMDKA 1212
Cdd:COG0070 1119 TAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRA 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1213 IDHWKRDGLDLSKILSPAEiIYKDTEVFNTQKQNHNLEKSLDIKLLKKIKTHIKTKKKIIIDSKIGNTNRVFGTIISNEV 1292
Cdd:COG0070 1199 VDHWKAKGLDLSPLLYKPD-VPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEI 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1293 AKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFVPNENIILGNVALYG 1372
Cdd:COG0070 1278 AKRYGNEGLPEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYG 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1373 ATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFKKNCNMSTF 1452
Cdd:COG0070 1358 ATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMV 1437
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*.
gi 297170345 1453 DLEKMVIKEDKEELKTLISNHFKYTKSDVAEKILSNWVKELSNFKKVMPIDFKRVL 1508
Cdd:COG0070 1438 ELERLDEEEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVL 1493
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
28-452 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 697.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 28 CGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLPEKGNYAVGNIFLP 107
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 108 QKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSKKadVGPAALDCKPNIEQIFIKSKKDVDQNYFERKLYLVRKIFTKK 187
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSV--LGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 188 LRQESNLSQalmFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQPCRYMCHNGEI 267
Cdd:pfam00310 159 IGVEGGDKD---FYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 268 NTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIPEAWQNDKNMSKVKK 347
Cdd:pfam00310 236 NTLRGNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 348 DFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVLRKGRLQPGKMFLID 427
Cdd:pfam00310 316 AFYEYHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVD 395
|
410 420
....*....|....*....|....*
gi 297170345 428 FEKGKLISDEEIKKEVANQHPYGDW 452
Cdd:pfam00310 396 LEEGRIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
28-447 |
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: 682.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 28 CGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLPEKGNYAVGNIFLP 107
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 108 QKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSKkaDVGPAALDCKPNIEQIFIKSKKDVDQNYFERKLYLVRKIFTKK 187
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNS--VLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 188 LRQESNlsqalMFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQPCRYMCHNGEI 267
Cdd:cd00713 159 IRAADE-----DFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 268 NTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIPEAWQNDKNMSKVKK 347
Cdd:cd00713 234 NTIRGNRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 348 DFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVLRKGRLQPGKMFLID 427
Cdd:cd00713 314 AFYEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVD 393
|
410 420
....*....|....*....|
gi 297170345 428 FEKGKLISDEEIKKEVANQH 447
Cdd:cd00713 394 LEEGRILDDEEIKDQLAKRH 413
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1321-1468 |
1.69e-07 |
|
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.
Pssm-ID: 274439 [Multi-domain] Cd Length: 257 Bit Score: 54.27 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1321 WATKGMT---LSLEGDANDYVGKGLSGGKLIIYPPADSSFVPN----ENIILGNVALY----------GATDGEAYFRGI 1383
Cdd:TIGR03122 73 RIGENMSageIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEmkggEIIIKGNAGDYvgsayrgewrGMSGGKIIVEGN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1384 AAERFCVRNSGAKVVVEG-IGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFkkncnMSTF----DLEKMV 1458
Cdd:TIGR03122 153 AGDYLGERMRGGEILIKGnAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDEL-----LPTFkfegLHELPF 227
|
170
....*....|
gi 297170345 1459 IKEDKEELKT 1468
Cdd:TIGR03122 228 LLKSAFTQAI 237
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
15-1501 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1667.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 15 KQGLYDPEFERDSCGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLP 94
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 95 EkgNYAVGNIFLPQKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSkkaDV-GPAALDCKPNIEQIFIKSKKDVDQNYF 173
Cdd:PRK11750 82 K--NYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNP---SVlGEIALSSLPRIEQVFVNAPAGWRERDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 174 ERKLYLVRKIFTKKLRQESNlsqalmFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWD 253
Cdd:PRK11750 157 ERRLFIARRRIEKRLADDKD------FYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 254 RAQPCRYMCHNGEINTLKGNMNLMQSRQGKADSDLYKNkINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIP 333
Cdd:PRK11750 231 LAQPFRYLAHNGEINTITGNRQWARARAYKFQTPLIPD-LQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 334 EAWQNDKNMSKVKKDFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVL 413
Cdd:PRK11750 310 PAWQNNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 414 RKGRLQPGKMFLIDFEKGKLISDEEIKKEVANQHPYGDW---NANQIIELDDLPERSKTYVVPD---LISKMKAFGYTTE 487
Cdd:PRK11750 390 EKGRVGPGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWlekNVRRLVPFEELPDEQVGSRELDddtLKSYQKQFQYSFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 488 TLEFMLLPLVTELRDPLGSMGNDAALACLSDKPRMIYDYFKQLFAQITNPPIDSIREEIIMSLECLIGPEGNLLSTDETN 567
Cdd:PRK11750 470 ELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGH 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 568 VRRLRLEHPILSNQELEKIRSIKTKGYKSKTIDITYKkgLGKKGLTKALDKICKESLKAIDDGYSFIILSDKSITSDKLA 647
Cdd:PRK11750 550 AHRVIFKSPVLSYSDFKQLTTLDEEHYRADTLDLNYD--PEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLP 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 648 LSTLLACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALedenLNNAFDLVK 727
Cdd:PRK11750 628 IPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEI----LKDYRQVML 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 728 AYKKGVAKGMLKVMAKMGISTLQSYKGAQIFEAVGLSDEIIEKSFPGTPSRVQGVTFEILSEEMERRHLMGFpenseNNV 807
Cdd:PRK11750 704 NYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAW-----LAR 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 808 ASLPNPGDFHWRNGGDSHMWDPKSISALQIAARNNDESAYWNFSNHANEETTknSTLRGLMKFKFSKNPIPLDKVEPEKE 887
Cdd:PRK11750 779 KPIDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPV--ATLRDLLALKPADNPIPLDEVEPAEE 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 888 IVKRFATGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRFkpledGSSKRSAIKQVASGRFGVTMWYLTNADEL 967
Cdd:PRK11750 857 LFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVL 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 968 QIKIAQGAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGT 1047
Cdd:PRK11750 932 QIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGT 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1048 IAAGVVKAKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAE 1127
Cdd:PRK11750 1012 IATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAE 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1128 EFGFSTAPLVTLGCIMMRKCHLNTCPVGIATQDKELRKK-FKGSPENVVNYLFMVAKELRMIMANLGITKLDNLIGRVDL 1206
Cdd:PRK11750 1092 SFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDL 1171
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1207 LE-MDKAIDhwKRDGLDLSKILSPAEIIyKDTEVFNTQKQNHNLEK-SLDIKLLKKIKTHIKTKKKIIIDSKIGNTNRVF 1284
Cdd:PRK11750 1172 LEeLEGETA--KQQKLDLSPLLETAEPP-AGKALYCTEERNPPFDKgLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSV 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1285 GTIISNEVAKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFVPNENII 1364
Cdd:PRK11750 1249 GARLSGEIARRHGNQGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAI 1328
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1365 LGNVALYGATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFK 1444
Cdd:PRK11750 1329 IGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFV 1408
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 297170345 1445 KNCNMSTFDLEKMVIKEDKEE-LKTLISNHFKYTKSDVAEKILSNWVKELSNFKKVMP 1501
Cdd:PRK11750 1409 DRVNHELVEILRVEDLEIHREhLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
17-1508 |
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: 1371.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 17 GLYDPEFERDSCGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLPEK 96
Cdd:COG0070 16 GGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 97 GNYAVGNIFLPQKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDskKADVGPAALDCKPNIEQIFIKSKKDVDQNYFERK 176
Cdd:COG0070 96 GLAAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVL--LALGVRAAALARREAELSELAARRRLRLRRLALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 177 LYLVRKIFTKKLRqesnlsqalmFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQ 256
Cdd:COG0070 174 RRRRRRRRREFRR----------RSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 257 PCRYMCHNGEINTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIPEAW 336
Cdd:COG0070 244 APRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 337 QNDKNMSKVKKDFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVLRKG 416
Cdd:COG0070 324 PAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 417 RLQPGKMFLIDFEKGKLISDEEIKKEVANQHPYGDWNANQIIELDDLPERSKTYVVPDLISKMKAFGYTTETLEFMLLPL 496
Cdd:COG0070 404 RELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 497 VTELR---DPLGSMGNDAALACLSDKPRMIYDYFKQLFAQITNPPIDSIREEIIMSLECLIGPEGNLLSTDETNVRRLRL 573
Cdd:COG0070 484 LAEALeeeEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 574 EHPILSNQELEKIRSIKTKGYKSKTIDITYKKGLGKKGLTKALDKICKESLKAIDD-GYSFIILSDKSITSDKLALSTLL 652
Cdd:COG0070 564 LLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAaVAAILAASIRDSALLLALLPALL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 653 ACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALEDENLnnafDLVKAYKKG 732
Cdd:COG0070 644 ALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLL----EAAAYKAKA 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 733 VAKGMLKVMAKMGISTLQSYKGAQIFEAVGLSDEIIEKSFPGTPSRVQGVTFEILSEEMERRHLMGFPENSENNVASLPN 812
Cdd:COG0070 720 ALKAGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGG 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 813 PGDFHWRNGGDSHMWDPKSISALQIAARNNDESAYWNFSNhANEETTKNSTLRGLMKFKFSKNPIPLDKVEPEKEIVKRF 892
Cdd:COG0070 800 GGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAY-EDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRF 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 893 ATGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRFKPLEDGSSKRSAIKQVASGRFGVTMWYLTNADELQIKIA 972
Cdd:COG0070 879 ATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMA 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 973 QGAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGTIAAGV 1052
Cdd:COG0070 959 QGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGV 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1053 VKAKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAEEFGFS 1132
Cdd:COG0070 1039 AKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFA 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1133 TAPLVTLGCIMMRKCHLNTCPVGIATQDKELRKKFKGSPENVVNYLFMVAKELRMIMANLGITKLDNLIGRVDLLEMDKA 1212
Cdd:COG0070 1119 TAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRA 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1213 IDHWKRDGLDLSKILSPAEiIYKDTEVFNTQKQNHNLEKSLDIKLLKKIKTHIKTKKKIIIDSKIGNTNRVFGTIISNEV 1292
Cdd:COG0070 1199 VDHWKAKGLDLSPLLYKPD-VPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEI 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1293 AKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFVPNENIILGNVALYG 1372
Cdd:COG0070 1278 AKRYGNEGLPEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYG 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1373 ATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFKKNCNMSTF 1452
Cdd:COG0070 1358 ATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMV 1437
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*.
gi 297170345 1453 DLEKMVIKEDKEELKTLISNHFKYTKSDVAEKILSNWVKELSNFKKVMPIDFKRVL 1508
Cdd:COG0070 1438 ELERLDEEEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVL 1493
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
12-1511 |
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: 1314.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 12 RPKKQGLYDPEFERDSCGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKI 91
Cdd:COG0067 7 LPAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 92 NLPEKGNYAVGNIFLPQKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSkkADVGPAALDCKPNIEQIFIKSKKDVDQN 171
Cdd:COG0067 87 ELPEPGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDP--SVLGETARATEPVIEQVFVARPDGLDGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 172 YFERKLYLVRKIFTKKLRQESNlsQALMFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPS 251
Cdd:COG0067 165 AFERKLYVARKRIEKAIRALGL--DDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 252 WDRAQPCRYMCHNGEINTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMM 331
Cdd:COG0067 243 WPLAQPFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMML 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 332 IPEAWQNDKNMSKVKKDFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKT 411
Cdd:COG0067 323 IPEAWENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPED 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 412 VLRKGRLQPGKMFLIDFEKGKLISDEEIKKEVANQHPYGDWNANQIIELDDLPERSKTYVVPD--LISKMKAFGYTTETL 489
Cdd:COG0067 403 IVEKGRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDdlLLRRQQAFGYTEEEE 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 490 EFMLLPLVTELRDPLGSMGNDAALACLSDKPRMIYDYFKQLFAQITNPPIDSIREEIIMSLECLIGPEGNLLSTDETNVR 569
Cdd:COG0067 483 LLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEARR 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 570 RLRLEHPILSNQELEKIRSIKTKGYKSKTIDITYKKGLGKKGLTKALDKICKESLKAIDDGYSFIILSDKSITSDKLALS 649
Cdd:COG0067 563 RLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDAAPA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 650 TLLACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALEDENLNNAFDLVKAY 729
Cdd:COG0067 643 PLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAAAAKKKK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 730 KKGVAKGMLKVMAKMGISTLQSYKGAQIFEAVGLSDEIIEKSFPGTPSRVQGVTFEILSEEMERRHLMGFPENSENNVAS 809
Cdd:COG0067 723 KKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLLGL 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 810 LPNPGDFHWRNGGDSHMWDPKSISALQIAARNNDESAYWNFSNHANEETTKNSTLRGLMKFKFSKNPIPLDKVEPEKEIV 889
Cdd:COG0067 803 GGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEEEEEESSA 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 890 KRFATGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRfkplEDGSSKRSAIKQVASGRFGVTMWYLTNADELQI 969
Cdd:COG0067 883 IAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGAAAAEGGG 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 970 KIAQGAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGTIA 1049
Cdd:COG0067 959 GGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAA 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1050 AGVVKAKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAEEF 1129
Cdd:COG0067 1039 AAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGAL 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1130 GFSTAPLVTLGCIMMRKCHLNTCPVGIATQDKELRKKFKGSPENVVNYLFMVAKELRMIMANLGITKLDNLIGRVDLLEM 1209
Cdd:COG0067 1119 GGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLGVVELLL 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1210 DKAIDHWKRDGLDLSKILSPAEIIYKDTEVFNTQKQNHNLEKSLDIKLLKKIKTHIKTKKKIIIDSKIGNTNRVFGTIIS 1289
Cdd:COG0067 1199 LLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGGGGG 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1290 NEVAKSwGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFVPNENIILGNVA 1369
Cdd:COG0067 1279 GGGGGG-GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGA 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1370 LYGATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFKKNCNM 1449
Cdd:COG0067 1358 GGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDEEE 1437
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297170345 1450 STFDLEKMVIKEDKEELKTLISNHFKYTKSDVAEKILSNWVKELSNFKKVMPIDFKRVLMET 1511
Cdd:COG0067 1438 EEELEELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAA 1499
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
652-1391 |
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: 958.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 652 LACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALEDEnlnnAFDLVKAYKK 731
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLD----LEEAVKNYIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 732 GVAKGMLKVMAKMGISTLQSYKGAQIFEAVGLSDEIIEKSFpgtpsrvqgvtfeilsEEMERRHLMGFPENsennvasLP 811
Cdd:COG0069 77 AIEKGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDIGI----------------ADVLTQHRHAILRN-------LP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 812 NPGDFHWR--------------NGGDSHMWDPKSISALQIAARNndESAYWNFSNHANEETTKNSTLRGLMKFKFSKNPI 877
Cdd:COG0069 134 VGGRYRYRfesigpeirqyffeSDGEEHPFNRETRSLLYQAAKN--EEDYKPFGTLVDYQPGYEWTLRSLFPFKADRPPI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 878 PLD-KVEPEKEIVKRFATGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRFkpledGSSKRSAIKQVASGRFGV 956
Cdd:COG0069 212 PIGePVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 957 TMW---YLTNADELQIKIAQGAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSS 1033
Cdd:COG0069 287 RDEdgeYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1034 RISVKLVSEIGVGTIAA--GVVK--AKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTD 1109
Cdd:COG0069 367 PVGVKLVSGAGVGTIAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIAD 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1110 GQLKTGRDVAIAAILGAEEFGFSTAPLVTLGCIMMRKCHLNTCPVGIATQDKELRKKFK--GSPENVVNYLFMVAKELRM 1187
Cdd:COG0069 447 GKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVRE 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1188 IMANLGITKLDNLIGRVDLLEMDKAiDHWKRDGLDLSKILSPAEIIyKDTEVFNTQKQNHNLEKSLDIKLLKKIKTHIKT 1267
Cdd:COG0069 527 ILAALGVRSPDELIGRHDLLRVRDG-EHWKAKGLDLSPLLYKPELP-EGVPRRCQEEQDHGLDKALDLELIAAAAAAAEE 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1268 KKKIIIDSKIGNTNRVFGTIISNEVAKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKL 1347
Cdd:COG0069 605 GKPVVLITNIRNNNRRVGGMLSGEIAKRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGI 684
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 297170345 1348 IIYPPADSSFVPNENIILGNVALYGATDGEAYFRGIAAERFCVR 1391
Cdd:COG0069 685 IVPPPPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
28-452 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 697.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 28 CGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLPEKGNYAVGNIFLP 107
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 108 QKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSKKadVGPAALDCKPNIEQIFIKSKKDVDQNYFERKLYLVRKIFTKK 187
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSV--LGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 188 LRQESNLSQalmFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQPCRYMCHNGEI 267
Cdd:pfam00310 159 IGVEGGDKD---FYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 268 NTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIPEAWQNDKNMSKVKK 347
Cdd:pfam00310 236 NTLRGNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 348 DFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVLRKGRLQPGKMFLID 427
Cdd:pfam00310 316 AFYEYHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVD 395
|
410 420
....*....|....*....|....*
gi 297170345 428 FEKGKLISDEEIKKEVANQHPYGDW 452
Cdd:pfam00310 396 LEEGRIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
28-447 |
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: 682.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 28 CGVGLVANIKGVPSREIMDDAYIINSRMDHRGGCGFEENTGDGAGILLALPHDFFKKEAKKLKINLPEKGNYAVGNIFLP 107
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 108 QKKSEKDFCKKTIEDVLKQEKLELLGWRQVPIDSKkaDVGPAALDCKPNIEQIFIKSKKDVDQNYFERKLYLVRKIFTKK 187
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNS--VLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 188 LRQESNlsqalMFYACSLSSRLIVYKGMLTPSQLFPFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQPCRYMCHNGEI 267
Cdd:cd00713 159 IRAADE-----DFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 268 NTLKGNMNLMQSRQGKADSDLYKNKINKLFPIAEPDCSDSGSFDNVLELLIMTGRKLPEAVMMMIPEAWQNDKNMSKVKK 347
Cdd:cd00713 234 NTIRGNRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 348 DFYRYSSSLMEPWDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPKTVLRKGRLQPGKMFLID 427
Cdd:cd00713 314 AFYEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVD 393
|
410 420
....*....|....*....|
gi 297170345 428 FEKGKLISDEEIKKEVANQH 447
Cdd:cd00713 394 LEEGRILDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
825-1195 |
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: 572.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 825 HMWDPKSISALQIAARNNDESAYWNFSNHANEETTKNsTLRGLMKFKFSKNPIPLDKVEPEKEIVKRFATGAMSLGSIST 904
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERVPIG-ALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 905 EAHESLALAMNKLGGKSNTGEGGEDPIRFKPLEDGsskrsAIKQVASGRFGVTMWYLTNADELQIKIAQGAKPGEGGELP 984
Cdd:pfam01645 80 EAHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-----AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 985 GTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGTIAAGVVKAKTDHLVIAG 1064
Cdd:pfam01645 155 GEKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1065 HDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAEEFGFSTAPLVTLGCIMM 1144
Cdd:pfam01645 235 YDGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMC 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 297170345 1145 RKCHLNTCPVGIATQDKELRK--KFKGSPENVVNYLFMVAKELRMIMANLGIT 1195
Cdd:pfam01645 315 RVCHTNTCPVGVATQDPELRKrlDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
829-1207 |
2.51e-172 |
|
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: 521.72 E-value: 2.51e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 829 PKSISALQIAARN--NDESAYWNFSNHANEETTKNSTLRGLMKFKFSKNPIPLD-------------KVEPEKEIVKRFA 893
Cdd:cd02808 2 LLEIERLEEIQYFvfNRAERYGVYNRAGNSRGRPFGTLRDLLEFGAQLAKHPLEpdeevddrvtigpNAEKPLKLDSPFN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 894 TGAMSLGSISTEAHESLALAMNKLGGKSNTGEGGEDPIRFKpledgsSKRSAIKQVASGRFGVTMWYLTNADELQIKIAQ 973
Cdd:cd02808 82 ISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEERE------GGGDIIKQVASGRFGVRPEYLNKADAIEIKIGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 974 GAKPGEGGELPGTKVDKYIAKIRHSTPGVGLISPPPHHDIYSIEDIAQLIHDLKNANRSSRISVKLVSEIGVGTIAAGVV 1053
Cdd:cd02808 156 GAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1054 KAKTDHLVIAGHDGGTGASPLTSIKHAGLPWELGIAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAEEFGFST 1133
Cdd:cd02808 236 AAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGT 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297170345 1134 APLVTLGCIMMRKCHLNTCPVGIATQDKEL--RKKFKGSPENVVNYLFMVAKELRMIMANLGITKLDnLIGRVDLL 1207
Cdd:cd02808 316 AALIALGCIQARKCHTNTCPVGVATQDPELrrRLDVEGKAERVANYLKSLAEELRELAAALGKRSLE-LLGRSDLL 390
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
478-764 |
1.36e-154 |
|
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: 469.94 E-value: 1.36e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 478 KMKAFGYTTETLEFMLLPLVTELRDPLGSMGNDAALACLSDKPRMIYDYFKQLFAQITNPPIDSIREEIIMSLECLIGPE 557
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 558 GNLLSTDETNVRRLRLEHPILSNQELEKIRSIKTKGYKSKTIDITYkkglgkKGLTKALDKICKESLKAIDDGYSFIILS 637
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITF------DGLEAALERLCEEAEEAVRDGANILILS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 638 DKSITSDKLALSTLLACSTVHNFLVKKEKRTQIGIVLESGEAREVHHHCLLIGYGADAINPYLAFAVLEKSLKDGALEDE 717
Cdd:pfam04898 156 DRGVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGKGKLT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 297170345 718 NLnNAFDLVKAYKKGVAKGMLKVMAKMGISTLQSYKGAQIFEAVGLS 764
Cdd:pfam04898 236 DE-DLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1279-1501 |
2.84e-137 |
|
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: 422.71 E-value: 2.84e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1279 NTNRVFGTIISNEVAKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFV 1358
Cdd:cd00982 28 NTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELEGDANDYVGKGLSGGRIVVRPPKDATFK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1359 PNENIILGNVALYGATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYD 1438
Cdd:cd00982 108 PEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGTVVVLGKTGRNFAAGMSGGVAYVLD 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297170345 1439 PKNNFKKNCNMSTFDLEKMVIKEDKEELKTLISNHFKYTKSDVAEKILSNWVKELSNFKKVMP 1501
Cdd:cd00982 188 EDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWEAYLKKFVKVIP 250
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1279-1464 |
3.45e-115 |
|
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: 360.19 E-value: 3.45e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1279 NTNRVFGTIISNEVAKSWGAAGLPNDTLRFNLSGSAGQSFGAWATKGMTLSLEGDANDYVGKGLSGGKLIIYPPADSSFV 1358
Cdd:pfam01493 5 NTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAESTFK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1359 PNENIILGNVALYGATDGEAYFRGIAAERFCVRNSGAKVVVEGIGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYD 1438
Cdd:pfam01493 85 AEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIAYVLD 164
|
170 180
....*....|....*....|....*.
gi 297170345 1439 PKNNFKKNCNMSTFDLEKMVIKEDKE 1464
Cdd:pfam01493 165 EDGDFPEKLNKEMVELERVTDEDEEA 190
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1282-1438 |
5.45e-68 |
|
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: 225.53 E-value: 5.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1282 RVFGTIISNEVAKSwgaAGLPNDTLRFNLSGSAGQSFGAWAtKGMTLSLEGDANDYVGKGLSGGKLIIYPPADssfvpNE 1361
Cdd:cd00504 1 RAVGTRGSRYIGKR---PGLPEDTVEIIINGSAGQSFGAFM-AGGTITVEGNANDYVGKGMSGGEIVIHPPAG-----DE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297170345 1362 NIILGNVALYGATDGEAYFRGIAAERFCVRNSGAKVVVEGIGD-HGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYD 1438
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
201-424 |
2.97e-31 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 122.94 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 201 YACSLSSRLIVYKGMLTPSQlfpFFPDLEDKTFETHLAMVHSRFSTNTFPSWDRAQPCR------YMCHNGEINTLKGNM 274
Cdd:cd00352 37 IAVYDGDGLFVEKRAGPVSD---VALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 275 NLMQSRQGKADSDlyknkinklfpiaepdcSDSGSFDNVLELLIMTGRkLPEAVMMMIPEawqndknmskvkkdfyryss 354
Cdd:cd00352 114 EELEARGYRFEGE-----------------SDSEVILHLLERLGREGG-LFEAVEDALKR-------------------- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297170345 355 slmepWDGPASIVFTDG--TQVGAVLDRNGLRPSRFYVTDNDKVIMASEVGVLEVEPktVLRKGRLQPGKMF 424
Cdd:cd00352 156 -----LDGPFAFALWDGkpDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALLALP--FKGVRRLPPGELL 220
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1300-1491 |
4.78e-13 |
|
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.
Pssm-ID: 238481 [Multi-domain] Cd Length: 232 Bit Score: 70.41 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1300 GLPNDtLRFNLSGSAGQSFGAWaTKGMTLSLEGDANDYVGKGLSGGKLIIYPPAdssfvpneniilGNVALYGATDGEAY 1379
Cdd:cd00981 42 GLPGN-VRINIYGVPGNDLGAF-MSGPTIIVYGNAQDDVGNTMNDGKIVIHGSA------------GDVLGYAMRGGKIF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1380 FRGIAAERFCVRNSGAK-----VVVEGI-GDHGCEYMTGGRAVILG------PTGRNFGAGMSGGIAYVydpknnfkkNC 1447
Cdd:cd00981 108 IRGNAGYRVGIHMKEYKdkvpvLVIGGTaGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIYI---------RG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297170345 1448 NMSTFDLEKMVIK-----EDKEELKTLISNHFKYTKSDVAEKILSNWVK 1491
Cdd:cd00981 179 KVERSKLGKEVPKfelteEDLEFIEKYIEEFCKEFGYDKAEILDEEFTK 227
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1312-1452 |
2.84e-09 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 59.82 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1312 GSAGQSFGAWATKGmTLSLEGDANDYVGKGLSGGKLIIYppadssfvpneniilGNV------ALYGATDG----EAYFR 1381
Cdd:COG2218 88 GDVGMYLGAGMKGG-KITVNGNAGSFAGAEMKGGEIEIN---------------GNAgdflgaAYRGDWRGmsggTIIVK 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297170345 1382 GIAAERFCVRNSGAKVVVEG-IGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFkkncnMSTF 1452
Cdd:COG2218 152 GNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPEEL-----LPTF 218
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1321-1437 |
6.89e-08 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 54.66 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1321 WATKGMT---LSLEGDANDYVGKGLSGGKLIIYPPADS----SFVPNENIILGNVALY----------GATDGEAYFRGI 1383
Cdd:cd00980 32 RIGARMTageIVVEGDVGMYVGAGMKGGKLVVEGNAGSwagcEMKGGEITIKGNAGDYvgsayrgdwrGMSGGTITIEGN 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 297170345 1384 AAERFCVRNSGAKVVVEG-IGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVY 1437
Cdd:cd00980 112 AGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIG 166
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1321-1468 |
1.69e-07 |
|
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.
Pssm-ID: 274439 [Multi-domain] Cd Length: 257 Bit Score: 54.27 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1321 WATKGMT---LSLEGDANDYVGKGLSGGKLIIYPPADSSFVPN----ENIILGNVALY----------GATDGEAYFRGI 1383
Cdd:TIGR03122 73 RIGENMSageIVVEGDVGMHVGAEMKGGKIVVNGNADSWAGCEmkggEIIIKGNAGDYvgsayrgewrGMSGGKIIVEGN 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1384 AAERFCVRNSGAKVVVEG-IGDHGCEYMTGGRAVILGPTGRNFGAGMSGGIAYVYDPKNNFkkncnMSTF----DLEKMV 1458
Cdd:TIGR03122 153 AGDYLGERMRGGEILIKGnAGIFAGIHMNGGTIIIDGDIGRRPGGEMKRGTIVVGGKVDEL-----LPTFkfegLHELPF 227
|
170
....*....|
gi 297170345 1459 IKEDKEELKT 1468
Cdd:TIGR03122 228 LLKSAFTQAI 237
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
201-402 |
2.41e-06 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 50.73 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 201 YACSLSSRLIVYKGMLTPSQLFPFFpDLEDktFETHLAMVHSRFSTNTFPSWDRAQP-CRY-MC--HNGEINTLKGNMNL 276
Cdd:cd01907 46 FVYSSGKDMEVFKGVGYPEDIARRY-DLEE--YKGYHWIAHTRQPTNSAVWWYGAHPfSIGdIAvvHNGEISNYGSNREY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 277 MQSRQGKADSDlyknkinklfpiaepdcSDSGSFDNVLELLIMTGrKLPEAVMMMIPEAWQNDKNMSKVKKdfYRYSSSL 356
Cdd:cd01907 123 LERFGYKFETE-----------------TDTEVIAYYLDLLLRKG-GLPLEYYKHIIRMPEEERELLLALR--LTYRLAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 297170345 357 MepwDGPASIVFTDGTQVGAVLDRNGLRPSRFYVTDnDKVIMASEV 402
Cdd:cd01907 183 L---DGPFTIIVGTPDGFIVIRDRIKLRPAVVAETD-DYVAIASEE 224
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
1009-1133 |
9.03e-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: 42.19 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170345 1009 PHHDIYSIEDIAQLIHDLKNANrssrISVKLVSEIGVGT--IAAGVVKAKTDHLVIAGHDGGTGASPLTsikhaglpwel 1086
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAV----PDVKVVVKLSPTGelAAAAAEEAGVDEVGLGNGGGGGGGRDAV----------- 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 297170345 1087 giAETHQTLVMNNLRSRVVLQTDGQLKTGRDVAIAAILGAEEFGFST 1133
Cdd:cd04722 156 --PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| |
