|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
10-1506 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1770.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 10 GLYTPELEHDACGIGFVAHLKNRKSHQVVTQALDMLARMEHRGGQGCDPCSGDGAGILLQKPHEFLLEEAVKLGIKLPsf 89
Cdd:PRK11750 4 GLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 90 EKYGVGVVLFPKDEHKRAQCRDILERNAKRLDLDVIGYRVLPTNNSMLGADPLSTEPQFEHVFISGGPGMQPDELERKLY 169
Cdd:PRK11750 82 KNYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERRLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 170 VLRNYT-VRVCLEsvsnigDDFYINSMSYKTLVYKGQLTTEQVPQYFLDLQNPTMVTALALVHSRFSTNTFPKWRLAQPF 248
Cdd:PRK11750 162 IARRRIeKRLADD------KDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 249 RYIAHNGEINTVRGNLNWMKAREAILQSKLFtqAEIDMLLPICQEGASDSANFDMVLELLVLSGRSLPHALMMMIPEAWQ 328
Cdd:PRK11750 236 RYLAHNGEINTITGNRQWARARAYKFQTPLI--PDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 329 ENKAMDPKRRAFYQYHANVMEPWDGPASVCFTDGVQVGATLDRNGLRPSRYTVTKDDFLIMASESGVVEIDPANVEYRGR 408
Cdd:PRK11750 314 NNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 409 LQPGRIFVADLEQGRIISDEEVKDGIASAQPYEKWVEENLLSLK---KLPDADNVHSQPSPERLLHRQQAFGVSSEEVND 485
Cdd:PRK11750 394 VGPGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVpfeELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 486 IILTLAQTGYEPLGSMGADWPVAVLSHQSQHLSNYFKQLFAQVTNPPIDPIRERMVMSLNTYIGRDQNLLAETPAHCRKV 565
Cdd:PRK11750 474 VIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRV 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 566 ELESPVISNAELEKIRAIDNEHLQAKTLDIVFRASdEPGkLERALKRICQYAEDAVIDGYSIILLTDRAVNSNHAAIPAM 645
Cdd:PRK11750 554 IFKSPVLSYSDFKQLTTLDEEHYRADTLDLNYDPE-ETG-LEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAA 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 646 LAVGAVHHHLIRKGLRSKCGIVVETGDARETHHFATLLGYGANAVNPYLVVETIVDLKRQKKLDADVSveKYFENYRKGV 725
Cdd:PRK11750 632 MAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYR--QVMLNYRKGI 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 726 NGGLLKIFSKMGISTLQSYHGAQIFEALGISKAVVDKYFTGTITRIQGLTLDDIAKEVLVRHRIGYPTReiplQVLDVGG 805
Cdd:PRK11750 710 NKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLAR----KPIDQGG 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 806 VYQWKQRGEQHLFNPETIHLLQESTRHKNYQQFKKYAAAVDSQgdKAVTLRSQLDfVKNPAGSIPIEEVEPIESIVKRFA 885
Cdd:PRK11750 786 LLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNER--PVATLRDLLA-LKPADNPIPLDEVEPAEELFKRFD 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 886 TGAMSFGSISYEAHSTLAIAMNRLGAKSNSGEGGEDPMRFepnanGDSERSAIKQVASGRFGVTSYYLTNADEIQIKMAQ 965
Cdd:PRK11750 863 SAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQ 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 966 GAKPGEGGQLPGDKVDEWIGATRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANRKGRVNVKLVSEAGVGTIASGVA 1045
Cdd:PRK11750 938 GAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1046 KAKADVVLIAGHDGGTGASPISSIRHTGLPWELGLAETHQTLLKNGLRNRIVVQADGQMKTPRDIAIAVLLGAEEWGVAT 1125
Cdd:PRK11750 1018 KAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGT 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1126 AALVVEGCIMMRKCHKNTCPVGIATQNKTLR-ERFAGRVDDVVTFFQYMAQGLREIMAELGFRTINEMVGQAHKLKVRDD 1204
Cdd:PRK11750 1098 GPMVALGCKYLRICHLNNCATGVATQDEKLRkNHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEG 1177
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1205 IGHwKYKNLDLSPILFIEQPRSEDGIYCQTQQNHQLEN-VLDRTLIQLATPALERGEAVKAELPIINTDRSTGTMLSNEI 1283
Cdd:PRK11750 1178 ETA-KQQKLDLSPLLETAEPPAGKALYCTEERNPPFDKgLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEI 1256
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1284 CKVYKDQGLP-QPMQVKFNGSAGQSFGAFLTKSVYFEVEGDANDYWGKGLSGGTLVLYPNRNATIVPEENIVVGNVCFYG 1362
Cdd:PRK11750 1257 ARRHGNQGMAdAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYG 1336
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1363 ATSGESYIRGLAGERFCVRNSGAKVVVEGIGDHGCEYMTGGVAVILGSTGRNFAAGMSGGVAYVWDKSGDFQSKLNAELV 1442
Cdd:PRK11750 1337 ATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELV 1416
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2263065038 1443 DLDPIE--AEDRALLKEMLTKHVQFTGSEVAKAFLANFDASLATMVKVMPR--DYKAVLQKRKAQEQQ 1506
Cdd:PRK11750 1417 EILRVEdlEIHREHLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPKaaDVKALLGHRSRSAAE 1484
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
10-1512 |
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: 1415.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 10 GLYTPELEHDACGIGFVAHLKNRKSHQVVTQALDMLARMEHRGGQGCDPCSGDGAGILLQKPHEFLLEEAVKLGIKLPSF 89
Cdd:COG0070 3 GAGAMGAAAAAGGGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 90 EKYGVGVVLFPKDEHKRAQCRDILERNAKRLDLDVIGYRVLPTNNSMLGADP----LSTEPQFEHVFISGGPGMQPDELE 165
Cdd:COG0070 83 GALLAGGGAFFAAGLAAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAEtlvvLLALGVRAAALARREAELSELAAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 166 RKLYVLRNYTVRVCLESVSNIGDDFYINSMSYKTLVYKGQLTTEQVPQYFLDLQNPTMVTALALVHSRFSTNTFPKWRLA 245
Cdd:COG0070 163 RRLRLRRLALLRRRRRRRRREFRRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 246 QPFRYIAHNGEINTVRGNLNWMkAREAILQSKLFTQAEIDMLLPICQEGASDSANFDMVLELLVLSGRSLPHALMMMIPE 325
Cdd:COG0070 243 FAPRTLAANNNNNNNNNNNNNN-NRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 326 AWQENKAMDPKRRAFYQYHANVMEPWDGPASVCFTDGVQVGATLDRNGLRPSRYTVTKDDFLIMASESGVVEIDPANVEY 405
Cdd:COG0070 322 AAPAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 406 RGRLQPGRIFVADLEQGRIISDEEVKDGIASAQPYEKWVEENLLSLKKLPDADNVHSQPSPERLLHRQQAFGVSSEEVND 485
Cdd:COG0070 402 KGRELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 486 IILTLAQTGYEPLGSMGADwPVAVLSHQSQHLSNYFKQLFAQVTNPPIDPIRERMVMSLNTYIGRDQNLLAETPAHCRKV 565
Cdd:COG0070 482 LLLAEALEEEEESGGAGAA-AAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 566 ELESPVISNAELEKIRAIDNEHLQAKTLDIVFRASDEPGK--LERALKRICQYAEDAVIDGYSIILLTDRAVNSNHAAIP 643
Cdd:COG0070 561 LLELLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGgaLAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 644 AMLAVGAVHHHLIRKGLRSKCGIVVETGDARETHHFATLLGYGANAVNPYLVVETIVDLKRQKKLDADVSVEKYFENYRK 723
Cdd:COG0070 641 ALLALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 724 GVNGGLLKIfSKMGISTLQSYHGAQIFEALGISKAVVDKYFTGTITRIQGLTLDDIAKEVLVRHRIGYPTREIPLQVLDV 803
Cdd:COG0070 721 LKAGVKKKL-KIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGG 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 804 GGVYQWKQRGEQHLFNPETIHLLQESTRHKNYQQFKKYAAAVDSQGDKAVTLRSQLDFVKNPagSIPIEEVEPIESIVKR 883
Cdd:COG0070 800 GGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRP--PIPIEEVEPEEEIVKR 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 884 FATGAMSFGSISYEAHSTLAIAMNRLGAKSNSGEGGEDPMRFEPNANGDSERSAIKQVASGRFGVTSYYLTNADEIQIKM 963
Cdd:COG0070 878 FATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKM 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 964 AQGAKPGEGGQLPGDKVDEWIGATRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANRKGRVNVKLVSEAGVGTIASG 1043
Cdd:COG0070 958 AQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAG 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1044 VAKAKADVVLIAGHDGGTGASPISSIRHTGLPWELGLAETHQTLLKNGLRNRIVVQADGQMKTPRDIAIAVLLGAEEWGV 1123
Cdd:COG0070 1038 VAKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGF 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1124 ATAALVVEGCIMMRKCHKNTCPVGIATQNKTLRERFAGRVDDVVTFFQYMAQGLREIMAELGFRTINEMVGQAHKLKVRD 1203
Cdd:COG0070 1118 ATAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRR 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1204 DIGHWKYKNLDLSPILFIEQPRSEDGIYCQTQQNHQLENVLDRTLIQLATPALERGEAVKAELPIINTDRSTGTMLSNEI 1283
Cdd:COG0070 1198 AVDHWKAKGLDLSPLLYKPDVPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEI 1277
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1284 CKVYKDQGLP-QPMQVKFNGSAGQSFGAFLTKSVYFEVEGDANDYWGKGLSGGTLVLYPNRNATIVPEENIVVGNVCFYG 1362
Cdd:COG0070 1278 AKRYGNEGLPeDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYG 1357
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1363 ATSGESYIRGLAGERFCVRNSGAKVVVEGIGDHGCEYMTGGVAVILGSTGRNFAAGMSGGVAYVWDKSGDFQSKLNAELV 1442
Cdd:COG0070 1358 ATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMV 1437
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2263065038 1443 DLDPI-EAEDRALLKEMLTKHVQFTGSEVAKAFLANFDASLATMVKVMPRDYKAVLQKRKAQEQQATLAAE 1512
Cdd:COG0070 1438 ELERLdEEEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDADE 1508
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
9-1513 |
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: 1380.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 9 RGLYTPELEHDACGIGFVAHLKNRKSHQVVTQALDMLARMEHRGGQGCDPCSGDGAGILLQKPHEFLLEEAVKLGIKLPS 88
Cdd:COG0067 11 QGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIELPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 89 FEKYGVGVVLFPKDEHKRAQCRDILERNAKRLDLDVIGYRVLPTNNSMLGADPLSTEPQFEHVFISGGPGMQPDELERKL 168
Cdd:COG0067 91 PGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFERKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 169 YVLRNYTVRVcLESVSNIGDDFYINSMSYKTLVYKGQLTTEQVPQYFLDLQNPTMVTALALVHSRFSTNTFPKWRLAQPF 248
Cdd:COG0067 171 YVARKRIEKA-IRALGLDDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQPF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 249 RYIAHNGEINTVRGNLNWMKAREAILQSKLFTqAEIDMLLPICQEGASDSANFDMVLELLVLSGRSLPHALMMMIPEAWQ 328
Cdd:COG0067 250 RYLAHNGEINTLRGNRNWMRAREALLASPLFG-DDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMMLIPEAWE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 329 ENKAMDPKRRAFYQYHANVMEPWDGPASVCFTDGVQVGATLDRNGLRPSRYTVTKDDFLIMASESGVVEIDPANVEYRGR 408
Cdd:COG0067 329 NNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 409 LQPGRIFVADLEQGRIISDEEVKDGIASAQPYEKWVEENLLSLKKLPDADNVHsQPSPERLLHRQQAFGVSSEEVNDIIL 488
Cdd:COG0067 409 LQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEP-APDDDLLLRRQQAFGYTEEEELLLLL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 489 TLAQTGYEPLGSMGADWPVAVLSHQSQHLSNYFKQLFAQVTNPPIDPIRERMVMSLNTYIGRDQNLLAETPAHCRKVELE 568
Cdd:COG0067 488 PMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEARRRLLLL 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 569 SPVISN-AELEKIRAIDNEHLQAKTLDIVFRASDEPGKLERALKRICQYAEDAVIDGYSIILLTDRAVNSNHAAIPAMLA 647
Cdd:COG0067 568 PPPLLNeLLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDAAPAPLAAA 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 648 VGAVHHHLIRKGLRSKCGIVVETGDARETHHFATLLGYGANAVNPYLVVETIVDLKRQKKLDADVSVEKYFENYRKGVNG 727
Cdd:COG0067 648 AAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAAAAKKKKKKKKG 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 728 GLLKIFSKMGISTLQSYHGAQIFEALGISKAVVDKYFTGTITRIQGLTLDDIAKEVLVRHRIGYPTREIPLQ---VLDVG 804
Cdd:COG0067 728 KLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLlglGGGGG 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 805 GVYQWKQRGEQHLFNPETIHLLQESTRHKNYQQFKKYAAAVDSQGDKavTLRSQLDFVKNPAGSIPIEEVEPIESIVKRF 884
Cdd:COG0067 808 GEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLL--LLLLLLLFEEEEEEEEPEEEEEEEESSAIAA 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 885 ATGAMSFGSISYEAHSTLAIAMNRLGAKSNSGEGGEDpmrfEPNANGDSERSAIKQVASGRFGVTSYYLTNADEIQIKMA 964
Cdd:COG0067 886 ASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGE----GRRASGGSGSSSSASVAAAGGGVVVGAGAAAAEGGGGGG 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 965 QGAKPGEGGQLPGDKVDEWIGATRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANRKGRVNVKLVSEAGVGTIASGV 1044
Cdd:COG0067 962 GGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAAAAA 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1045 AKAKADVVLIAGHDGGTGASPISSIRHTGLPWELGLAETHQTLLKNGLRNRIVVQADGQMKTPRDIAIAVLLGAEEWGVA 1124
Cdd:COG0067 1042 AAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGALGGG 1121
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1125 TAALVVEGCIMMRKCHKNTCPVGIATQNKTLRERFAGRVDDVVTFFQYMAQGLREIMAELGFRTINEMVGQAHKLKVRDD 1204
Cdd:COG0067 1122 AAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLGVVELLLLLL 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1205 IGHWKYKNLDLSPILFIEQPRSEDGIYCQTQQNHQLENVLDRTLIQLATPALERGEAVKAELPIINTDRSTGTMLSNEIC 1284
Cdd:COG0067 1202 LLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGGGGGGGG 1281
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1285 KVYKDQGLPQPMQVKFN--GSAGQSFGAFLTKSVYFEVEGDANDYWGKGLSGGTLVLYPNRNATIVPEENIVVGNVCFYG 1362
Cdd:COG0067 1282 GGGGGGGGGGGGGGGGGggGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGG 1361
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1363 ATSGESYIRGLAGERFCVRNSGAKVVVEGIGDHGCEYMTGGVAVILGSTGRNFAAGMSGGVAYVWDKSGDFQSKLNAELV 1442
Cdd:COG0067 1362 GGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDEEEEEEL 1441
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2263065038 1443 DLDPIEAEDRALLKEMLTKHVQFTGSEVAKAFLANFDASLATMVKVMPRDYKAVLQKRKAQEQQATLAAEA 1513
Cdd:COG0067 1442 EELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAAAAEA 1512
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
647-1381 |
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: 980.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 647 AVGAVHHHLIRKGLRSKCGIVVETGDARETHHFATLLGYGANAVNPYLVVETIVDLKRQKKLDaDVSVEKYFENYRKGVN 726
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLL-GLDLEEAVKNYIKAIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 727 GGLLKIFSKMGISTLQSYHGAQIFEALGISKAVVDKYFtgtitriqgltlddiaKEVLVRHRIGYptreipLQVLDVGGV 806
Cdd:COG0069 80 KGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDIGI----------------ADVLTQHRHAI------LRNLPVGGR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 807 YQWK--------------QRGEQHLFNPETIHLLQESTrhKNYQQFKKYAAAVDSQGDKAVTLRSQLDFVKNPAgSIPIE 872
Cdd:COG0069 138 YRYRfesigpeirqyffeSDGEEHPFNRETRSLLYQAA--KNEEDYKPFGTLVDYQPGYEWTLRSLFPFKADRP-PIPIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 873 E-VEPIESIVKRFATGAMSFGSISYEAHSTLAIAMNRLGAKSNSGEGGEDPMRFepnanGDSERSAIKQVASGRFGVT-- 949
Cdd:COG0069 215 EpVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRde 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 950 -SYYLTNADEIQIKMAQGAKPGEGGQLPGDKVDEWIGATRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANRKGRVN 1028
Cdd:COG0069 290 dGEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1029 VKLVSEAGVGTIA--SGVAK--AKADVVLIAGHDGGTGASPISSIRHTGLPWELGLAETHQTLLKNGLRNRIVVQADGQM 1104
Cdd:COG0069 370 VKLVSGAGVGTIAacKGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1105 KTPRDIAIAVLLGAEEWGVATAALVVEGCIMMRKCHKNTCPVGIATQNKTLRERF--AGRVDDVVTFFQYMAQGLREIMA 1182
Cdd:COG0069 450 KTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFvvEGKPERVVNYFRFTAEEVREILA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1183 ELGFRTINEMVGQAHKLKVRDDIgHWKYKNLDLSPILFIEQPRSEDGIYCQTQQNHQLENVLDRTLIQLATPALERGEAV 1262
Cdd:COG0069 530 ALGVRSPDELIGRHDLLRVRDGE-HWKAKGLDLSPLLYKPELPEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPV 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1263 KAELPIINTDRSTGTMLSNEICKVYKDQGLPQPM-QVKFNGSAGQSFGAFLTKSVYFEVEGDANDYWGKGLSGGTLVLYP 1341
Cdd:COG0069 609 VLITNIRNNNRRVGGMLSGEIAKRYGGAGLPDDTiILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPP 688
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2263065038 1342 NRNATIVPEENIVVGNVCFYGATSGESYIRGLAGERFCVR 1381
Cdd:COG0069 689 PPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
21-443 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 771.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 21 CGIGFVAHLKNRKSHQVVTQALDMLARMEHRGGQGCDPCSGDGAGILLQKPHEFLLEEAVKLGIKLPSFEKYGVGVVLFP 100
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 101 KDEHKRAQCRDILERNAKRLDLDVIGYRVLPTNNSMLGADPLSTEPQFEHVFISGGPGMQPDELERKLYVLRNytvRVCL 180
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARK---RIEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 181 E-SVSNIGDDFYINSMSYKTLVYKGQLTTEQVPQYFLDLQNPTMVTALALVHSRFSTNTFPKWRLAQPFRYIAHNGEINT 259
Cdd:pfam00310 158 EiGVEGGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 260 VRGNLNWMKAREAILQSKLFTQaEIDMLLPICQEGASDSANFDMVLELLVLSGRSLPHALMMMIPEAWQENKAMDPKRRA 339
Cdd:pfam00310 238 LRGNRNWMRAREALLKSELFGD-DLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 340 FYQYHANVMEPWDGPASVCFTDGVQVGATLDRNGLRPSRYTVTKDDFLIMASESGVVEIDPANVEYRGRLQPGRIFVADL 419
Cdd:pfam00310 317 FYEYHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDL 396
|
410 420
....*....|....*....|....
gi 2263065038 420 EQGRIISDEEVKDGIASAQPYEKW 443
Cdd:pfam00310 397 EEGRIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
21-438 |
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: 711.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 21 CGIGFVAHLKNRKSHQVVTQALDMLARMEHRGGQGCDPCSGDGAGILLQKPHEFLLEEAVKLGIKLPSFEKYGVGVVLFP 100
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 101 KDEHKRAQCRDILERNAKRLDLDVIGYRVLPTNNSMLGADPLSTEPQFEHVFISGGPGMQPDELERKLYVLRNYTVRvcl 180
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEK--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 181 eSVSNIGDDFYINSMSYKTLVYKGQLTTEQVPQYFLDLQNPTMVTALALVHSRFSTNTFPKWRLAQPFRYIAHNGEINTV 260
Cdd:cd00713 158 -AIRAADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 261 RGNLNWMKAREAILQSKLFtQAEIDMLLPICQEGASDSANFDMVLELLVLSGRSLPHALMMMIPEAWQENKAMDPKRRAF 340
Cdd:cd00713 237 RGNRNWMRAREGLLKSPLF-GEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 341 YQYHANVMEPWDGPASVCFTDGVQVGATLDRNGLRPSRYTVTKDDFLIMASESGVVEIDPANVEYRGRLQPGRIFVADLE 420
Cdd:cd00713 316 YEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLE 395
|
410
....*....|....*...
gi 2263065038 421 QGRIISDEEVKDGIASAQ 438
Cdd:cd00713 396 EGRILDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
816-1187 |
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: 556.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 816 HLFNPETIHLLQESTRHKNYQQFKKYAAAVDSQgDKAVTLRSQL--DFVKNPagsIPIEEVEPIESIVKRFATGAMSFGS 893
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNER-VPIGALRDLLefDFAEDP---IPLEEVEPALEIKTRFCTGAMSYGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 894 ISYEAHSTLAIAMNRLGAKSNSGEGGEDPMRFEPNANGdsersAIKQVASGRFGVTSYYLTNADEIQIKMAQGAKPGEGG 973
Cdd:pfam01645 77 LSEEAHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-----AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 974 QLPGDKVDEWIGATRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANRKGRVNVKLVSEAGVGTIASGVAKAKADVVL 1053
Cdd:pfam01645 152 HLPGEKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1054 IAGHDGGTGASPISSIRHTGLPWELGLAETHQTLLKNGLRNRIVVQADGQMKTPRDIAIAVLLGAEEWGVATAALVVEGC 1133
Cdd:pfam01645 232 IDGYDGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGC 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2263065038 1134 IMMRKCHKNTCPVGIATQNKTLRER--FAGRVDDVVTFFQYMAQGLREIMAELGFR 1187
Cdd:pfam01645 312 IMCRVCHTNTCPVGVATQDPELRKRldFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
819-1201 |
1.12e-169 |
|
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: 514.40 E-value: 1.12e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 819 NPETIHLLQESTR--HKNYQQFKKYAAAVDSQGDKAVTLRSQLDFvKNPAGSIPIEE-------------VEPIESIVKR 883
Cdd:cd02808 1 YLLEIERLEEIQYfvFNRAERYGVYNRAGNSRGRPFGTLRDLLEF-GAQLAKHPLEPdeevddrvtigpnAEKPLKLDSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 884 FATGAMSFGSISYEAHSTLAIAMNRLGAKSNSGEGGEDPMRFEPNangdseRSAIKQVASGRFGVTSYYLTNADEIQIKM 963
Cdd:cd02808 80 FNISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREGG------GDIIKQVASGRFGVRPEYLNKADAIEIKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 964 AQGAKPGEGGQLPGDKVDEWIGATRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANRKGRVNVKLVSEAGVGTIASG 1043
Cdd:cd02808 154 GQGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1044 VAKAKADVVLIAGHDGGTGASPISSIRHTGLPWELGLAETHQTLLKNGLRNRIVVQADGQMKTPRDIAIAVLLGAEEWGV 1123
Cdd:cd02808 234 VAAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1124 ATAALVVEGCIMMRKCHKNTCPVGIATQNKTLRER--FAGRVDDVVTFFQYMAQGLREIMAELGFRTInEMVGQAHKLKV 1201
Cdd:cd02808 314 GTAALIALGCIQARKCHTNTCPVGVATQDPELRRRldVEGKAERVANYLKSLAEELRELAAALGKRSL-ELLGRSDLLAL 392
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
472-756 |
9.10e-167 |
|
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: 502.30 E-value: 9.10e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 472 RQQAFGVSSEEVNDIILTLAQTGYEPLGSMGADWPVAVLSHQSQHLSNYFKQLFAQVTNPPIDPIRERMVMSLNTYIGRD 551
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 552 QNLLAETPAHCRKVELESPVISNAELEKIRAIDNEHLQAKTLDIVFRAsdepgkLERALKRICQYAEDAVIDGYSIILLT 631
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITFDG------LEAALERLCEEAEEAVRDGANILILS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 632 DRAVNSNHAAIPAMLAVGAVHHHLIRKGLRSKCGIVVETGDARETHHFATLLGYGANAVNPYLVVETIVDLKRQ-KKLDA 710
Cdd:pfam04898 156 DRGVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREgKGKLT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2263065038 711 DVSVEKYFENYRKGVNGGLLKIFSKMGISTLQSYHGAQIFEALGIS 756
Cdd:pfam04898 236 DEDLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1244-1491 |
2.98e-148 |
|
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: 451.98 E-value: 2.98e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1244 LDRTLIQLATPAL-ERGEAVKAELPIINTDRSTGTMLSNEICKVYKDQGLP-QPMQVKFNGSAGQSFGAFLTKSVYFEVE 1321
Cdd:cd00982 1 LDDKLIADAEPALiENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPeDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1322 GDANDYWGKGLSGGTLVLYPNRNATIVPEENIVVGNVCFYGATSGESYIRGLAGERFCVRNSGAKVVVEGIGDHGCEYMT 1401
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1402 GGVAVILGSTGRNFAAGMSGGVAYVWDKSGDFQSKLNAELVDLDPIE-AEDRALLKEMLTKHVQFTGSEVAKAFLANFDA 1480
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEdAEDEEQLKELIEEHVEYTGSEKAKEILANWEA 240
|
250
....*....|.
gi 2263065038 1481 SLATMVKVMPR 1491
Cdd:cd00982 241 YLKKFVKVIPR 251
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1266-1451 |
4.23e-110 |
|
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: 345.94 E-value: 4.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1266 LPIINTDRSTGTMLSNEICKVYKDQGLPQ-PMQVKFNGSAGQSFGAFLTKSVYFEVEGDANDYWGKGLSGGTLVLYPNRN 1344
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDdTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1345 ATIVPEENIVVGNVCFYGATSGESYIRGLAGERFCVRNSGAKVVVEGIGDHGCEYMTGGVAVILGSTGRNFAAGMSGGVA 1424
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180
....*....|....*....|....*..
gi 2263065038 1425 YVWDKSGDFQSKLNAELVDLDPIEAED 1451
Cdd:pfam01493 161 YVLDEDGDFPEKLNKEMVELERVTDED 187
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1273-1428 |
2.55e-65 |
|
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: 217.82 E-value: 2.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1273 RSTGTMLSNEICKvyKDQGLPQPMQVKFNGSAGQSFGAFLtKSVYFEVEGDANDYWGKGLSGGTLVLYPNRNativpEEN 1352
Cdd:cd00504 1 RAVGTRGSRYIGK--RPGLPEDTVEIIINGSAGQSFGAFM-AGGTITVEGNANDYVGKGMSGGEIVIHPPAG-----DEN 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2263065038 1353 IVVGNVCFYGATSGESYIRGLAGERFCVRNSGAKVVVEGIGD-HGCEYMTGGVAVILGSTGRNFAAGMSGGVAYVWD 1428
Cdd:cd00504 73 GIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
211-415 |
7.30e-34 |
|
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: 130.26 E-value: 7.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 211 VPQYFLDLQNPTMVTALALVHSRFSTNTFPKWRLAQPFR------YIAHNGEINTVRGNLNWMKAReailqsklftqaei 284
Cdd:cd00352 54 VSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEAR-------------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 285 dmllPICQEGASDSANFDMVLELLVLSGRsLPHALMMMIPEawqenkamdpkrrafyqyhanvmepWDGPASVCFTDGV- 363
Cdd:cd00352 120 ----GYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKR-------------------------LDGPFAFALWDGKp 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2263065038 364 -QVGATLDRNGLRPSRYTVTKDDFLIMASESGVveIDPANVEYRGRLQPGRIF 415
Cdd:cd00352 170 dRLFAARDRFGIRPLYYGITKDGGLVFASEPKA--LLALPFKGVRRLPPGELL 220
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1291-1478 |
2.10e-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: 71.56 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1291 GLPQPMQVKFNGSAGQSFGAFLTKSVyFEVEGDANDYWGKGLSGGTLVLYPNrnativpeenivVGNVCFYGATSGESYI 1370
Cdd:cd00981 42 GLPGNVRINIYGVPGNDLGAFMSGPT-IIVYGNAQDDVGNTMNDGKIVIHGS------------AGDVLGYAMRGGKIFI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1371 RGLAGERFCVRNSGAK-----VVVEGI-GDHGCEYMTGGVAVILG------STGRNFAAGMSGGVAYVWDKSGDfqSKLN 1438
Cdd:cd00981 109 RGNAGYRVGIHMKEYKdkvpvLVIGGTaGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIYIRGKVER--SKLG 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2263065038 1439 AElVDLDPIEAEDRALLKEMLTKHVQFTGSEVAKAFLANF 1478
Cdd:cd00981 187 KE-VPKFELTEEDLEFIEKYIEEFCKEFGYDKAEILDEEF 225
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1301-1429 |
2.07e-07 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1301 NGSAGQSFGAFLtKSVYFEVEGDANDYWGKGLSGGTLvlypnrnativpeenIVVGNV------CFYGATSGES----YI 1370
Cdd:COG2218 87 EGDVGMYLGAGM-KGGKITVNGNAGSFAGAEMKGGEI---------------EINGNAgdflgaAYRGDWRGMSggtiIV 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1371 RGLAGERFCVRNSGAKVVVEG-IGDHGCEYMTGGVAVILGSTGRNFAAGMSGGVAYVWDK 1429
Cdd:COG2218 151 KGNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGK 210
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1301-1433 |
6.45e-07 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 51.58 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1301 NGSAGQSFGAFLtKSVYFEVEGDANDYWGKGLSGGTLvlypnrnativpeenIVVGNVCFY----------GATSGESYI 1370
Cdd:cd00980 45 EGDVGMYVGAGM-KGGKLVVEGNAGSWAGCEMKGGEI---------------TIKGNAGDYvgsayrgdwrGMSGGTITI 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2263065038 1371 RGLAGERFCVRNSGAKVVVEG-IGDHGCEYMTGGVAVILGSTGRNFAAGMSGGVAYVWDKSGDF 1433
Cdd:cd00980 109 EGNAGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIGGEIEEL 172
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1317-1433 |
6.79e-05 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 46.34 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1317 YFEVEGDAN-------------DYWGKGLSGGTLvlypnrnativpeenIVVGNVCFY---GATSGESYIRGLAGeRFCV 1380
Cdd:COG2218 51 LFDVEGDDGdtkiviegdlsrvKRIGAGMTAGEI---------------IVEGDVGMYlgaGMKGGKITVNGNAG-SFAG 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2263065038 1381 RN-SGAKVVVEG-IGDH-GCEY------MTGGVAVILGSTGRNFAAGMSGGVAYVWDKSGDF 1433
Cdd:COG2218 115 AEmKGGEIEINGnAGDFlGAAYrgdwrgMSGGTIIVKGNAGDRLGDRMRRGTIIIEGDAGDF 176
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1319-1433 |
5.69e-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: 42.72 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1319 EVEGDANDYWGKGLSGGTLVlypnrnativpeeniVVGNVCFY---GATSGESYIRGLAGerfcvrnsgakvvvegigDH 1395
Cdd:cd00980 43 VVEGDVGMYVGAGMKGGKLV---------------VEGNAGSWagcEMKGGEITIKGNAG------------------DY 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2263065038 1396 -GCEY------MTGGVAVILGSTGRNFAAGMSGGVAYVWDKSGDF 1433
Cdd:cd00980 90 vGSAYrgdwrgMSGGTITIEGNAGDRLGERMRRGEILIKGDAGIF 134
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1317-1432 |
1.83e-03 |
|
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: 41.18 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1317 YFEVEGDANDywgkglsggtlvlypnRNATIVPEENivVGNVCFYGA--TSGESYIRGLAGERFCVRNSGAKVVVEGIGD 1394
Cdd:cd00980 7 FFEVSGDGAD----------------ADTKLVIEGD--VPRLKRIGArmTAGEIVVEGDVGMYVGAGMKGGKLVVEGNAG 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2263065038 1395 H--GCEyMTGGVAVILGSTG-------RNFAAGMSGGVAYVWDKSGD 1432
Cdd:cd00980 69 SwaGCE-MKGGEITIKGNAGdyvgsayRGDWRGMSGGTITIEGNAGD 114
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
1001-1125 |
3.03e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 40.65 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2263065038 1001 PHHDIYSIEDLAQLIFDLKNANRKGRVNVKLVseAGVGTIASGVAKAKADVVLIAGHDGGTGASPISsirhtglpwelgl 1080
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKLS--PTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAV------------- 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2263065038 1081 AETHQTLLKNGLRNRIVVQADGQMKTPRDIAIAVLLGAEEWGVAT 1125
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| |
