|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
9-1473 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1785.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 9 AQGLYRPEFEHDACGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECK--NINLP 86
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEeaGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 87 EKerYGVGMVFFSQKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDLKDNlSFER 166
Cdd:PRK11750 82 KN--YAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRER-DFER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 167 KLYVIRKQAENwGVTEGLDFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRY 246
Cdd:PRK11750 159 RLFIARRRIEK-RLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 247 LVHNGEINTLRGNINWMRAREQQFVSESFgEDLNKILPILNADGSDSSILDNAFEFFVMAGrKPAHTAM-MLIPEPWTEN 325
Cdd:PRK11750 238 LAHNGEINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLAGG-MDLFRAMrLLVPPAWQNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 326 THMSKEKRAFYEYHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLE 405
Cdd:PRK11750 316 PDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 406 PGKMLLIDLEEGRIISDEEVKTQIATEYPYQKWLEEELVQVNPDPESREEEQ----FSD--LLTRQKAFGYTYEDIQKYL 479
Cdd:PRK11750 396 PGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVgsreLDDdtLKSYQKQFQYSFEELDQVI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 480 IPVIKEGKDPLGSMGNDAPLAVLSDRAQSLFNYFKQLFAQVTNPPIDAIREQLVTSTMTWLGAEGDLLHPSERNVRRIKL 559
Cdd:PRK11750 476 RVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 560 YTPVLSNEQFYALKTIVHPDLKSQKIDVLFSE---DLERGLKDMFTQAEKAISQGVSLLILSDKKMNERLTPIPPLLAVS 636
Cdd:PRK11750 556 KSPVLSYSDFKQLTTLDEEHYRADTLDLNYDPeetGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVG 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 637 ALHQHLIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRLDISYEEAVSKYGKSITEGVVK 716
Cdd:PRK11750 636 AVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYK 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 717 VMSKMGISTVQSYRGAQIFEAVGISRDVIDRYFSGTASQLGGIDLQTIAEEAQRRHREAYQDdySKTLEPGSDFQWRNGG 796
Cdd:PRK11750 716 IMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLA--RKPIDQGGLLKYVHGG 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 797 EHHAFNPKTIHTLQWACRRNDYNLFKQYTKAADEERIGFLRNLFAFDGNRKPLKLEEVESAESIVKRFKTGAMSFGSLSK 876
Cdd:PRK11750 794 EYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSP 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 877 EAHEALAIAMNRLGGKSNSGEGGEDPKRFvpdenGDDRRSAIKQIASGRFGVKSHYLVNADELQIKMAQGAKPGEGGQLP 956
Cdd:PRK11750 874 EAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLP 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 957 GNKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVGTIAAGVAKATADVIVISG 1036
Cdd:PRK11750 949 GDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISG 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1037 YDGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFATAPLVVLGCVMM 1116
Cdd:PRK11750 1029 YDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYL 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1117 RACHLDTCPVGVATQNPELRKK-FMGDPDHIVNYMLFIAEEVREYMAALGFKTFDEMIGRTDVLHASERAKEhwKASQLD 1195
Cdd:PRK11750 1109 RICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETA--KQQKLD 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1196 LSTLLYQ---PEG-VRTFQSPQNHKIDQSLDITTILPAVQEAIESGKEADISIEINNTNR-VAGTITGsEISKRYGEEGL 1270
Cdd:PRK11750 1187 LSPLLETaepPAGkALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRsVGARLSG-EIARRHGNQGM 1265
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1271 PEDTIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGFNSASDDNVIIGNVAFYGATSGEAYIN 1350
Cdd:PRK11750 1266 ADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAA 1345
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1351 GRAGERFAVRNSGVNVVVEGIGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYVLTEDvKAFKRKCNLEMILFESLEDe 1430
Cdd:PRK11750 1346 GRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDED-GDFVDRVNHELVEILRVED- 1423
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*
gi 239938894 1431 KEIQQI--KAMLERHTAYTNSQKAEDLLDQWEDSVKKFVKVIPKN 1473
Cdd:PRK11750 1424 LEIHREhlRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPKA 1468
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
11-1493 |
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: 1456.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 11 GLYRPEFEHDACGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECKNINLPEKER 90
Cdd:COG0070 26 GLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 91 YGVGMVFFSQKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDLKDNLSFERKLYV 170
Cdd:COG0070 106 AAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 171 IRkqaenwgvtegldfYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRYLVHN 250
Cdd:COG0070 186 RR--------------SSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAAN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 251 GEINTLRGNINWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSK 330
Cdd:COG0070 252 NNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 331 EKRAFYEYHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLEPGKML 410
Cdd:COG0070 332 PAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 411 LIDLEEGRIISDEEVKTQIATEYPYQKWLEEELVQVNPDPESREE---EQFSDLLTRQKAFGYTYEDIQKYLIPVIKEGK 487
Cdd:COG0070 412 LVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEElllLEEELLQEREAELEQELLLLLLLLLAEALEEE 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 488 DPLGSMGNDAPLAVLSDRAQSLFNYFKQLFAQVTNPPIDAIREQLVTSTMTWLGAEGDLLHPSERNVRRIKLYTPVLSNE 567
Cdd:COG0070 492 EESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLAL 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 568 QFYALKTIVHPDLKSQKIDVLF------SEDLERGLKDMFTQAEKAISQGVSLLILSDKKMNERLTPIPPLLAVSALHQH 641
Cdd:COG0070 572 ALLLLLLLLLLLLGDATTLAAAleaaggGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHH 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 642 LIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRLDISYEEAVSKYGKSITEGVVKV-MSK 720
Cdd:COG0070 652 LLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKkLKI 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 721 MGISTVQSYRGAQIFEAVGISRDVIDRYFSGTASQLGGIDLQTIAEEAQRRH-REAYQDDYSKTLEPGSDFQWRNGGEHH 799
Cdd:COG0070 732 GGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHaAAADAAAAAALALGGGGGGGRGGGGEG 811
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 800 AFNPKTIHTLQWACRRNDYNLFKQYTKAADE--ERIGFLRNLFAFDGNRKPLKLEEVESAESIVKRFKTGAMSFGSLSKE 877
Cdd:COG0070 812 HHGGHYHHLLQQLAARTAAALYDDYYAYEDRadELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSE 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 878 AHEALAIAMNRLGGKSNSGEGGEDPKRFVPDENGDDRRSAIKQIASGRFGVKSHYLVNADELQIKMAQGAKPGEGGQLPG 957
Cdd:COG0070 892 AHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPG 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 958 NKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVGTIAAGVAKATADVIVISGY 1037
Cdd:COG0070 972 HKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGH 1051
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1038 DGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFATAPLVVLGCVMMR 1117
Cdd:COG0070 1052 DGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMR 1131
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1118 ACHLDTCPVGVATQNPELRKKFMGDPDHIVNYMLFIAEEVREYMAALGFKTFDEMIGRTDVLhASERAKEHWKASQLDLS 1197
Cdd:COG0070 1132 KCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLL-LVRRAVDHWKAKGLDLS 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1198 TLLYQPE----GVRTFQSPQNHKIDQSLDiTTILPAVQEAIESGKEADISIEINNTNRVAGTITGSEISKRYGEEGLPED 1273
Cdd:COG0070 1211 PLLYKPDvpadVPRYCTEEQNHGLEGALD-RELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPED 1289
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1274 TIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGFNSASDDNVIIGNVAFYGATSGEAYINGRA 1353
Cdd:COG0070 1290 TITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRA 1369
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1354 GERFAVRNSGVNVVVEGIGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYVLTEDvKAFKRKCNLEMILFESLEDEKEI 1433
Cdd:COG0070 1370 GERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDED-GDFEDRCNPEMVELERLDEEEDE 1448
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1434 QQIKAMLERHTAYTNSQKAEDLLDQWEDSVKKFVKVIPKNYKQMLASIEEQKAAGLSDEE 1493
Cdd:COG0070 1449 EELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDADE 1508
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
22-438 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 767.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 22 CGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECK--NINLPEKERYGVGMVFFS 99
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKelGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 100 QKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDlKDNLSFERKLYVIRKQAENWG 179
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAG-KSEDDFERKLYVARKRIEKEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 180 VTEGL--DFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRYLVHNGEINTLR 257
Cdd:pfam00310 160 GVEGGdkDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 258 GNINWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSKEKRAFYE 337
Cdd:pfam00310 240 GNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 338 YHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLEPGKMLLIDLEEG 417
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 239938894 418 RIISDEEVKTQIATEYPYQKW 438
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
22-433 |
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: 735.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 22 CGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECK--NINLPEKERYGVGMVFFS 99
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAeaGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 100 QKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDLkDNLSFERKLYVIRKQAENWG 179
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGD-DGEAFERKLYLLRKRIEKAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 180 VTEGLDFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRYLVHNGEINTLRGN 259
Cdd:cd00713 160 RAADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 260 INWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSKEKRAFYEYH 339
Cdd:cd00713 240 RNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 340 SSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLEPGKMLLIDLEEGRI 419
Cdd:cd00713 320 SSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRI 399
|
410
....*....|....
gi 239938894 420 ISDEEVKTQIATEY 433
Cdd:cd00713 400 LDDEEIKDQLAKRH 413
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1216-1433 |
4.34e-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: 53.11 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1216 KIDQSLDITTILPAVQEAIESGKEADISIEINNTNRVAGTITgsEISKrygeEGLPEDTiKLHFTGSAgqSFGAFVPKGM 1295
Cdd:TIGR03122 8 EPSVPLEADPILPDNLAGKSAEEIEALELWYGNKTVPLGDLF--DVEG----DGKPDET-RLVIDGDM--SRVKRIGENM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1296 T---LYLDGDSNDYVGKGLSGGKIIVK----SSEGFNSASDDNVIIGNVAFY----------GATSGEAYINGRAGERFA 1358
Cdd:TIGR03122 79 SageIVVEGDVGMHVGAEMKGGKIVVNgnadSWAGCEMKGGEIIIKGNAGDYvgsayrgewrGMSGGKIIVEGNAGDYLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1359 VRNSGVNVVVEG-----IGDHgceyMTGGSVVVLGDVGKNFAAGMSGGIAYV---LTEDVKAFKrKCNLEMILFESLEDE 1430
Cdd:TIGR03122 159 ERMRGGEILIKGnagifAGIH----MNGGTIIIDGDIGRRPGGEMKRGTIVVggkVDELLPTFK-FEGLHELPFLLKSAF 233
|
...
gi 239938894 1431 KEI 1433
Cdd:TIGR03122 234 TQA 236
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
9-1473 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1785.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 9 AQGLYRPEFEHDACGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECK--NINLP 86
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEeaGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 87 EKerYGVGMVFFSQKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDLKDNlSFER 166
Cdd:PRK11750 82 KN--YAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRER-DFER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 167 KLYVIRKQAENwGVTEGLDFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRY 246
Cdd:PRK11750 159 RLFIARRRIEK-RLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 247 LVHNGEINTLRGNINWMRAREQQFVSESFgEDLNKILPILNADGSDSSILDNAFEFFVMAGrKPAHTAM-MLIPEPWTEN 325
Cdd:PRK11750 238 LAHNGEINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLAGG-MDLFRAMrLLVPPAWQNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 326 THMSKEKRAFYEYHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLE 405
Cdd:PRK11750 316 PDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 406 PGKMLLIDLEEGRIISDEEVKTQIATEYPYQKWLEEELVQVNPDPESREEEQ----FSD--LLTRQKAFGYTYEDIQKYL 479
Cdd:PRK11750 396 PGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDEQVgsreLDDdtLKSYQKQFQYSFEELDQVI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 480 IPVIKEGKDPLGSMGNDAPLAVLSDRAQSLFNYFKQLFAQVTNPPIDAIREQLVTSTMTWLGAEGDLLHPSERNVRRIKL 559
Cdd:PRK11750 476 RVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 560 YTPVLSNEQFYALKTIVHPDLKSQKIDVLFSE---DLERGLKDMFTQAEKAISQGVSLLILSDKKMNERLTPIPPLLAVS 636
Cdd:PRK11750 556 KSPVLSYSDFKQLTTLDEEHYRADTLDLNYDPeetGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMAVG 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 637 ALHQHLIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRLDISYEEAVSKYGKSITEGVVK 716
Cdd:PRK11750 636 AVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYK 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 717 VMSKMGISTVQSYRGAQIFEAVGISRDVIDRYFSGTASQLGGIDLQTIAEEAQRRHREAYQDdySKTLEPGSDFQWRNGG 796
Cdd:PRK11750 716 IMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLA--RKPIDQGGLLKYVHGG 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 797 EHHAFNPKTIHTLQWACRRNDYNLFKQYTKAADEERIGFLRNLFAFDGNRKPLKLEEVESAESIVKRFKTGAMSFGSLSK 876
Cdd:PRK11750 794 EYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGALSP 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 877 EAHEALAIAMNRLGGKSNSGEGGEDPKRFvpdenGDDRRSAIKQIASGRFGVKSHYLVNADELQIKMAQGAKPGEGGQLP 956
Cdd:PRK11750 874 EAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLP 948
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 957 GNKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVGTIAAGVAKATADVIVISG 1036
Cdd:PRK11750 949 GDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISG 1028
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1037 YDGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFATAPLVVLGCVMM 1116
Cdd:PRK11750 1029 YDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYL 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1117 RACHLDTCPVGVATQNPELRKK-FMGDPDHIVNYMLFIAEEVREYMAALGFKTFDEMIGRTDVLHASERAKEhwKASQLD 1195
Cdd:PRK11750 1109 RICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETA--KQQKLD 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1196 LSTLLYQ---PEG-VRTFQSPQNHKIDQSLDITTILPAVQEAIESGKEADISIEINNTNR-VAGTITGsEISKRYGEEGL 1270
Cdd:PRK11750 1187 LSPLLETaepPAGkALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRsVGARLSG-EIARRHGNQGM 1265
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1271 PEDTIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGFNSASDDNVIIGNVAFYGATSGEAYIN 1350
Cdd:PRK11750 1266 ADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPVGSAFRSHETAIIGNTCLYGATGGKLFAA 1345
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1351 GRAGERFAVRNSGVNVVVEGIGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYVLTEDvKAFKRKCNLEMILFESLEDe 1430
Cdd:PRK11750 1346 GRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDED-GDFVDRVNHELVEILRVED- 1423
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*
gi 239938894 1431 KEIQQI--KAMLERHTAYTNSQKAEDLLDQWEDSVKKFVKVIPKN 1473
Cdd:PRK11750 1424 LEIHREhlRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPKA 1468
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
11-1493 |
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: 1456.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 11 GLYRPEFEHDACGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECKNINLPEKER 90
Cdd:COG0070 26 GLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 91 YGVGMVFFSQKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDLKDNLSFERKLYV 170
Cdd:COG0070 106 AAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 171 IRkqaenwgvtegldfYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRYLVHN 250
Cdd:COG0070 186 RR--------------SSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAAN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 251 GEINTLRGNINWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSK 330
Cdd:COG0070 252 NNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 331 EKRAFYEYHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLEPGKML 410
Cdd:COG0070 332 PAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 411 LIDLEEGRIISDEEVKTQIATEYPYQKWLEEELVQVNPDPESREE---EQFSDLLTRQKAFGYTYEDIQKYLIPVIKEGK 487
Cdd:COG0070 412 LVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEElllLEEELLQEREAELEQELLLLLLLLLAEALEEE 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 488 DPLGSMGNDAPLAVLSDRAQSLFNYFKQLFAQVTNPPIDAIREQLVTSTMTWLGAEGDLLHPSERNVRRIKLYTPVLSNE 567
Cdd:COG0070 492 EESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLAL 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 568 QFYALKTIVHPDLKSQKIDVLF------SEDLERGLKDMFTQAEKAISQGVSLLILSDKKMNERLTPIPPLLAVSALHQH 641
Cdd:COG0070 572 ALLLLLLLLLLLLGDATTLAAAleaaggGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPALLALLLLHHH 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 642 LIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRLDISYEEAVSKYGKSITEGVVKV-MSK 720
Cdd:COG0070 652 LLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKkLKI 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 721 MGISTVQSYRGAQIFEAVGISRDVIDRYFSGTASQLGGIDLQTIAEEAQRRH-REAYQDDYSKTLEPGSDFQWRNGGEHH 799
Cdd:COG0070 732 GGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHaAAADAAAAAALALGGGGGGGRGGGGEG 811
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 800 AFNPKTIHTLQWACRRNDYNLFKQYTKAADE--ERIGFLRNLFAFDGNRKPLKLEEVESAESIVKRFKTGAMSFGSLSKE 877
Cdd:COG0070 812 HHGGHYHHLLQQLAARTAAALYDDYYAYEDRadELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSE 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 878 AHEALAIAMNRLGGKSNSGEGGEDPKRFVPDENGDDRRSAIKQIASGRFGVKSHYLVNADELQIKMAQGAKPGEGGQLPG 957
Cdd:COG0070 892 AHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPG 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 958 NKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVGTIAAGVAKATADVIVISGY 1037
Cdd:COG0070 972 HKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGH 1051
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1038 DGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFATAPLVVLGCVMMR 1117
Cdd:COG0070 1052 DGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMR 1131
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1118 ACHLDTCPVGVATQNPELRKKFMGDPDHIVNYMLFIAEEVREYMAALGFKTFDEMIGRTDVLhASERAKEHWKASQLDLS 1197
Cdd:COG0070 1132 KCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLL-LVRRAVDHWKAKGLDLS 1210
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1198 TLLYQPE----GVRTFQSPQNHKIDQSLDiTTILPAVQEAIESGKEADISIEINNTNRVAGTITGSEISKRYGEEGLPED 1273
Cdd:COG0070 1211 PLLYKPDvpadVPRYCTEEQNHGLEGALD-RELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPED 1289
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1274 TIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGFNSASDDNVIIGNVAFYGATSGEAYINGRA 1353
Cdd:COG0070 1290 TITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFVAEENIIIGNTCLYGATGGELYAAGRA 1369
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1354 GERFAVRNSGVNVVVEGIGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYVLTEDvKAFKRKCNLEMILFESLEDEKEI 1433
Cdd:COG0070 1370 GERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDED-GDFEDRCNPEMVELERLDEEEDE 1448
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1434 QQIKAMLERHTAYTNSQKAEDLLDQWEDSVKKFVKVIPKNYKQMLASIEEQKAAGLSDEE 1493
Cdd:COG0070 1449 EELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDADE 1508
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
1-1501 |
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: 1404.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1 MTYN-QMPKAQGLYRPEFEHDACGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKE 79
Cdd:COG0067 1 MTENsGLPAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 80 CK--NINLPEKERYGVGMVFFSQKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSD 157
Cdd:COG0067 81 AAelGIELPEPGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 158 LkDNLSFERKLYVIRKQAENWGVTEGL---DFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNT 234
Cdd:COG0067 161 L-DGDAFERKLYVARKRIEKAIRALGLddeDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 235 FPTWERAHPNRYLVHNGEINTLRGNINWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTA 314
Cdd:COG0067 240 FPSWPLAQPFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 315 MMLIPEPWTENTHMSKEKRAFYEYHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVE 394
Cdd:COG0067 320 MMLIPEAWENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 395 QENVLYKNRLEPGKMLLIDLEEGRIISDEEVKTQIATEYPYQKWLEEELVQVN--PDPESREEEQFSDLLTRQKAFGYTY 472
Cdd:COG0067 400 PEDIVEKGRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEdlPEPEEEPAPDDDLLLRRQQAFGYTE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 473 EDIQKYLIPVIKEGKDPLGSMGNDAPLAVLSDRAQSLFNYFKQLFAQVTNPPIDAIREQLVTSTMTWLGAEGDLLHPSER 552
Cdd:COG0067 480 EEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 553 NVRRIKLYTPVLSNEQFYALKTIVHPDLKSQKIDVLF-----SEDLERGLKDMFTQAEKAISQGVSLLILSDKKMNERLT 627
Cdd:COG0067 560 ARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLdladgAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDA 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 628 PIPPLLAVSAL-HQHLIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRLDISYEEAVSKY 706
Cdd:COG0067 640 APAPLAAAAAAhHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAAAAK 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 707 GKSITE---GVVKVMSKMGISTVQSYRGAQIFEAVGISRDVIDRYFSGTASQLGGIDLQTIAEEAQRRHREAYQDD---- 779
Cdd:COG0067 720 KKKKKKkgkLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPggll 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 780 YSKTLEPGSDFQWRNGGEHHAFNPKTIHTLQWACRRNDYNLFKQYTKAADEER-IGFLRNLFAFDGNRKPLKLEEVESAE 858
Cdd:COG0067 800 LGLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRlLLLLLLLLFEEEEEEEEPEEEEEEEE 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 859 SIVKRFKTGAMSFGSLSKEAHEALAIAMNRLGGKSNSGEGGEDPKRfvpdENGDDRRSAIKQIASGRFGVKSHYLVNADE 938
Cdd:COG0067 880 SSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGAAAAE 955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 939 LQIKMAQGAKPGEGGQLPGNKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVG 1018
Cdd:COG0067 956 GGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAG 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1019 TIAAGVAKATADVIVISGYDGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGA 1098
Cdd:COG0067 1036 VAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGA 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1099 EEFGFATAPLVVLGCVMMRACHLDTCPVGVATQNPELRKKFMGDPDHIVNYMLFIAEEVREYMAALGFKTFDEMIGRTDV 1178
Cdd:COG0067 1116 GALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLGVVE 1195
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1179 LHASERAKEHWKASQLDLSTLLY--QPEGVRTFQSPQNHKIDQSLDITTILPAVQEAIESGKEADISIEINNTNRVAGTI 1256
Cdd:COG0067 1196 LLLLLLLLLLLAKLLLLLLLLLLplLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGG 1275
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1257 TGSEISKRYGEEGLPEDTIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGFNSASDDNVIIGN 1336
Cdd:COG0067 1276 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1355
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1337 VAFYGATSGEAYINGRAGERFAVRNSGVNVVVEGIGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYVLTEDVKAFKRK 1416
Cdd:COG0067 1356 GAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDE 1435
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1417 CNLEMILFESLEDEKEIQQIKAMLERHTAYTNSQKAEDLLDQWEDSVKKFVKVIPKNYKQMLASIEEQKAAGLSDEEAIM 1496
Cdd:COG0067 1436 EEEEELEELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAAAAEAAAA 1515
|
....*
gi 239938894 1497 FAFEA 1501
Cdd:COG0067 1516 AAAEA 1520
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
633-1360 |
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: 1047.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 633 LAVSALHQHLIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRLDISYEEAVSKYGKSITE 712
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 713 GVVKVMSKMGISTVQSYRGAQIFEAVGISRDVIDRYFsgtasqlggidlqtiaEEAQRRHREAYQddysKTLEPGSDFQW 792
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDIGI----------------ADVLTQHRHAIL----RNLPVGGRYRY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 793 R--------------NGGEHHAFNPKTIHTLQWACRRNDynLFKQYTKAADEE--RIGFLRNLFAFDGNRKPLKLEE-VE 855
Cdd:COG0069 141 RfesigpeirqyffeSDGEEHPFNRETRSLLYQAAKNEE--DYKPFGTLVDYQpgYEWTLRSLFPFKADRPPIPIGEpVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 856 SAESIVKRFKTGAMSFGSLSKEAHEALAIAMNRLGGKSNSGEGGEDPKRFvpdenGDDRRSAIKQIASGRFGV---KSHY 932
Cdd:COG0069 219 PPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVrdeDGEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 933 LVNADELQIKMAQGAKPGEGGQLPGNKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLV 1012
Cdd:COG0069 294 LPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVGVKLV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1013 SKAGVGTIAA--GVAK--ATADVIVISGYDGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGR 1088
Cdd:COG0069 374 SGAGVGTIAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1089 DVVMAALLGAEEFGFATAPLVVLGCVMMRACHLDTCPVGVATQNPELRKKF--MGDPDHIVNYMLFIAEEVREYMAALGF 1166
Cdd:COG0069 454 DVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFvvEGKPERVVNYFRFTAEEVREILAALGV 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1167 KTFDEMIGRTDVLHASERakEHWKASQLDLSTLLYQPEGV----RTFQSPQNHKIDQSLDITTILPAVQEAIESGKEADI 1242
Cdd:COG0069 534 RSPDELIGRHDLLRVRDG--EHWKAKGLDLSPLLYKPELPegvpRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLI 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1243 SIEINNTNRVAGTITGSEIsKRYGEEGLPEDTIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSE 1322
Cdd:COG0069 612 TNIRNNNRRVGGMLSGEIA-KRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPP 690
|
730 740 750
....*....|....*....|....*....|....*...
gi 239938894 1323 GFNSASDDNVIIGNVAFYGATSGEAYINGRAGERFAVR 1360
Cdd:COG0069 691 GASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
22-438 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 767.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 22 CGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECK--NINLPEKERYGVGMVFFS 99
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKelGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 100 QKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDlKDNLSFERKLYVIRKQAENWG 179
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAG-KSEDDFERKLYVARKRIEKEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 180 VTEGL--DFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRYLVHNGEINTLR 257
Cdd:pfam00310 160 GVEGGdkDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 258 GNINWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSKEKRAFYE 337
Cdd:pfam00310 240 GNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 338 YHSSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLEPGKMLLIDLEEG 417
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 239938894 418 RIISDEEVKTQIATEYPYQKW 438
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
22-433 |
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: 735.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 22 CGIGLYAHLKGKQTHDIVKQGLKMLCQLDHRGGQGSDPDTGDGAGLLVQIPDAFFRKECK--NINLPEKERYGVGMVFFS 99
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAeaGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 100 QKEDERKKIEKQINALIEQEGQVVLGWRTVPVNVGKIGTVAQKSCPFVRQVFIGASSDLkDNLSFERKLYVIRKQAENWG 179
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGD-DGEAFERKLYLLRKRIEKAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 180 VTEGLDFYFASLSSQTIVYKGLLTPEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHPNRYLVHNGEINTLRGN 259
Cdd:cd00713 160 RAADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 260 INWMRAREQQFVSESFGEDLNKILPILNADGSDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSKEKRAFYEYH 339
Cdd:cd00713 240 RNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 340 SSLMEPWDGPTAISFTDGKQIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIEVEQENVLYKNRLEPGKMLLIDLEEGRI 419
Cdd:cd00713 320 SSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRI 399
|
410
....*....|....
gi 239938894 420 ISDEEVKTQIATEY 433
Cdd:cd00713 400 LDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
799-1167 |
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: 632.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 799 HAFNPKTIHTLQWACRRNDYNLFKQYTKAADE-ERIGFLRNLFAFDGNRKPLKLEEVESAESIVKRFKTGAMSFGSLSKE 877
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNErVPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 878 AHEALAIAMNRLGGKSNSGEGGEDPKRFVPDENGddrrsAIKQIASGRFGVKSHYLVNADELQIKMAQGAKPGEGGQLPG 957
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-----AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 958 NKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVGTIAAGVAKATADVIVISGY 1037
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1038 DGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFATAPLVVLGCVMMR 1117
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 239938894 1118 ACHLDTCPVGVATQNPELRK--KFMGDPDHIVNYMLFIAEEVREYMAALGFK 1167
Cdd:pfam01645 316 VCHTNTCPVGVATQDPELRKrlDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
802-1180 |
1.30e-176 |
|
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: 532.89 E-value: 1.30e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 802 NPKTIHTLQWACR--RNDYNLFKQYT--KAADEERIGFLRNLFAFDGNRKPLKLEE-------------VESAESIVKRF 864
Cdd:cd02808 1 YLLEIERLEEIQYfvFNRAERYGVYNraGNSRGRPFGTLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 865 KTGAMSFGSLSKEAHEALAIAMNRLGGKSNSGEGGEDPKRFvpdengDDRRSAIKQIASGRFGVKSHYLVNADELQIKMA 944
Cdd:cd02808 81 NISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEER------EGGGDIIKQVASGRFGVRPEYLNKADAIEIKIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 945 QGAKPGEGGQLPGNKVYPWVADVRGSTPGVGLISPPPHHDIYSIEDLAQLIHDLKNANRDARISVKLVSKAGVGTIAAGV 1024
Cdd:cd02808 155 QGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1025 AKATADVIVISGYDGGTGASPKTSIKHTGLPWELGLAEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFA 1104
Cdd:cd02808 235 AAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIG 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239938894 1105 TAPLVVLGCVMMRACHLDTCPVGVATQNPEL--RKKFMGDPDHIVNYMLFIAEEVREYMAALGFKTfDEMIGRTDVLH 1180
Cdd:cd02808 315 TAALIALGCIQARKCHTNTCPVGVATQDPELrrRLDVEGKAERVANYLKSLAEELRELAAALGKRS-LELLGRSDLLA 391
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
463-741 |
2.37e-162 |
|
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: 490.74 E-value: 2.37e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 463 TRQKAFGYTYEDIQKYLIPVIKEGKDPLGSMGNDAPLAVLSDRAQSLFNYFKQLFAQVTNPPIDAIREQLVTSTMTWLGA 542
Cdd:pfam04898 1 RRQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 543 EGDLLHPSERNVRRIKLYTPVLSNEQFYALKTIVHPDLKSQKIDVLFsEDLERGLKDMFTQAEKAISQGVSLLILSDKKM 622
Cdd:pfam04898 81 EGNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITF-DGLEAALERLCEEAEEAVRDGANILILSDRGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 623 NERLTPIPPLLAVSALHQHLIRKGLRTKVSIIVESGEAREVHHFAALIGYGADAINPYLAYATYKQEIDEGRL---DISY 699
Cdd:pfam04898 160 DADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGKGkltDEDL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 239938894 700 EEAVSKYGKSITEGVVKVMSKMGISTVQSYRGAQIFEAVGIS 741
Cdd:pfam04898 240 EEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1221-1472 |
1.37e-153 |
|
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: 466.23 E-value: 1.37e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1221 LDITTILPAVQEAIESGKEADISIEINNTNRVAGTITGSEISKRYGEEGLPEDTIKLHFTGSAGQSFGAFVPKGMTLYLD 1300
Cdd:cd00982 1 LDDKLIADAEPALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1301 GDSNDYVGKGLSGGKIIVKSSEGFNSASDDNVIIGNVAFYGATSGEAYINGRAGERFAVRNSGVNVVVEGIGDHGCEYMT 1380
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1381 GGSVVVLGDVGKNFAAGMSGGIAYVLTEDVKaFKRKCNLEMILFESLEDEKEIQQIKAMLERHTAYTNSQKAEDLLDQWE 1460
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGD-FEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWE 239
|
250
....*....|..
gi 239938894 1461 DSVKKFVKVIPK 1472
Cdd:cd00982 240 AYLKKFVKVIPR 251
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1244-1434 |
7.71e-117 |
|
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: 364.43 E-value: 7.71e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1244 IEINNTNRVAGTITGSEISKRYGEEGLPEDTIKLHFTGSAGQSFGAFVPKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEG 1323
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1324 FNSASDDNVIIGNVAFYGATSGEAYINGRAGERFAVRNSGVNVVVEGIGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIA 1403
Cdd:pfam01493 81 STFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIA 160
|
170 180 190
....*....|....*....|....*....|.
gi 239938894 1404 YVLTEDvKAFKRKCNLEMILFESLEDEKEIQ 1434
Cdd:pfam01493 161 YVLDED-GDFPEKLNKEMVELERVTDEDEEA 190
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1251-1406 |
1.07e-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: 227.45 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1251 RVAGTITGSEISKRygeEGLPEDTIKLHFTGSAGQSFGAFVpKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGfnsasDD 1330
Cdd:cd00504 1 RAVGTRGSRYIGKR---PGLPEDTVEIIINGSAGQSFGAFM-AGGTITVEGNANDYVGKGMSGGEIVIHPPAG-----DE 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239938894 1331 NVIIGNVAFYGATSGEAYINGRAGERFAVRNSGVNVVVEGIGD-HGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYVL 1406
Cdd:cd00504 72 NGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVR 148
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
204-410 |
1.27e-35 |
|
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: 135.27 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 204 PEQVDAFYSDLQDEAFVSAFALVHSRFSTNTFPTWERAHP------NRYLVHNGEINTLRGNINWMRAREQQFVSESfge 277
Cdd:cd00352 51 AGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPfrsedgRIALVHNGEIYNYRELREELEARGYRFEGES--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 278 dlnkilpilnadgsDSSILDNAFEFFVMAGRkPAHTAMMLIPEpwtenthmskekrafyeyhsslmepWDGPTAISFTDG 357
Cdd:cd00352 128 --------------DSEVILHLLERLGREGG-LFEAVEDALKR-------------------------LDGPFAFALWDG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 239938894 358 K--QIGAILDRNGLRPARYYVTKDDYIIFSSEVGVIevEQENVLYKNRLEPGKML 410
Cdd:cd00352 168 KpdRLFAARDRFGIRPLYYGITKDGGLVFASEPKAL--LALPFKGVRRLPPGELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
196-388 |
4.00e-12 |
|
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: 68.06 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 196 IVYKGLLTPEQVDAFYsDLqdEAFVSAFALVHSRFSTNTFPTWERAHP----NRYLVHNGEINTLRGNINWMRAREQQFV 271
Cdd:cd01907 55 EVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPfsigDIAVVHNGEISNYGSNREYLERFGYKFE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 272 SESfgedlnkilpilnadgsDSSILDNAFEFFVMAGRKPAHTAMMLIPEPWTENTHMSKEKRafyEYHSSLMepwDGPTA 351
Cdd:cd01907 132 TET-----------------DTEVIAYYLDLLLRKGGLPLEYYKHIIRMPEEERELLLALRL---TYRLADL---DGPFT 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 239938894 352 ISFTDGKQIGAILDRNGLRPArYYVTKDDYIIFSSEV 388
Cdd:cd01907 189 IIVGTPDGFIVIRDRIKLRPA-VVAETDDYVAIASEE 224
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1236-1406 |
9.72e-11 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 64.06 E-value: 9.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1236 SGKEADISIEINN-TNRVagtitgseisKRYGEeGLPEDTIKLHftGSAGQSFGAFVpKGMTLYLDGDSNDYVGKGLSGG 1314
Cdd:COG2218 55 EGDDGDTKIVIEGdLSRV----------KRIGA-GMTAGEIIVE--GDVGMYLGAGM-KGGKITVNGNAGSFAGAEMKGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1315 KIIVKssegfnsasddnviiGNV------AFYGATSG----EAYINGRAGERFAVRNSGVNVVVEG-IGDHGCEYMTGGS 1383
Cdd:COG2218 121 EIEIN---------------GNAgdflgaAYRGDWRGmsggTIIVKGNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGT 185
|
170 180
....*....|....*....|...
gi 239938894 1384 VVVLGDVGKNFAAGMSGGIAYVL 1406
Cdd:COG2218 186 IIVKGNAGRRPGYGMKRGTIVVA 208
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1281-1402 |
7.57e-09 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 57.36 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1281 GSAGQSFGAFVpKGMTLYLDGDSNDYVGKGLSGGKIIVKSSEGFNSASddnviignvAFYGA----TSGEAYINGRAGER 1356
Cdd:cd00980 46 GDVGMYVGAGM-KGGKLVVEGNAGSWAGCEMKGGEITIKGNAGDYVGS---------AYRGDwrgmSGGTITIEGNAGDR 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 239938894 1357 FAVRNSGVNVVVEG-IGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGI 1402
Cdd:cd00980 116 LGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGT 162
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1296-1405 |
8.24e-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: 54.28 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1296 TLYLDGDSN--DYVGKGLSGGKIIVKSSEGFNS----ASDDNVIIGNVAFY---GATSGEAYINGRAGERF--AVRN--- 1361
Cdd:cd00980 20 KLVIEGDVPrlKRIGARMTAGEIVVEGDVGMYVgagmKGGKLVVEGNAGSWagcEMKGGEITIKGNAGDYVgsAYRGdwr 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 239938894 1362 --SGVNVVVEG-IGDHGCEYMTGGSVVVLGDVGKNFAAGMSGGIAYV 1405
Cdd:cd00980 100 gmSGGTITIEGnAGDRLGERMRRGEILIKGDAGIFAGIRMNGGTIIV 146
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1229-1472 |
1.31e-07 |
|
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.
Pssm-ID: 238481 [Multi-domain] Cd Length: 232 Bit Score: 54.23 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1229 AVQEAIESGKEAdisIEINNtnrVAGtitgseisKRYGEEGLPED-TIKLHftGSAGQSFGAFVPKG------------- 1294
Cdd:cd00981 16 KIREAVEKGADE---IVLDN---VLG--------QRYIGDGLPGNvRINIY--GVPGNDLGAFMSGPtiivygnaqddvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1295 --M---TLYLDGDSNDYVGKGLSGGKIIVKssegfnsasddnviiGNVAFYGATSGEAYingragerfaVRNSGVnVVVE 1369
Cdd:cd00981 80 ntMndgKIVIHGSAGDVLGYAMRGGKIFIR---------------GNAGYRVGIHMKEY----------KDKVPV-LVIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1370 GI-GDHGCEYMTGGSVVVLG------DVGKNFAAGMSGGIAYVLTedvKAFKRKCNLEMILFE-SLEDEKEIQQikamle 1441
Cdd:cd00981 134 GTaGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIYIRG---KVERSKLGKEVPKFElTEEDLEFIEK------ 204
|
250 260 270
....*....|....*....|....*....|.
gi 239938894 1442 rhtaYTNSQKAEDLLDQWEDSVKKFVKVIPK 1472
Cdd:cd00981 205 ----YIEEFCKEFGYDKAEILDEEFTKLKPK 231
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1216-1433 |
4.34e-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: 53.11 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1216 KIDQSLDITTILPAVQEAIESGKEADISIEINNTNRVAGTITgsEISKrygeEGLPEDTiKLHFTGSAgqSFGAFVPKGM 1295
Cdd:TIGR03122 8 EPSVPLEADPILPDNLAGKSAEEIEALELWYGNKTVPLGDLF--DVEG----DGKPDET-RLVIDGDM--SRVKRIGENM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1296 T---LYLDGDSNDYVGKGLSGGKIIVK----SSEGFNSASDDNVIIGNVAFY----------GATSGEAYINGRAGERFA 1358
Cdd:TIGR03122 79 SageIVVEGDVGMHVGAEMKGGKIVVNgnadSWAGCEMKGGEIIIKGNAGDYvgsayrgewrGMSGGKIIVEGNAGDYLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 1359 VRNSGVNVVVEG-----IGDHgceyMTGGSVVVLGDVGKNFAAGMSGGIAYV---LTEDVKAFKrKCNLEMILFESLEDE 1430
Cdd:TIGR03122 159 ERMRGGEILIKGnagifAGIH----MNGGTIIIDGDIGRRPGGEMKRGTIVVggkVDELLPTFK-FEGLHELPFLLKSAF 233
|
...
gi 239938894 1431 KEI 1433
Cdd:TIGR03122 234 TQA 236
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
981-1105 |
4.78e-06 |
|
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: 49.12 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239938894 981 PHHDIYSIEDLAQLIHDLKNANRDARISVKLVskAGVGTIAAGVAKATADVIVISGYDGGTGASPKTsikhtglpwelgl 1060
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKLS--PTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAV------------- 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 239938894 1061 AEAHQTLMLNGLRDRVVLETDGKLMTGRDVVMAALLGAEEFGFAT 1105
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
629-678 |
1.25e-03 |
|
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: 42.91 E-value: 1.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 239938894 629 IPPLLAVSALHQHLIRKGLRTKVSIIVeSGEAREVHHFAALIGYGADAIN 678
Cdd:cd02808 264 LPTELGLARAHQALVKNGLRDRVSLIA-SGGLRTGADVAKALALGADAVG 312
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1352-1401 |
4.98e-03 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 40.56 E-value: 4.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 239938894 1352 RAGERFAV--RNSGVNVVVEG-------IGdhgcEYMTGGSVVVLGDVGKNFAAGMSGG 1401
Cdd:COG2218 47 PLGDLFDVegDDGDTKIVIEGdlsrvkrIG----AGMTAGEIIVEGDVGMYLGAGMKGG 101
|
|
| |
