|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
9-1455 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1486.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 9 GLYDYREEHDACGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTDFDIPGEGE 88
Cdd:PRK11750 4 GLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLAKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 89 YAVG-LFFSKERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDI---RDIEDVEKRLFLA 164
Cdd:PRK11750 84 YAVGmVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNApagWRERDFERRLFIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 165 RKQLEFYSTQcDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNG 244
Cdd:PRK11750 164 RRRIEKRLAD-DKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLAHNG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 245 EINTIKGNVNWMRARQHKLIETLFgEDQHKVFQIVDEDGSDSAIVDNALE-FLSLAMEPEKAAMLLIPEPWLYNEANDAN 323
Cdd:PRK11750 243 EINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLElLLAGGMDLFRAMRLLVPPAWQNNPDMDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 324 VRAFYEFYSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLL 403
Cdd:PRK11750 322 LRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 404 VDFKQNKVIEN----NDLKGAiageLPYKAWIDNH----KVDFDFENIQYQDSQWKDETLFKLQRQFAYTKEEIHKYIQE 475
Cdd:PRK11750 402 IDTRTGRILHSaeidNDLKSR----HPYKEWLEKNvrrlVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 476 LVEGKKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGGEGNLLAPDETVLDRIQLKR 555
Cdd:PRK11750 478 LAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 556 PVLNES---HLAAINQEHFKLTYLSTVY---EGDLEDALEALGREAVDAVKQGAQILVLDDSGLVDSNgFAMPMLLAISH 629
Cdd:PRK11750 558 PVLSYSdfkQLTTLDEEHYRADTLDLNYdpeETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGR-LPIPAAMAVGA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 630 VHQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQGTVVDNVKTYTDVLSEGVIKV 709
Cdd:PRK11750 637 VQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYKI 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 710 MAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFTGTQSKLSGISIDQIDAENK---ARQQSDDNYLASGSTFQWRQQGQHH 786
Cdd:PRK11750 717 MSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKnlsKRAWLARKPIDQGGLLKYVHGGEYH 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 787 AFNPESIFLLQHACKENDYAQFKAYSEAVNKNRTDHIRHLLEFK-ACTPIDIDQVEPVSDIVKRFNTGAMSYGSISAEAH 865
Cdd:PRK11750 797 AYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKpADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAH 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 866 ETLAQAMNQLGGKSNSGEGGEDAKRYevqvdGSNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPGEGGQLPGTK 945
Cdd:PRK11750 877 EALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDK 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 946 VYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFADKIVISGYDG 1025
Cdd:PRK11750 952 VNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDG 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1026 GTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVVLGCIMMRVC 1105
Cdd:PRK11750 1032 GTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRIC 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1106 HKDTCPVGVATQNKDLRA-LYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLVGRTDLLQRSSTLKAnsKAASIDVEK 1184
Cdd:PRK11750 1112 HLNNCATGVATQDEKLRKnHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETA--KQQKLDLSP 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1185 LL----CPFDGPNTKEIQQNHNLEHGFDLTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYGEAGLPENT 1260
Cdd:PRK11750 1190 LLetaePPAGKALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAP 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1261 INVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVKAP----FEERQNEIIaGNVSFYGATGGKAFINGSA 1336
Cdd:PRK11750 1270 IKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPvgsaFRSHETAII-GNTCLYGATGGKLFAAGRA 1348
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1337 GERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYVIPSDvEAFVE--NNQL-DTLSFTKIK-H 1412
Cdd:PRK11750 1349 GERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDED-GDFVDrvNHELvEILRVEDLEiH 1427
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|...
gi 446473515 1413 QEekaFIKQMLEEHVSHTNSTRAIHVLKHFDRIEDVVVKVIPK 1455
Cdd:PRK11750 1428 RE---HLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPK 1467
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
1-1476 |
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: 1173.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1 MHNEKLIKGLYDYREEHDACGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTD 80
Cdd:COG0070 18 GGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 81 FDIPGEGEYAVGLFFSKERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDIRDIEDVEKR 160
Cdd:COG0070 98 AAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 161 LFLARKQLEFYstqcdlelYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRML 240
Cdd:COG0070 178 RRRRREFRRRS--------SSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 241 MHNGEINTIKGNVNWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLAMEPEKAAMLLIPEPWLYNEAN 320
Cdd:COG0070 250 ANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 321 DANVRAFYEFYSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGK 400
Cdd:COG0070 330 APPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 401 LLLVDFKQNKVIENNDLKGAIAGELPYKAWI-DNHKVDFDFENIQYQDSQWKDETLFKLQRQFAYTKEEIHKYIQELVEG 479
Cdd:COG0070 410 GLLVGGGGGGLLDDEEEDAEELEELLPELQDlLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 480 KKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGGEGNLLAPDETVLDRIQLKRPVLN 559
Cdd:COG0070 490 EEEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 560 ESHLAAIN---------QEHFKLTYLSTVYEGDLEDALEALGREAVDAVKQGAQILVLDDSGLVDSNGfAMPMLLAISHV 630
Cdd:COG0070 570 ALALLLLLlllllllgdATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLA-LLPALLALLLL 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 631 HQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQ-GTVVDNVKTYTDVLSEGVIKV 709
Cdd:COG0070 649 HHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALlGLLEAAAYKAKAALKAGVKKK 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 710 MAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFTGTQSKLSGISID---------QIDAENKARQQSDDNYLASGSTFQWR 780
Cdd:COG0070 729 LKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEilgeggaarHAAAADAAAAAALALGGGGGGGRGGG 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 781 QQGQHHAFNPESIFLLQHACKENDYAQFKAYSEAVNKNRTDHIRHLLEFKACTPIDIDQVEPVSDIVKRFNTGAMSYGSI 860
Cdd:COG0070 809 GEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSS 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 861 SAEAHETLAQAMNQLGGKSNSGEGGEDAKRYEVQVDGSNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPGEGGQ 940
Cdd:COG0070 889 SSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQ 968
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 941 LPGTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFADKIVI 1020
Cdd:COG0070 969 LPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILI 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1021 SGYDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVVLGCI 1100
Cdd:COG0070 1049 SGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCI 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1101 MMRVCHKDTCPVGVATQNKDLRALYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLVGRTDLLQRSStLKANSKAASI 1180
Cdd:COG0070 1129 MMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRR-AVDHWKAKGL 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1181 DVEKLL----CPFDGPNTKEIQQNHNLEHGFDlTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYGEAGL 1256
Cdd:COG0070 1208 DLSPLLykpdVPADVPRYCTEEQNHGLEGALD-RELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGL 1286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1257 PENTINVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVK----APFEERQNeIIAGNVSFYGATGGKAFI 1332
Cdd:COG0070 1287 PEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRppagSTFVAEEN-IIIGNTCLYGATGGELYA 1365
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1333 NGSAGERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYVIPSDvEAFVENNQLDTLSFTKIKH 1412
Cdd:COG0070 1366 AGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDED-GDFEDRCNPEMVELERLDE 1444
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446473515 1413 QEEKAFIKQMLEEHVSHTNSTRAIHVLKHFDRIEDVVVKVIPKDYQLMMQKIHLHKSLHDNEDE 1476
Cdd:COG0070 1445 EEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDADE 1508
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
20-424 |
0e+00 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 623.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 20 CGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTD--FDIPGEGEYAVG-LFFS 96
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEagIELPEAGEYAVGmLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 97 KERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFI---DIRDIEDVEKRLFLARKQLEFYST 173
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVgapSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 174 QCDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNGEINTIKGNV 253
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 254 NWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLA-MEPEKAAMLLIPEPWLYNEANDANVRAFYEFYS 332
Cdd:cd00713 241 NWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSgRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 333 YLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLLVDFKQNKVI 412
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|..
gi 446473515 413 ENNDLKGAIAGE 424
Cdd:cd00713 401 DDEEIKDQLAKR 412
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
20-430 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 587.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 20 CGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTD--FDIPGEGEYAVG-LFFS 96
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKElgIELPEAGQYAVGmVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 97 KERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDIR---DIEDVEKRLFLARKQLE--FY 171
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPagkSEDDFERKLYVARKRIEkeIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 172 STQCDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNGEINTIKG 251
Cdd:pfam00310 161 VEGGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 252 NVNWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLA-MEPEKAAMLLIPEPWLYNEANDANVRAFYEF 330
Cdd:pfam00310 241 NRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGgRSLPEALMMLIPEAWQNNPSMDPEKRAFYEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 331 YSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLLVDFKQNK 410
Cdd:pfam00310 321 HSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEGR 400
|
410 420
....*....|....*....|
gi 446473515 411 VIENNDLKGAIAGELPYKAW 430
Cdd:pfam00310 401 IIDDEEIKQQIASRHPYGEW 420
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1287-1384 |
2.16e-06 |
|
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.
Pssm-ID: 274439 [Multi-domain] Cd Length: 257 Bit Score: 50.80 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1287 GDANDYVGKGLSGGTVIVK------APFEERQNEI-IAGNVSFY----------GATGGKAFINGSAGERFCIRNSGVDV 1349
Cdd:TIGR03122 87 GDVGMHVGAEMKGGKIVVNgnadswAGCEMKGGEIiIKGNAGDYvgsayrgewrGMSGGKIIVEGNAGDYLGERMRGGEI 166
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446473515 1350 VVEG-----IGDHgleyMTGGHVINLGDVGKNFGQGMSGG 1384
Cdd:TIGR03122 167 LIKGnagifAGIH----MNGGTIIIDGDIGRRPGGEMKRG 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
9-1455 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1486.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 9 GLYDYREEHDACGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTDFDIPGEGE 88
Cdd:PRK11750 4 GLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLAKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 89 YAVG-LFFSKERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDI---RDIEDVEKRLFLA 164
Cdd:PRK11750 84 YAVGmVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNApagWRERDFERRLFIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 165 RKQLEFYSTQcDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNG 244
Cdd:PRK11750 164 RRRIEKRLAD-DKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYLAHNG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 245 EINTIKGNVNWMRARQHKLIETLFgEDQHKVFQIVDEDGSDSAIVDNALE-FLSLAMEPEKAAMLLIPEPWLYNEANDAN 323
Cdd:PRK11750 243 EINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLElLLAGGMDLFRAMRLLVPPAWQNNPDMDPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 324 VRAFYEFYSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLL 403
Cdd:PRK11750 322 LRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGELLV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 404 VDFKQNKVIEN----NDLKGAiageLPYKAWIDNH----KVDFDFENIQYQDSQWKDETLFKLQRQFAYTKEEIHKYIQE 475
Cdd:PRK11750 402 IDTRTGRILHSaeidNDLKSR----HPYKEWLEKNvrrlVPFEELPDEQVGSRELDDDTLKSYQKQFQYSFEELDQVIRV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 476 LVEGKKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGGEGNLLAPDETVLDRIQLKR 555
Cdd:PRK11750 478 LAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCETEGHAHRVIFKS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 556 PVLNES---HLAAINQEHFKLTYLSTVY---EGDLEDALEALGREAVDAVKQGAQILVLDDSGLVDSNgFAMPMLLAISH 629
Cdd:PRK11750 558 PVLSYSdfkQLTTLDEEHYRADTLDLNYdpeETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGR-LPIPAAMAVGA 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 630 VHQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQGTVVDNVKTYTDVLSEGVIKV 709
Cdd:PRK11750 637 VQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGLYKI 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 710 MAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFTGTQSKLSGISIDQIDAENK---ARQQSDDNYLASGSTFQWRQQGQHH 786
Cdd:PRK11750 717 MSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKnlsKRAWLARKPIDQGGLLKYVHGGEYH 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 787 AFNPESIFLLQHACKENDYAQFKAYSEAVNKNRTDHIRHLLEFK-ACTPIDIDQVEPVSDIVKRFNTGAMSYGSISAEAH 865
Cdd:PRK11750 797 AYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPVATLRDLLALKpADNPIPLDEVEPAEELFKRFDSAAMSIGALSPEAH 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 866 ETLAQAMNQLGGKSNSGEGGEDAKRYevqvdGSNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPGEGGQLPGTK 945
Cdd:PRK11750 877 EALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDK 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 946 VYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFADKIVISGYDG 1025
Cdd:PRK11750 952 VNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDG 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1026 GTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVVLGCIMMRVC 1105
Cdd:PRK11750 1032 GTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRIC 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1106 HKDTCPVGVATQNKDLRA-LYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLVGRTDLLQRSSTLKAnsKAASIDVEK 1184
Cdd:PRK11750 1112 HLNNCATGVATQDEKLRKnHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEELEGETA--KQQKLDLSP 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1185 LL----CPFDGPNTKEIQQNHNLEHGFDLTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYGEAGLPENT 1260
Cdd:PRK11750 1190 LLetaePPAGKALYCTEERNPPFDKGLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGNQGMADAP 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1261 INVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVKAP----FEERQNEIIaGNVSFYGATGGKAFINGSA 1336
Cdd:PRK11750 1270 IKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPvgsaFRSHETAII-GNTCLYGATGGKLFAAGRA 1348
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1337 GERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYVIPSDvEAFVE--NNQL-DTLSFTKIK-H 1412
Cdd:PRK11750 1349 GERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDED-GDFVDrvNHELvEILRVEDLEiH 1427
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|...
gi 446473515 1413 QEekaFIKQMLEEHVSHTNSTRAIHVLKHFDRIEDVVVKVIPK 1455
Cdd:PRK11750 1428 RE---HLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKPK 1467
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
1-1476 |
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: 1173.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1 MHNEKLIKGLYDYREEHDACGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTD 80
Cdd:COG0070 18 GGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 81 FDIPGEGEYAVGLFFSKERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDIRDIEDVEKR 160
Cdd:COG0070 98 AAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 161 LFLARKQLEFYstqcdlelYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRML 240
Cdd:COG0070 178 RRRRREFRRRS--------SSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 241 MHNGEINTIKGNVNWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLAMEPEKAAMLLIPEPWLYNEAN 320
Cdd:COG0070 250 ANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 321 DANVRAFYEFYSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGK 400
Cdd:COG0070 330 APPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 401 LLLVDFKQNKVIENNDLKGAIAGELPYKAWI-DNHKVDFDFENIQYQDSQWKDETLFKLQRQFAYTKEEIHKYIQELVEG 479
Cdd:COG0070 410 GLLVGGGGGGLLDDEEEDAEELEELLPELQDlLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 480 KKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGGEGNLLAPDETVLDRIQLKRPVLN 559
Cdd:COG0070 490 EEEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 560 ESHLAAIN---------QEHFKLTYLSTVYEGDLEDALEALGREAVDAVKQGAQILVLDDSGLVDSNGfAMPMLLAISHV 630
Cdd:COG0070 570 ALALLLLLlllllllgdATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLA-LLPALLALLLL 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 631 HQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQ-GTVVDNVKTYTDVLSEGVIKV 709
Cdd:COG0070 649 HHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALlGLLEAAAYKAKAALKAGVKKK 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 710 MAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFTGTQSKLSGISID---------QIDAENKARQQSDDNYLASGSTFQWR 780
Cdd:COG0070 729 LKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEilgeggaarHAAAADAAAAAALALGGGGGGGRGGG 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 781 QQGQHHAFNPESIFLLQHACKENDYAQFKAYSEAVNKNRTDHIRHLLEFKACTPIDIDQVEPVSDIVKRFNTGAMSYGSI 860
Cdd:COG0070 809 GEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSS 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 861 SAEAHETLAQAMNQLGGKSNSGEGGEDAKRYEVQVDGSNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPGEGGQ 940
Cdd:COG0070 889 SSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQ 968
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 941 LPGTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFADKIVI 1020
Cdd:COG0070 969 LPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILI 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1021 SGYDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVVLGCI 1100
Cdd:COG0070 1049 SGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCI 1128
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1101 MMRVCHKDTCPVGVATQNKDLRALYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLVGRTDLLQRSStLKANSKAASI 1180
Cdd:COG0070 1129 MMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRR-AVDHWKAKGL 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1181 DVEKLL----CPFDGPNTKEIQQNHNLEHGFDlTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYGEAGL 1256
Cdd:COG0070 1208 DLSPLLykpdVPADVPRYCTEEQNHGLEGALD-RELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGL 1286
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1257 PENTINVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVK----APFEERQNeIIAGNVSFYGATGGKAFI 1332
Cdd:COG0070 1287 PEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRppagSTFVAEEN-IIIGNTCLYGATGGELYA 1365
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1333 NGSAGERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYVIPSDvEAFVENNQLDTLSFTKIKH 1412
Cdd:COG0070 1366 AGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDED-GDFEDRCNPEMVELERLDE 1444
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446473515 1413 QEEKAFIKQMLEEHVSHTNSTRAIHVLKHFDRIEDVVVKVIPKDYQLMMQKIHLHKSLHDNEDE 1476
Cdd:COG0070 1445 EEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDADE 1508
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
9-1482 |
0e+00 |
|
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 439837 [Multi-domain] Cd Length: 1520 Bit Score: 1106.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 9 GLYDYREEHDACGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHV--TDFDIPGE 86
Cdd:COG0067 12 GLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAaeLGIELPEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 87 GEYAVG-LFFSKERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFI---DIRDIEDVEKRLF 162
Cdd:COG0067 92 GEYAVGmVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVarpDGLDGDAFERKLY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 163 LARKQLE---FYSTQCDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRM 239
Cdd:COG0067 172 VARKRIEkaiRALGLDDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQPFRY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 240 LMHNGEINTIKGNVNWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLA-MEPEKAAMLLIPEPWLYNE 318
Cdd:COG0067 252 LAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGgRSLPHAMMMLIPEAWENNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 319 ANDANVRAFYEFYSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNP 398
Cdd:COG0067 332 DMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGRLQP 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 399 GKLLLVDFKQNKVIENNDLKGAIAGELPYKAWIDNHKVDFDFENIQYQDSQWKDETLFKLQRQFAYTKEEIHKYIQELVE 478
Cdd:COG0067 412 GKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDLLLRRQQAFGYTEEEELLLLLPMAA 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 479 GKKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGGEGNLLAPDETVLDRIQLKRPVL 558
Cdd:COG0067 492 GGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEARRRLLLLPPPL 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 559 NESHLAAINQEHFKLTYLSTV--------YEGDLEDALEALGREAVDAVKQGAQILVLDDSGLVDSNGFAMPMLLAISHV 630
Cdd:COG0067 572 LNELLLLLLRLLDGDFKSTTTitlldladGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDDSDAAPAPLAAAAAAH 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 631 HQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQGTVVD---NVKTYTDVLSEGVI 707
Cdd:COG0067 652 HHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAaaaAKKKKKKKKGKLKK 731
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 708 KVMAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFTGTQSKLSGISIDQIDAENKARQQSDDNYLASGST---------FQ 778
Cdd:COG0067 732 KKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLLglggggggeYG 811
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 779 WRQQGQHHAFNPESIFLLQHACKENDYAQFKAYSEAVNKNR--TDHIRHLLEFKACTPIDIDQVEPVSDIVKRFNTGAMS 856
Cdd:COG0067 812 RRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRllLLLLLLLFEEEEEEEEPEEEEEEEESSAIAAASSAAA 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 857 YGSISAEAHETLAQAMNQLGGKSNSGEGGEDAKRyevqVDGSNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPG 936
Cdd:COG0067 892 SAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGAAAAEGGGGGGGGGGGG 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 937 EGGQLPGTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFAD 1016
Cdd:COG0067 968 GGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAAAAGVAAAAAAAAAAA 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1017 KIVISGYDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVV 1096
Cdd:COG0067 1048 AVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAALGAGALGGGAAALVV 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1097 LGCIMMRVCHKDTCPVGVATQNKDLRALYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLVGRT----DLLQRSSTLK 1172
Cdd:COG0067 1128 VGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLGVvellLLLLLLLLLA 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1173 ANSKAASIDVEKLLCPFDGPNTKEIQQNHNLEHGFDLTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYG 1252
Cdd:COG0067 1208 KLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRARRRGGGGGGGGGGGGGGG 1287
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1253 EAGLPENTINVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIV-KAPFEERQNEIIAGNVSFYGATGGKAF 1331
Cdd:COG0067 1288 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGgGGGGGGGGGGGGGGGGAGGGGGGGGGA 1367
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1332 INGSAGERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYVIPSDVEAFVENNQLDTLSFTKIK 1411
Cdd:COG0067 1368 GGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLDVVLDEEEEEELEELLLL 1447
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446473515 1412 HQEEKAFIKQMLEEHVSHTNSTRAIHVLKHFDRIEDVVVKVIPKDYQLMMQKIHLHKSLHDNEDEAMLAAF 1482
Cdd:COG0067 1448 LEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAAAAEAAAAAAA 1518
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
625-1343 |
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: 868.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 625 LAISHVHQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQGTVVDNVKTYTDVLSE 704
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 705 GVIKVMAKMGISTVQSYQGAQIFEAIGLSHDVIDRYFtgtqsklsgisidqIDAENKARQQSDDNYlASGSTFQWR---- 780
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELVDIGI--------------ADVLTQHRHAILRNL-PVGGRYRYRfesi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 781 ----QQ------GQHHAFNPESIFLLQHACKENDyaQFKAYSEAVNkNRTDH---IRHLLEFKACT-PIDIDQ-VEPVSD 845
Cdd:COG0069 146 gpeiRQyffesdGEEHPFNRETRSLLYQAAKNEE--DYKPFGTLVD-YQPGYewtLRSLFPFKADRpPIPIGEpVEPPYS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 846 IVKRFNTGAMSYGSISAEAHETLAQAMNQLGGKSNSGEGGEDAKRYevqvdGSNKVSAIKQVASGRFGVT---SDYLQHA 922
Cdd:COG0069 223 IVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRdedGEYLPNA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 923 KEIQIKVAQGAKPGEGGQLPGTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTG 1002
Cdd:COG0069 298 KMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVGVKLVSGAG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1003 VGTIA--SGVAK--AFADKIVISGYDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAY 1078
Cdd:COG0069 378 VGTIAacKGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1079 ACALGAEEFGFATAPLVVLGCIMMRVCHKDTCPVGVATQNKDLRALYR--GKAHHVVNFMHFIAQELREILASLGLKRVE 1156
Cdd:COG0069 458 AAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVREILAALGVRSPD 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1157 DLVGRTDLLQRSSTlkANSKAASIDVEKLLCPFDGPNTKEIQ----QNHNLEHGFDLTNLYEVTKPYIAEGRRYTGSFTV 1232
Cdd:COG0069 538 ELIGRHDLLRVRDG--EHWKAKGLDLSPLLYKPELPEGVPRRcqeeQDHGLDKALDLELIAAAAAAAEEGKPVVLITNIR 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1233 NNEQRDVGVITGSEISKqYGEAGLPENTINVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVKAPFEER- 1311
Cdd:COG0069 616 NNNRRVGGMLSGEIAKR-YGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPPGASf 694
|
730 740 750
....*....|....*....|....*....|....
gi 446473515 1312 --QNEIIAGNVSFYGATGGKAFINGSAGERFCIR 1343
Cdd:COG0069 695 fpEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
20-424 |
0e+00 |
|
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a homodimer that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine, an important step in ammonia assimilation in bacteria, cyanobacteria and plants. The N-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamic acid and ammonia, and has a fold similar to that of other glutamine amidotransferases such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), and beta lactam synthetase (beta-LS), as well as the Ntn hydrolase folds of the proteasomal alpha and beta subunits.
Pssm-ID: 238365 [Multi-domain] Cd Length: 413 Bit Score: 623.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 20 CGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTD--FDIPGEGEYAVG-LFFS 96
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEagIELPEAGEYAVGmLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 97 KERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFI---DIRDIEDVEKRLFLARKQLEFYST 173
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVgapSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 174 QCDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNGEINTIKGNV 253
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 254 NWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLA-MEPEKAAMLLIPEPWLYNEANDANVRAFYEFYS 332
Cdd:cd00713 241 NWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSgRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 333 YLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLLVDFKQNKVI 412
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|..
gi 446473515 413 ENNDLKGAIAGE 424
Cdd:cd00713 401 DDEEIKDQLAKR 412
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
20-430 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 587.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 20 CGIGFYANMDNKRSHDIIDKSLEMLRRLDHRGGVGADGITGDGAGIMTEIPFAFFKQHVTD--FDIPGEGEYAVG-LFFS 96
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKElgIELPEAGQYAVGmVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 97 KERILGSEHEVVFKKYFEGEGLSILGYRNVPVNKDAIAKHVADTMPVIQQVFIDIR---DIEDVEKRLFLARKQLE--FY 171
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPagkSEDDFERKLYVARKRIEkeIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 172 STQCDLELYFTSLSRKTIVYKGWLRSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHPNRMLMHNGEINTIKG 251
Cdd:pfam00310 161 VEGGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 252 NVNWMRARQHKLIETLFGEDQHKVFQIVDEDGSDSAIVDNALEFLSLA-MEPEKAAMLLIPEPWLYNEANDANVRAFYEF 330
Cdd:pfam00310 241 NRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGgRSLPEALMMLIPEAWQNNPSMDPEKRAFYEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 331 YSYLMEPWDGPTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPGKLLLVDFKQNK 410
Cdd:pfam00310 321 HSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEGR 400
|
410 420
....*....|....*....|
gi 446473515 411 VIENNDLKGAIAGELPYKAW 430
Cdd:pfam00310 401 IIDDEEIKQQIASRHPYGEW 420
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
786-1151 |
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: 550.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 786 HAFNPESIFLLQHACKENDYAQFKAYSEAVNkNRTDH--IRHLLEFK-ACTPIDIDQVEPVSDIVKRFNTGAMSYGSISA 862
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLN-ERVPIgaLRDLLEFDfAEDPIPLEEVEPALEIKTRFCTGAMSYGALSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 863 EAHETLAQAMNQLGGKSNSGEGGEDAKRYEVQVDGsnkvsAIKQVASGRFGVTSDYLQHAKEIQIKVAQGAKPGEGGQLP 942
Cdd:pfam01645 80 EAHEALAKAMNRLGTKSNTGEGGEDPERLKYADNI-----AIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 943 GTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGVAKAFADKIVISG 1022
Cdd:pfam01645 155 GEKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1023 YDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFATAPLVVLGCIMM 1102
Cdd:pfam01645 235 YDGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMC 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446473515 1103 RVCHKDTCPVGVATQNKDLRAL--YRGKAHHVVNFMHFIAQELREILASLG 1151
Cdd:pfam01645 315 RVCHTNTCPVGVATQDPELRKRldFEGAPERVVNYFRFLAEEVRELLAALG 365
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
789-1167 |
1.70e-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: 513.63 E-value: 1.70e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 789 NPESIFLLQHACKE--NDYAQFKAYSEAVNKNRT--DHIRHLLEFKA-------------CTPIDID-QVEPVSDIVKRF 850
Cdd:cd02808 1 YLLEIERLEEIQYFvfNRAERYGVYNRAGNSRGRpfGTLRDLLEFGAqlakhplepdeevDDRVTIGpNAEKPLKLDSPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 851 NTGAMSYGSISAEAHETLAQAMNQLGGKSNSGEGGEDAKRYEvqvdgsNKVSAIKQVASGRFGVTSDYLQHAKEIQIKVA 930
Cdd:cd02808 81 NISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEERE------GGGDIIKQVASGRFGVRPEYLNKADAIEIKIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 931 QGAKPGEGGQLPGTKVYPWIAKTRGSTPGIGLISPPPHHDIYSIEDLAQLIHDLKNANKDADIAVKLVSKTGVGTIASGV 1010
Cdd:cd02808 155 QGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1011 AKAFADKIVISGYDGGTGASPKTSIQHAGVPWEIGLAETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFA 1090
Cdd:cd02808 235 AAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIG 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446473515 1091 TAPLVVLGCIMMRVCHKDTCPVGVATQNKDL--RALYRGKAHHVVNFMHFIAQELREILASLGLKRVEDLvGRTDLLQR 1167
Cdd:cd02808 315 TAALIALGCIQARKCHTNTCPVGVATQDPELrrRLDVEGKAERVANYLKSLAEELRELAAALGKRSLELL-GRSDLLAL 392
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
457-733 |
2.60e-126 |
|
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: 394.05 E-value: 2.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 457 KLQRQFAYTKEEIHKYIQELVEGKKDPIGAMGYDAPIAVLNERPESLFNYFKQLFAQVTNPPIDAYREKIVTSELSYLGG 536
Cdd:pfam04898 1 RRQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 537 EGNLLAPDETVLDRIQLKRPVLNESHLAAI---NQEHFKLTYLSTVYEGdLEDALEALGREAVDAVKQGAQILVLDDSGl 613
Cdd:pfam04898 81 EGNLLEETPEHCRRLELPSPILTNEELEKLrslKGPGFKVATLDITFDG-LEAALERLCEEAEEAVRDGANILILSDRG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 614 VDSNGFAMPMLLAISHVHQLLIKADLRMSTSLVAKSGETREVHHVACLLAYGANAIVPYLAQRTVEQLTLTEGLQGTVVD 693
Cdd:pfam04898 159 VDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGKGKLTDED 238
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446473515 694 N---VKTYTDVLSEGVIKVMAKMGISTVQSYQGAQIFEAIGLS 733
Cdd:pfam04898 239 LeeaVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1207-1455 |
2.87e-111 |
|
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: 351.83 E-value: 2.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1207 FDLTNLYEVTKPYIAEGRRYTGSFTVNNEQRDVGVITGSEISKQYGEAGLPENTINVYTNGHAGQSLAAYAPKGLMIHHT 1286
Cdd:cd00982 1 LDDKLIADAEPALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1287 GDANDYVGKGLSGGTVIVK----APFEeRQNEIIAGNVSFYGATGGKAFINGSAGERFCIRNSGVDVVVEGIGDHGLEYM 1362
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRppkdATFK-PEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1363 TGGHVINLGDVGKNFGQGMSGGIAYVIPSDVEaFVENNQLDTLSFTKIKHQEEKAFIKQMLEEHVSHTNSTRAIHVLKHF 1442
Cdd:cd00982 160 TGGTVVVLGKTGRNFAAGMSGGVAYVLDEDGD-FEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANW 238
|
250
....*....|...
gi 446473515 1443 DRIEDVVVKVIPK 1455
Cdd:cd00982 239 EAYLKKFVKVIPR 251
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1230-1417 |
1.82e-84 |
|
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: 274.29 E-value: 1.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1230 FTVNNEQRDVGVITGSEISKQYGEAGLPENTINVYTNGHAGQSLAAYAPKGLMIHHTGDANDYVGKGLSGGTVIVK---- 1305
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYppae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1306 APFEERQNeIIAGNVSFYGATGGKAFINGSAGERFCIRNSGVDVVVEGIGDHGLEYMTGGHVINLGDVGKNFGQGMSGGI 1385
Cdd:pfam01493 81 STFKAEEN-IIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGI 159
|
170 180 190
....*....|....*....|....*....|..
gi 446473515 1386 AYVIPSDvEAFVENNQLDTLSFTKIKHQEEKA 1417
Cdd:pfam01493 160 AYVLDED-GDFPEKLNKEMVELERVTDEDEEA 190
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1237-1388 |
4.47e-60 |
|
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: 202.80 E-value: 4.47e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1237 RDVGVITGSEISKQYGeagLPENTINVYTNGHAGQSLAAYApKGLMIHHTGDANDYVGKGLSGGTVIVKAPFEErqNEII 1316
Cdd:cd00504 1 RAVGTRGSRYIGKRPG---LPEDTVEIIINGSAGQSFGAFM-AGGTITVEGNANDYVGKGMSGGEIVIHPPAGD--ENGI 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446473515 1317 AGNVSFYGATGGKAFINGSAGERFCIRNSGVDVVVEGIGD-HGLEYMTGGHVINLGDVGKNFGQGMSGGIAYV 1388
Cdd:cd00504 75 AGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYV 147
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
196-402 |
1.33e-29 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 117.93 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 196 RSDQIKKLYTDLSDDLYQSKLGLVHSRFSTNTFPSWKRAHP------NRMLMHNGEINTIKGNVNWMRARQHKLietlfg 269
Cdd:cd00352 50 RAGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPfrsedgRIALVHNGEIYNYRELREELEARGYRF------ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 270 edqhkvfqivdEDGSDSAIVDNALEFLSLAMEPEKAAMLLIPEpwlyneandanvrafyefysylmepWDGP--TMISFC 347
Cdd:cd00352 124 -----------EGESDSEVILHLLERLGREGGLFEAVEDALKR-------------------------LDGPfaFALWDG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446473515 348 NGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDvpESNVAFKGQLNPGKLL 402
Cdd:cd00352 168 KPDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALL--ALPFKGVRRLPPGELL 220
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1255-1388 |
2.20e-11 |
|
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.
Pssm-ID: 238481 [Multi-domain] Cd Length: 232 Bit Score: 65.40 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1255 GLPEN-TINVYtnGHAGQSLAAYAPKGLMIHHtGDANDYVGKGLSGGTVIVKAPfeerqneiiAGNVSFYGATGGKAFIN 1333
Cdd:cd00981 42 GLPGNvRINIY--GVPGNDLGAFMSGPTIIVY-GNAQDDVGNTMNDGKIVIHGS---------AGDVLGYAMRGGKIFIR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446473515 1334 GSAGERFCIR------NSGVdVVVEGI-GDHGLEYMTGGHVINLG------DVGKNFGQGMSGGIAYV 1388
Cdd:cd00981 110 GNAGYRVGIHmkeykdKVPV-LVIGGTaGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIYI 176
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1266-1385 |
7.81e-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: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1266 NGHAGQSLAAYApKGLMIHHTGDANDYVGKGLSGGTVIVKapfeerqneiiaGNVSFY----------GATGGKAFINGS 1335
Cdd:cd00980 45 EGDVGMYVGAGM-KGGKLVVEGNAGSWAGCEMKGGEITIK------------GNAGDYvgsayrgdwrGMSGGTITIEGN 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446473515 1336 AGERFCIRNSGVDVVVEG-IGDHGLEYMTGGHVINLGDVGKNFGQGMSGGI 1385
Cdd:cd00980 112 AGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGT 162
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
189-399 |
1.61e-08 |
|
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238888 [Multi-domain] Cd Length: 249 Bit Score: 57.28 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 189 IVYKGWLRSDQIKKLYtDLSDdlYQSKLGLVHSRFSTNTFPSWKRAHP----NRMLMHNGEINTIKGNVNWMRARQHKlI 264
Cdd:cd01907 55 EVFKGVGYPEDIARRY-DLEE--YKGYHWIAHTRQPTNSAVWWYGAHPfsigDIAVVHNGEISNYGSNREYLERFGYK-F 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 265 ETlfgedqhkvfqivdedGSDS----AIVDNALEFLSLAMEPEKAAMLLIPEPWLYNEAndanvrafyEFYSYLMEPWDG 340
Cdd:cd01907 131 ET----------------ETDTeviaYYLDLLLRKGGLPLEYYKHIIRMPEEERELLLA---------LRLTYRLADLDG 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446473515 341 PTMISFCNGDKLGALTDRNGLRPGRYTITKDNFIVFSSEVGVVDVPESNVAFKGQLNPG 399
Cdd:cd01907 186 PFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPG 244
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1283-1388 |
7.57e-08 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 55.20 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1283 IHHTGDANDYVGKGLSGGTVIVK---APF---EERQNEI-IAGNV----------SFYGATGGKAFINGSAGERF--CIR 1343
Cdd:COG2218 84 IIVEGDVGMYLGAGMKGGKITVNgnaGSFagaEMKGGEIeINGNAgdflgaayrgDWRGMSGGTIIVKGNAGDRLgdRMR 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446473515 1344 NsGVdVVVEG-IGDHGLEYMTGGHVINLGDVGKNFGQGMSGGIAYV 1388
Cdd:COG2218 164 R-GT-IIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVV 207
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
967-1091 |
1.06e-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: 51.05 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 967 PHHDIYSIEDLAQLIHDLKNANKDADIAVKLVskTGVGTIASGVAKAFADKIVISGYDGGTGASpktsiqhagvpweIGL 1046
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKLS--PTGELAAAAAEEAGVDEVGLGNGGGGGGGR-------------DAV 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446473515 1047 AETHQTLKLNDLRSRVKLETDGKLLTGKDVAYACALGAEEFGFAT 1091
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1287-1384 |
2.16e-06 |
|
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family are subunit C of the formylmethanofuran dehydrogenase. Nomenclature in some bacteria may reflect inclusion of the formyltransferase described by TIGR03119 as part of the complex, and therefore call this protein formyltransferase/hydrolase complex Fhc subunit C. Note that this model does not distinguish tungsten (FwdC) from molybdenum-containing (FmdC) forms of this enzyme.
Pssm-ID: 274439 [Multi-domain] Cd Length: 257 Bit Score: 50.80 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1287 GDANDYVGKGLSGGTVIVK------APFEERQNEI-IAGNVSFY----------GATGGKAFINGSAGERFCIRNSGVDV 1349
Cdd:TIGR03122 87 GDVGMHVGAEMKGGKIVVNgnadswAGCEMKGGEIiIKGNAGDYvgsayrgewrGMSGGKIIVEGNAGDYLGERMRGGEI 166
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446473515 1350 VVEG-----IGDHgleyMTGGHVINLGDVGKNFGQGMSGG 1384
Cdd:TIGR03122 167 LIKGnagifAGIH----MNGGTIIIDGDIGRRPGGEMKRG 202
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1291-1388 |
3.39e-04 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 43.49 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446473515 1291 DYVGKGLSGGTVIVKapfeerqneiiaGNVSFY---GATGGKAFINGSAGERFCIRNSGVDVVVEG-IGDH-GLEY---- 1361
Cdd:cd00980 31 KRIGARMTAGEIVVE------------GDVGMYvgaGMKGGKLVVEGNAGSWAGCEMKGGEITIKGnAGDYvGSAYrgdw 98
|
90 100
....*....|....*....|....*....
gi 446473515 1362 --MTGGHVINLGDVGKNFGQGMSGGIAYV 1388
Cdd:cd00980 99 rgMSGGTITIEGNAGDRLGERMRRGEILI 127
|
|
| |
