|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
12-1471 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1801.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 12 GLYQSDYEHDACGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEFILL----QGIPVPEK 86
Cdd:PRK11750 4 GLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADgKTGDGCGLLLQKPDRFFRAvaeeAGWRLAKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 87 gkYGTGLVFLPKDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFV---TGVSEDNvpvFER 163
Cdd:PRK11750 84 --YAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVnapAGWRERD---FER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 164 ILYKVRKRIENRI-DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLL 242
Cdd:PRK11750 159 RLFIARRRIEKRLaDDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 243 AHNGEINTIRGNRGWMKARESVLSSEALGDIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESFNDKNPI 322
Cdd:PRK11750 239 AHNGEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 323 SEDLKAFYEYHSILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGK 402
Cdd:PRK11750 319 DPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 403 ILLIDTQEGKIYYDGEIKEKLAKAHPYREWLAENRVQL---EKLKSGRKVDNGVSDLQ----QKLvtFGFGQEDIDKTII 475
Cdd:PRK11750 399 LLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLvpfEELPDEQVGSRELDDDTlksyQKQ--FQYSFEELDQVIR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 476 PMATAGQEPVAAMGNDTPLAVISDRPQVLFNYFRQQFAQVTNPAIDPIREELVMSLTEYIGAvGTNILTPDASNCKMVRL 555
Cdd:PRK11750 477 VLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGR-EMNVFCETEGHAHRVIF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 556 PQPVLTNTQLDILCNIRYKGFNTKKLPIVFEMAkgEEGLRQALDDLCHQAEASVDEGVNYIILSDRDLDDTHAAIPSLLA 635
Cdd:PRK11750 556 KSPVLSYSDFKQLTTLDEEHYRADTLDLNYDPE--ETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 636 VSAVHHYLISVGKRVQTALIVESGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKIQEEYATAEKNYIKAVDKGL 715
Cdd:PRK11750 634 VGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGL 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 716 KKIMSKMGISTIRSYRGAKIFESIGLSEDLLRRYFGTEVSTIGGVGLKEIARDAIALH-EAAKEQTLLQNQGQFAWRKDG 794
Cdd:PRK11750 714 YKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSkRAWLARKPIDQGGLLKYVHGG 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 795 IKHAWNPETIAKLQLATRQGNYEKFKQWSKLVDEKesPI-FIRDFFGFKKAAKPTPIDEVESVESIVKHFVTGAMSFGAL 873
Cdd:PRK11750 794 EYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNER--PVaTLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGAL 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 874 SIEAHEALALAMNKLGARSNTGEGGEDNARYHSEvdgvsLSSKTKQIASGRFGVTAEYLVNAEEIQIKVAQGAKPGEGGQ 953
Cdd:PRK11750 872 SPEAHEALAIAMNRLGGRSNSGEGGEDPARYGTE-----KVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQ 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 954 LPGFKVNEIIAKTRNAIPGISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAESGVGTIAAGVAKAKADLIVI 1033
Cdd:PRK11750 947 LPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITI 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1034 SGAEGGTGASPASSMRFAGiSP-EIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAMLGADEFSFGTLPLIVLGC 1112
Cdd:PRK11750 1027 SGYDGGTGASPLTSVKYAG-SPwELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGC 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1113 VMMRKCNTNTCPMGVATQNPELRK-HFEGRAEYVVNFFTFLAEQVREYLSEIGVKSLKEIIGHTELIEVnTENATDKQKT 1191
Cdd:PRK11750 1106 KYLRICHLNNCATGVATQDEKLRKnHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEE-LEGETAKQQK 1184
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1192 IDFARLLHKP--ATDKALYW--DRGA-YTKvtGVKDEEMIKAAQKAIENQEEVTLDYAIKNTDRAVGTMLSGVIAQKYGE 1266
Cdd:PRK11750 1185 LDLSPLLETAepPAGKALYCteERNPpFDK--GLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGN 1262
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1267 EGLPDGTIKIKFKGSAGQSFGAFAVKGLDLRLEGETNDYFGKGLSGGRISILPParRSDDFKAEENIIAGNTGLYGATSG 1346
Cdd:PRK11750 1263 QGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPP--VGSAFRSHETAIIGNTCLYGATGG 1340
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1347 ELYINGKVGERFGVRNSGAIAVIEGAGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYDPDHTFDYFCNMDMVELSL 1426
Cdd:PRK11750 1341 KLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILR 1420
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*.
gi 502828279 1427 VEDSVSRKE-LLELIREHYLHTGSALAGRMLDDWHRYIEDFIQVVP 1471
Cdd:PRK11750 1421 VEDLEIHREhLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
20-1492 |
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: 1339.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 20 HDACGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAE-TRDKTGDGAGIMVQIPHEFILLQGIPVPEKGKYGTGLVFLPK 98
Cdd:COG0070 27 LGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGgGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 99 DEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVTGVSEDNVPVFERILYKVRKRIENRIDD 178
Cdd:COG0070 107 AVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFRR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 179 EDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLLAHNGEINTIRGNRGWM 258
Cdd:COG0070 187 RSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNNNNNNNR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 259 KARESVLSSEALGDIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESFNDKNPISEDLKAFYEYHSILME 338
Cdd:COG0070 267 NAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAAAADLYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 339 PWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGKILLIDTQEGKIYYDGE 418
Cdd:COG0070 347 AAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGLLDDEEE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 419 IKEKLAKAHPYREWLAENRVQLEKLKSGRKVDNGVSDLQQKLVTFGFGQEDIDKTIIPMATAGQEPVAAMGNDTPLAVIS 498
Cdd:COG0070 427 DAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAAAAALDL 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 499 DRPQVLFNYFRQQFAQVTNPAIDPIREELVMSLTEYIGAVGTNILTPDASNCKMVRLPQPVLTNTQLDILCNIRYKGFNT 578
Cdd:COG0070 507 LDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLLLLLLGD 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 579 KKLPIVFEMAKGEEGLRQALDDLCHQAEASVDEGVN-YIILSDRDLDDTHAAIPSLLAVSAVHHYLISVGKRVQTALIVE 657
Cdd:COG0070 587 ATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAaILAASIRDSALLLALLPALLALLLLHHHLLRALGRVLVLLVEA 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 658 SGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKIQEEYATAEKNYIKAVDKGLKKIMSKMGISTIRSYRGAKIFE 737
Cdd:COG0070 667 LLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSSGGGIIE 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 738 SIGLSEDLLRRYFGTEVSTIGGVGLKEIARDAIALHEA------AKEQTLLQNQGQFAWRKDGIKHAWNPETIAKLQLAT 811
Cdd:COG0070 747 GAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAaaadaaAAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQLAA 826
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 812 RQGNYEKFKQWSKLVDEKESPIFIRDFFGFKKAAKPTPIDEVESVESIVKHFVTGAMSFGALSIEAHEALALAMNKLGAR 891
Cdd:COG0070 827 RTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAMNRIGGK 906
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 892 SNTGEGGEDNARYHSEVDGVSLSSKTKQIASGRFGVTAEYLVNAEEIQIKVAQGAKPGEGGQLPGFKVNEIIAKTRNAIP 971
Cdd:COG0070 907 SNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTP 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 972 GISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAESGVGTIAAGVAKAKADLIVISGAEGGTGASPASSMRFA 1051
Cdd:COG0070 987 GVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPLSSIKHA 1066
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1052 GISPEIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAMLGADEFSFGTLPLIVLGCVMMRKCNTNTCPMGVATQN 1131
Cdd:COG0070 1067 GLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQD 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1132 PELRKHFEGRAEYVVNFFTFLAEQVREYLSEIGVKSLKEIIGHTELIEVNTENATDKQKTIDFARLLHKPAT--DKALYW 1209
Cdd:COG0070 1147 PELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPDVpaDVPRYC 1226
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1210 DRGAYTKVTGVKDEEMIKAAQKAIENQEEVTLDYAIKNTDRAVGTMLSGVIAQKYGEEGLPDGTIKIKFKGSAGQSFGAF 1289
Cdd:COG0070 1227 TEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTGSAGQSFGAF 1306
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1290 AVKGLDLRLEGETNDYFGKGLSGGRISILPPArrSDDFKAEENIIAGNTGLYGATSGELYINGKVGERFGVRNSGAIAVI 1369
Cdd:COG0070 1307 LAKGLTLELEGDANDYVGKGLSGGKIIVRPPA--GSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATAVV 1384
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1370 EGAGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYDPDHTFDYFCNMDMVELSLVEDSVSRKELLELIREHYLHTGS 1449
Cdd:COG0070 1385 EGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEEHVEYTGS 1464
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|...
gi 502828279 1450 ALAGRMLDDWHRYIEDFIQVVPIEYKRVLEEEKMARLHEKIAD 1492
Cdd:COG0070 1465 ARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDAD 1507
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
23-427 |
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: 663.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 23 CGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEF----ILLQGIPVPEKGKYGTGLVFLP 97
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADgKTGDGAGILIQIPHEFfreeLAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 98 KDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVTGVSEDNVPVFERILYKVRKRIENRI- 176
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 177 -DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLLAHNGEINTIRGNR 255
Cdd:cd00713 161 aADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 256 GWMKARESVLSSEALG-DIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESFNDKNPISEDLKAFYEYHS 334
Cdd:cd00713 241 NWMRAREGLLKSPLFGeDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 335 ILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGKILLIDTQEGKIY 414
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|...
gi 502828279 415 YDGEIKEKLAKAH 427
Cdd:cd00713 401 DDEEIKDQLAKRH 413
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
23-432 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 652.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 23 CGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEFI----LLQGIPVPEKGKYGTGLVFLP 97
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADpDTGDGAGILTQIPDEFFrkeaKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 98 KDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVTGVSEDNVPVFERILYKVRKRIENRI- 176
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 177 ---DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLLAHNGEINTIRG 253
Cdd:pfam00310 161 vegGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 254 NRGWMKARESVLSSEALG-DIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESF-NDKNpISEDLKAFYE 331
Cdd:pfam00310 241 NRNWMRAREALLKSELFGdDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWqNNPS-MDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 332 YHSILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGKILLIDTQEG 411
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 502828279 412 KIYYDGEIKEKLAKAHPYREW 432
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1263-1409 |
2.18e-05 |
|
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: 47.72 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1263 KYGEEGLPDGTIKIKfkGSAGQSFGAFaVKGLDLRLEGETNDYFGKGLSGGRIsilpparrsddfkaeenIIAGNTGLY- 1341
Cdd:TIGR03122 72 KRIGENMSAGEIVVE--GDVGMHVGAE-MKGGKIVVNGNADSWAGCEMKGGEI-----------------IIKGNAGDYv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1342 GATSGelyingkvGERFGVrnSGAIAVIEG-AGDHCCEYM-------------------TGGRVVVLGKTGRNFAAGMSG 1401
Cdd:TIGR03122 132 GSAYR--------GEWRGM--SGGKIIVEGnAGDYLGERMrggeilikgnagifagihmNGGTIIIDGDIGRRPGGEMKR 201
|
....*...
gi 502828279 1402 GVAYVYDP 1409
Cdd:TIGR03122 202 GTIVVGGK 209
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
12-1471 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1801.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 12 GLYQSDYEHDACGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEFILL----QGIPVPEK 86
Cdd:PRK11750 4 GLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADgKTGDGCGLLLQKPDRFFRAvaeeAGWRLAKN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 87 gkYGTGLVFLPKDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFV---TGVSEDNvpvFER 163
Cdd:PRK11750 84 --YAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVnapAGWRERD---FER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 164 ILYKVRKRIENRI-DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLL 242
Cdd:PRK11750 159 RLFIARRRIEKRLaDDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 243 AHNGEINTIRGNRGWMKARESVLSSEALGDIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESFNDKNPI 322
Cdd:PRK11750 239 AHNGEINTITGNRQWARARAYKFQTPLIPDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQNNPDM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 323 SEDLKAFYEYHSILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGK 402
Cdd:PRK11750 319 DPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGPGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 403 ILLIDTQEGKIYYDGEIKEKLAKAHPYREWLAENRVQL---EKLKSGRKVDNGVSDLQ----QKLvtFGFGQEDIDKTII 475
Cdd:PRK11750 399 LLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLvpfEELPDEQVGSRELDDDTlksyQKQ--FQYSFEELDQVIR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 476 PMATAGQEPVAAMGNDTPLAVISDRPQVLFNYFRQQFAQVTNPAIDPIREELVMSLTEYIGAvGTNILTPDASNCKMVRL 555
Cdd:PRK11750 477 VLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGR-EMNVFCETEGHAHRVIF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 556 PQPVLTNTQLDILCNIRYKGFNTKKLPIVFEMAkgEEGLRQALDDLCHQAEASVDEGVNYIILSDRDLDDTHAAIPSLLA 635
Cdd:PRK11750 556 KSPVLSYSDFKQLTTLDEEHYRADTLDLNYDPE--ETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIAKGRLPIPAAMA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 636 VSAVHHYLISVGKRVQTALIVESGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKIQEEYATAEKNYIKAVDKGL 715
Cdd:PRK11750 634 VGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQVMLNYRKGINKGL 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 716 KKIMSKMGISTIRSYRGAKIFESIGLSEDLLRRYFGTEVSTIGGVGLKEIARDAIALH-EAAKEQTLLQNQGQFAWRKDG 794
Cdd:PRK11750 714 YKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSkRAWLARKPIDQGGLLKYVHGG 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 795 IKHAWNPETIAKLQLATRQGNYEKFKQWSKLVDEKesPI-FIRDFFGFKKAAKPTPIDEVESVESIVKHFVTGAMSFGAL 873
Cdd:PRK11750 794 EYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNER--PVaTLRDLLALKPADNPIPLDEVEPAEELFKRFDSAAMSIGAL 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 874 SIEAHEALALAMNKLGARSNTGEGGEDNARYHSEvdgvsLSSKTKQIASGRFGVTAEYLVNAEEIQIKVAQGAKPGEGGQ 953
Cdd:PRK11750 872 SPEAHEALAIAMNRLGGRSNSGEGGEDPARYGTE-----KVSKIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQ 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 954 LPGFKVNEIIAKTRNAIPGISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAESGVGTIAAGVAKAKADLIVI 1033
Cdd:PRK11750 947 LPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITI 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1034 SGAEGGTGASPASSMRFAGiSP-EIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAMLGADEFSFGTLPLIVLGC 1112
Cdd:PRK11750 1027 SGYDGGTGASPLTSVKYAG-SPwELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGC 1105
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1113 VMMRKCNTNTCPMGVATQNPELRK-HFEGRAEYVVNFFTFLAEQVREYLSEIGVKSLKEIIGHTELIEVnTENATDKQKT 1191
Cdd:PRK11750 1106 KYLRICHLNNCATGVATQDEKLRKnHYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRTDLLEE-LEGETAKQQK 1184
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1192 IDFARLLHKP--ATDKALYW--DRGA-YTKvtGVKDEEMIKAAQKAIENQEEVTLDYAIKNTDRAVGTMLSGVIAQKYGE 1266
Cdd:PRK11750 1185 LDLSPLLETAepPAGKALYCteERNPpFDK--GLLNEQMLQQAKPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRHGN 1262
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1267 EGLPDGTIKIKFKGSAGQSFGAFAVKGLDLRLEGETNDYFGKGLSGGRISILPParRSDDFKAEENIIAGNTGLYGATSG 1346
Cdd:PRK11750 1263 QGMADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPP--VGSAFRSHETAIIGNTCLYGATGG 1340
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1347 ELYINGKVGERFGVRNSGAIAVIEGAGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYDPDHTFDYFCNMDMVELSL 1426
Cdd:PRK11750 1341 KLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGFAYVLDEDGDFVDRVNHELVEILR 1420
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....*.
gi 502828279 1427 VEDSVSRKE-LLELIREHYLHTGSALAGRMLDDWHRYIEDFIQVVP 1471
Cdd:PRK11750 1421 VEDLEIHREhLRGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
20-1492 |
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: 1339.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 20 HDACGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAE-TRDKTGDGAGIMVQIPHEFILLQGIPVPEKGKYGTGLVFLPK 98
Cdd:COG0070 27 LGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGgGTGGGGGGGGGGGGGGGLGALLAGGGAFFAAGLAAGLLALAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 99 DEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVTGVSEDNVPVFERILYKVRKRIENRIDD 178
Cdd:COG0070 107 AVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLRLRRLALLRRRRRRRRREFRR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 179 EDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLLAHNGEINTIRGNRGWM 258
Cdd:COG0070 187 RSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFFAPRTLAANNNNNNNNNNNNNNNR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 259 KARESVLSSEALGDIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESFNDKNPISEDLKAFYEYHSILME 338
Cdd:COG0070 267 NAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAAPAPRAAAPPAAAAAFAAAADLYA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 339 PWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGKILLIDTQEGKIYYDGE 418
Cdd:COG0070 347 AAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKGRELPGGGLLVGGGGGGLLDDEEE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 419 IKEKLAKAHPYREWLAENRVQLEKLKSGRKVDNGVSDLQQKLVTFGFGQEDIDKTIIPMATAGQEPVAAMGNDTPLAVIS 498
Cdd:COG0070 427 DAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLLLAEALEEEEESGGAGAAAAALDL 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 499 DRPQVLFNYFRQQFAQVTNPAIDPIREELVMSLTEYIGAVGTNILTPDASNCKMVRLPQPVLTNTQLDILCNIRYKGFNT 578
Cdd:COG0070 507 LDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLELLLLLLALALLLLLLLLLLLLGD 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 579 KKLPIVFEMAKGEEGLRQALDDLCHQAEASVDEGVN-YIILSDRDLDDTHAAIPSLLAVSAVHHYLISVGKRVQTALIVE 657
Cdd:COG0070 587 ATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAaILAASIRDSALLLALLPALLALLLLHHHLLRALGRVLVLLVEA 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 658 SGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKIQEEYATAEKNYIKAVDKGLKKIMSKMGISTIRSYRGAKIFE 737
Cdd:COG0070 667 LLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLEAAAYKAKAALKAGVKKKLKIGGSSISSSSGGGIIE 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 738 SIGLSEDLLRRYFGTEVSTIGGVGLKEIARDAIALHEA------AKEQTLLQNQGQFAWRKDGIKHAWNPETIAKLQLAT 811
Cdd:COG0070 747 GAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAaaadaaAAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQLAA 826
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 812 RQGNYEKFKQWSKLVDEKESPIFIRDFFGFKKAAKPTPIDEVESVESIVKHFVTGAMSFGALSIEAHEALALAMNKLGAR 891
Cdd:COG0070 827 RTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGAMSGGSSSSEAHEELAIAMNRIGGK 906
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 892 SNTGEGGEDNARYHSEVDGVSLSSKTKQIASGRFGVTAEYLVNAEEIQIKVAQGAKPGEGGQLPGFKVNEIIAKTRNAIP 971
Cdd:COG0070 907 SNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTP 986
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 972 GISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAESGVGTIAAGVAKAKADLIVISGAEGGTGASPASSMRFA 1051
Cdd:COG0070 987 GVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPLSSIKHA 1066
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1052 GISPEIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAMLGADEFSFGTLPLIVLGCVMMRKCNTNTCPMGVATQN 1131
Cdd:COG0070 1067 GLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQD 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1132 PELRKHFEGRAEYVVNFFTFLAEQVREYLSEIGVKSLKEIIGHTELIEVNTENATDKQKTIDFARLLHKPAT--DKALYW 1209
Cdd:COG0070 1147 PELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPDVpaDVPRYC 1226
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1210 DRGAYTKVTGVKDEEMIKAAQKAIENQEEVTLDYAIKNTDRAVGTMLSGVIAQKYGEEGLPDGTIKIKFKGSAGQSFGAF 1289
Cdd:COG0070 1227 TEEQNHGLEGALDRELIEDARPAIENGEPVELEYPIRNTDRSVGTRLSGEIAKRYGNEGLPEDTITLRFTGSAGQSFGAF 1306
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1290 AVKGLDLRLEGETNDYFGKGLSGGRISILPPArrSDDFKAEENIIAGNTGLYGATSGELYINGKVGERFGVRNSGAIAVI 1369
Cdd:COG0070 1307 LAKGLTLELEGDANDYVGKGLSGGKIIVRPPA--GSTFVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATAVV 1384
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1370 EGAGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYDPDHTFDYFCNMDMVELSLVEDSVSRKELLELIREHYLHTGS 1449
Cdd:COG0070 1385 EGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLDEDGDFEDRCNPEMVELERLDEEEDEEELRELIEEHVEYTGS 1464
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|...
gi 502828279 1450 ALAGRMLDDWHRYIEDFIQVVPIEYKRVLEEEKMARLHEKIAD 1492
Cdd:COG0070 1465 ARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAGLDAD 1507
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
1-1492 |
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: 1271.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1 MTKRKQTQPKKGLYQSDYEHDACGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEF---- 75
Cdd:COG0067 1 MTENSGLPAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADgKTGDGAGILIQIPDAFfrae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 76 ILLQGIPVPEKGKYGTGLVFLPKDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVT---G 152
Cdd:COG0067 81 AAELGIELPEPGEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVArpdG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 153 VSEDnvpVFERILYKVRKRIENRI-----DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFST 227
Cdd:COG0067 161 LDGD---AFERKLYVARKRIEKAIralglDDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFST 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 228 NTFPKWKLAQPFRLLAHNGEINTIRGNRGWMKARESVLSSEALG-DIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQ 306
Cdd:COG0067 238 NTFPSWPLAQPFRYLAHNGEINTLRGNRNWMRAREALLASPLFGdDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPH 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 307 AMAILVPESFNDKNPISEDLKAFYEYHSILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMD 386
Cdd:COG0067 318 AMMMLIPEAWENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 387 FEPGDVVSKGRLQPGKILLIDTQEGKIYYDGEIKEKLAKAHPYREWLAENRVQLEKLKSGRKVDNGVSD-LQQKLVTFGF 465
Cdd:COG0067 398 IPPEDIVEKGRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDlLLRRQQAFGY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 466 GQEDIDKTIIPMATAGQEPVAAMGNDTPLAVISDRPQVLFNYFRQQFAQVTNPAIDPIREELVMSLTEYIGaVGTNILTP 545
Cdd:COG0067 478 TEEEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGG-GGNNLLLE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 546 DASNCKMVRLPQPVLTNTQLDILCNIRYKGFNTKKLPIVFEMAKGEEGLRQALDDLCHQAEASVDEGVNYIILSDRDLDD 625
Cdd:COG0067 557 EEEARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDDD 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 626 THAAIPSLLAVSAVHHYLISVGKRVQTALIVESGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKIQEEYATAE- 704
Cdd:COG0067 637 SDAAPAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAAa 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 705 ---KNYIKAVDKGLKKIMSKMGISTIRSYRGAKIFESIGLSEDLLRRYFGTEVSTIGGVGLKEIARDAIALHEAAKEQT- 780
Cdd:COG0067 717 aakKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPg 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 781 ------LLQNQGQFAWRKDGIKHAWNPETIAKLQLATRQGNYEKFKQWSKLVDEKESPIFIRDFFGFKKAAKPTPIDEVE 854
Cdd:COG0067 797 glllglGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEEE 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 855 SVESIVKHFVTGAMSFGALSIEAHEALALAMNKLGARSNTGEGGEDNARyhseVDGVSLSSKTKQIASGRFGVTAEYLVN 934
Cdd:COG0067 877 EEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGAA 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 935 AEEIQIKVAQGAKPGEGGQLPGFKVNEIIAKTRNAIPGISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAES 1014
Cdd:COG0067 953 AAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVAA 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1015 GVGTIAAGVAKAKADLIVISGAEGGTGASPASSMRFAGISPEIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAM 1094
Cdd:COG0067 1033 AAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAAA 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1095 LGADEFSFGTLPLIVLGCVMMRKCNTNTCPMGVATQNPELRKHFEGRAEYVVNFFTFLAEQVREYLSEIGVKSLKEIIGH 1174
Cdd:COG0067 1113 LGAGALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELLRLLEEGLG 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1175 TELIEVNTENATDKQKTIDFARLLHKPATDKALYWDRGAYTKV---TGVKDEEMIKAAQKAIENQEEVTLDYAIKNTDRA 1251
Cdd:COG0067 1193 VVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDellLLLALLLLLLALALALLAAVRVALRAALGRARRR 1272
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1252 VGTMLSGVIAQKYGEEGLPDGTIKIKFKGSAGQSFGAFAVKGLDLRLEGETNDYFGKGLSGGRISILPPArrSDDFKAEE 1331
Cdd:COG0067 1273 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG--GGGGGGGG 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1332 NIIAGNTGLYGATSGELYINGKVGERFGVRNSGAIAVIEGAGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYDPDH 1411
Cdd:COG0067 1351 GGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDLD 1430
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1412 TFDYFCNMDMVELSLVEDSVSRKELLELIREHYLHTGSALAGRMLDDWHRYIEDFIQVVPIEYKRVLEEEKMARLHEKIA 1491
Cdd:COG0067 1431 VVLDEEEEEELEELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAAAA 1510
|
.
gi 502828279 1492 D 1492
Cdd:COG0067 1511 E 1511
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
634-1361 |
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: 913.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 634 LAVSAVHHYLISVGKRVQTALIVESGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKIQEEYATAEKNYIKAVDK 713
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLGLDLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 714 GLKKIMSKMGISTIRSYRGAKIFESIGLSEDLLrryfgtevstigGVGLkeiaRDAIALHEAAKEQTLlQNQGQFAWRK- 792
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELV------------DIGI----ADVLTQHRHAILRNL-PVGGRYRYRFe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 793 -------------DGIKHAWNPETIAKLQLATRqgNYEKFKQWSKLVDEKES-PIFIRDFFGFKKAAKPTPIDE-VESVE 857
Cdd:COG0069 144 sigpeirqyffesDGEEHPFNRETRSLLYQAAK--NEEDYKPFGTLVDYQPGyEWTLRSLFPFKADRPPIPIGEpVEPPY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 858 SIVKHFVTGAMSFGALSIEAHEALALAMNKLGARSNTGEGGEDNARYhsevdGVSLSSKTKQIASGRFGVT---AEYLVN 934
Cdd:COG0069 222 SIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRdedGEYLPN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 935 AEEIQIKVAQGAKPGEGGQLPGFKVNEIIAKTRNAIPGISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAES 1014
Cdd:COG0069 297 AKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPVGVKLVSGA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1015 GVGTIAA--GVAK--AKADLIVISGAEGGTGASPASSMRFAGISPEIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVI 1090
Cdd:COG0069 377 GVGTIAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1091 IMAMLGADEFSFGTLPLIVLGCVMMRKCNTNTCPMGVATQNPELRKHF--EGRAEYVVNFFTFLAEQVREYLSEIGVKSL 1168
Cdd:COG0069 457 IAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFvvEGKPERVVNYFRFTAEEVREILAALGVRSP 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1169 KEIIGHTELIEVNtENATDKQKTIDFARLLHKPA--TDKALYWDRGAYTKVTGVKDEEMIKAAQKAIENQEEVTLDYAIK 1246
Cdd:COG0069 537 DELIGRHDLLRVR-DGEHWKAKGLDLSPLLYKPElpEGVPRRCQEEQDHGLDKALDLELIAAAAAAAEEGKPVVLITNIR 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1247 NTDRAVGTMLSGVIAQKYGEEGLPDGTIKIKFKGSAGQSFGAFAVKGLDLRLEGETNDYFGKGLSGGRISILPPARRSdd 1326
Cdd:COG0069 616 NNNRRVGGMLSGEIAKRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGGGIIVPPPPGAS-- 693
|
730 740 750
....*....|....*....|....*....|....*
gi 502828279 1327 FKAEENIIAGNTGLYGATSGELYINGKVGERFGVR 1361
Cdd:COG0069 694 FFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
23-427 |
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: 663.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 23 CGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEF----ILLQGIPVPEKGKYGTGLVFLP 97
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADgKTGDGAGILIQIPHEFfreeLAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 98 KDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVTGVSEDNVPVFERILYKVRKRIENRI- 176
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 177 -DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLLAHNGEINTIRGNR 255
Cdd:cd00713 161 aADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 256 GWMKARESVLSSEALG-DIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESFNDKNPISEDLKAFYEYHS 334
Cdd:cd00713 241 NWMRAREGLLKSPLFGeDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYHS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 335 ILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGKILLIDTQEGKIY 414
Cdd:cd00713 321 SLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRIL 400
|
410
....*....|...
gi 502828279 415 YDGEIKEKLAKAH 427
Cdd:cd00713 401 DDEEIKDQLAKRH 413
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
23-432 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 652.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 23 CGVGMVVNIHGGKSHDLVDNALKVLENMEHRGAETRD-KTGDGAGIMVQIPHEFI----LLQGIPVPEKGKYGTGLVFLP 97
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADpDTGDGAGILTQIPDEFFrkeaKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 98 KDEKAQQQILSVMIEEIEREGLQLMHLRTVPTNPEVLGVAAREVEPDIKQIFVTGVSEDNVPVFERILYKVRKRIENRI- 176
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 177 ---DDEDFYLCSLSSKNIIYKGMLTSGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWKLAQPFRLLAHNGEINTIRG 253
Cdd:pfam00310 161 vegGDKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 254 NRGWMKARESVLSSEALG-DIKDLRPIVQDGMSDSASLDNVFEFLMMSGLSLPQAMAILVPESF-NDKNpISEDLKAFYE 331
Cdd:pfam00310 241 NRNWMRAREALLKSELFGdDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWqNNPS-MDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 332 YHSILMEPWDGPAALLFSDGRYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMDFEPGDVVSKGRLQPGKILLIDTQEG 411
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 502828279 412 KIYYDGEIKEKLAKAHPYREW 432
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
797-1166 |
3.44e-173 |
|
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: 522.28 E-value: 3.44e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 797 HAWNPETIAKLQLATRQGNYEKFKQWSKLVDEKESPIFIRDFFGFKKAAKPTPIDEVESVESIVKHFVTGAMSFGALSIE 876
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERVPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 877 AHEALALAMNKLGARSNTGEGGEDNARYHSEVDGVslsskTKQIASGRFGVTAEYLVNAEEIQIKVAQGAKPGEGGQLPG 956
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYADNIA-----IKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 957 FKVNEIIAKTRNAIPGISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAESGVGTIAAGVAKAKADLIVISGA 1036
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1037 EGGTGASPASSMRFAGISPEIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAMLGADEFSFGTLPLIVLGCVMMR 1116
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 502828279 1117 KCNTNTCPMGVATQNPELRKH--FEGRAEYVVNFFTFLAEQVREYLSEIGVK 1166
Cdd:pfam01645 316 VCHTNTCPVGVATQDPELRKRldFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
458-742 |
5.20e-156 |
|
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: 473.41 E-value: 5.20e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 458 QKLVTFGFGQEDIDKTIIPMATAGQEPVAAMGNDTPLAVISDRPQVLFNYFRQQFAQVTNPAIDPIREELVMSLTEYIGA 537
Cdd:pfam04898 1 RRQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 538 VGtNILTPDASNCKMVRLPQPVLTNTQLDILCNIRYKGFNTKKLPIVFEmakgeeGLRQALDDLCHQAEASVDEGVNYII 617
Cdd:pfam04898 81 EG-NLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITFD------GLEAALERLCEEAEEAVRDGANILI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 618 LSDRDLDDTHAAIPSLLAVSAVHHYLISVGKRVQTALIVESGEIREVMHAALLLGYGASALCPYMTFAVLDDLVKHHKI- 696
Cdd:pfam04898 154 LSDRGVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREGKGk 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 502828279 697 --QEEYATAEKNYIKAVDKGLKKIMSKMGISTIRSYRGAKIFESIGLS 742
Cdd:pfam04898 234 ltDEDLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
800-1178 |
1.22e-154 |
|
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: 474.34 E-value: 1.22e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 800 NPETIAKLQLATRQ--GNYEKFKQWSKLVDEKESPIF-IRDFFGFKKAAKPTPIDE-------------VESVESIVKHF 863
Cdd:cd02808 1 YLLEIERLEEIQYFvfNRAERYGVYNRAGNSRGRPFGtLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 864 VTGAMSFGALSIEAHEALALAMNKLGARSNTGEGGEDNARYHSEvdgvslSSKTKQIASGRFGVTAEYLVNAEEIQIKVA 943
Cdd:cd02808 81 NISAMSFGALSKEAKEALAIGAALAGTASNTGEGGELPEEREGG------GDIIKQVASGRFGVRPEYLNKADAIEIKIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 944 QGAKPGEGGQLPGFKVNEIIAKTRNAIPGISLISPPPHHDIYSIEDLAQLIFDLKNINPTAAVSVKLVAESGVGTIAAGV 1023
Cdd:cd02808 155 QGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1024 AKAKADLIVISGAEGGTGASPASSMRFAGISPEIGLAETQQTLVMNGLRNQVRLQTDGQLKTAKDVIIMAMLGADEFSFG 1103
Cdd:cd02808 235 AAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIG 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502828279 1104 TLPLIVLGCVMMRKCNTNTCPMGVATQNPEL--RKHFEGRAEYVVNFFTFLAEQVREYLSEIGVKSLkEIIGHTELI 1178
Cdd:cd02808 315 TAALIALGCIQARKCHTNTCPVGVATQDPELrrRLDVEGKAERVANYLKSLAEELRELAAALGKRSL-ELLGRSDLL 390
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1222-1471 |
1.06e-146 |
|
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: 447.36 E-value: 1.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1222 DEEMIKAAQKA-IENQEEVTLDYAIKNTDRAVGTMLSGVIAQKYGEEGLPDGTIKIKFKGSAGQSFGAFAVKGLDLRLEG 1300
Cdd:cd00982 2 DDKLIADAEPAlIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1301 ETNDYFGKGLSGGRISILPParRSDDFKAEENIIAGNTGLYGATSGELYINGKVGERFGVRNSGAIAVIEGAGDHCCEYM 1380
Cdd:cd00982 82 DANDYVGKGLSGGRIVVRPP--KDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1381 TGGRVVVLGKTGRNFAAGMSGGVAYVYDPDHTFDYFCNMDMVELSLVEDSVSRKELLELIREHYLHTGSALAGRMLDDWH 1460
Cdd:cd00982 160 TGGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWE 239
|
250
....*....|.
gi 502828279 1461 RYIEDFIQVVP 1471
Cdd:cd00982 240 AYLKKFVKVIP 250
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1243-1430 |
2.90e-119 |
|
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: 370.98 E-value: 2.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1243 YAIKNTDRAVGTMLSGVIAQKYGEEGLPDGTIKIKFKGSAGQSFGAFAVKGLDLRLEGETNDYFGKGLSGGRISILPPAr 1322
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1323 rSDDFKAEENIIAGNTGLYGATSGELYINGKVGERFGVRNSGAIAVIEGAGDHCCEYMTGGRVVVLGKTGRNFAAGMSGG 1402
Cdd:pfam01493 80 -ESTFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGG 158
|
170 180
....*....|....*....|....*...
gi 502828279 1403 VAYVYDPDHTFDYFCNMDMVELSLVEDS 1430
Cdd:pfam01493 159 IAYVLDEDGDFPEKLNKEMVELERVTDE 186
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1250-1408 |
2.18e-67 |
|
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: 223.60 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1250 RAVGTMLSGVIAQKygeEGLPDGTIKIKFKGSAGQSFGAFaVKGLDLRLEGETNDYFGKGLSGGRISILPPArrsddfkA 1329
Cdd:cd00504 1 RAVGTRGSRYIGKR---PGLPEDTVEIIINGSAGQSFGAF-MAGGTITVEGNANDYVGKGMSGGEIVIHPPA-------G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1330 EENIIAGNTGLYGATSGELYINGKVGERFGVRNSGAIAVIEG-AGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYD 1408
Cdd:cd00504 70 DENGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGvGDDFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
155-404 |
4.29e-34 |
|
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.
Pssm-ID: 238212 [Multi-domain] Cd Length: 220 Bit Score: 131.03 E-value: 4.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 155 EDNVPVFERILYKVRKRIENRIDDEDFYLCSLSSKNIIYKGMltsGQLRRYFPDLSNDYFTSGLALVHSRFSTNTFPKWK 234
Cdd:cd00352 10 DGAASLLLLLLLRGLAALEHRGPDGAGIAVYDGDGLFVEKRA---GPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 235 LAQPFR------LLAHNGEINTIRGNRGWMKAresvlssealgdikdlRPIVQDGMSDSASLDNVFEFLMMSGLsLPQAM 308
Cdd:cd00352 87 NAQPFRsedgriALVHNGEIYNYRELREELEA----------------RGYRFEGESDSEVILHLLERLGREGG-LFEAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 309 AILVPEsfndknpisedlkafyeyhsilmepWDGPAALLFSDG--RYAGGMLDRNGLRPSRYTITKQGMMVVASEVGVMD 386
Cdd:cd00352 150 EDALKR-------------------------LDGPFAFALWDGkpDRLFAARDRFGIRPLYYGITKDGGLVFASEPKALL 204
|
250
....*....|....*...
gi 502828279 387 FEPGDvvSKGRLQPGKIL 404
Cdd:cd00352 205 ALPFK--GVRRLPPGELL 220
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1267-1426 |
6.97e-14 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 73.31 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1267 EGLPDGTIKIKfkGSAGQSFGAFAvKGLDLRLEGETNDYFGKGLSGGRIsilpparrsddfkaeenIIAGNTG------- 1339
Cdd:COG2218 77 AGMTAGEIIVE--GDVGMYLGAGM-KGGKITVNGNAGSFAGAEMKGGEI-----------------EINGNAGdflgaay 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1340 ---LYGATSGELYINGKVGERFGVRNSGAIAVIEG-AGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVY-DPDH--- 1411
Cdd:COG2218 137 rgdWRGMSGGTIIVKGNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAgKPEEllp 216
|
170
....*....|....*
gi 502828279 1412 TFDYFCNMDMVELSL 1426
Cdd:COG2218 217 TFVDCGTHELVFLRL 231
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1263-1448 |
5.32e-12 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 66.60 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1263 KYGEEGLPDGTIKIKfkGSAGQSFGaFAVKGLDLRLEGETNDYFGKGLSGGRIsilpparrsddfkaeenIIAGNTGLY- 1341
Cdd:cd00980 31 KRIGARMTAGEIVVE--GDVGMYVG-AGMKGGKLVVEGNAGSWAGCEMKGGEI-----------------TIKGNAGDYv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1342 ---------GATSGELYINGKVGERFGVRNSGAIAVIEG-AGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVY-DPD 1410
Cdd:cd00980 91 gsayrgdwrGMSGGTITIEGNAGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIGgEIE 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 502828279 1411 HTFDYFcnmdmVELSLVEDSVSRKEllELIREHYLHTG 1448
Cdd:cd00980 171 ELLPTF-----KEEGTEEDVFVSGE--ELSGTFYKFTG 201
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1256-1406 |
1.26e-09 |
|
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: 60.39 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1256 LSGVIAQKYGEEGLPdGTIKIKFKGSAGQSFGAFaVKGLDLRLEGETNDYFGKGLSGGRIsilpparrsddfkaeenIIA 1335
Cdd:cd00981 30 LDNVLGQRYIGDGLP-GNVRINIYGVPGNDLGAF-MSGPTIIVYGNAQDDVGNTMNDGKI-----------------VIH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1336 GNTG---LYGATSGELYINGKVGERFGV-----RNSGAIAVIEG-AGDHCCEYMTGGRVVVLGK------TGRNFAAGMS 1400
Cdd:cd00981 91 GSAGdvlGYAMRGGKIFIRGNAGYRVGIhmkeyKDKVPVLVIGGtAGDFLGEYMAGGVIIVLGLgtdeepVGRYIGTGMH 170
|
....*.
gi 502828279 1401 GGVAYV 1406
Cdd:cd00981 171 GGVIYI 176
|
|
| one_C_dehyd_C |
TIGR03122 |
formylmethanofuran dehydrogenase subunit C; Members of this largely archaeal protein family ... |
1263-1409 |
2.18e-05 |
|
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: 47.72 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1263 KYGEEGLPDGTIKIKfkGSAGQSFGAFaVKGLDLRLEGETNDYFGKGLSGGRIsilpparrsddfkaeenIIAGNTGLY- 1341
Cdd:TIGR03122 72 KRIGENMSAGEIVVE--GDVGMHVGAE-MKGGKIVVNGNADSWAGCEMKGGEI-----------------IIKGNAGDYv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 1342 GATSGelyingkvGERFGVrnSGAIAVIEG-AGDHCCEYM-------------------TGGRVVVLGKTGRNFAAGMSG 1401
Cdd:TIGR03122 132 GSAYR--------GEWRGM--SGGKIIVEGnAGDYLGERMrggeilikgnagifagihmNGGTIIIDGDIGRRPGGEMKR 201
|
....*...
gi 502828279 1402 GVAYVYDP 1409
Cdd:TIGR03122 202 GTIVVGGK 209
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1338-1408 |
2.56e-04 |
|
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: 44.21 E-value: 2.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502828279 1338 TGLYGatSGELYINGKVGERFGVRNSGAIAVIEG-AGDHCCEYMTGGRVVVLGKTGRNFAAGMSGGVAYVYD 1408
Cdd:cd00981 41 DGLPG--NVRINIYGVPGNDLGAFMSGPTIIVYGnAQDDVGNTMNDGKIVIHGSAGDVLGYAMRGGKIFIRG 110
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
187-382 |
9.52e-04 |
|
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: 42.64 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 187 SSKNI-IYKGMLTSGQLRRYFpDLSNdyFTSGLALVHSRFSTNTFPKWKLAQPFRL----LAHNGEINTIRGNRGWMKar 261
Cdd:cd01907 50 SGKDMeVFKGVGYPEDIARRY-DLEE--YKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGSNREYLE-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 262 esvlssealgdikdLRPIVQDGMSDSASLDNVFEFLMMSGLsLPQAMAILVPESFNDKNPISEDLKafYEYHSILMepwD 341
Cdd:cd01907 125 --------------RFGYKFETETDTEVIAYYLDLLLRKGG-LPLEYYKHIIRMPEEERELLLALR--LTYRLADL---D 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502828279 342 GPAALLFSDGRYAGGMLDRNGLRPSrYTITKQGMMVVASEV 382
Cdd:cd01907 185 GPFTIIVGTPDGFIVIRDRIKLRPA-VVAETDDYVAIASEE 224
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
206-381 |
7.28e-03 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 39.95 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 206 FPDLSnDYFTSGLALVHSRFST-------NTfpkwklaQPFR----LLAHNGEIntirgnRGWMKARESVLssEALGDIK 274
Cdd:COG0121 67 LRLLA-RPIKSRLVIAHVRKATvgpvsleNT-------HPFRggrwLFAHNGQL------DGFDRLRRRLA--EELPDEL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502828279 275 DLRPIvqdGMSDSASLdnvF----EFLMMSGLSLPQAMAILVpesfndknpisEDLKAFYEYHSILmepwdgpaALLFSD 350
Cdd:COG0121 131 YFQPV---GTTDSELA---FalllSRLRDGGPDPAEALAEAL-----------RELAELARAPGRL--------NLLLSD 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 502828279 351 GRY-----AGGMLDRNGLRPSRYTITKQGMMVVASE 381
Cdd:COG0121 186 GERlyatrYTSDDPYPTLYYLTRTTPDDRVVVVASE 221
|
|
| |
