|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
6-1516 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1627.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 6 GLYRSEFEHDACGVGFIAHIKGQKSHSIVSQALDVLKNLRHRGAVGADPLQGDGAGILIQIPDQLYRDDMMNQGVKLPPa 85
Cdd:PRK11750 4 GLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLAK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 86 gEYGVGMVFLPQEAASRHACEEEIERAVAAEGQMILGWRDVPIDRSMpMSPVVREKEPVIRQVFIGhSPDVLVTDALERK 165
Cdd:PRK11750 83 -NYAVGMVFLNQDPELAAAARRILEEELQRETLSVVGWREVPTNPSV-LGEIALSSLPRIEQVFVN-APAGWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 166 LYIIRKRSSIAIAnlhlkHCKEFYICSCSARTVVYKGQLLATQVGIYYRDLQDARCISALAMIHQRFSTNTFPQWQLAHP 245
Cdd:PRK11750 160 LFIARRRIEKRLA-----DDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 246 FRYIAHNGEINTLRGNFNWILAREKHISSPVLgDDLKKLWPLIFQGQSDSASFDNAFELLTMAGYSLAQAALMLIPEAWE 325
Cdd:PRK11750 235 FRYLAHNGEINTITGNRQWARARAYKFQTPLI-PDLQEAAPFVNETGSDSSSLDNMLELLLAGGMDLFRAMRLLVPPAWQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 326 KNKTMNPRLRALYEYNAAMMEPWDGPAAVAFTNGRQLGAILDRNGLRPARYLETKDDLVILASESGAAVIDESRIRRRWR 405
Cdd:PRK11750 314 NNPDMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 406 LEPGKILLLDLEQGRIIGNDEVKGSLAAQHPYREWIDKIRIRLDDIPQTPASaplLLGRNEL--------MRVFGFSRED 477
Cdd:PRK11750 394 VGPGELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEKNVRRLVPFEELPDE---QVGSRELdddtlksyQKQFQYSFEE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 478 VERILKSMAYQGQDPVMSMGNDAPLACLSERPQMLYDYFRQLFAQVTNPPIDPIREAMVTSLVSFIGPRpdlLNIMAVNP 557
Cdd:PRK11750 471 LDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGRE---MNVFCETE 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 558 --PVRLEVEQPVLTGAQMERIRAIadfTDGKFHSKEIDITYPLAwgREAIEARLASIRAAAVDAVRSGINILILTDRKVS 635
Cdd:PRK11750 548 ghAHRVIFKSPVLSYSDFKQLTTL---DEEHYRADTLDLNYDPE--ETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIA 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 636 RERVAIPALLATSAVHQCLVEEGLRTSTGLVVETGSARSVHDFAVLGGYGAEAVHPYLALAVVESLAKNEEERAKYVD-- 713
Cdd:PRK11750 623 KGRLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYRQvm 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 714 -NYLHAIMKGLNKIMARMGISTYMSYIGAQIFEAVGLKKSFIDQYFTNTPSPVEGLDLFDVAGEAVTVHKRAFEAieRKv 792
Cdd:PRK11750 703 lNYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLA--RK- 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 793 iPLAAGGQYMYRQGGEHHLWTPDAVVHLQRAVREGSWAEYQTYAGLINNQA----RDLLTIRGlfefvPGKAIPLESVES 868
Cdd:PRK11750 780 -PIDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKLVNERPvatlRDLLALKP-----ADNPIPLDEVEP 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 869 EASIIRRFSTAAMSVGAISTEAHVTMAVAMNRMKGASNSGEGGEDVRRnapvttetslrailgddvevdYplhpGDSLRS 948
Cdd:PRK11750 854 AEELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPAR---------------------Y----GTEKVS 908
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 949 RVRQVASGRFGVTTDYLAHGDLIQIKMAQGAKPGEGGQLPGKKVSKYIGMLRHSLPGVGLVSPPPHHDIYSIEDLAQLIL 1028
Cdd:PRK11750 909 KIKQVASGRFGVTPAYLVNAEVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIF 988
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1029 DLKYANPHAGIGVKLVSQAGIGTVAAGVAKCKADHIVVSGHDGGTGAAPATSIKHAGSAWEIGLAEVEQTLVMNNLRGRV 1108
Cdd:PRK11750 989 DLKQVNPKALVSVKLVSEPGVGTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKI 1068
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1109 RLQVDGQIKTGRDVVIGAMLGADEFGFGTTPLVAMGCLMMRKCQKNTCPAGIATQDPALRRQ-FEGRPEHVENYFHFVAR 1187
Cdd:PRK11750 1069 RLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAE 1148
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1188 EVREIMAQLGVAKFDDLIGHVEYLRKrsgLDGL--KAAKLSLEKILYKLPNPKGFPLLSTEPQDHELEKA-FDLRYAAEL 1264
Cdd:PRK11750 1149 ETREWMAQLGVRSLEDLIGRTDLLEE---LEGEtaKQQKLDLSPLLETAEPPAGKALYCTEERNPPFDKGlLNEQMLQQA 1225
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1265 SEALKAKRPMRVQTRVGNTDRAVGTMLSGIAAQE--AQGeLPDDFALFELVGTAGQSFGAFLGKGVSLRLTGGANDYVGK 1342
Cdd:PRK11750 1226 KPAIEAKQGGEFWFDIRNTDRSVGARLSGEIARRhgNQG-MADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGK 1304
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1343 GLSGGSIAVK--KSPSFdgRPNENVIAGNACLYGATSGEAFISGVVGERFAVRNSGASTVAEGCGDHGCEYMTGGTAVIL 1420
Cdd:PRK11750 1305 GMAGGKIVIRppVGSAF--RSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVL 1382
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1421 GRTGRNFAAGMSGGIAYVWDPNDELAEKMSDgafELSHVLPAAeqgsDEPLHygqkdEVLLKRLVERHAELTGSPTAREM 1500
Cdd:PRK11750 1383 GKTGVNFGAGMTGGFAYVLDEDGDFVDRVNH---ELVEILRVE----DLEIH-----REHLRGLITEHVEETGSEWGEEI 1450
|
1530
....*....|....*.
gi 2553857559 1501 LADWPAALGRFTKVFP 1516
Cdd:PRK11750 1451 LANFDDYLRKFWLVKP 1466
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
6-1530 |
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: 1276.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 6 GLYRSEFEHDACGVGFIAHIKGQKSHSIVSQALDVLKNLRHRGAVGADPLQGDGAGILIQIPDQLYRDDMMNQGVKLPPA 85
Cdd:COG0067 12 GLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIELPEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 86 GEYGVGMVFLPQEAASRHACEEEIERAVAAEGQMILGWRDVPIDRSMpMSPVVREKEPVIRQVFIGhSPDVLVTDALERK 165
Cdd:COG0067 92 GEYAVGMVFLPQDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSV-LGETARATEPVIEQVFVA-RPDGLDGDAFERK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 166 LYIIRKRSSIAIANLHLkHCKEFYICSCSARTVVYKGQLLATQVGIYYRDLQDARCISALAMIHQRFSTNTFPQWQLAHP 245
Cdd:COG0067 170 LYVARKRIEKAIRALGL-DDEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 246 FRYIAHNGEINTLRGNFNWILAREKHISSPVLGDDLKKLWPLIFQGQSDSASFDNAFELLTMAGYSLAQAALMLIPEAWE 325
Cdd:COG0067 249 FRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVLGGRSLPHAMMMLIPEAWE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 326 KNKTMNPRLRALYEYNAAMMEPWDGPAAVAFTNGRQLGAILDRNGLRPARYLETKDDLVILASESGAAVIDESRIRRRWR 405
Cdd:COG0067 329 NNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEKGR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 406 LEPGKILLLDLEQGRIIGNDEVKGSLAAQHPYREWIDKIRIRLDDIPQTPAS-APLLLGRNELMRVFGFSREDVERILKS 484
Cdd:COG0067 409 LQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEpAPDDDLLLRRQQAFGYTEEEELLLLLP 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 485 MAYQGQDPVMSMGNDAPLACLSERPQMLYDYFRQLFAQVTNPPIDPIREAMVTSLVSFIGPRPDLLNIMAVNPPVRLEVE 564
Cdd:COG0067 489 MAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLLEEEEARRRLLLLP 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 565 QPVLTGAQMERIRAIADFTDGKFHSKEIDITYPLAWGREAIEARLAsirAAAVDAVRSGINILILTDRKVSRERVAIPAL 644
Cdd:COG0067 569 PPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAE---AAAAAAAAAVLLILIIDLSDDDSDAAPAPLA 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 645 LATSAVHQCLVEEGLRTSTGLVVETGSARSVHDFAVLGGYGAEAVHPYLALAVVESLAKNEEERAKYVD---NYLHAIMK 721
Cdd:COG0067 646 AAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALELLLDGLLLGLEDAAAaaaAKKKKKKK 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 722 GLNKIMARMGISTYMSYIGAQIFEAVGLKKSFIDQYFTNTPSPVEGLDLFDVAGEAVTVHKRAFEAIERKVIPLAA---- 797
Cdd:COG0067 726 KGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEPGGLLLGlggg 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 798 -GGQYMYRQGGEHHLWTPDAVVHLQRAVREGSWAEYQTYAGLINNQARDLLTIRGLFEFVPGKAIPLESVESEASIIRRF 876
Cdd:COG0067 806 gGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEEEEEESSAIAA 885
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 877 STAAMSVGAISTEAHVTMAVAMNRMKGASNSGEGGEDVRRNApvttetslrailgddvevdyplhpGDSLRSRVRQVASG 956
Cdd:COG0067 886 ASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRRAS------------------------GGSGSSSSASVAAA 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 957 RFGVTTDYLAHGDLIQIKMAQGAKPGEGGQLPGKKVSKYIGMLRHSLPGVGLVSPPPHHDIYSIEDLAQLILDLKYANPH 1036
Cdd:COG0067 942 GGGVVVGAGAAAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAV 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1037 AGIGVKLVSQAGIGTVAAGVAKCKADHIVVSGHDGGTGAAPATSIKHAGSAWEIGLAEVEQTLVMNNLRGRVRLQVDGQI 1116
Cdd:COG0067 1022 AAAVAVVVVAAAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLG 1101
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1117 KTGRDVVIGAMLGADEFGFGTTPLVAMGCLMMRKCQKNTCPAGIATQDPALRRQFEGRPEHVENYFHFVAREVREIMAQL 1196
Cdd:COG0067 1102 GGGGGGGGAAALGAGALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALL 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1197 GVAKFDDLIGHVEYLRKRSGLDGLKAAKLSLEKILYKLPNPKGFPLLSTEPQDHELEKAFDLRYAAELSEALKAKRPMRV 1276
Cdd:COG0067 1182 ELLRLLEEGLGVVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVA 1261
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1277 QTRVGNTDRAVGTMLSG-IAAQEAQGELPDDFALFELVGTAGQSFGAFLGKGVSLRLTGGANDYVGKGLSGGSIAVKKSP 1355
Cdd:COG0067 1262 LRAALGRARRRGGGGGGgGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1341
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1356 SFDGRPNENVIAGNACLYGATSGEAFISGVVGERFAVRNSGASTVAEGCGDHGCEYMTGGTAVILGRTGRNFAAGMSGGI 1435
Cdd:COG0067 1342 GGGGGGGGGGGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1421
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1436 AYVWDPNDELAEKMSDGAFELSHVLPAAEqgsdeplhygqkDEVLLKRLVERHAELTGSPTAREMLADWPAALGRFTKVF 1515
Cdd:COG0067 1422 GGGGGLDLDVVLDEEEEEELEELLLLLEE------------EEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLL 1489
|
1530
....*....|....*
gi 2553857559 1516 PLEYKHALASLKKEE 1530
Cdd:COG0067 1490 LLLLAAAAAAAEAAA 1504
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
5-1530 |
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: 1174.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 5 CGLYRSEFEHDACGVGFIAHIKGQKSHSIVSQALDVLKNLRHRGAVGADPLQGDGAGILIQIPDQLYRDDMMNQGVKLPP 84
Cdd:COG0070 15 GGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALLAGGGAFFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 85 AGEYGVGMVFLPQEAASRHACEEEIERAVAAEGQMILGWRDVPIDRSmpmsPVVREKEPVIRQVFIGHSPDVLVTDALER 164
Cdd:COG0070 95 AGLAAGLLALAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLA----LGVRAAALARREAELSELAARRRLRLRRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 165 KLYIIRKRSSIAIAnlhlkhcKEFYICSCSARTVVYKGQLLATQVGIYYRDLQDARCISALAMIHQRFSTNTFPQWQLAH 244
Cdd:COG0070 171 ALLRRRRRRRRREF-------RRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLFF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 245 PFRYIAHNGEINTLRGNFNWILAREKHISSPVLGDDLKKLWPLIFQGQSDSASFDNAFELLTMAGYSLAQAALMLIPEAW 324
Cdd:COG0070 244 APRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 325 EKNKTMNPRLRALYEYNAAMMEPWDGPAAVAFTNGRQLGAILDRNGLRPARYLETKDDLVILASESGAAVIDESRIRRRW 404
Cdd:COG0070 324 PAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGKG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 405 RLEPGKILLLDLEQGRIIGNDEVKGSLAAQHPYREWIDKIRIRLDDIPQTPASAPLLLGRNELMRVFGFSREDVERILKS 484
Cdd:COG0070 404 RELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLLLLL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 485 MAYQGQDPVMSMGNDAPLACLSERPQMLYDYFRQLFAQVTNPPIDPIREAMVTSLVSFIGPRPDLLNIMAVNPPVRLEVE 564
Cdd:COG0070 484 LAEALEEEEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLLLLLLLEELLLLE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 565 QPVLTGAqMERIRAIADFTDGKFHSKEIDITYPLAWGREAIEARLASIRAAAVDAVRSGINILILTDRKVSRERVAIPAL 644
Cdd:COG0070 564 LLLLLLA-LALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRDSALLLALLPAL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 645 LATSAVHQCLVEEGLRTSTGLVVETGSARSVHDFAVLGGYGAEAVHPYLALAVVESLAKN----EEERAKYVDNYLHAIM 720
Cdd:COG0070 643 LALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLayalLGLLEAAAYKAKAALK 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 721 KGLNKIMARMGISTYMSYIGAQIFEAVGLKKSFIDQYFTNTPSPVEGLDLFDVAGEAVTVHKRAFEAIERKVIPLAAGGQ 800
Cdd:COG0070 723 AGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAAAAAALALGGGGG 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 801 YMYRQGGEHHLWTPDAVVHLQRAVREGSWAEYQTYAGLINNQARDLLTIRGLFEFVPGKAIPLESVESEASIIRRFSTAA 880
Cdd:COG0070 803 GGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEPEEEIVKRFATGA 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 881 MSVGAISTEAHVTMAVAMNRMKGASNSGEGGEDVRRnapvttetslrailgddvevDYPLHPGDSLRSRVRQVASGRFGV 960
Cdd:COG0070 883 MSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGR--------------------EDPLRNGDSRRSAIKQVASGRFGV 942
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 961 TTDYLAHGDLIQIKMAQGAKPGEGGQLPGKKVSKYIGMLRHSLPGVGLVSPPPHHDIYSIEDLAQLILDLKYANPHAGIG 1040
Cdd:COG0070 943 TSEYLVNADEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARIS 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1041 VKLVSQAGIGTVAAGVAKCKADHIVVSGHDGGTGAAPATSIKHAGSAWEIGLAEVEQTLVMNNLRGRVRLQVDGQIKTGR 1120
Cdd:COG0070 1023 VKLVSEVGVGTIAAGVAKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGR 1102
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1121 DVVIGAMLGADEFGFGTTPLVAMGCLMMRKCQKNTCPAGIATQDPALRRQFEGRPEHVENYFHFVAREVREIMAQLGVAK 1200
Cdd:COG0070 1103 DVVIAALLGAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRT 1182
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1201 FDDLIGHVEYLRKRSGLDGLKAAKLSLEKILYKLPNPKGFPLLSTEPQDHELEKAFDLRYAAELSEALKAKRPMRVQTRV 1280
Cdd:COG0070 1183 LDEEIGRRDLLLVRRAVDHWKAKGLDLSPLLYKPDVPADVPRYCTEEQNHGLEGALDRELIEDARPAIENGEPVELEYPI 1262
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1281 GNTDRAVGTMLSG-IAAQ-EAQGeLPDDFALFELVGTAGQSFGAFLGKGVSLRLTGGANDYVGKGLSGGSIAVKKSPSFD 1358
Cdd:COG0070 1263 RNTDRSVGTRLSGeIAKRyGNEG-LPEDTITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGST 1341
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1359 GRPNENVIAGNACLYGATSGEAFISGVVGERFAVRNSGASTVAEGCGDHGCEYMTGGTAVILGRTGRNFAAGMSGGIAYV 1438
Cdd:COG0070 1342 FVAEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYV 1421
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1439 WDPNDELAEKMSDGAFELSHVLPAAeqgsdeplhygqkDEVLLKRLVERHAELTGSPTAREMLADWPAALGRFTKVFPLE 1518
Cdd:COG0070 1422 LDEDGDFEDRCNPEMVELERLDEEE-------------DEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKD 1488
|
1530
....*....|..
gi 2553857559 1519 YKHALASLKKEE 1530
Cdd:COG0070 1489 YKRVLEAIAEAE 1500
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
645-1393 |
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: 847.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 645 LATSAVHQCLVEEGLRTSTGLVVETGSARSVHDFAVLGGYGAEAVHPYLALAVVESLAKNEEE---RAKYVDNYLHAIMK 721
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGGLLgldLEEAVKNYIKAIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 722 GLNKIMARMGISTYMSYIGAQIFEAVGLKKSFIDqyftntpspvegLDLFDVAgeavTVHKRAFeaieRKVIPLaaGG-- 799
Cdd:COG0069 81 GLLKIMSKMGISTLASYRGAQIFEAVGLSRELVD------------IGIADVL----TQHRHAI----LRNLPV--GGry 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 800 ------------QYMYRQGGEHHLWTPDAVVHLQRAVRegSWAEYQTYAGLINNQARDLLTIRGLFEFVPG-KAIPL-ES 865
Cdd:COG0069 139 ryrfesigpeirQYFFESDGEEHPFNRETRSLLYQAAK--NEEDYKPFGTLVDYQPGYEWTLRSLFPFKADrPPIPIgEP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 866 VESEASIIRRFSTAAMSVGAISTEAHVTMAVAMNRMKGASNSGEGGEDvrrnapvttetslrailgddvevdyPLHPGDS 945
Cdd:COG0069 217 VEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGES-------------------------PYHLGDG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 946 LRSRVRQVASGRFGVTTD---YLAHGDLIQIKMAQGAKPGEGGQLPGKKVSKYIGMLRHSLPGVGLVSPPPHHDIYSIED 1022
Cdd:COG0069 272 GGDAIKQIASGRFGVRDEdgeYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1023 LAQLILDLKYANPHAGIGVKLVSQAGIGTVAA--GVAK--CKADHIVVSGHDGGTGAAPATSIKHAGSAWEIGLAEVEQT 1098
Cdd:COG0069 352 LAQLIFDLRELNPGAPVGVKLVSGAGVGTIAAckGVAKtgAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQT 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1099 LVMNNLRGRVRLQVDGQIKTGRDVVIGAMLGADEFGFGTTPLVAMGCLMMRKCQKNTCPAGIATQDPALRRQF--EGRPE 1176
Cdd:COG0069 432 LVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFvvEGKPE 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1177 HVENYFHFVAREVREIMAQLGVAKFDDLIGHVEYLRKRSGlDGLKAAKLSLEKILYKLPNPKGFPLLSTEPQDHELEKAF 1256
Cdd:COG0069 512 RVVNYFRFTAEEVREILAALGVRSPDELIGRHDLLRVRDG-EHWKAKGLDLSPLLYKPELPEGVPRRCQEEQDHGLDKAL 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1257 DLRYAAELSEALKAKRPMRVQTRVGNTDRAVGTMLSG-IAAQEAQGELPDDFALFELVGTAGQSFGAFLGKGVSLRLTGG 1335
Cdd:COG0069 591 DLELIAAAAAAAEEGKPVVLITNIRNNNRRVGGMLSGeIAKRYGGAGLPDDTIILGFAGGAGQSFGAFGAGGGLLLLEGD 670
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 2553857559 1336 ANDYVGKGLSGGSIAVKKSPSFDGRPNENVIAGNACLYGATSGEAFISGVVGERFAVR 1393
Cdd:COG0069 671 DNDYVGKGGGGGGIIVPPPPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
17-440 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 702.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 17 CGVGFIAHIKGQKSHSIVSQALDVLKNLRHRGAVGADPLQGDGAGILIQIPDQLYRDDMMNQGVKLPPAGEYGVGMVFLP 96
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 97 QEAASRHACEEEIERAVAAEGQMILGWRDVPIDRSMpMSPVVREKEPVIRQVFIGHSPDvLVTDALERKLYIIRKRSSIA 176
Cdd:pfam00310 81 QDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSV-LGEAALESEPQIEQVFVGSPAG-KSEDDFERKLYVARKRIEKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 177 IANLHLKHckEFYICSCSARTVVYKGQLLATQVGIYYRDLQDARCISALAMIHQRFSTNTFPQWQLAHPFRYIAHNGEIN 256
Cdd:pfam00310 159 IGVEGGDK--DFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 257 TLRGNFNWILAREKHISSPVLGDDLKKLWPLIFQGQSDSASFDNAFELLTMAGYSLAQAALMLIPEAWEKNKTMNPRLRA 336
Cdd:pfam00310 237 TLRGNRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGGRSLPEALMMLIPEAWQNNPSMDPEKRA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 337 LYEYNAAMMEPWDGPAAVAFTNGRQLGAILDRNGLRPARYLETKDDLVILASESGAAVIDESRIRRRWRLEPGKILLLDL 416
Cdd:pfam00310 317 FYEYHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDL 396
|
410 420
....*....|....*....|....
gi 2553857559 417 EQGRIIGNDEVKGSLAAQHPYREW 440
Cdd:pfam00310 397 EEGRIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
17-435 |
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: 688.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 17 CGVGFIAHIKGQKSHSIVSQALDVLKNLRHRGAVGADPLQGDGAGILIQIPDQLYRDDMMNQGVKLPPAGEYGVGMVFLP 96
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 97 QEAASRHACEEEIERAVAAEGQMILGWRDVPIDRSMpMSPVVREKEPVIRQVFIGhSPDVLVTDALERKLYIIRKRSSIA 176
Cdd:cd00713 81 RDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSV-LGPTARATEPLIEQVFVG-APSGDDGEAFERKLYLLRKRIEKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 177 IANLHlkhcKEFYICSCSARTVVYKGQLLATQVGIYYRDLQDARCISALAMIHQRFSTNTFPQWQLAHPFRYIAHNGEIN 256
Cdd:cd00713 159 IRAAD----EDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEIN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 257 TLRGNFNWILAREKHISSPVLGDDLKKLWPLIFQGQSDSASFDNAFELLTMAGYSLAQAALMLIPEAWEKNKTMNPRLRA 336
Cdd:cd00713 235 TIRGNRNWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVRSGRSLPEAMMMLIPEAWQNNPTMDPELRA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 337 LYEYNAAMMEPWDGPAAVAFTNGRQLGAILDRNGLRPARYLETKDDLVILASESGAAVIDESRIRRRWRLEPGKILLLDL 416
Cdd:cd00713 315 FYEYHSSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDL 394
|
410
....*....|....*....
gi 2553857559 417 EQGRIIGNDEVKGSLAAQH 435
Cdd:cd00713 395 EEGRILDDEEIKDQLAKRH 413
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
820-1198 |
4.15e-161 |
|
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: 491.08 E-value: 4.15e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 820 LQRAVREGSWAEYQTYAGLINNQARdLLTIRGLFEFVPGK-AIPLESVESEASIIRRFSTAAMSVGAISTEAHVTMAVAM 898
Cdd:pfam01645 11 LQIAVQVESYPSYDKYREPLNERVP-IGALRDLLEFDFAEdPIPLEEVEPALEIKTRFCTGAMSYGALSEEAHEALAKAM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 899 NRMKGASNSGEGGEDVRRNAPvttetslrailGDDVevdyplhpgdslrsRVRQVASGRFGVTTDYLAHGDLIQIKMAQG 978
Cdd:pfam01645 90 NRLGTKSNTGEGGEDPERLKY-----------ADNI--------------AIKQVASGRFGVTPEYLNNADAIEIKIAQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 979 AKPGEGGQLPGKKVSKYIGMLRHSLPGVGLVSPPPHHDIYSIEDLAQLILDLKYANPHAGIGVKLVSQAGIGTVAAGVAK 1058
Cdd:pfam01645 145 AKPGEGGHLPGEKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1059 CKADHIVVSGHDGGTGAAPATSIKHAGSAWEIGLAEVEQTLVMNNLRGRVRLQVDGQIKTGRDVVIGAMLGADEFGFGTT 1138
Cdd:pfam01645 225 AGADIILIDGYDGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTA 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2553857559 1139 PLVAMGCLMMRKCQKNTCPAGIATQDPALRRQ--FEGRPEHVENYFHFVAREVREIMAQLGV 1198
Cdd:pfam01645 305 ALIALGCIMCRVCHTNTCPVGVATQDPELRKRldFEGAPERVVNYFRFLAEEVRELLAALGI 366
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
466-749 |
1.51e-144 |
|
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: 443.36 E-value: 1.51e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 466 ELMRVFGFSREDVERILKSMAYQGQDPVMSMGNDAPLACLSERPQMLYDYFRQLFAQVTNPPIDPIREAMVTSLVSFIGP 545
Cdd:pfam04898 1 RRQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 546 RPDLLNIMAVNPPvRLEVEQPVLTGAQMERIRAIADFtdgKFHSKEIDITYPlawgreAIEARLASIRAAAVDAVRSGIN 625
Cdd:pfam04898 81 EGNLLEETPEHCR-RLELPSPILTNEELEKLRSLKGP---GFKVATLDITFD------GLEAALERLCEEAEEAVRDGAN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 626 ILILTDRKVSRERVAIPALLATSAVHQCLVEEGLRTSTGLVVETGSARSVHDFAVLGGYGAEAVHPYLALAVVESLAKN- 704
Cdd:pfam04898 151 ILILSDRGVDADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREg 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2553857559 705 -----EEERAKYVDNYLHAIMKGLNKIMARMGISTYMSYIGAQIFEAVGL 749
Cdd:pfam04898 231 kgkltDEDLEEAVKNYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGL 280
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
811-1204 |
6.72e-144 |
|
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: 446.22 E-value: 6.72e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 811 LWTPDAVVHLQRAVReGSWAEYQTYAGLINNQARDLLTIRGLFEF--VPGKAIPLESVESEASII------------RRF 876
Cdd:cd02808 2 LLEIERLEEIQYFVF-NRAERYGVYNRAGNSRGRPFGTLRDLLEFgaQLAKHPLEPDEEVDDRVTigpnaekplkldSPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 877 STAAMSVGAISTEAHVTMAVAMNRMKGASNSGEGGEDvrrnapvttetslrailgddvevDYPLHPGDSLrsrVRQVASG 956
Cdd:cd02808 81 NISAMSFGALSKEAKEALAIGAALAGTASNTGEGGEL-----------------------PEEREGGGDI---IKQVASG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 957 RFGVTTDYLAHGDLIQIKMAQGAKPGEGGQLPGKKVSKYIGMLRHSLPGVGLVSPPPHHDIYSIEDLAQLILDLKYANPH 1036
Cdd:cd02808 135 RFGVRPEYLNKADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGVDLISPPPHHDIYSIEDLAQLIEDLREATGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1037 AGIGVKLVSQAGIGTVAAGVAKCKADHIVVSGHDGGTGAAPATSIKHAGSAWEIGLAEVEQTLVMNNLRGRVRLQVDGQI 1116
Cdd:cd02808 215 KPIGVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTGAAPLTFIDHVGLPTELGLARAHQALVKNGLRDRVSLIASGGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1117 KTGRDVVIGAMLGADEFGFGTTPLVAMGCLMMRKCQKNTCPAGIATQDPALRRQ--FEGRPEHVENYFHFVAREVREIMA 1194
Cdd:cd02808 295 RTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCPVGVATQDPELRRRldVEGKAERVANYLKSLAEELRELAA 374
|
410
....*....|
gi 2553857559 1195 QLGVAKFDDL 1204
Cdd:cd02808 375 ALGKRSLELL 384
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1256-1516 |
3.51e-117 |
|
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: 368.39 E-value: 3.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1256 FDLRYAAELSEALKAKR-PMRVQTRVGNTDRAVGTMLSG-IAAQEAQGELPDDFALFELVGTAGQSFGAFLGKGVSLRLT 1333
Cdd:cd00982 1 LDDKLIADAEPALIENGePVTLEYPIRNTDRAVGTMLSGeIAKRYGEEGLPEDTIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1334 GGANDYVGKGLSGGSIAVKKSPSFDGRPNENVIAGNACLYGATSGEAFISGVVGERFAVRNSGASTVAEGCGDHGCEYMT 1413
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1414 GGTAVILGRTGRNFAAGMSGGIAYVWDPNDELAEKMSDGAFELSHVLPAaeqgsdeplhygqKDEVLLKRLVERHAELTG 1493
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDA-------------EDEEQLKELIEEHVEYTG 227
|
250 260
....*....|....*....|...
gi 2553857559 1494 SPTAREMLADWPAALGRFTKVFP 1516
Cdd:cd00982 228 SEKAKEILANWEAYLKKFVKVIP 250
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1280-1465 |
1.12e-90 |
|
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: 292.01 E-value: 1.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1280 VGNTDRAVGTMLSGIAAQE--AQGeLPDDFALFELVGTAGQSFGAFLGKGVSLRLTGGANDYVGKGLSGGSIAVKKSPSF 1357
Cdd:pfam01493 3 IRNTDRSVGTILSGEIAKRygEDG-LPDDTITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPAES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1358 DGRPNENVIAGNACLYGATSGEAFISGVVGERFAVRNSGASTVAEGCGDHGCEYMTGGTAVILGRTGRNFAAGMSGGIAY 1437
Cdd:pfam01493 82 TFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGIAY 161
|
170 180
....*....|....*....|....*...
gi 2553857559 1438 VWDPNDELAEKMSDGAFELSHVLPAAEQ 1465
Cdd:pfam01493 162 VLDEDGDFPEKLNKEMVELERVTDEDEE 189
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1285-1440 |
3.90e-58 |
|
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: 197.02 E-value: 3.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1285 RAVGTMLSGIAAQeaQGELPDDFALFELVGTAGQSFGAFLgKGVSLRLTGGANDYVGKGLSGGSIAVKKSPSfdgrpNEN 1364
Cdd:cd00504 1 RAVGTRGSRYIGK--RPGLPEDTVEIIINGSAGQSFGAFM-AGGTITVEGNANDYVGKGMSGGEIVIHPPAG-----DEN 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2553857559 1365 VIAGNACLYGATSGEAFISGVVGERFAVRNSGASTVAEGCGD-HGCEYMTGGTAVILGRTGRNFAAGMSGGIAYVWD 1440
Cdd:cd00504 73 GIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
206-412 |
2.18e-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: 131.80 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 206 ATQVGIYYRDLQDARCISALAMIHQRFSTNTFPQWQLAHPFR------YIAHNGEINTLRGNFNWILARekhisspvlgd 279
Cdd:cd00352 51 AGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEAR----------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 280 dlkklwPLIFQGQSDSASFDNAFELLTMAGYsLAQAALMLIPEaweknktmnprlralyeynaammepWDGPAAVAFTNG 359
Cdd:cd00352 120 ------GYRFEGESDSEVILHLLERLGREGG-LFEAVEDALKR-------------------------LDGPFAFALWDG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2553857559 360 --RQLGAILDRNGLRPARYLETKDDLVILASESGAavIDESRIRRRWRLEPGKIL 412
Cdd:cd00352 168 kpDRLFAARDRFGIRPLYYGITKDGGLVFASEPKA--LLALPFKGVRRLPPGELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
199-409 |
6.68e-10 |
|
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: 61.52 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 199 VYKGQLLATQVGIYYRdLQDARciSALAMIHQRFSTNTFPQWQLAHPFRY----IAHNGEINtlrgNFNWIlaREKhiss 274
Cdd:cd01907 56 VFKGVGYPEDIARRYD-LEEYK--GYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEIS----NYGSN--REY---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 275 pvlgddLKKLwPLIFQGQSDSASFDNAFELLtMAGYSLAQAALMLIPEAWEKNKTMNPRLRalYEYNAAMMepwDGPAAV 354
Cdd:cd01907 123 ------LERF-GYKFETETDTEVIAYYLDLL-LRKGGLPLEYYKHIIRMPEEERELLLALR--LTYRLADL---DGPFTI 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2553857559 355 AFTNGRQLGAILDRNGLRPArYLETKDDLVILASE-SGAAVIDESRIRRRWRLEPG 409
Cdd:cd01907 190 IVGTPDGFIVIRDRIKLRPA-VVAETDDYVAIASEeCAIREIPDRDNAKVWEPRPG 244
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1314-1445 |
3.99e-09 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1314 GTAGQSFGAFLgKGVSLRLTGGANDYVGKGLSGGSIavkkspsfdgrpnenVIAGNA------CLYGATSG----EAFIS 1383
Cdd:COG2218 88 GDVGMYLGAGM-KGGKITVNGNAGSFAGAEMKGGEI---------------EINGNAgdflgaAYRGDWRGmsggTIIVK 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2553857559 1384 GVVGERFAVRNSGASTVAEG-CGDHGCEYMTGGTAVILGRTGRNFAAGMSGGIAYVWDPNDEL 1445
Cdd:COG2218 152 GNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPEEL 214
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1310-1438 |
2.18e-07 |
|
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown function found in the large subunit of glutamate synthase, which is encoded by gltB and found in most bacteria and eukaryotes. It is predicted to be homologous to the C-terminal domain of glutamate synthase based upon sequence similarity coupled with genome organization data, showing that this domain is found in a gene cluster with other domains of Glts, which are annotated. This domain is found primarily in archaea, but is also present in a few bacteria, likely as a result of lateral gene transfer.
Pssm-ID: 238481 [Multi-domain] Cd Length: 232 Bit Score: 53.46 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1310 FELVGTAGQSFGAFLGKGVSlRLTGGANDYVGKGLSGGSIAVKKSpsfdgrpnenviAGNACLYGATSGEAFISGVVGER 1389
Cdd:cd00981 49 INIYGVPGNDLGAFMSGPTI-IVYGNAQDDVGNTMNDGKIVIHGS------------AGDVLGYAMRGGKIFIRGNAGYR 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2553857559 1390 FAVR------NSGASTVAEGCGDHGCEYMTGGTAVILG------RTGRNFAAGMSGGIAYV 1438
Cdd:cd00981 116 VGIHmkeykdKVPVLVIGGTAGDFLGEYMAGGVIIVLGlgtdeePVGRYIGTGMHGGVIYI 176
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1314-1435 |
3.86e-05 |
|
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: 46.19 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1314 GTAGQSFGAFLgKGVSLRLTGGANDYVGKGLSGGSIAVKkspsfdgrpnenviaGNA-----CLY-----GATSGEAFIS 1383
Cdd:cd00980 46 GDVGMYVGAGM-KGGKLVVEGNAGSWAGCEMKGGEITIK---------------GNAgdyvgSAYrgdwrGMSGGTITIE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2553857559 1384 GVVGERFAVRNSGASTVAEG-CGDHGCEYMTGGTAVILGRTGRNFAAGMSGGI 1435
Cdd:cd00980 110 GNAGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGT 162
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
632-732 |
8.81e-05 |
|
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: 46.56 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 632 RKVSRERVAIPALLATSAVHQCLVEEGLRTSTGLVVeTGSARSVHDFAVLGGYGAEAVH----PYLALAVV--------- 698
Cdd:pfam01645 243 PKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIA-DGGLRTGADVAKAAALGADAVYigtaALIALGCImcrvchtnt 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2553857559 699 ---------ESLAKNE--EERAKYVDNYLHAIMKGLNKIMARMGI 732
Cdd:pfam01645 322 cpvgvatqdPELRKRLdfEGAPERVVNYFRFLAEEVRELLAALGI 366
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1326-1425 |
3.13e-03 |
|
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran dehydrogenase, an enzyme that catalyzes the first step in methane formation from CO2 in methanogenic archaea, hyperthermophiles and bacteria. There are two isoenzymes, a tungsten-containing isoenzyme (Fwd) and a molybdenum-containing isoenzyme (Fmd). The subunits C of both isoenzymes (FwdC/FmdC) are characterized by a repeated GXXGXXXG motif.
Pssm-ID: 238480 [Multi-domain] Cd Length: 203 Bit Score: 40.80 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2553857559 1326 KGVSLRLTGGANDYVG-------KGLSGGSIAVKKSpsfdgrpnenviAGNACLYGATSGEAFISGVVGERFAVRNSGAS 1398
Cdd:cd00980 76 KGGEITIKGNAGDYVGsayrgdwRGMSGGTITIEGN------------AGDRLGERMRRGEILIKGDAGIFAGIRMNGGT 143
|
90 100
....*....|....*....|....*...
gi 2553857559 1399 TVAEG-CGDHGCEYMTGGTAVILGRTGR 1425
Cdd:cd00980 144 IIVRGdAGAHPGYEMKRGTIVIGGEIEE 171
|
|
| |
