|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
75-1564 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1551.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 75 KQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLP 154
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 155 ELgdYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQ 232
Cdd:PRK11750 82 KN--YAVGMVFLnqDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 233 VFVLRKRAShELIKPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVL 312
Cdd:PRK11750 160 LFIARRRIE-KRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 313 AHNGEINTLRGNVNLMKAREGVMQSDLFGDqLKKLYPVVEPNLSDSGSFDCVLEFLtMASDRSLPESVMTMVPEAWQNDK 392
Cdd:PRK11750 239 AHNGEINTITGNRQWARARAYKFQTPLIPD-LQEAAPFVNETGSDSSSLDNMLELL-LAGGMDLFRAMRLLVPPAWQNNP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 393 TMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKP 472
Cdd:PRK11750 317 DMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 473 GRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQkitldeirnaNVLNTPPVDELAKLPASERGiFDPRL-----SLFG 547
Cdd:PRK11750 397 GELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEK----------NVRRLVPFEELPDEQVGSRE-LDDDTlksyqKQFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 548 YSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQP 627
Cdd:PRK11750 466 YSFEELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 628 SAQQVHRIWLTNPILSIPD-TQLLKRNTHrGWRTKVLDITfqYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 706
Cdd:PRK11750 546 TEGHAHRVIFKSPVLSYSDfKQLTTLDEE-HYRADTLDLN--YDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIA 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 707 iDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVNdk 786
Cdd:PRK11750 623 -KGRLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYR-- 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 787 QIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKAT 866
Cdd:PRK11750 700 QVMLNYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARK 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 867 PdtriLRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTtLDSVKKCALRGQLEFVTDRQSIDISEVEPA 946
Cdd:PRK11750 780 P----IDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKL-VNERPVATLRDLLALKPADNPIPLDEVEPA 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 947 SEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVTASYLANAD 1026
Cdd:PRK11750 855 EELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAE 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1027 DLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGV 1106
Cdd:PRK11750 930 VLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGV 1009
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1107 GVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLG 1186
Cdd:PRK11750 1010 GTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILG 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1187 ADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKK-FTGKPEHVINFFFMLAEDIRKIMAGLGIRKFQDLIGRT 1265
Cdd:PRK11750 1090 AESFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGRT 1169
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1266 DLLRVASQRDAKASNLDLKLLLQPAlELRPGtnivggsvKQDFQLEKRS---DNELIakAQQIFSGADDNV------TVK 1336
Cdd:PRK11750 1170 DLLEELEGETAKQQKLDLSPLLETA-EPPAG--------KALYCTEERNppfDKGLL--NEQMLQQAKPAIeakqggEFW 1238
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1337 MRIHNEERAFGSTLSYHIACKYGEAGLpAGKSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQD 1416
Cdd:PRK11750 1239 FDIRNTDRSVGARLSGEIARRHGNQGM-ADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPPV 1317
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1417 TVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGI 1496
Cdd:PRK11750 1318 GSAFRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGGF 1397
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24665539 1497 AYVYDLDGSFKPKVNPESVELLPLE---IEKDVLlvKELLADFIEKTGSKVAKELLDNWAEAQGKFVKVFP 1564
Cdd:PRK11750 1398 AYVLDEDGDFVDRVNHELVEILRVEdleIHREHL--RGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
68-1583 |
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: 1247.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 68 MPWEAPGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALA 147
Cdd:COG0070 7 MGAAAAAGGGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 148 KQGVTLPELGDYATGIF-YLDEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDE 226
Cdd:COG0070 87 AGGGAFFAAGLAAGLLAlAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 227 KAFERQVFVLRKRASHELikpgRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERA 306
Cdd:COG0070 167 LRRLALLRRRRRRRRREF----RRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 307 HPLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASDRSLPESVMTMVPE 386
Cdd:COG0070 243 FAPRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 387 AWQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTL 466
Cdd:COG0070 323 APAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 467 KSRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQKITLDEIRNANVLNTPPVDElaklpasergiFDPRLSLF 546
Cdd:COG0070 403 GRELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEE-----------LLQEREAE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 547 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLL- 625
Cdd:COG0070 472 LEQELLLLLLLLLAEALEEEEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLl 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 626 QPSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGA 705
Cdd:COG0070 552 LLLLLEELLLLELLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 706 GIDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVND 785
Cdd:COG0070 632 SALLLALLPALLALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 786 KQIYAAYAQAIdTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 865
Cdd:COG0070 712 AAAYKAKAALK-AGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 866 TPDTRILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEVEP 945
Cdd:COG0070 791 AAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEP 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 946 ASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYLNQDPNNSRRSAIKQVASGRFGVTASYLANA 1025
Cdd:COG0070 871 EEEIVKRFATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNA 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1026 DDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVG 1105
Cdd:COG0070 951 DEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVG 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1106 VGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALL 1185
Cdd:COG0070 1031 VGTIAAGVAKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALL 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1186 GADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKKFTGKPEHVINFFFMLAEDIRKIMAGLGIRKFQDLIGRT 1265
Cdd:COG0070 1111 GAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRR 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1266 DLLRVASQRD-AKASNLDL-KLLLQPAL-ELRPGTNivggSVKQDFQLEKRSDNELIAKAQQ-IFSGAddNVTVKMRIHN 1341
Cdd:COG0070 1191 DLLLVRRAVDhWKAKGLDLsPLLYKPDVpADVPRYC----TEEQNHGLEGALDRELIEDARPaIENGE--PVELEYPIRN 1264
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1342 EERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQDTVPFE 1421
Cdd:COG0070 1265 TDRSVGTRLSGEIAKRYGNEGLPED-TITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFV 1343
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1422 SHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYD 1501
Cdd:COG0070 1344 AEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLD 1423
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1502 LDGSFKPKVNPESVELLPLEIEKDVLLVKELLADFIEKTGSKVAKELLDNWAEAQGKFVKVFPYEYQKALKDMAEQQAVE 1581
Cdd:COG0070 1424 EDGDFEDRCNPEMVELERLDEEEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAG 1503
|
..
gi 24665539 1582 QP 1583
Cdd:COG0070 1504 LD 1505
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
73-1582 |
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: 1199.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 73 PGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVT 152
Cdd:COG0067 8 PAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 153 LPELGDYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFE 230
Cdd:COG0067 88 LPEPGEYAVGMVFLpqDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 231 RQVFVLRKRASHELIKPG---RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAH 307
Cdd:COG0067 168 RKLYVARKRIEKAIRALGlddEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 308 PLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEA 387
Cdd:COG0067 248 PFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVL-GGRSLPHAMMMLIPEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 388 WQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLK 467
Cdd:COG0067 327 WENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 468 SRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWL-QQKITLDEIRNANVLNTPPVDELAKlpasergifdpRLSLF 546
Cdd:COG0067 407 GRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLkENRIRLEDLPEPEEEPAPDDDLLLR-----------RQQAF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 547 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQ 626
Cdd:COG0067 476 GYTEEEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 627 PSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 706
Cdd:COG0067 556 EEEEARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 707 IDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELA-QALRDDGVIAPEVND 785
Cdd:COG0067 636 DSDAAPAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALElLLDGLLLGLEDAAAA 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 786 KQIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 865
Cdd:COG0067 716 AAAKKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEP 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 866 TPDT--RILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEV 943
Cdd:COG0067 796 GGLLlgLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 944 EPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRylnqDPNNSRRSAIKQVASGRFGVTASYLA 1023
Cdd:COG0067 876 EEEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1024 NADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSE 1103
Cdd:COG0067 952 AAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1104 VGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAA 1183
Cdd:COG0067 1032 AAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAA 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1184 LLGADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKKFTGKPEHVINFFFMLAEDIRKIMAGLGIRkfQDLIG 1263
Cdd:COG0067 1112 ALGAGALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELL--RLLEE 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1264 RTDLLRVASQRDAKASNLDLKLLLQPALELRPGTNIVGGSVKQDFQLEKRSDNELIAKAQQIFSGADDNVTVKMRIHNEE 1343
Cdd:COG0067 1190 GLGVVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRA 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1344 RAFGSTLSYHIACKYGEAGLPAGKSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQDTVPFESH 1423
Cdd:COG0067 1270 RRRGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1349
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1424 LNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYDLD 1503
Cdd:COG0067 1350 GGGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDL 1429
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665539 1504 GSFKPKVNPESVELLPLEIEKDVLLVKELLADFIEKTGSKVAKELLDNWAEAQGKFVKVFPYEYQKALKDMAEQQAVEQ 1582
Cdd:COG0067 1430 DVVLDEEEEEELEELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAA 1508
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
717-1454 |
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: 846.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 717 LALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGviAPEVNDKQIYAAYAQAI 796
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGG--LLGLDLEEAVKNYIKAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 797 DTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAkcfrgtqsriggVTLEilakEGLQRYQLTYgkatpdTRILRNPG 876
Cdd:COG0069 79 EKGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVD------------IGIA----DVLTQHRHAI------LRNLPVGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 877 QYHWRH--------------GGEAHINEPSSIGSLQEAAvnKNLDAFEAFKkTTLD--SVKKCALRGQLEFVTDRQSIDI 940
Cdd:COG0069 137 RYRYRFesigpeirqyffesDGEEHPFNRETRSLLYQAA--KNEEDYKPFG-TLVDyqPGYEWTLRSLFPFKADRPPIPI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 941 SE-VEPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVT- 1018
Cdd:COG0069 214 GEpVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRd 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1019 --ASYLANADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARI 1096
Cdd:COG0069 289 edGEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1097 SVKLVSEVGV----GVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQ 1172
Cdd:COG0069 369 GVKLVSGAGVgtiaACKGVAKTGAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1173 LRTGFDVVVAALLGADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKKFT--GKPEHVINFFFMLAEDIRKIM 1250
Cdd:COG0069 449 LKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVREIL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1251 AGLGIRKFQDLIGRTDLLRVASQRDAKASNLDLKLLLQP--ALELRPGTNIvggsVKQDFQLEKRSDNELIAKAQQIFSG 1328
Cdd:COG0069 529 AALGVRSPDELIGRHDLLRVRDGEHWKAKGLDLSPLLYKpeLPEGVPRRCQ----EEQDHGLDKALDLELIAAAAAAAEE 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1329 ADDNVTVkMRIHNEERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGG 1408
Cdd:COG0069 605 GKPVVLI-TNIRNNNRRVGGMLSGEIAKRYGGAGLPDD-TIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGG 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 24665539 1409 NVVIMPQDTVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVR 1454
Cdd:COG0069 683 GIIVPPPPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1622-2105 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 826.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1622 KTRGFVKYKRESAPYRDAGERQKDWDEVY-NFPhvRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQ 1700
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKEFYePFS--EEQAKIQAARCMDCGIPFCH---WGCPVHNYIPEWNDLVYRGRWE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1701 EALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLA 1780
Cdd:PRK12810 78 EAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1781 ASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTG 1860
Cdd:PRK12810 158 AADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1861 STWPRDLPLANRDLKGIHFAMEFLEAQQKKQLG-GKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEP 1939
Cdd:PRK12810 238 AYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGdETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDIMPMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1940 PQKRAQDNPWPQWPKVFRVDYGHEEvklkwGkDPRQYCTTTKEFVGENGAIKGVNTVEVEWtktetGQWRMQEVAGSEKY 2019
Cdd:PRK12810 318 PSRRNKNNPWPYWPMKLEVSNAHEE-----G-VEREFNVQTKEFEGENGKVTGVKVVRTEL-----GEGDFEPVEGSEFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2020 FPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTG 2099
Cdd:PRK12810 387 LPADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMG 466
|
....*.
gi 24665539 2100 RpSGLP 2105
Cdd:PRK12810 467 S-TALP 471
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
1622-2105 |
0e+00 |
|
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.
Pssm-ID: 162300 [Multi-domain] Cd Length: 485 Bit Score: 771.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1622 KTRGFVKYKRESAPYRDAGERQKDWDEVYNfPHVRKNLKVQAARCMECGVPFCQsNSTGCPLGNIIPKWNDLVFHGEWQE 1701
Cdd:TIGR01317 1 KPTGFLEYKRRKPTERDPRTRLKDWKEFTN-PFDKESAKYQAARCMDCGTPFCH-NDSGCPLNNLIPEFNDLVFRGRWKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1702 ALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLAA 1781
Cdd:TIGR01317 79 ALDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1782 SQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGS 1861
Cdd:TIGR01317 159 ADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1862 TWPRDLPLANRDLKGIHFAMEFLEAQQKKQLGGK---NDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPE 1938
Cdd:TIGR01317 239 TKPRDLPIPGRELKGIHYAMEFLPSATKALLGKDfkdIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEIMPK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1939 PPQKRAQDNPWPQWPKVFRVDYGHEEVKLKWGKDPRQYCTTTKEFVG-ENGAIKGVNTVEVEWTKTETGQWRMQEVAGSE 2017
Cdd:TIGR01317 319 PPEARAKDNPWPEWPRVYRVDYAHEEAAAHYGRDPREYSILTKEFIGdDEGKVTALRTVRVEWKKSQDGKWQFVEIPGSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2018 KYFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYL 2097
Cdd:TIGR01317 399 EVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYL 478
|
....*...
gi 24665539 2098 TGRpSGLP 2105
Cdd:TIGR01317 479 MGS-SVLP 485
|
|
| GATase_2 |
pfam00310 |
Glutamine amidotransferases class-II; |
88-504 |
0e+00 |
|
Glutamine amidotransferases class-II;
Pssm-ID: 395245 [Multi-domain] Cd Length: 420 Bit Score: 745.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:pfam00310 81 qDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 246 KPG--RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRG 323
Cdd:pfam00310 161 VEGgdKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 324 NVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASdRSLPESVMTMVPEAWQNDKTMPQEKRDFYQ 403
Cdd:pfam00310 241 NRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGG-RSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 404 WAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEK 483
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 24665539 484 KLIQDIELKAKIAKSRPHSEW 504
Cdd:pfam00310 400 RIIDDEEIKQQIASRHPYGEW 420
|
|
| GltS |
cd00713 |
Glutamine amidotransferases class-II (Gn-AT), glutamate synthase (GltS)-type. GltS is a ... |
88-499 |
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: 710.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:cd00713 81 rDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 246 KPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRGNV 325
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 326 NLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEAWQNDKTMPQEKRDFYQWA 405
Cdd:cd00713 241 NWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVR-SGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 406 ACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEKKL 485
Cdd:cd00713 320 SSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRI 399
|
410
....*....|....
gi 24665539 486 IQDIELKAKIAKSR 499
Cdd:cd00713 400 LDDEEIKDQLAKRH 413
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
1642-2096 |
0e+00 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 627.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1642 RQKDWDEVYNfPHVRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCP 1721
Cdd:COG0493 1 RIKDFREVYP-GLSEEEAIEQAARCLDCGDPPCQ---TGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1722 APCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRV 1801
Cdd:COG0493 77 APCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1802 GGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAM 1881
Cdd:COG0493 157 GGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1882 EFLEAQQKKQLggkNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEppqkraQDNPwpqwPKVFRVDYG 1961
Cdd:COG0493 237 DFLTAVNLGEA---PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTR------EEMP----ASKEEVEEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1962 HEE-VKlkwgkdpRQYCTTTKEFVG-ENGAIKGVNTVEVEWTKT-ETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTV 2038
Cdd:COG0493 304 LEEgVE-------FLFLVAPVEIIGdENGRVTGLECVRMELGEPdESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGL 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 24665539 2039 PSELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSY 2096
Cdd:COG0493 377 EEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
887-1256 |
1.19e-177 |
|
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: 545.00 E-value: 1.19e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 887 HINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEVEPASEIVKRFATGAMSFGSISLE 966
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERVPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 967 AHQTLSITMNRIGGKSNTGEGGEDSDRYLNQDpnnsrRSAIKQVASGRFGVTASYLANADDLQIKMAQGAKPGEGGELPG 1046
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYAD-----NIAIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1047 YKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGVGVVASGVAKGKAEHIVISGH 1126
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1127 DGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLGADEFGFSTAPLIVMGCTMMR 1206
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24665539 1207 KCHLNTCPVGIATQDPELRK--KFTGKPEHVINFFFMLAEDIRKIMAGLGIR 1256
Cdd:pfam01645 316 VCHTNTCPVGVATQDPELRKrlDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
917-1270 |
8.87e-162 |
|
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: 502.46 E-value: 8.87e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 917 LDSVKKCALRGQLEFVTDRQSIDISE-------------VEPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSN 983
Cdd:cd02808 31 SRGRPFGTLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPFNISAMSFGALSKEAKEALAIGAALAGTASN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 984 TGEGGEDSDRYLNqdpnnsRRSAIKQVASGRFGVTASYLANADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGV 1063
Cdd:cd02808 111 TGEGGELPEEREG------GGDIIKQVASGRFGVRPEYLNKADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1064 GLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGL 1143
Cdd:cd02808 185 DLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTGAAPLTFIDHVGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1144 PWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLGADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPE 1223
Cdd:cd02808 265 PTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCPVGVATQDPE 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 24665539 1224 L--RKKFTGKPEHVINFFFMLAEDIRKIMAGLGIRKfQDLIGRTDLLRV 1270
Cdd:cd02808 345 LrrRLDVEGKAERVANYLKSLAEELRELAAALGKRS-LELLGRSDLLAL 392
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
1624-2102 |
8.00e-145 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 458.10 E-value: 8.00e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1624 RGFVKYKRESAPYRDAGERQKDWDEV---YNFPHVrknlKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQ 1700
Cdd:PRK11749 1 LKFLTTPRIPMPRQDAEERAQNFDEVapgYTPEEA----IEEASRCLQCKDAPCV---KACPVSIDIPEFIRLIAEGNLK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1701 EALRQLLQTNNFPEFTGRVCPAP--CEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEvRTGKRVAIVGSGPSG 1778
Cdd:PRK11749 74 GAAETILETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAP-KTGKKVAVIGAGPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1779 LAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLT 1858
Cdd:PRK11749 153 LTAAHRLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1859 TGSTWPRDLPLANRDLKGIHFAMEFLEAQqkKQLGGKNDIIsaAGKNVIIIGGGDTGCDCIATSLRQGAKSIT-----TF 1933
Cdd:PRK11749 233 TGAGLPRFLGIPGENLGGVYSAVDFLTRV--NQAVADYDLP--VGKRVVVIGGGNTAMDAARTAKRLGAESVTivyrrGR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1934 EILPEppqkraqdnpwpqwpKVFRVDYGHEE-VKLKWGKDPrqyctttKEFVGENGAIKGVNTVEVEWTKTETGQWRMQE 2012
Cdd:PRK11749 309 EEMPA---------------SEEEVEHAKEEgVEFEWLAAP-------VEILGDEGRVTGVEFVRMELGEPDASGRRRVP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2013 VAGSEKYFPADLILLAMGFlGPEKTVPS-ELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAAR 2091
Cdd:PRK11749 367 IEGSEFTLPADLVIKAIGQ-TPNPLILStTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAE 445
|
490
....*....|.
gi 24665539 2092 QVDSYLTGRPS 2102
Cdd:PRK11749 446 AIHEYLEGAAS 456
|
|
| gltB_C |
cd00982 |
gltb_C. This domain is found at the C-terminus of the large subunit (gltB) of glutamate ... |
1315-1564 |
2.52e-143 |
|
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: 445.05 E-value: 2.52e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1315 DNELIAKAQQIFSGADDNVTVKMRIHNEERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLK 1394
Cdd:cd00982 2 DDKLIADAEPALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPED-TIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1395 GDANDYVGKGLCGGNVVIMPQDTVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMT 1474
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1475 GGVVVILGLTGRNFAAGMSGGIAYVYDLDGSFKPKVNPESVELLPLEIEKDVLLVKELLADFIEKTGSKVAKELLDNWAE 1554
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWEA 240
|
250
....*....|
gi 24665539 1555 AQGKFVKVFP 1564
Cdd:cd00982 241 YLKKFVKVIP 250
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
542-827 |
2.24e-142 |
|
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: 443.75 E-value: 2.24e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 542 RLSLFGYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPE 621
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 622 ANLLQPSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFqynegvQGYIDAIDRICREGYAAAQAGYQLLVIS 701
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITF------DGLEAALERLCEEAEEAVRDGANILILS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 702 DRGAGiDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGviAP 781
Cdd:pfam04898 156 DRGVD-ADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREG--KG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24665539 782 EVNDKQIYAA---YAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLG 827
Cdd:pfam04898 233 KLTDEDLEEAvknYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1337-1526 |
2.39e-105 |
|
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: 334.38 E-value: 2.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1337 MRIHNEERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQD 1416
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDD-TITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1417 TVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGI 1496
Cdd:pfam01493 80 ESTFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGI 159
|
170 180 190
....*....|....*....|....*....|
gi 24665539 1497 AYVYDLDGSFKPKVNPESVELLPLEIEKDV 1526
Cdd:pfam01493 160 AYVLDEDGDFPEKLNKEMVELERVTDEDEE 189
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1641-2097 |
2.66e-90 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 309.37 E-value: 2.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1641 ERQKDWDEVYnFPHVRKNLKVQAARCMECGV-PFCQSNstgCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRV 1719
Cdd:PRK12769 203 ARKTGFDEIY-LPFRADQAQREASRCLKCGEhSICEWT---CPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1720 CPAP--CEGSCVLGISEPAVTIKNIECAIIDHAFEQGWiKPEIPEVR-TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFE 1796
Cdd:PRK12769 279 CPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGW-RPDLSQVTkSDKRVAIIGAGPAGLACADVLARNGVAVTVYD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1797 RNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKG 1876
Cdd:PRK12769 358 RHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPNEDAPG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1877 IHFAMEFLEAQQKKQLG----GKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTfeilpepPQKRAQDNpWPQW 1952
Cdd:PRK12769 438 VYDALPFLIANTKQVMGleelPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTC-------AYRRDEAN-MPGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1953 PKvfRVDYGHEE-VKLKWGKDPRQYCtttkefVGENGAIKGVNTVEVEWTKTE-TGQWRMQEVAGSEKYFPADLILLAMG 2030
Cdd:PRK12769 510 KK--EVKNAREEgANFEFNVQPVALE------LNEQGHVCGIRFLRTRLGEPDaQGRRRPVPIPGSEFVMPADAVIMAFG 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2031 FLGPEKTVPSELGLELDPRGNIKA---SNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYL 2097
Cdd:PRK12769 582 FNPHGMPWLESHGVTVDKWGRIIAdveSQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
1672-2101 |
2.75e-82 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 282.92 E-value: 2.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1672 PFCQSnstGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKNIECAIIDHAF 1751
Cdd:PRK12771 47 PPCNA---ACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1752 EQGWiKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGI 1831
Cdd:PRK12771 124 ANGW-KFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1832 EFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKkqlgGKNDIIsaaGKNVIIIGG 1911
Cdd:PRK12771 203 EVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGE----GEPPFL---GKRVVVIGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1912 GDTGCDCIATSLRQGAKSIT-----TFEILPeppqkrAQDnpwpqwpkvFRVDYGHEE-VKLKWGkdprqycTTTKEFVG 1985
Cdd:PRK12771 276 GNTAMDAARTARRLGAEEVTivyrrTREDMP------AHD---------EEIEEALREgVEINWL-------RTPVEIEG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1986 ENGAIKGVNTVEVE-WTKTETGqwRMQEVAGSEKYFPADLILLAMG---FLGPEKTVPselGLElDPRGNIKASNGQYGT 2061
Cdd:PRK12771 334 DENGATGLRVITVEkMELDEDG--RPSPVTGEEETLEADLVVLAIGqdiDSAGLESVP---GVE-VGRGVVQVDPNFMMT 407
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 24665539 2062 SNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGRP 2101
Cdd:PRK12771 408 GRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLGGEP 447
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
1630-2101 |
1.57e-79 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 271.51 E-value: 1.57e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1630 KRESAPYRDAGERQKDWDEV---YNFPHVRKnlkvQAARCMECGVPFCQSnstGCPLGNIIPKWNDLVFHGEWQEALRQL 1706
Cdd:PRK12831 7 KRVPVREQDPEVRATNFEEVclgYNEEEAVK----EASRCLQCKKPKCVK---GCPVSINIPGFISKLKEGDFEEAAKII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1707 LQTNNFPEFTGRVCP--APCEGSCVLGISEPAVTIKNIECAIIDHAFEQGwIKPEIPEVRTGKRVAIVGSGPSGLAASQQ 1784
Cdd:PRK12831 80 AKYNALPAVCGRVCPqeSQCEGKCVLGIKGEPVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1785 LNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKE-VVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQE--YDAVLLTTGS 1861
Cdd:PRK12831 159 LAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1862 TWPRDLPLANRDLKGIHFAMEFL-EAQQKKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEPP 1940
Cdd:PRK12831 239 GLPKFMGIPGENLNGVFSANEFLtRVNLMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSEEEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1941 QKRAQDnpwpqwpkvfrVDYGHEE-VKLKWGKDPrqyctttKEFVG-ENGAIKGVNTVEVEW-TKTETGQWRMQEVAGSE 2017
Cdd:PRK12831 319 PARVEE-----------VHHAKEEgVIFDLLTNP-------VEILGdENGWVKGMKCIKMELgEPDASGRRRPVEIEGSE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2018 KYFPADLILLAMGfLGPEKTVPSEL-GLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSY 2096
Cdd:PRK12831 381 FVLEVDTVIMSLG-TSPNPLISSTTkGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEY 459
|
....*
gi 24665539 2097 LTGRP 2101
Cdd:PRK12831 460 LSKKW 464
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1604-2093 |
2.04e-71 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 253.41 E-value: 2.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1604 EAIQDVVLEQKRAdrVLDKTrgfvkyKRESAPYRDAGERQKDWDEVYNfPHVRKNLKVQAARCMECG-VPFCQSNstgCP 1682
Cdd:PRK12809 157 KASSDAQPSRSAA--LLPVN------SRKGADKISASERKTHFGEIYC-GLDPQQATYESDRCVYCAeKANCNWH---CP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1683 LGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAP--CEGSCVLGISEPAVTIKNIECAIIDHAFEQGWiKPEI 1760
Cdd:PRK12809 225 LHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGW-RPDV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1761 PEVRTGK-RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHV 1839
Cdd:PRK12809 304 SKVVPRSeKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1840 GKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKKQLG----GKNDIISAAGKNVIIIGGGDTG 1915
Cdd:PRK12809 384 GRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGlpesEEYPLTDVEGKRVVVLGGGDTT 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1916 CDCIATSLRQGAKSITTfeilpeppQKRAQDNPWPQWPKVFrVDYGHEEVKLKWGKDPrQYCTTTkefvgENGAIKGVNT 1995
Cdd:PRK12809 464 MDCLRTSIRLNAASVTC--------AYRRDEVSMPGSRKEV-VNAREEGVEFQFNVQP-QYIACD-----EDGRLTAVGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1996 VEVEWTKT-ETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQYG---TSNSKVFAAGD 2071
Cdd:PRK12809 529 IRTAMGEPgPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLptqTHLKKVFAGGD 608
|
490 500
....*....|....*....|..
gi 24665539 2072 CRRGQSLVVWAITEGRQAARQV 2093
Cdd:PRK12809 609 AVHGADLVVTAMAAGRQAARDM 630
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
1641-2097 |
6.84e-69 |
|
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130383 [Multi-domain] Cd Length: 449 Bit Score: 240.16 E-value: 6.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1641 ERQKDWDEVyNFPHVRKNLKVQAARCMECGvPFCQSNSTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVC 1720
Cdd:TIGR01316 4 ERSKLFQEA-ALGYTEQLALVEAQRCLNCK-DATKPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1721 PAP--CEGSCVLG-----ISEPaVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVT 1793
Cdd:TIGR01316 82 PQErqCEGQCTVGkmfkdVGKP-VSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1794 VFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRD 1873
Cdd:TIGR01316 161 VFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1874 LKGIHFAMEFLEAQQ--KKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEPPQKRAQDnpwpq 1951
Cdd:TIGR01316 241 LCGVYSANDFLTRANlmKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAEVHCLYRRTREDMTARVEE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1952 wpkvfrVDYGHEE-VKLKWgkdprqYCTTTkEFVG-ENGAIKGVNTVEVE-WTKTETGQWRMQEVAGSEKYFPADLILLA 2028
Cdd:TIGR01316 316 ------IAHAEEEgVKFHF------LCQPV-EIIGdEEGNVRAVKFRKMDcQEQIDSGERRFLPCGDAECKLEADAVIVA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665539 2029 MGfLGPEKTVPSELGLELDPRGNIKAsNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYL 2097
Cdd:TIGR01316 383 IG-NGSNPIMAETTRLKTSERGTIVV-DEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
1566-2100 |
2.38e-66 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 241.18 E-value: 2.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1566 EYQKALKDMAEQQAVEQplksaieNGNGKHEPHIKDIEEAIQDVVLEQKRADRvldktrgfvkyKRESAPYRDAGERQKD 1645
Cdd:PRK12778 249 DFDEMLKRMGAYKTIEG-------EELLKLEERTAAWRAELRKSMKPKERTAI-----------ERVPMPELDPEYRAHN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1646 WDEVYNFPHVRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCP--AP 1723
Cdd:PRK12778 311 RFEEVNLGLTKEQAMTEAKRCLDCKNPGCV---EGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPqeKQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1724 CEGSCVLGIS-EPAVTIKNIECAIIDHAFEQGwiKPEIPEV--RTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDR 1800
Cdd:PRK12778 388 CESKCIHGKMgEEAVAIGYLERFVADYERESG--NISVPEVaeKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1801 VGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQE-YDAVLLTTGSTWPRDLPLANRDLKGIHF 1879
Cdd:PRK12778 466 IGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIASGAGLPNFMNIPGENSNGVMS 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1880 AMEFL-EAQQKKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFeilpeppQKRAQDnpwpQWP-KVFR 1957
Cdd:PRK12778 546 SNEYLtRVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIV-------YRRSEE----EMPaRLEE 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1958 VDYGHEE-VKLKWGKDPRQYCTTtkefvgENGAIKGVNTVEVEWTKTE-TGQWRMQEVAGSEKYFPADLILLAMGfLGPE 2035
Cdd:PRK12778 615 VKHAKEEgIEFLTLHNPIEYLAD------EKGWVKQVVLQKMELGEPDaSGRRRPVAIPGSTFTVDVDLVIVSVG-VSPN 687
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24665539 2036 KTVPSEL-GLELDPRGNIKAsNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGR 2100
Cdd:PRK12778 688 PLVPSSIpGLELNRKGTIVV-DEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| GXGXG |
cd00504 |
GXGXG domain. This domain of unknown function is found at the C-terminus of the large subunit ... |
1344-1501 |
1.25e-63 |
|
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: 213.20 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1344 RAFGSTLSYHIACKYGeagLPAGkSIDIFLEGSAGQSFCAFLArGVNVTLKGDANDYVGKGLCGGNVVIMPQdtvpfESH 1423
Cdd:cd00504 1 RAVGTRGSRYIGKRPG---LPED-TVEIIINGSAGQSFGAFMA-GGTITVEGNANDYVGKGMSGGEIVIHPP-----AGD 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24665539 1424 LNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGD-HGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYD 1501
Cdd:cd00504 71 ENGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
1656-2105 |
1.56e-60 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 221.53 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1656 RKNL-KVQAARCMECGVPfCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAPCEGSCVL-GIS 1733
Cdd:PRK12814 86 RQSLeRLIEQHCGDCLGP-CE---LACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRhGVD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1734 EPaVTIknieCAIIDHAFEQGWIKPE--IPEVR--TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGI 1809
Cdd:PRK12814 162 EP-VSI----CALKRYAADRDMESAEryIPERApkSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1810 PTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLeaqQK 1889
Cdd:PRK12814 237 PRFRLPESVIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL---RN 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1890 KQLGGKndiiSAAGKNVIIIGGGDTGCDCIATSLRQGAKSITtfeIL-----PEPPQKRAQDNpwpqwpkvfrvDYGHEE 1964
Cdd:PRK12814 314 VALGTA----LHPGKKVVVIGGGNTAIDAARTALRLGAESVT---ILyrrtrEEMPANRAEIE-----------EALAEG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1965 VKLKWGKDPRQYCTTtkefvgeNGAIKgVNTVEVEWTK-TETGQWRMQEVAGSEKYFPADLILLAMG-FLGPEKTVPSel 2042
Cdd:PRK12814 376 VSLRELAAPVSIERS-------EGGLE-LTAIKMQQGEpDESGRRRPVPVEGSEFTLQADTVISAIGqQVDPPIAEAA-- 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24665539 2043 GLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGRPSGLP 2105
Cdd:PRK12814 446 GIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAP 508
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
1558-2098 |
9.55e-57 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 215.96 E-value: 9.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1558 KFVKVFPYEYQKALKDMAEQQAVEQPLKSAIENGNgKHEPHIKDIEeaiQDVVLEQKRADRVLDKtrgfVKYKRESAPYR 1637
Cdd:PRK12775 234 KFACVDGPDFDGHKVDFKELHARQKRFKSQEDRAN-EDYAHVCNLE---KQLFEEGKRNYKKLKT----LVPHQTPMPER 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1638 DAGERQKDWDEVyNFPHVRKNLKVQAARCMECGVPFCQSnstGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTG 1717
Cdd:PRK12775 306 DAVERARNFKEV-NLGYSLEDALQEAERCIQCAKPTCIA---GCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICG 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1718 RVCP--APCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEvRTGKrVAIVGSGPSGLAASQQLNRAGHFVTVF 1795
Cdd:PRK12775 382 RVCPqeTQCEAQCIIAKKHESVGIGRLERFVGDNARAKPVKPPRFSK-KLGK-VAICGSGPAGLAAAADLVKYGVDVTVY 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1796 ERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQE--YDAVLLTTGSTWPRDLPLANRD 1873
Cdd:PRK12775 460 EALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGEF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1874 LKGIHFAMEFLeaQQKKQLGGKN----DIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFeilpeppqKRAQDNPW 1949
Cdd:PRK12775 540 AGQVYSANEFL--TRVNLMGGDKfpflDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCV--------YRRSEAEA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1950 PQwpKVFRVDYGHEEvklkwGKDPRQYCTTTKEFVGENGAIKGVNTVEVEWTKTETGQWRMQEVAGSEKYFPADLILLAM 2029
Cdd:PRK12775 610 PA--RIEEIRHAKEE-----GIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPTGEFKDLECDTVIYAL 682
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24665539 2030 GFLGPEKTVPSELGLELDPRGNIKASNGQYGTSNSK----VFAAGDCRRGQSLVVWAITEGRQAARQVDSYLT 2098
Cdd:PRK12775 683 GTKANPIITQSTPGLALNKWGNIAADDGKLESTQSTnlpgVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
1662-2099 |
4.38e-54 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 201.15 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1662 QAARCMECGVpfCQSNstgCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKN 1741
Cdd:PRK13984 183 EAARCVECGI--CTDT---CPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRW 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1742 IECAIIDHAFEQGWIK-PEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVK 1820
Cdd:PRK13984 258 LKRYIVDNVPVEKYSEiLDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1821 RRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEaQQKKQLGGKNDIIS 1900
Cdd:PRK13984 338 KDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPLLR-EIRDYLRGEGPKPK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1901 AAgKNVIIIGGGDTGCDcIATSLRQ------GAKSIT------TFEILPEPPQKraqdnpwpqwpkvfrVDYGHEE-VKL 1967
Cdd:PRK13984 417 IP-RSLVVIGGGNVAMD-IARSMARlqkmeyGEVNVKvtslerTFEEMPADMEE---------------IEEGLEEgVVI 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1968 KWGKDPRqyctttkEFVGENGAIKGVNTVEVEWTKTETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTVPSELGLELD 2047
Cdd:PRK13984 480 YPGWGPM-------EVVIENDKVKGVKFKKCVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDYSYLPEELKSKLE 552
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 24665539 2048 -PRGNIKaSNGQYGTSNSKVFAAGDCRRGQSlVVWAITEGRQAARQVDSYLTG 2099
Cdd:PRK13984 553 fVRGRIL-TNEYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRK 603
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
1759-2100 |
1.77e-48 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 177.49 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1759 EIPEvRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVH 1838
Cdd:PRK12770 12 EKPP-PTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1839 V---------------GKDLKAEQLLQEYDAVLLTTGsTW-PRDLPLANRDLKGIHFAMEFLEAQQKKQLGG--KNDIIS 1900
Cdd:PRK12770 91 VccgeplheeegdefvERIVSLEELVKKYDAVLIATG-TWkSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYlpWEKVPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1901 AAGKNVIIIGGGDTGCDCIATSLRQGAKSITTF--EILPEPPQKRAQDNpwpqwpkvfRVdyghEEVKLKWgkdpRQYCT 1978
Cdd:PRK12770 170 VEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAyrRTINEAPAGKYEIE---------RL----IARGVEF----LELVT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1979 TTkEFVGEnGAIKGVNTVEVEWTK-TETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNg 2057
Cdd:PRK12770 233 PV-RIIGE-GRVEGVELAKMRLGEpDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDE- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 24665539 2058 QYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGR 2100
Cdd:PRK12770 310 KHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
1634-2093 |
1.08e-36 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 151.91 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1634 APY-RDAGERQKDWDEV-----------YNFPHVRKNLKVQAARCMEC-------GVPFCQSNST--GCPLGNIIPKWND 1692
Cdd:PRK12779 146 PPYiRPAEERAVDFDLVnqgylgyqslgYSVREVELFVWLEVMRDKQCddkpcelGVLVQGKAEPkgGCPVKIHIPEMLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1693 LVFHGEWQEALRQLLQTNNFPEFTGRVCPAP--CEGSCVLgiSEPAVTIKNIECAIIDHAFEQG-------------WIK 1757
Cdd:PRK12779 226 LLGNGKHREALELIESCNPLPNVTGRVCPQElqCQGVCTH--TKRPIEIGQLEWYLPQHEKLVNpnanerfagrispWAA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1758 PEIPEVrtgkrvAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNV 1837
Cdd:PRK12779 304 AVKPPI------AVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNF 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1838 HVGK-----DLKAEQLLQeydaVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKKQlGGKND----IISAAGKNVII 1908
Cdd:PRK12779 378 VVGKtatleDLKAAGFWK----IFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNLMR-GLDDDyetpLPEVKGKEVFV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1909 IGGGDTGCDCIATSLRQGAKSITTFeilpeppqKRAQDnpwpQWPKvfRVDYGH----EEVKLKWGKDPRqyctttkEFV 1984
Cdd:PRK12779 453 IGGGNTAMDAARTAKRLGGNVTIVY--------RRTKS----EMPA--RVEELHhaleEGINLAVLRAPR-------EFI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1985 GEN------GAIKGVNTVEvewTKTETGQWRMQEVAGSEKyFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQ 2058
Cdd:PRK12779 512 GDDhthfvtHALLDVNELG---EPDKSGRRSPKPTGEIER-VPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGS 587
|
490 500 510
....*....|....*....|....*....|....*
gi 24665539 2059 YGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQV 2093
Cdd:PRK12779 588 QRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
274-476 |
8.15e-32 |
|
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: 124.87 E-value: 8.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 274 DYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLR------VLAHNGEINTLRGNVNLMKAREGVMQSDlfgdqlkkl 347
Cdd:cd00352 56 DVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEARGYRFEGE--------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 348 ypvvepnlSDSGSFDCVLEFLTMASDrsLPESVMTMVPEawqndktmpqekrdfyqwaacvmepWDGPALISFTDG--RY 425
Cdd:cd00352 127 --------SDSEVILHLLERLGREGG--LFEAVEDALKR-------------------------LDGPFAFALWDGkpDR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24665539 426 IGAVLDRNGLRPSRFYVTKENVLVMASEVGVydVDPSQVTLKSRLKPGRML 476
Cdd:cd00352 172 LFAARDRFGIRPLYYGITKDGGLVFASEPKA--LLALPFKGVRRLPPGELL 220
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
1642-1755 |
1.27e-27 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 108.78 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1642 RQKDWDEVYNfPHVRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCP 1721
Cdd:pfam14691 1 RIKNFEEVAL-GYTEEEAIAEASRCLQCKDPPCV---KGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCP 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 24665539 1722 A--PCEGSCVLGISEP-AVTIKNIECAIIDHAFEQGW 1755
Cdd:pfam14691 77 QerQCEGACVLGKKGFePVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
1769-2101 |
7.30e-25 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 107.13 E-value: 7.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERnDRVGGLLQ--------YGIP--------TMKLSKEVVKRRVDLMADE--G 1830
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPegisgpelAERLREQAERFGAEILLEEvtS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1831 IEFRTNVHV-----GKDLKAeqllqeyDAVLLTTGSTwPRDLPLANRDL---KGIHFAmefleaqqkkqlgGKNDIISAA 1902
Cdd:COG0492 82 VDKDDGPFRvttddGTEYEA-------KAVIIATGAG-PRKLGLPGEEEfegRGVSYC-------------ATCDGFFFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1903 GKNVIIIGGGDTGCDcIATSLRQGAKSITtfeILPEPPQKRAQDNpwpQWPKVFRvdygHEEVKLKWGkdprqycTTTKE 1982
Cdd:COG0492 141 GKDVVVVGGGDSALE-EALYLTKFASKVT---LIHRRDELRASKI---LVERLRA----NPKIEVLWN-------TEVTE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1983 FVGENgaikGVNTVEVEWTKTetgqwrmqevaGSEKYFPADLILLAMGFLgPEKTVPSELGLELDPRGNIKAsNGQYGTS 2062
Cdd:COG0492 203 IEGDG----RVEGVTLKNVKT-----------GEEKELEVDGVFVAIGLK-PNTELLKGLGLELDEDGYIVV-DEDMETS 265
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 24665539 2063 NSKVFAAGDCRRGQS-LVVWAITEGRQAARQVDSYLTGRP 2101
Cdd:COG0492 266 VPGVFAAGDVRDYKYrQAATAAGEGAIAALSAARYLEPLK 305
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1767-2086 |
2.71e-23 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 102.78 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDR---VGGLLQYGIPTMKLSKEVVKRRVDLMAD---------EGIEFR 1834
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpyGGCVLSKALLGAAEAPEIASLWADLYKRkeevvkklnNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1835 TNVHV------GKDLKAEQLLQ------EYDAVLLTTGStWPRDLPLANRDLKGIHFA-----MEFLEAQQKkqlggknd 1897
Cdd:pfam07992 81 LGTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGA-RPRLPPIPGVELNVGFLVrtldsAEALRLKLL-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1898 iisaaGKNVIIIGGGDTGCDCiATSLRQGAKSITTFEILPEPpqKRAQDNPWPQW-PKVFRvdygHEEVKLKWGkdprqy 1976
Cdd:pfam07992 152 -----PKRVVVVGGGYIGVEL-AAALAKLGKEVTLIEALDRL--LRAFDEEISAAlEKALE----KNGVEVRLG------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1977 cTTTKEFVGENGAIKgvntvevewTKTETGQwrmqevagsekYFPADLILLAMGFlGPEKTVPSELGLELDPRGNIKAsN 2056
Cdd:pfam07992 214 -TSVKEIIGDGDGVE---------VILKDGT-----------EIDADLVVVAIGR-RPNTELLEAAGLELDERGGIVV-D 270
|
330 340 350
....*....|....*....|....*....|.
gi 24665539 2057 GQYGTSNSKVFAAGDCRRGQ-SLVVWAITEG 2086
Cdd:pfam07992 271 EYLRTSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
1792-2112 |
2.69e-18 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 88.33 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1792 VTVFERNDRVGGLlQYGIPTM-----KLSKEVVKRRVDLMADEGIEFRTNVHVGK-DLKAEQLL------QEYDAVLLTT 1859
Cdd:COG0446 8 ITVIEKGPHHSYQ-PCGLPYYvgggiKDPEDLLVRTPESFERKGIDVRTGTEVTAiDPEAKTVTlrdgetLSYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1860 GStWPRDLPLANRDLKGIHFAMEFLEAQQKKQLggkndIISAAGKNVIIIGGGDTGCDcIATSLRQGAKSITTFEilpep 1939
Cdd:COG0446 87 GA-RPRPPPIPGLDLPGVFTLRTLDDADALREA-----LKEFKGKRAVVIGGGPIGLE-LAEALRKRGLKVTLVE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1940 pqkrAQDNPWPQWPKVFrVDYGHEE-----VKLKWGkdprqycTTTKEFVGENGaikgvntVEVEWTKTETgqwrmqeva 2014
Cdd:COG0446 155 ----RAPRLLGVLDPEM-AALLEEElrehgVELRLG-------ETVVAIDGDDK-------VAVTLTDGEE--------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2015 gsekyFPADLILLAMGFlGPEKTVPSELGLELDPRGNIKAsNGQYGTSNSKVFAAGDCRR------GQSLVVW----AIT 2084
Cdd:COG0446 207 -----IPADLVVVAPGV-RPNTELAKDAGLALGERGWIKV-DETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasaANK 279
|
330 340
....*....|....*....|....*...
gi 24665539 2085 EGRQAARQvdsyLTGRPSGLPGPGGVIA 2112
Cdd:COG0446 280 QGRVAAEN----ILGGPAPFPGLGTFIS 303
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
1768-1932 |
1.45e-13 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 75.50 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRA--GHFVTVFERNDRVGGLLQYGI-PTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLK 1844
Cdd:PLN02852 28 HVCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1845 AEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLR 1924
Cdd:PLN02852 108 LSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLKSSDTAVVLGQGNVALDCARILLR 187
|
....*...
gi 24665539 1925 QGAKSITT 1932
Cdd:PLN02852 188 PTDELAST 195
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
1769-2097 |
1.45e-11 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 67.65 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLL------QY-GIPTMKLSKEVVKRrvdlMADEGIEFRTNV---H 1838
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTttteveNYpGFPEGISGPELMEK----MKEQAVKFGAEIiyeE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1839 VGKDLKAEQLL-------QEY--DAVLLTTGSTwPRDLPLANRDlkgihfamEFLeaqqkkqlgGKNdiISAA------- 1902
Cdd:TIGR01292 78 VIKVDKSDRPFkvytgdgKEYtaKAVIIATGAS-ARKLGIPGED--------EFW---------GRG--VSYCatcdgpf 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1903 --GKNVIIIGGGDTGCDcIATSLRQGAKSIT------TF---EILpeppQKRAQDNPwpqwpkvfrvdygheevklkwgK 1971
Cdd:TIGR01292 138 fkNKEVAVVGGGDSAIE-EALYLTRIAKKVTlvhrrdKFraeKIL----LDRLKKNP----------------------K 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1972 DPRQYCTTTKEFVGENGaikgVNTVEVEWTKTetgqwrmqevaGSEKYFPADLILLAMGFLGPEKTVPSELglELDPRGN 2051
Cdd:TIGR01292 191 IEFLWNSTVEEIVGDNK----VEGVKIKNTVT-----------GEEEELEVDGVFIAIGHEPNTELLKGLL--ELDENGY 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 24665539 2052 IKASNGQYgTSNSKVFAAGDCR-RGQSLVVWAITEGRQAARQVDSYL 2097
Cdd:TIGR01292 254 IVTDEGMR-TSVPGVFAAGDVRdKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1767-2107 |
8.08e-11 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 66.32 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHF--VTVF--ERN---DRVggLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHV 1839
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDgeITVIgaEPHppyNRP--PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1840 GK-DLKAEQLL------QEYDAVLLTTGSTwPRDLPLANRDLKGIHF------AMEFLEAqqkkqlggkndiiSAAGKNV 1906
Cdd:COG1251 80 TAiDRAARTVTladgetLPYDKLVLATGSR-PRVPPIPGADLPGVFTlrtlddADALRAA-------------LAPGKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1907 IIIGGGDTGCDcIATSLRQGAKSITTFEilpeppqkrAQDNPWPQWpkvfrVDYG--------HEE--VKLKWGkdprqy 1976
Cdd:COG1251 146 VVIGGGLIGLE-AAAALRKRGLEVTVVE---------RAPRLLPRQ-----LDEEagallqrlLEAlgVEVRLG------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1977 cTTTKEFVGEnGAIKGVntvevewtKTETGQWrmqevagsekyFPADLILLAMGflgpekTVPS-EL----GLELDpRGn 2051
Cdd:COG1251 205 -TGVTEIEGD-DRVTGV--------RLADGEE-----------LPADLVVVAIG------VRPNtELaraaGLAVD-RG- 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24665539 2052 IKAsNGQYGTSNSKVFAAGDC---------RRGQSLVVWAITEGRQAARQvdsyLTGRPSGLPGP 2107
Cdd:COG1251 256 IVV-DDYLRTSDPDIYAAGDCaehpgpvygRRVLELVAPAYEQARVAAAN----LAGGPAAYEGS 315
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
1767-1806 |
3.80e-10 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 64.47 E-value: 3.80e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQ 1806
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1367-1565 |
9.66e-10 |
|
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: 61.16 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1367 KSIDIFLEGSAGQSFCAFLArGVNVTLKGDANDYVGKGLCGGNVVImpqdtvpfesHLNVivGNVCLYGATEGTAYFRGI 1446
Cdd:cd00981 45 GNVRINIYGVPGNDLGAFMS-GPTIIVYGNAQDDVGNTMNDGKIVI----------HGSA--GDVLGYAMRGGKIFIRGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1447 ASERFCVR----NSGVTAVVEG--VGDHGCEYMTGGVVVILGL------TGRNFAAGMSGGIAYVydldgsfKPKVNPE- 1513
Cdd:cd00981 112 AGYRVGIHmkeyKDKVPVLVIGgtAGDFLGEYMAGGVIIVLGLgtdeepVGRYIGTGMHGGVIYI-------RGKVERSk 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24665539 1514 -SVELLPLEI-EKDVLLVKELLADFIEKTGSKVAKELldnwaeaQGKFVKVFPY 1565
Cdd:cd00981 185 lGKEVPKFELtEEDLEFIEKYIEEFCKEFGYDKAEIL-------DEEFTKLKPK 231
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
1768-1805 |
9.83e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 63.37 E-value: 9.83e-10
10 20 30
....*....|....*....|....*....|....*...
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLL 1805
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLA 38
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1769-2093 |
1.29e-09 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 62.80 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERnDRVGG------------LL-------------QYGIPTMKLS---KEVVK 1820
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskaLLhaaevahearhaaEFGISAGAPSvdwAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1821 RR-----------VDLMADEGIEF----------RTnVHV--GKDLKAeqllqeyDAVLLTTGSTwPRDLPLANRDLKGI 1877
Cdd:COG1249 85 RKdkvvdrlrggvEELLKKNGVDVirgrarfvdpHT-VEVtgGETLTA-------DHIVIATGSR-PRVPPIPGLDEVRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1878 HFAMEFLEAQQkkqlggkndiisaAGKNVIIIGGGDTGCDcIATSLRQ-GAKsITTFE----ILP-EPPQ--KRAQdnpw 1949
Cdd:COG1249 156 LTSDEALELEE-------------LPKSLVVIGGGYIGLE-FAQIFARlGSE-VTLVErgdrLLPgEDPEisEALE---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1950 pqwpKVFRvdygHEEVKLkwgkdprqyctttkefvgengaIKGVNTVEVEwtKTETGQWRMQEVAGSEKYFPADLILLAM 2029
Cdd:COG1249 217 ----KALE----KEGIDI----------------------LTGAKVTSVE--KTGDGVTVTLEDGGGEEAVEADKVLVAT 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 2030 GF------LGPEKTvpselGLELDPRGNIKAsNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQV 2093
Cdd:COG1249 265 GRrpntdgLGLEAA-----GVELDERGGIKV-DEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI 328
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
1764-1803 |
1.89e-08 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 59.16 E-value: 1.89e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 24665539 1764 RTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
1771-1803 |
3.45e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 52.15 E-value: 3.45e-08
10 20 30
....*....|....*....|....*....|...
gi 24665539 1771 IVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1767-1803 |
5.41e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 57.94 E-value: 5.41e-08
10 20 30
....*....|....*....|....*....|....*..
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
1765-1803 |
7.31e-08 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 57.05 E-value: 7.31e-08
10 20 30
....*....|....*....|....*....|....*....
gi 24665539 1765 TGKRVAIVGSGPSGLAASQQLNRAgHFVTVFERNDRVGG 1803
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
1765-1877 |
9.52e-08 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 56.36 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1765 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGllqygiptmKLSKEVVKRRVDLMADEGIEFRTNVHVgKDLK 1844
Cdd:COG0446 123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---------VLDPEMAALLEEELREHGVELRLGETV-VAID 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24665539 1845 AEQLLQ---------EYDAVLLTTG----STWPRDLPLANRDLKGI 1877
Cdd:COG0446 193 GDDKVAvtltdgeeiPADLVVVAPGvrpnTELAKDAGLALGERGWI 238
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1768-1839 |
1.19e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 51.05 E-value: 1.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGllqygiptmKLSKEVVKRRVDLMADEGIEFRTNVHV 1839
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
1767-1803 |
1.67e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 55.65 E-value: 1.67e-07
10 20 30
....*....|....*....|....*....|....*..
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1761-1928 |
2.10e-07 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 55.64 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1761 PEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG-----------------LLQY------GIPTMKLSKE 1817
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpshLYSLpffpnwSDDPDFPTGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1818 VVK-------RRVDLMADegIEFRTNVHVGKDLKAEQLLQ---------EYDAVLLTTGSTW-PRdLPlanrDLKGIH-F 1879
Cdd:COG2072 81 EILayleayaDKFGLRRP--IRFGTEVTSARWDEADGRWTvttddgetlTARFVVVATGPLSrPK-IP----DIPGLEdF 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24665539 1880 AMEFLEAQQKK---QLggkndiisaAGKNVIIIGGGDTGCDCIATSLRQGAK 1928
Cdd:COG2072 154 AGEQLHSADWRnpvDL---------AGKRVLVVGTGASAVQIAPELARVAAH 196
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1765-1860 |
2.87e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 54.63 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1765 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLqygipTMKLSKEVVKRrvdlMADEGIEFRTNVHV----G 1840
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-----DEEISAALEKA----LEKNGVEVRLGTSVkeiiG 221
|
90 100
....*....|....*....|....*
gi 24665539 1841 KDLKAEQLLQE-----YDAVLLTTG 1860
Cdd:pfam07992 222 DGDGVEVILKDgteidADLVVVAIG 246
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
252-454 |
5.11e-07 |
|
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: 53.04 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 252 YICSLSDRTVVYKGLFTSDQLWDYYtDLkdPEFETYLALVHTRFSTNTFPSWERAHPLRV----LAHNGEINTLRGNVNL 327
Cdd:cd01907 46 FVYSSGKDMEVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGSNREY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 328 MKaREGV---MQSD------LFGDQLKKLYPVVEpnlsdsgsfdcvlefltmasdrsLPESVMTMVPEAWQNDKTMPQEK 398
Cdd:cd01907 123 LE-RFGYkfeTETDteviayYLDLLLRKGGLPLE-----------------------YYKHIIRMPEEERELLLALRLTY 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24665539 399 R--DFyqwaacvmepwDGP-ALISFTDGRYIGAVlDRNGLRPSRFYVTKENVlVMASEV 454
Cdd:cd01907 179 RlaDL-----------DGPfTIIVGTPDGFIVIR-DRIKLRPAVVAETDDYV-AIASEE 224
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
1765-1807 |
8.32e-07 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 54.10 E-value: 8.32e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 24665539 1765 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQY 1807
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1356-1519 |
1.34e-06 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 52.12 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1356 CKYGEAGLPAGKsidIFLEGSAGqSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMpqdtvpfeshlnvivGNV---- 1431
Cdd:COG2218 72 VKRIGAGMTAGE---IIVEGDVG-MYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEIN---------------GNAgdfl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1432 --CLYGA----TEGTAYFRGIASERFCVRNSGVTAVVEG-VGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYDLDG 1504
Cdd:COG2218 133 gaAYRGDwrgmSGGTIIVKGNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPE 212
|
170
....*....|....*
gi 24665539 1505 SFKPKVNPESVELLP 1519
Cdd:COG2218 213 ELLPTFVDCGTHELV 227
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
1767-2106 |
1.93e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 52.74 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNR--AGHFVTVFERNDR-----------VGG---------------LLQYGIpTMKLSKEV 1818
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRlnKELEITVYEKTDIvsfgacglpyfVGGffddpntmiartpeeFIKSGI-DVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1819 VKrrvdlmadegIEFRTNVHVGKDLKAEQLLQE-YDAVLLTTGSTwPRDLPLANRDLKGIHFAMEFLEAQQKKQLGGKND 1897
Cdd:PRK09564 80 VK----------VDAKNKTITVKNLKTGSIFNDtYDKLMIATGAR-PIIPPIKNINLENVYTLKSMEDGLALKELLKDEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1898 IisaagKNVIIIGGGDTGCDcIATSLRQGAKSITTFE----ILPEPPQKRAQDnpwpqwpkVFRVDYGHEEVKLKWGKdp 1973
Cdd:PRK09564 149 I-----KNIVIIGAGFIGLE-AVEAAKHLGKNVRIIQledrILPDSFDKEITD--------VMEEELRENGVELHLNE-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1974 rqyctTTKEFVGENGaIKGVNTvevewtktetgqwrmqevagSEKYFPADLILLAMGFlGPEKTVPSELGLELDPRGNIK 2053
Cdd:PRK09564 213 -----FVKSLIGEDK-VEGVVT--------------------DKGEYEADVVIVATGV-KPNTEFLEDTGLKTLKNGAII 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24665539 2054 ASngQYG-TSNSKVFAAGDCRrgqslVVWAITEGRQA-----------ARQVDSYLTGRPSGLPG 2106
Cdd:PRK09564 266 VD--EYGeTSIENIYAAGDCA-----TIYNIVSNKNVyvplattanklGRMVGENLAGRHVSFKG 323
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
1758-1839 |
2.07e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 52.94 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1758 PEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGL---LQYGIPTMKLSKEVVKRRV-DLMADEGIEF 1833
Cdd:COG1148 132 LEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEPLIaEVEANPNITV 211
|
....*.
gi 24665539 1834 RTNVHV 1839
Cdd:COG1148 212 YTGAEV 217
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
1765-1803 |
3.33e-06 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 51.78 E-value: 3.33e-06
10 20 30
....*....|....*....|....*....|....*....
gi 24665539 1765 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
1767-1804 |
4.75e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 51.43 E-value: 4.75e-06
10 20 30
....*....|....*....|....*....|....*...
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGL 1804
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
1757-1806 |
5.22e-06 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 51.55 E-value: 5.22e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 24665539 1757 KPEIPEVRTGKRVAIVGSGPSGLAASQQLNRA-GHFVTVFERNDRVGGLLQ 1806
Cdd:PLN02576 3 IAEGSAAASSKDVAVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGGNIT 53
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1767-2101 |
5.55e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 50.90 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNR---AGHFVTVFERNDR--VGGLLqYGIPTMKLSKEVVKRRV-DLMADEGIEFR----TN 1836
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYhlFQPLL-PEVAAGTLSPDDIAIPLrELLRRAGVRFIqgevTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1837 VHV---------GKDLkaeqllqEYDAVLLTTGSTwPRDLPLAN-----RDLKGIHFAMEF-------LEAQQKKQLGgk 1895
Cdd:COG1252 81 IDPeartvtladGRTL-------SYDYLVIATGSV-TNFFGIPGlaehaLPLKTLEDALALrerllaaFERAERRRLL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1896 ndiisaagkNVIIIGGGDTGCD---CIATSLRQGAK---------SITTFE----ILPE-PP--QKRAQdnpwpqwpKVF 1956
Cdd:COG1252 151 ---------TIVVVGGGPTGVElagELAELLRKLLRypgidpdkvRITLVEagprILPGlGEklSEAAE--------KEL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1957 RvDYGheeVKLKWGkdprqycTTTKEfVGENGAIkgvntvevewtkTETGQWrmqevagsekyFPADLILLAMGFLGPEk 2036
Cdd:COG1252 214 E-KRG---VEVHTG-------TRVTE-VDADGVT------------LEDGEE-----------IPADTVIWAAGVKAPP- 257
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24665539 2037 tVPSELGLELDPRGNIKASNGQYGTSNSKVFAAGDC-----RRGQSL---VVWAITEGRQAARQVDSYLTGRP 2101
Cdd:COG1252 258 -LLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCaavpdPDGKPVpktAQAAVQQAKVLAKNIAALLRGKP 329
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
1768-1873 |
5.98e-06 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 51.42 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRAGHF-VTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDL-MADEGIEFRTNVHVGKDLKA 1845
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHERVkVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDPvFLSPNYRFFGNVHVGVDLKM 120
|
90 100
....*....|....*....|....*...
gi 24665539 1846 EQLLQEYDAVLLTTGSTwPRDLPLANRD 1873
Cdd:PTZ00188 121 EELRNHYNCVIFCCGAS-EVSIPIGQQD 147
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1357-1519 |
9.33e-06 |
|
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: 48.50 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1357 KYGEAGLPAGKsidIFLEGSAGQsFCAFLARGVNVTLKGDANDYVGKGLCGGNVVImpqdtvpfESHLNVIVGnvCLY-- 1434
Cdd:cd00980 31 KRIGARMTAGE---IVVEGDVGM-YVGAGMKGGKLVVEGNAGSWAGCEMKGGEITI--------KGNAGDYVG--SAYrg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1435 ---GATEGTAYFRGIASERFCVRNSGVTAVVEG-VGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYDLDGSFKPKV 1510
Cdd:cd00980 97 dwrGMSGGTITIEGNAGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIGGEIEELLPTF 176
|
....*....
gi 24665539 1511 NPESVELLP 1519
Cdd:cd00980 177 KEEGTEEDV 185
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
1767-1950 |
2.92e-05 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 48.80 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHF---VTVFERNDRVGGLLQYGI--PTMKLSkeVVKRRVDLMADEGIEF-----RTN 1836
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRAPEplrITLFEPRPELGRGVAYSTdsPEHLLN--VPAGRMSAFPDDPDHFlrwlrENG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1837 VHVGKDLKAEQ-----LLQEY-----------------------------------------------DAVLLTTGSTWP 1864
Cdd:COG4529 84 ARAAPAIDPDAfvprrLFGEYlrerlaealarapagvrlrhiraevvdlerddggyrvtladgetlraDAVVLATGHPPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1865 RDLPLANRDLKGIH---FAMEFLEaqqkkqlggknDIisAAGKNVIIIGGGDTGCDCIATSLRQGAK-SITTFE---ILP 1937
Cdd:COG4529 164 APPPGLAAGSPRYIadpWPPGALA-----------RI--PPDARVLIIGTGLTAIDVVLSLAARGHRgPITALSrrgLLP 230
|
250
....*....|...
gi 24665539 1938 EPpqkRAQDNPWP 1950
Cdd:COG4529 231 RA---HPPGAPLP 240
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1767-1860 |
3.23e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 48.64 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLlqygiptmkLSKEVVKRRVDLMADEgIEFRTNVHV-----GK 1841
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL---------EDPEVSKQAQKILSKE-FKIKLGAKVtsvekSG 239
|
90 100
....*....|....*....|....*.
gi 24665539 1842 DLKAEQLLQ-------EYDAVLLTTG 1860
Cdd:PRK06292 240 DEKVEELEKggktetiEADYVLVATG 265
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1768-1802 |
3.33e-05 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 48.40 E-value: 3.33e-05
10 20 30
....*....|....*....|....*....|....*
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVG 1802
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
1768-1854 |
3.66e-05 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 48.16 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVG--------GLLQYGIPTM------KLSKEVVKRRVDLMADEGIE- 1832
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLepselaRLALEALDLWEELEEELGIDc 80
|
90 100
....*....|....*....|....*
gi 24665539 1833 -FRTN--VHVGKDLKAEQLLQEYDA 1854
Cdd:pfam01266 81 gFRRCgvLVLARDEEEEALEKLLAA 105
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
1766-1803 |
3.73e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 49.10 E-value: 3.73e-05
10 20 30
....*....|....*....|....*....|....*...
gi 24665539 1766 GKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
1756-1838 |
3.74e-05 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 48.86 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1756 IKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLqygiptmkLSKEVVKRRVDLMADEGIEFRT 1835
Cdd:PLN03000 174 IKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRV--------YTKKMEANRVGAAADLGGSVLT 245
|
...
gi 24665539 1836 NVH 1838
Cdd:PLN03000 246 GTL 248
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1731-1870 |
3.79e-05 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 48.21 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1731 GISEPAVTIKNIECAI-----IDHAFEQGwikpeipEVRTGKRVAIVGSGPSG----LAASQQLNRAGHF---------V 1792
Cdd:COG1252 116 GLAEHALPLKTLEDALalrerLLAAFERA-------ERRRLLTIVVVGGGPTGvelaGELAELLRKLLRYpgidpdkvrI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1793 TVFERNDRVGGllqygiptmKLSKEVVKRRVDLMADEGIEFRTNVHVgKDLKAEQLL------QEYDAVLLTTG---STW 1863
Cdd:COG1252 189 TLVEAGPRILP---------GLGEKLSEAAEKELEKRGVEVHTGTRV-TEVDADGVTledgeeIPADTVIWAAGvkaPPL 258
|
....*..
gi 24665539 1864 PRDLPLA 1870
Cdd:COG1252 259 LADLGLP 265
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
1777-1803 |
5.50e-05 |
|
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.
Pssm-ID: 396255 [Multi-domain] Cd Length: 446 Bit Score: 47.87 E-value: 5.50e-05
10 20
....*....|....*....|....*..
gi 24665539 1777 SGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGG 28
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1769-2072 |
8.69e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 47.48 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERND------RVG-----GLL-------------QYGIPTMKLS---KEVVKR 1821
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclNVGcipskALIaaaeafheakhaeEFGIHADGPKidfKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1822 RvdlmaDEGIEFRTNvHVGKDLK---AEQLLQEY------------------DAVLLTTGSTWPRDLPLANRDLKGIHFA 1880
Cdd:PRK06292 86 V-----RRERDRFVG-GVVEGLEkkpKIDKIKGTarfvdpntvevngerieaKNIVIATGSRVPPIPGVWLILGDRLLTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1881 MEFLEaqQKKQlggkndiisaaGKNVIIIGGGDTGCDcIATSL-RQGAKsITTFE----ILP-EPP--QKRAQDnpwpQW 1952
Cdd:PRK06292 160 DDAFE--LDKL-----------PKSLAVIGGGVIGLE-LGQALsRLGVK-VTVFErgdrILPlEDPevSKQAQK----IL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1953 PKVFRVDYGHEEVKlkwgkdprqyctttkefvgengaIKGVNTVEVEWTktetgqwrmqEVAGSEKYFPADLILLAMG-- 2030
Cdd:PRK06292 221 SKEFKIKLGAKVTS-----------------------VEKSGDEKVEEL----------EKGGKTETIEADYVLVATGrr 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24665539 2031 ----FLGPEKTvpselGLELDPRGNIKAsNGQYGTSNSKVFAAGDC 2072
Cdd:PRK06292 268 pntdGLGLENT-----GIELDERGRPVV-DEHTQTSVPGIYAAGDV 307
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
1767-1806 |
1.13e-04 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 47.15 E-value: 1.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNRAG--HFVTVFERNDRVGGLLQ 1806
Cdd:PRK11883 1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQ 42
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
1766-1869 |
3.91e-04 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 45.07 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1766 GKRVAIVGSGPSGLAASQQLNRAGHFVTVFErndrvggllqygiptmklSKEVVKRRVDLMADEGIEFRTNVHvgkdlkA 1845
Cdd:COG0771 4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSD------------------DRPAPELAAAELEAPGVEVVLGEH------P 59
|
90 100
....*....|....*....|....
gi 24665539 1846 EQLLQEYDAVLLTTGstWPRDLPL 1869
Cdd:COG0771 60 EELLDGADLVVKSPG--IPPDHPL 81
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
2012-2072 |
4.02e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 45.19 E-value: 4.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24665539 2012 EVAGSEKYFPADLILLAMG------FLGPEKTvpselGLELDPRGNIKAsNGQYGTSNSKVFAAGDC 2072
Cdd:PRK06370 250 DCNGGAPEITGSHILVAVGrvpntdDLGLEAA-----GVETDARGYIKV-DDQLRTTNPGIYAAGDC 310
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
1769-1881 |
4.92e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 44.91 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYG-----IPTMKLSKEVVKRRVD-----LMADEGIEFRT--- 1835
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSGlvgpdMGFYLNKEQVVGGIARefrqrLRARGGLPGPYglr 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 24665539 1836 ------NVHVGKDLkAEQLLQEYDAVLLTtgSTWPRDLPLANRDLKGIHFAM 1881
Cdd:pfam12831 82 ggwvpfDPEVAKAV-LDEMLAEAGVTVLL--HTRVVGVVKEGGRITGVTVET 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1762-1867 |
6.27e-04 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 44.36 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1762 EVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLqygiptmkLSKEVVKRRVDLMADEGIEFRTNVHVgk 1841
Cdd:COG1251 138 ALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ--------LDEEAGALLQRLLEALGVEVRLGTGV-- 207
|
90 100
....*....|....*....|....*...
gi 24665539 1842 dlkaEQLLQEYD--AVLLTTGSTWPRDL 1867
Cdd:COG1251 208 ----TEIEGDDRvtGVRLADGEELPADL 231
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
1070-1194 |
9.55e-04 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 42.57 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1070 PHHDIYSIEDLAELIYDLKCSNPNARISVKLvSEVGVGVVASGVAKGKAEhIVISGHDGGTGASSwtgiknaglpwelGV 1149
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKL-SPTGELAAAAAEEAGVDE-VGLGNGGGGGGGRD-------------AV 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24665539 1150 AETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLGADEFGFST 1194
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1768-1856 |
1.29e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 43.36 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1768 RVAIVGSGPSGLAASQQLNRAGHFVTVFERND-------RVGGLLQYGIPTM------KLSKEVVKRRVDLMADEGI--E 1832
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRpgsgasgRNAGQLRPGLAALadralvRLAREALDLWRELAAELGIdcD 83
|
90 100
....*....|....*....|....*.
gi 24665539 1833 FRTN--VHVGKDLKAEQLLQEYDAVL 1856
Cdd:COG0665 84 FRRTgvLYLARTEAELAALRAEAEAL 109
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1759-1839 |
2.07e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 42.88 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1759 EIPEvrtgkRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVggllqygiptmkLSKE------VVKrrvDLMADEGIE 1832
Cdd:PRK06370 169 ELPE-----HLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL------------LPREdedvaaAVR---EILEREGID 228
|
....*..
gi 24665539 1833 FRTNVHV 1839
Cdd:PRK06370 229 VRLNAEC 235
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
1767-1832 |
2.52e-03 |
|
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213540 [Multi-domain] Cd Length: 462 Bit Score: 42.52 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24665539 1767 KRVAIVGSGPSGLAASQQLNR----AGHFVTVFERNDRVGG----------LLQYGIPTMKLSKEVVkrrVDLMADEGIE 1832
Cdd:TIGR00562 3 KHVVIIGGGISGLCAAYYLEKeipeLPVELTLVEASDRVGGkiqtvkedgyLIERGPDSFLERKKSA---PDLVKDLGLE 79
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
1758-1803 |
3.32e-03 |
|
lysine-specific histone demethylase 1
Pssm-ID: 178144 [Multi-domain] Cd Length: 738 Bit Score: 42.57 E-value: 3.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24665539 1758 PEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:PLN02529 152 SPIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
1769-1801 |
3.84e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 42.20 E-value: 3.84e-03
10 20 30
....*....|....*....|....*....|...
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRV 1801
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
1769-1839 |
5.74e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 40.53 E-value: 5.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHF-VTVFERNDRVGGLLQYGipTMKLSKEVVKRRVDLMADE-GI---EFRTNVHV 1839
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAKNRGLkVAIIERSVSPGGGAWLG--GQLFSAMVVRKPAHLFLDEfGIpyeDEGDYVVV 93
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
1766-1839 |
5.87e-03 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 40.87 E-value: 5.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24665539 1766 GKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDrvggllqygipTMKLSKEVVKRrvdLMADEGIEFRTNVHV 1839
Cdd:COG0492 141 GKDVVVVGGGDSALEEALYLTKFASKVTLIHRRD-----------ELRASKILVER---LRANPKIEVLWNTEV 200
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
1769-1803 |
7.07e-03 |
|
probable polyamine oxidase
Pssm-ID: 177909 [Multi-domain] Cd Length: 435 Bit Score: 41.21 E-value: 7.07e-03
10 20 30
....*....|....*....|....*....|....*
gi 24665539 1769 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1803
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
|
|
| |
