|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
75-1565 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1551.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 75 KQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLP 154
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 155 ELgdYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQ 232
Cdd:PRK11750 82 KN--YAVGMVFLnqDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 233 VFVLRKRAShELIKPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVL 312
Cdd:PRK11750 160 LFIARRRIE-KRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 313 AHNGEINTLRGNVNLMKAREGVMQSDLFGDqLKKLYPVVEPNLSDSGSFDCVLEFLtMASDRSLPESVMTMVPEAWQNDK 392
Cdd:PRK11750 239 AHNGEINTITGNRQWARARAYKFQTPLIPD-LQEAAPFVNETGSDSSSLDNMLELL-LAGGMDLFRAMRLLVPPAWQNNP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 393 TMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKP 472
Cdd:PRK11750 317 DMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 473 GRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQkmitldeirnaNVLNTPPVDELAKLPASERGiFDPRL-----SLF 547
Cdd:PRK11750 397 GELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEK-----------NVRRLVPFEELPDEQVGSRE-LDDDTlksyqKQF 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 548 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQ 627
Cdd:PRK11750 465 QYSFEELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFC 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 628 PSAQQVHRIWLTNPILSIPD-TQLLKRNTHrGWRTKVLDITfqYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGA 706
Cdd:PRK11750 545 ETEGHAHRVIFKSPVLSYSDfKQLTTLDEE-HYRADTLDLN--YDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNI 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 707 GiDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVNd 786
Cdd:PRK11750 622 A-KGRLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYR- 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 787 kQIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 866
Cdd:PRK11750 700 -QVMLNYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLAR 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 867 TPdtriLRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTtLDSVKKCALRGQLEFVTDRQSIDISEVEP 946
Cdd:PRK11750 779 KP----IDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKL-VNERPVATLRDLLALKPADNPIPLDEVEP 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 947 ASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVTASYLANA 1026
Cdd:PRK11750 854 AEELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNA 928
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1027 DDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVG 1106
Cdd:PRK11750 929 EVLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPG 1008
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1107 VGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALL 1186
Cdd:PRK11750 1009 VGTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAIL 1088
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1187 GADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKK-FTGKPEHVINFFFMLAEDIRKIMAGLGIRKFQDLIGR 1265
Cdd:PRK11750 1089 GAESFGFGTGPMVALGCKYLRICHLNNCATGVATQDEKLRKNhYHGLPEMVMNYFEFIAEETREWMAQLGVRSLEDLIGR 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1266 TDLLRVASQRDAKASNLDLKLLLQPAlELRPGtnivggsvKQDFQLEKRS---DNELIakAQQIFSGADDNV------TV 1336
Cdd:PRK11750 1169 TDLLEELEGETAKQQKLDLSPLLETA-EPPAG--------KALYCTEERNppfDKGLL--NEQMLQQAKPAIeakqggEF 1237
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1337 KMRIHNEERAFGSTLSYHIACKYGEAGLpAGKSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQ 1416
Cdd:PRK11750 1238 WFDIRNTDRSVGARLSGEIARRHGNQGM-ADAPIKLRFTGTAGQSFGVWNAGGLELYLEGDANDYVGKGMAGGKIVIRPP 1316
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1417 DTVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGG 1496
Cdd:PRK11750 1317 VGSAFRSHETAIIGNTCLYGATGGKLFAAGRAGERFAVRNSGAIAVVEGIGDHGCEYMTGGIVCVLGKTGVNFGAGMTGG 1396
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386771285 1497 IAYVYDLDGSFKPKVNPESVELLPLE---IEKDVLlvKELLADFIEKTGSKVAKELLDNWAEAQGKFVKVFP 1565
Cdd:PRK11750 1397 FAYVLDEDGDFVDRVNHELVEILRVEdleIHREHL--RGLITEHVEETGSEWGEEILANFDDYLRKFWLVKP 1466
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
68-1584 |
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: 1247.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 68 MPWEAPGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALA 147
Cdd:COG0070 7 MGAAAAAGGGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 148 KQGVTLPELGDYATGIF-YLDEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDE 226
Cdd:COG0070 87 AGGGAFFAAGLAAGLLAlAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 227 KAFERQVFVLRKRASHELikpgRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERA 306
Cdd:COG0070 167 LRRLALLRRRRRRRRREF----RRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 307 HPLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASDRSLPESVMTMVPE 386
Cdd:COG0070 243 FAPRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 387 AWQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTL 466
Cdd:COG0070 323 APAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 467 KSRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQKMITLDEIRNANVLNTPPVDELAKLPASERGIFDPRLsl 546
Cdd:COG0070 403 GRELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEELLQEREAELEQELLLLL-- 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 547 fgysTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQpipyeYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLL 626
Cdd:COG0070 481 ----LLLLAEALEEEEESGGAGAAAAALDLLDLLLLLDF-----QFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 627 QPSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGA 706
Cdd:COG0070 552 LLLLLEELLLLELLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 707 GIDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVND 786
Cdd:COG0070 632 SALLLALLPALLALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 787 KQIYAAYAQAIdTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 866
Cdd:COG0070 712 AAAYKAKAALK-AGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 867 TPDTRILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEVEP 946
Cdd:COG0070 791 AAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEP 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 947 ASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYLNQDPNNSRRSAIKQVASGRFGVTASYLANA 1026
Cdd:COG0070 871 EEEIVKRFATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNA 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1027 DDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVG 1106
Cdd:COG0070 951 DEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVG 1030
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1107 VGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALL 1186
Cdd:COG0070 1031 VGTIAAGVAKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRRVVVQTDGGLKTGRDVVIAALL 1110
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1187 GADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKKFTGKPEHVINFFFMLAEDIRKIMAGLGIRKFQDLIGRT 1266
Cdd:COG0070 1111 GAEEFGFATAPLVVLGCIMMRKCHLNTCPVGVATQDPELRKRFFGGPEHVVNFFFFFAEEVRELMAALGGRTLDEEIGRR 1190
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1267 DLLRVASQRD-AKASNLDL-KLLLQPAL-ELRPGTNivggSVKQDFQLEKRSDNELIAKAQQ-IFSGAddNVTVKMRIHN 1342
Cdd:COG0070 1191 DLLLVRRAVDhWKAKGLDLsPLLYKPDVpADVPRYC----TEEQNHGLEGALDRELIEDARPaIENGE--PVELEYPIRN 1264
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1343 EERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQDTVPFE 1422
Cdd:COG0070 1265 TDRSVGTRLSGEIAKRYGNEGLPED-TITLRFTGSAGQSFGAFLAKGLTLELEGDANDYVGKGLSGGKIIVRPPAGSTFV 1343
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1423 SHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYD 1502
Cdd:COG0070 1344 AEENIIIGNTCLYGATGGELYAAGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGVVVVLGPTGRNFGAGMSGGIAYVLD 1423
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1503 LDGSFKPKVNPESVELLPLEIEKDVLLVKELLADFIEKTGSKVAKELLDNWAEAQGKFVKVFPYEYQKALKDMAEQQAVE 1582
Cdd:COG0070 1424 EDGDFEDRCNPEMVELERLDEEEDEEELRELIEEHVEYTGSARAKEILDNWDEYLPKFVKVMPKDYKRVLEAIAEAEAAG 1503
|
..
gi 386771285 1583 QP 1584
Cdd:COG0070 1504 LD 1505
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
73-1583 |
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: 1203.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 73 PGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVT 152
Cdd:COG0067 8 PAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 153 LPELGDYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFE 230
Cdd:COG0067 88 LPEPGEYAVGMVFLpqDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 231 RQVFVLRKRASHELIKPG---RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAH 307
Cdd:COG0067 168 RKLYVARKRIEKAIRALGlddEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 308 PLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEA 387
Cdd:COG0067 248 PFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVL-GGRSLPHAMMMLIPEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 388 WQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLK 467
Cdd:COG0067 327 WENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 468 SRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQKMITLDEIRNANVLNTPPVDELAKlpasergifdpRLSLF 547
Cdd:COG0067 407 GRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLKENRIRLEDLPEPEEEPAPDDDLLLR-----------RQQAF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 548 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQ 627
Cdd:COG0067 476 GYTEEEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 628 PSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 707
Cdd:COG0067 556 EEEEARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 708 IDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELA-QALRDDGVIAPEVND 786
Cdd:COG0067 636 DSDAAPAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALElLLDGLLLGLEDAAAA 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 787 KQIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 866
Cdd:COG0067 716 AAAKKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEP 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 867 TPDT--RILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEV 944
Cdd:COG0067 796 GGLLlgLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 945 EPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRylnqDPNNSRRSAIKQVASGRFGVTASYLA 1024
Cdd:COG0067 876 EEEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1025 NADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSE 1104
Cdd:COG0067 952 AAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVA 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1105 VGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAA 1184
Cdd:COG0067 1032 AAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLLGVVVLGGLGGGGGGGGGAA 1111
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1185 LLGADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKKFTGKPEHVINFFFMLAEDIRKIMAGLGIRkfQDLIG 1264
Cdd:COG0067 1112 ALGAGALGGGAAALVVVGCGVAMCCVVLLCTVGGAAAGELERRRFRFAGEEVVVEEFFEAAEEEEEEALLELL--RLLEE 1189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1265 RTDLLRVASQRDAKASNLDLKLLLQPALELRPGTNIVGGSVKQDFQLEKRSDNELIAKAQQIFSGADDNVTVKMRIHNEE 1344
Cdd:COG0067 1190 GLGVVELLLLLLLLLLLAKLLLLLLLLLLPLLPPDDPRDLALEEDDELLLLLALLLLLLALALALLAAVRVALRAALGRA 1269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1345 RAFGSTLSYHIACKYGEAGLPAGKSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQDTVPFESH 1424
Cdd:COG0067 1270 RRRGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 1349
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1425 LNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYDLD 1504
Cdd:COG0067 1350 GGGGGGGAGGGGGGGGGAGGGGGGGGGGVGGGGGGGGVGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGLDL 1429
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386771285 1505 GSFKPKVNPESVELLPLEIEKDVLLVKELLADFIEKTGSKVAKELLDNWAEAQGKFVKVFPYEYQKALKDMAEQQAVEQ 1583
Cdd:COG0067 1430 DVVLDEEEEEELEELLLLLEEEEEEELELEEEEAELLELADAALLLLLLVKVKAAVKVLLLLLLAAAAAAAEAAAAAAA 1508
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
718-1455 |
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 386771285 718 LALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGviAPEVNDKQIYAAYAQAI 797
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGG--LLGLDLEEAVKNYIKAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 798 DTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAkcfrgtqsriggVTLEilakEGLQRYQLTYgkatpdTRILRNPG 877
Cdd:COG0069 79 EKGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVD------------IGIA----DVLTQHRHAI------LRNLPVGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 878 QYHWRH--------------GGEAHINEPSSIGSLQEAAvnKNLDAFEAFKkTTLD--SVKKCALRGQLEFVTDRQSIDI 941
Cdd:COG0069 137 RYRYRFesigpeirqyffesDGEEHPFNRETRSLLYQAA--KNEEDYKPFG-TLVDyqPGYEWTLRSLFPFKADRPPIPI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 942 SE-VEPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVT- 1019
Cdd:COG0069 214 GEpVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRd 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1020 --ASYLANADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARI 1097
Cdd:COG0069 289 edGEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1098 SVKLVSEVGV----GVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQ 1173
Cdd:COG0069 369 GVKLVSGAGVgtiaACKGVAKTGAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDRIRLIADGK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1174 LRTGFDVVVAALLGADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPELRKKFT--GKPEHVINFFFMLAEDIRKIM 1251
Cdd:COG0069 449 LKTGRDVAIAAALGADEFGFARAFMVALGCIMARKCHLNTCPVGVATQDPELRKGFVveGKPERVVNYFRFTAEEVREIL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1252 AGLGIRKFQDLIGRTDLLRVASQRDAKASNLDLKLLLQP--ALELRPGTNIvggsVKQDFQLEKRSDNELIAKAQQIFSG 1329
Cdd:COG0069 529 AALGVRSPDELIGRHDLLRVRDGEHWKAKGLDLSPLLYKpeLPEGVPRRCQ----EEQDHGLDKALDLELIAAAAAAAEE 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1330 ADDNVTVkMRIHNEERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGG 1409
Cdd:COG0069 605 GKPVVLI-TNIRNNNRRVGGMLSGEIAKRYGGAGLPDD-TIILGFAGGAGQSFGAFGAGGGLLLLEGDDNDYVGKGGGGG 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 386771285 1410 NVVIMPQDTVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVR 1455
Cdd:COG0069 683 GIIVPPPPGASFFPEENIIIGNTGLYGATGGGAYFAGGAGERFAVR 728
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1623-2106 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 827.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1623 KTRGFVKYKRESAPYRDAGERQKDWDEVY-NFPhvRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQ 1701
Cdd:PRK12810 3 KPTGFLEYDRVDPKKRPVAERIKDFKEFYePFS--EEQAKIQAARCMDCGIPFCH---WGCPVHNYIPEWNDLVYRGRWE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1702 EALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLA 1781
Cdd:PRK12810 78 EAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1782 ASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTG 1861
Cdd:PRK12810 158 AADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1862 STWPRDLPLANRDLKGIHFAMEFLEAQQKKQLG-GKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEP 1940
Cdd:PRK12810 238 AYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGdETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDIMPMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1941 PQKRAQDNPWPQWPKVFRVDYGHEEvklkwGkDPRQYCTTTKEFVGENGAIKGVNTVEVEWtktetGQWRMQEVAGSEKY 2020
Cdd:PRK12810 318 PSRRNKNNPWPYWPMKLEVSNAHEE-----G-VEREFNVQTKEFEGENGKVTGVKVVRTEL-----GEGDFEPVEGSEFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2021 FPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTG 2100
Cdd:PRK12810 387 LPADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMG 466
|
....*.
gi 386771285 2101 RpSGLP 2106
Cdd:PRK12810 467 S-TALP 471
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
1623-2106 |
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 386771285 1623 KTRGFVKYKRESAPYRDAGERQKDWDEVYNfPHVRKNLKVQAARCMECGVPFCQsNSTGCPLGNIIPKWNDLVFHGEWQE 1702
Cdd:TIGR01317 1 KPTGFLEYKRRKPTERDPRTRLKDWKEFTN-PFDKESAKYQAARCMDCGTPFCH-NDSGCPLNNLIPEFNDLVFRGRWKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1703 ALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLAA 1782
Cdd:TIGR01317 79 ALDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1783 SQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGS 1862
Cdd:TIGR01317 159 ADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1863 TWPRDLPLANRDLKGIHFAMEFLEAQQKKQLGGK---NDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPE 1939
Cdd:TIGR01317 239 TKPRDLPIPGRELKGIHYAMEFLPSATKALLGKDfkdIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEIMPK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1940 PPQKRAQDNPWPQWPKVFRVDYGHEEVKLKWGKDPRQYCTTTKEFVG-ENGAIKGVNTVEVEWTKTETGQWRMQEVAGSE 2018
Cdd:TIGR01317 319 PPEARAKDNPWPEWPRVYRVDYAHEEAAAHYGRDPREYSILTKEFIGdDEGKVTALRTVRVEWKKSQDGKWQFVEIPGSE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2019 KYFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYL 2098
Cdd:TIGR01317 399 EVFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYL 478
|
....*...
gi 386771285 2099 TGRpSGLP 2106
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 386771285 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:pfam00310 81 qDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 246 KPG--RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRG 323
Cdd:pfam00310 161 VEGgdKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 324 NVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASdRSLPESVMTMVPEAWQNDKTMPQEKRDFYQ 403
Cdd:pfam00310 241 NRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGG-RSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 404 WAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEK 483
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 386771285 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 386771285 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:cd00713 81 rDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 246 KPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRGNV 325
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 326 NLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEAWQNDKTMPQEKRDFYQWA 405
Cdd:cd00713 241 NWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVR-SGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 406 ACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEKKL 485
Cdd:cd00713 320 SSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRI 399
|
410
....*....|....
gi 386771285 486 IQDIELKAKIAKSR 499
Cdd:cd00713 400 LDDEEIKDQLAKRH 413
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
1643-2097 |
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 386771285 1643 RQKDWDEVYNfPHVRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCP 1722
Cdd:COG0493 1 RIKDFREVYP-GLSEEEAIEQAARCLDCGDPPCQ---TGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1723 APCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRV 1802
Cdd:COG0493 77 APCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1803 GGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAM 1882
Cdd:COG0493 157 GGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1883 EFLEAQQKKQLggkNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEppqkraQDNPwpqwPKVFRVDYG 1962
Cdd:COG0493 237 DFLTAVNLGEA---PDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTR------EEMP----ASKEEVEEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1963 HEE-VKlkwgkdpRQYCTTTKEFVG-ENGAIKGVNTVEVEWTKT-ETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTV 2039
Cdd:COG0493 304 LEEgVE-------FLFLVAPVEIIGdENGRVTGLECVRMELGEPdESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGL 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 386771285 2040 PSELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSY 2097
Cdd:COG0493 377 EEELGLELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
888-1257 |
1.21e-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: 1.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 888 HINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEVEPASEIVKRFATGAMSFGSISLE 967
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERVPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 968 AHQTLSITMNRIGGKSNTGEGGEDSDRYLNQDpnnsrRSAIKQVASGRFGVTASYLANADDLQIKMAQGAKPGEGGELPG 1047
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYAD-----NIAIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1048 YKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGVGVVASGVAKGKAEHIVISGH 1127
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1128 DGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLGADEFGFSTAPLIVMGCTMMR 1207
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGCIMCR 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 386771285 1208 KCHLNTCPVGIATQDPELRK--KFTGKPEHVINFFFMLAEDIRKIMAGLGIR 1257
Cdd:pfam01645 316 VCHTNTCPVGVATQDPELRKrlDFEGAPERVVNYFRFLAEEVRELLAALGIN 367
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
918-1271 |
9.12e-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: 9.12e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 918 LDSVKKCALRGQLEFVTDRQSIDISE-------------VEPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSN 984
Cdd:cd02808 31 SRGRPFGTLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPFNISAMSFGALSKEAKEALAIGAALAGTASN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 985 TGEGGEDSDRYLNqdpnnsRRSAIKQVASGRFGVTASYLANADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGV 1064
Cdd:cd02808 111 TGEGGELPEEREG------GGDIIKQVASGRFGVRPEYLNKADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1065 GLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGL 1144
Cdd:cd02808 185 DLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTGAAPLTFIDHVGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1145 PWELGVAETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLGADEFGFSTAPLIVMGCTMMRKCHLNTCPVGIATQDPE 1224
Cdd:cd02808 265 PTELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIALGCIQARKCHTNTCPVGVATQDPE 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 386771285 1225 L--RKKFTGKPEHVINFFFMLAEDIRKIMAGLGIRKfQDLIGRTDLLRV 1271
Cdd:cd02808 345 LrrRLDVEGKAERVANYLKSLAEELRELAAALGKRS-LELLGRSDLLAL 392
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
1625-2103 |
7.29e-145 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 458.49 E-value: 7.29e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1625 RGFVKYKRESAPYRDAGERQKDWDEV---YNFPHVrknlKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQ 1701
Cdd:PRK11749 1 LKFLTTPRIPMPRQDAEERAQNFDEVapgYTPEEA----IEEASRCLQCKDAPCV---KACPVSIDIPEFIRLIAEGNLK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1702 EALRQLLQTNNFPEFTGRVCPAP--CEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEvRTGKRVAIVGSGPSG 1779
Cdd:PRK11749 74 GAAETILETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAP-KTGKKVAVIGAGPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1780 LAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLT 1859
Cdd:PRK11749 153 LTAAHRLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1860 TGSTWPRDLPLANRDLKGIHFAMEFLEAQqkKQLGGKNDIIsaAGKNVIIIGGGDTGCDCIATSLRQGAKSIT-----TF 1934
Cdd:PRK11749 233 TGAGLPRFLGIPGENLGGVYSAVDFLTRV--NQAVADYDLP--VGKRVVVIGGGNTAMDAARTAKRLGAESVTivyrrGR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1935 EILPEppqkraqdnpwpqwpKVFRVDYGHEE-VKLKWGKDPrqyctttKEFVGENGAIKGVNTVEVEWTKTETGQWRMQE 2013
Cdd:PRK11749 309 EEMPA---------------SEEEVEHAKEEgVEFEWLAAP-------VEILGDEGRVTGVEFVRMELGEPDASGRRRVP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2014 VAGSEKYFPADLILLAMGFlGPEKTVPS-ELGLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAAR 2092
Cdd:PRK11749 367 IEGSEFTLPADLVIKAIGQ-TPNPLILStTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAE 445
|
490
....*....|.
gi 386771285 2093 QVDSYLTGRPS 2103
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 ... |
1316-1565 |
2.48e-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: 2.48e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1316 DNELIAKAQQIFSGADDNVTVKMRIHNEERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLK 1395
Cdd:cd00982 2 DDKLIADAEPALIENGEPVTLEYPIRNTDRAVGTMLSGEIAKRYGEEGLPED-TIKIKFEGSAGQSFGAFLAKGVTLELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1396 GDANDYVGKGLCGGNVVIMPQDTVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMT 1475
Cdd:cd00982 81 GDANDYVGKGLSGGRIVVRPPKDATFKPEENIIIGNVCLYGATSGEAFIRGRAGERFAVRNSGATAVVEGVGDHGCEYMT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1476 GGVVVILGLTGRNFAAGMSGGIAYVYDLDGSFKPKVNPESVELLPLEIEKDVLLVKELLADFIEKTGSKVAKELLDNWAE 1555
Cdd:cd00982 161 GGTVVVLGKTGRNFAAGMSGGVAYVLDEDGDFEKKVNHEMVDLERLEDAEDEEQLKELIEEHVEYTGSEKAKEILANWEA 240
|
250
....*....|
gi 386771285 1556 AQGKFVKVFP 1565
Cdd:cd00982 241 YLKKFVKVIP 250
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
543-828 |
2.36e-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: 2.36e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 543 RLSLFGYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPE 622
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 623 ANLLQPSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFqynegvQGYIDAIDRICREGYAAAQAGYQLLVIS 702
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITF------DGLEAALERLCEEAEEAVRDGANILILS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 703 DRGAGiDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGviAP 782
Cdd:pfam04898 156 DRGVD-ADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREG--KG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 386771285 783 EVNDKQIYAA---YAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLG 828
Cdd:pfam04898 233 KLTDEDLEEAvknYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| GXGXG |
pfam01493 |
GXGXG motif; This domain is found in glutamate synthase, tungsten formylmethanofuran ... |
1338-1527 |
2.41e-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: 2.41e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1338 MRIHNEERAFGSTLSYHIACKYGEAGLPAGkSIDIFLEGSAGQSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMPQD 1417
Cdd:pfam01493 1 YEIRNTDRSVGTILSGEIAKRYGEDGLPDD-TITIKFNGSAGQSFGAFLPKGLTLELEGDANDYVGKGLSGGKIIIYPPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1418 TVPFESHLNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGDHGCEYMTGGVVVILGLTGRNFAAGMSGGI 1497
Cdd:pfam01493 80 ESTFKAEENIIIGNTCLYGATGGELFINGRAGERFAVRNSGATAVVEGVGDHGCEYMTGGRVVVLGKTGRNFGAGMSGGI 159
|
170 180 190
....*....|....*....|....*....|
gi 386771285 1498 AYVYDLDGSFKPKVNPESVELLPLEIEKDV 1527
Cdd:pfam01493 160 AYVLDEDGDFPEKLNKEMVELERVTDEDEE 189
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1642-2098 |
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 386771285 1642 ERQKDWDEVYnFPHVRKNLKVQAARCMECGV-PFCQSNstgCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRV 1720
Cdd:PRK12769 203 ARKTGFDEIY-LPFRADQAQREASRCLKCGEhSICEWT---CPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1721 CPAP--CEGSCVLGISEPAVTIKNIECAIIDHAFEQGWiKPEIPEVR-TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFE 1797
Cdd:PRK12769 279 CPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGW-RPDLSQVTkSDKRVAIIGAGPAGLACADVLARNGVAVTVYD 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1798 RNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKG 1877
Cdd:PRK12769 358 RHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPNEDAPG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1878 IHFAMEFLEAQQKKQLG----GKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTfeilpepPQKRAQDNpWPQW 1953
Cdd:PRK12769 438 VYDALPFLIANTKQVMGleelPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTC-------AYRRDEAN-MPGS 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1954 PKvfRVDYGHEE-VKLKWGKDPRQYCtttkefVGENGAIKGVNTVEVEWTKTE-TGQWRMQEVAGSEKYFPADLILLAMG 2031
Cdd:PRK12769 510 KK--EVKNAREEgANFEFNVQPVALE------LNEQGHVCGIRFLRTRLGEPDaQGRRRPVPIPGSEFVMPADAVIMAFG 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2032 FLGPEKTVPSELGLELDPRGNIKA---SNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYL 2098
Cdd:PRK12769 582 FNPHGMPWLESHGVTVDKWGRIIAdveSQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
1673-2102 |
2.72e-82 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 282.92 E-value: 2.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1673 PFCQSnstGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKNIECAIIDHAF 1752
Cdd:PRK12771 47 PPCNA---ACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1753 EQGWiKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGI 1832
Cdd:PRK12771 124 ANGW-KFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1833 EFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKkqlgGKNDIIsaaGKNVIIIGG 1912
Cdd:PRK12771 203 EVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRAVGE----GEPPFL---GKRVVVIGG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1913 GDTGCDCIATSLRQGAKSIT-----TFEILPeppqkrAQDnpwpqwpkvFRVDYGHEE-VKLKWGkdprqycTTTKEFVG 1986
Cdd:PRK12771 276 GNTAMDAARTARRLGAEEVTivyrrTREDMP------AHD---------EEIEEALREgVEINWL-------RTPVEIEG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1987 ENGAIKGVNTVEVE-WTKTETGqwRMQEVAGSEKYFPADLILLAMG---FLGPEKTVPselGLElDPRGNIKASNGQYGT 2062
Cdd:PRK12771 334 DENGATGLRVITVEkMELDEDG--RPSPVTGEEETLEADLVVLAIGqdiDSAGLESVP---GVE-VGRGVVQVDPNFMMT 407
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 386771285 2063 SNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGRP 2102
Cdd:PRK12771 408 GRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLGGEP 447
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
1631-2102 |
1.60e-79 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 271.51 E-value: 1.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1631 KRESAPYRDAGERQKDWDEV---YNFPHVRKnlkvQAARCMECGVPFCQSnstGCPLGNIIPKWNDLVFHGEWQEALRQL 1707
Cdd:PRK12831 7 KRVPVREQDPEVRATNFEEVclgYNEEEAVK----EASRCLQCKKPKCVK---GCPVSINIPGFISKLKEGDFEEAAKII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1708 LQTNNFPEFTGRVCP--APCEGSCVLGISEPAVTIKNIECAIIDHAFEQGwIKPEIPEVRTGKRVAIVGSGPSGLAASQQ 1785
Cdd:PRK12831 80 AKYNALPAVCGRVCPqeSQCEGKCVLGIKGEPVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1786 LNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKE-VVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQE--YDAVLLTTGS 1862
Cdd:PRK12831 159 LAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1863 TWPRDLPLANRDLKGIHFAMEFL-EAQQKKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEPP 1941
Cdd:PRK12831 239 GLPKFMGIPGENLNGVFSANEFLtRVNLMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSEEEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1942 QKRAQDnpwpqwpkvfrVDYGHEE-VKLKWGKDPrqyctttKEFVG-ENGAIKGVNTVEVEW-TKTETGQWRMQEVAGSE 2018
Cdd:PRK12831 319 PARVEE-----------VHHAKEEgVIFDLLTNP-------VEILGdENGWVKGMKCIKMELgEPDASGRRRPVEIEGSE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2019 KYFPADLILLAMGfLGPEKTVPSEL-GLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSY 2097
Cdd:PRK12831 381 FVLEVDTVIMSLG-TSPNPLISSTTkGLKINKRGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEY 459
|
....*
gi 386771285 2098 LTGRP 2102
Cdd:PRK12831 460 LSKKW 464
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1605-2094 |
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 386771285 1605 EAIQDVVLEQKRAdrVLDKTrgfvkyKRESAPYRDAGERQKDWDEVYNfPHVRKNLKVQAARCMECG-VPFCQSNstgCP 1683
Cdd:PRK12809 157 KASSDAQPSRSAA--LLPVN------SRKGADKISASERKTHFGEIYC-GLDPQQATYESDRCVYCAeKANCNWH---CP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1684 LGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAP--CEGSCVLGISEPAVTIKNIECAIIDHAFEQGWiKPEI 1761
Cdd:PRK12809 225 LHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGW-RPDV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1762 PEVRTGK-RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHV 1840
Cdd:PRK12809 304 SKVVPRSeKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEI 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1841 GKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKKQLG----GKNDIISAAGKNVIIIGGGDTG 1916
Cdd:PRK12809 384 GRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFLTAHTRQLMGlpesEEYPLTDVEGKRVVVLGGGDTT 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1917 CDCIATSLRQGAKSITTfeilpeppQKRAQDNPWPQWPKVFrVDYGHEEVKLKWGKDPrQYCTTTkefvgENGAIKGVNT 1996
Cdd:PRK12809 464 MDCLRTSIRLNAASVTC--------AYRRDEVSMPGSRKEV-VNAREEGVEFQFNVQP-QYIACD-----EDGRLTAVGL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1997 VEVEWTKT-ETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQYG---TSNSKVFAAGD 2072
Cdd:PRK12809 529 IRTAMGEPgPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMPWLQGSGIKLDKWGLIQTGDVGYLptqTHLKKVFAGGD 608
|
490 500
....*....|....*....|..
gi 386771285 2073 CRRGQSLVVWAITEGRQAARQV 2094
Cdd:PRK12809 609 AVHGADLVVTAMAAGRQAARDM 630
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
1642-2098 |
6.91e-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: 6.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1642 ERQKDWDEVyNFPHVRKNLKVQAARCMECGvPFCQSNSTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVC 1721
Cdd:TIGR01316 4 ERSKLFQEA-ALGYTEQLALVEAQRCLNCK-DATKPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1722 PAP--CEGSCVLG-----ISEPaVTIKNIECAIIDHAFEQGWIKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVT 1794
Cdd:TIGR01316 82 PQErqCEGQCTVGkmfkdVGKP-VSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1795 VFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRD 1874
Cdd:TIGR01316 161 VFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1875 LKGIHFAMEFLEAQQ--KKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFEILPEPPQKRAQDnpwpq 1952
Cdd:TIGR01316 241 LCGVYSANDFLTRANlmKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAEVHCLYRRTREDMTARVEE----- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1953 wpkvfrVDYGHEE-VKLKWgkdprqYCTTTkEFVG-ENGAIKGVNTVEVE-WTKTETGQWRMQEVAGSEKYFPADLILLA 2029
Cdd:TIGR01316 316 ------IAHAEEEgVKFHF------LCQPV-EIIGdEEGNVRAVKFRKMDcQEQIDSGERRFLPCGDAECKLEADAVIVA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386771285 2030 MGfLGPEKTVPSELGLELDPRGNIKAsNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYL 2098
Cdd:TIGR01316 383 IG-NGSNPIMAETTRLKTSERGTIVV-DEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
1567-2101 |
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 386771285 1567 EYQKALKDMAEQQAVEQplksaieNGNGKHEPHIKDIEEAIQDVVLEQKRADRvldktrgfvkyKRESAPYRDAGERQKD 1646
Cdd:PRK12778 249 DFDEMLKRMGAYKTIEG-------EELLKLEERTAAWRAELRKSMKPKERTAI-----------ERVPMPELDPEYRAHN 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1647 WDEVYNFPHVRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCP--AP 1724
Cdd:PRK12778 311 RFEEVNLGLTKEQAMTEAKRCLDCKNPGCV---EGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPqeKQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1725 CEGSCVLGIS-EPAVTIKNIECAIIDHAFEQGwiKPEIPEV--RTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDR 1801
Cdd:PRK12778 388 CESKCIHGKMgEEAVAIGYLERFVADYERESG--NISVPEVaeKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1802 VGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQE-YDAVLLTTGSTWPRDLPLANRDLKGIHF 1880
Cdd:PRK12778 466 IGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIASGAGLPNFMNIPGENSNGVMS 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1881 AMEFL-EAQQKKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFeilpeppQKRAQDnpwpQWP-KVFR 1958
Cdd:PRK12778 546 SNEYLtRVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIV-------YRRSEE----EMPaRLEE 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1959 VDYGHEE-VKLKWGKDPRQYCTTtkefvgENGAIKGVNTVEVEWTKTE-TGQWRMQEVAGSEKYFPADLILLAMGfLGPE 2036
Cdd:PRK12778 615 VKHAKEEgIEFLTLHNPIEYLAD------EKGWVKQVVLQKMELGEPDaSGRRRPVAIPGSTFTVDVDLVIVSVG-VSPN 687
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386771285 2037 KTVPSEL-GLELDPRGNIKAsNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGR 2101
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 ... |
1345-1502 |
1.30e-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: 1.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1345 RAFGSTLSYHIACKYGeagLPAGkSIDIFLEGSAGQSFCAFLArGVNVTLKGDANDYVGKGLCGGNVVIMPQdtvpfESH 1424
Cdd:cd00504 1 RAVGTRGSRYIGKRPG---LPED-TVEIIINGSAGQSFGAFMA-GGTITVEGNANDYVGKGMSGGEIVIHPP-----AGD 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386771285 1425 LNVIVGNVCLYGATEGTAYFRGIASERFCVRNSGVTAVVEGVGD-HGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYD 1502
Cdd:cd00504 71 ENGIAGNVALYGATGGKIFVRGNAGERFGVRMSGGTIVVEGVGDdFGGEYMTGGTIVVLGDAGRNFGAGMSGGVIYVRG 149
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
1657-2106 |
1.57e-60 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 221.53 E-value: 1.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1657 RKNL-KVQAARCMECGVPfCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAPCEGSCVL-GIS 1734
Cdd:PRK12814 86 RQSLeRLIEQHCGDCLGP-CE---LACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRhGVD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1735 EPaVTIknieCAIIDHAFEQGWIKPE--IPEVR--TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGI 1810
Cdd:PRK12814 162 EP-VSI----CALKRYAADRDMESAEryIPERApkSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1811 PTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLeaqQK 1890
Cdd:PRK12814 237 PRFRLPESVIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL---RN 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1891 KQLGGKndiiSAAGKNVIIIGGGDTGCDCIATSLRQGAKSITtfeIL-----PEPPQKRAQDNpwpqwpkvfrvDYGHEE 1965
Cdd:PRK12814 314 VALGTA----LHPGKKVVVIGGGNTAIDAARTALRLGAESVT---ILyrrtrEEMPANRAEIE-----------EALAEG 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1966 VKLKWGKDPRQYCTTtkefvgeNGAIKgVNTVEVEWTK-TETGQWRMQEVAGSEKYFPADLILLAMG-FLGPEKTVPSel 2043
Cdd:PRK12814 376 VSLRELAAPVSIERS-------EGGLE-LTAIKMQQGEpDESGRRRPVPVEGSEFTLQADTVISAIGqQVDPPIAEAA-- 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386771285 2044 GLELDPRGNIKASNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGRPSGLP 2106
Cdd:PRK12814 446 GIGTSRNGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGKPVTAP 508
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
1559-2099 |
9.56e-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: 9.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1559 KFVKVFPYEYQKALKDMAEQQAVEQPLKSAIENGNgKHEPHIKDIEeaiQDVVLEQKRADRVLDKtrgfVKYKRESAPYR 1638
Cdd:PRK12775 234 KFACVDGPDFDGHKVDFKELHARQKRFKSQEDRAN-EDYAHVCNLE---KQLFEEGKRNYKKLKT----LVPHQTPMPER 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1639 DAGERQKDWDEVyNFPHVRKNLKVQAARCMECGVPFCQSnstGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTG 1718
Cdd:PRK12775 306 DAVERARNFKEV-NLGYSLEDALQEAERCIQCAKPTCIA---GCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICG 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1719 RVCP--APCEGSCVLGISEPAVTIKNIECAIIDHAFEQGWIKPEIPEvRTGKrVAIVGSGPSGLAASQQLNRAGHFVTVF 1796
Cdd:PRK12775 382 RVCPqeTQCEAQCIIAKKHESVGIGRLERFVGDNARAKPVKPPRFSK-KLGK-VAICGSGPAGLAAAADLVKYGVDVTVY 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1797 ERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLKAEQLLQE--YDAVLLTTGSTWPRDLPLANRD 1874
Cdd:PRK12775 460 EALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGEF 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1875 LKGIHFAMEFLeaQQKKQLGGKN----DIISAAGKNVIIIGGGDTGCDCIATSLRQGAKSITTFeilpeppqKRAQDNPW 1950
Cdd:PRK12775 540 AGQVYSANEFL--TRVNLMGGDKfpflDTPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCV--------YRRSEAEA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1951 PQwpKVFRVDYGHEEvklkwGKDPRQYCTTTKEFVGENGAIKGVNTVEVEWTKTETGQWRMQEVAGSEKYFPADLILLAM 2030
Cdd:PRK12775 610 PA--RIEEIRHAKEE-----GIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKPMPTGEFKDLECDTVIYAL 682
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386771285 2031 GFLGPEKTVPSELGLELDPRGNIKASNGQYGTSNSK----VFAAGDCRRGQSLVVWAITEGRQAARQVDSYLT 2099
Cdd:PRK12775 683 GTKANPIITQSTPGLALNKWGNIAADDGKLESTQSTnlpgVFAGGDIVTGGATVILAMGAGRRAARSIATYLR 755
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
1663-2100 |
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 386771285 1663 QAARCMECGVpfCQSNstgCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCPAPCEGSCVLGISEPAVTIKN 1742
Cdd:PRK13984 183 EAARCVECGI--CTDT---CPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRW 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1743 IECAIIDHAFEQGWIK-PEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVK 1821
Cdd:PRK13984 258 LKRYIVDNVPVEKYSEiLDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1822 RRVDLMADEGIEFRTNVHVGKDLKAEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEaQQKKQLGGKNDIIS 1901
Cdd:PRK13984 338 KDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPLLR-EIRDYLRGEGPKPK 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1902 AAgKNVIIIGGGDTGCDcIATSLRQ------GAKSIT------TFEILPEPPQKraqdnpwpqwpkvfrVDYGHEE-VKL 1968
Cdd:PRK13984 417 IP-RSLVVIGGGNVAMD-IARSMARlqkmeyGEVNVKvtslerTFEEMPADMEE---------------IEEGLEEgVVI 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1969 KWGKDPRqyctttkEFVGENGAIKGVNTVEVEWTKTETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTVPSELGLELD 2048
Cdd:PRK13984 480 YPGWGPM-------EVVIENDKVKGVKFKKCVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDYSYLPEELKSKLE 552
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 386771285 2049 -PRGNIKaSNGQYGTSNSKVFAAGDCRRGQSlVVWAITEGRQAARQVDSYLTG 2100
Cdd:PRK13984 553 fVRGRIL-TNEYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRK 603
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
1760-2101 |
1.75e-48 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 177.49 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1760 EIPEvRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVH 1839
Cdd:PRK12770 12 EKPP-PTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1840 V---------------GKDLKAEQLLQEYDAVLLTTGsTW-PRDLPLANRDLKGIHFAMEFLEAQQKKQLGG--KNDIIS 1901
Cdd:PRK12770 91 VccgeplheeegdefvERIVSLEELVKKYDAVLIATG-TWkSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYlpWEKVPP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1902 AAGKNVIIIGGGDTGCDCIATSLRQGAKSITTF--EILPEPPQKRAQDNpwpqwpkvfRVdyghEEVKLKWgkdpRQYCT 1979
Cdd:PRK12770 170 VEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAyrRTINEAPAGKYEIE---------RL----IARGVEF----LELVT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1980 TTkEFVGEnGAIKGVNTVEVEWTK-TETGQWRMQEVAGSEKYFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNg 2058
Cdd:PRK12770 233 PV-RIIGE-GRVEGVELAKMRLGEpDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDE- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 386771285 2059 QYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQVDSYLTGR 2101
Cdd:PRK12770 310 KHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
1635-2094 |
1.11e-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: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1635 APY-RDAGERQKDWDEV-----------YNFPHVRKNLKVQAARCMEC-------GVPFCQSNST--GCPLGNIIPKWND 1693
Cdd:PRK12779 146 PPYiRPAEERAVDFDLVnqgylgyqslgYSVREVELFVWLEVMRDKQCddkpcelGVLVQGKAEPkgGCPVKIHIPEMLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1694 LVFHGEWQEALRQLLQTNNFPEFTGRVCPAP--CEGSCVLgiSEPAVTIKNIECAIIDHAFEQG-------------WIK 1758
Cdd:PRK12779 226 LLGNGKHREALELIESCNPLPNVTGRVCPQElqCQGVCTH--TKRPIEIGQLEWYLPQHEKLVNpnanerfagrispWAA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1759 PEIPEVrtgkrvAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNV 1838
Cdd:PRK12779 304 AVKPPI------AVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNF 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1839 HVGK-----DLKAEQLLQeydaVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKKQlGGKND----IISAAGKNVII 1909
Cdd:PRK12779 378 VVGKtatleDLKAAGFWK----IFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNLMR-GLDDDyetpLPEVKGKEVFV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1910 IGGGDTGCDCIATSLRQGAKSITTFeilpeppqKRAQDnpwpQWPKvfRVDYGH----EEVKLKWGKDPRqyctttkEFV 1985
Cdd:PRK12779 453 IGGGNTAMDAARTAKRLGGNVTIVY--------RRTKS----EMPA--RVEELHhaleEGINLAVLRAPR-------EFI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1986 GEN------GAIKGVNTVEvewTKTETGQWRMQEVAGSEKyFPADLILLAMGFLGPEKTVPSELGLELDPRGNIKASNGQ 2059
Cdd:PRK12779 512 GDDhthfvtHALLDVNELG---EPDKSGRRSPKPTGEIER-VPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGS 587
|
490 500 510
....*....|....*....|....*....|....*
gi 386771285 2060 YGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQV 2094
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 386771285 274 DYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLR------VLAHNGEINTLRGNVNLMKAREGVMQSDlfgdqlkkl 347
Cdd:cd00352 56 DVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEARGYRFEGE--------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 348 ypvvepnlSDSGSFDCVLEFLTMASDrsLPESVMTMVPEawqndktmpqekrdfyqwaacvmepWDGPALISFTDG--RY 425
Cdd:cd00352 127 --------SDSEVILHLLERLGREGG--LFEAVEDALKR-------------------------LDGPFAFALWDGkpDR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 386771285 426 IGAVLDRNGLRPSRFYVTKENVLVMASEVGVydVDPSQVTLKSRLKPGRML 476
Cdd:cd00352 172 LFAARDRFGIRPLYYGITKDGGLVFASEPKA--LLALPFKGVRRLPPGELL 220
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
1643-1756 |
1.26e-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: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1643 RQKDWDEVYNfPHVRKNLKVQAARCMECGVPFCQsnsTGCPLGNIIPKWNDLVFHGEWQEALRQLLQTNNFPEFTGRVCP 1722
Cdd:pfam14691 1 RIKNFEEVAL-GYTEEEAIAEASRCLQCKDPPCV---KGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCP 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 386771285 1723 A--PCEGSCVLGISEP-AVTIKNIECAIIDHAFEQGW 1756
Cdd:pfam14691 77 QerQCEGACVLGKKGFePVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
1770-2102 |
7.16e-25 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 107.13 E-value: 7.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERnDRVGGLLQ--------YGIP--------TMKLSKEVVKRRVDLMADE--G 1831
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPegisgpelAERLREQAERFGAEILLEEvtS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1832 IEFRTNVHV-----GKDLKAeqllqeyDAVLLTTGSTwPRDLPLANRDL---KGIHFAmefleaqqkkqlgGKNDIISAA 1903
Cdd:COG0492 82 VDKDDGPFRvttddGTEYEA-------KAVIIATGAG-PRKLGLPGEEEfegRGVSYC-------------ATCDGFFFR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1904 GKNVIIIGGGDTGCDcIATSLRQGAKSITtfeILPEPPQKRAQDNpwpQWPKVFRvdygHEEVKLKWGkdprqycTTTKE 1983
Cdd:COG0492 141 GKDVVVVGGGDSALE-EALYLTKFASKVT---LIHRRDELRASKI---LVERLRA----NPKIEVLWN-------TEVTE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1984 FVGENgaikGVNTVEVEWTKTetgqwrmqevaGSEKYFPADLILLAMGFLgPEKTVPSELGLELDPRGNIKAsNGQYGTS 2063
Cdd:COG0492 203 IEGDG----RVEGVTLKNVKT-----------GEEKELEVDGVFVAIGLK-PNTELLKGLGLELDEDGYIVV-DEDMETS 265
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 386771285 2064 NSKVFAAGDCRRGQS-LVVWAITEGRQAARQVDSYLTGRP 2102
Cdd:COG0492 266 VPGVFAAGDVRDYKYrQAATAAGEGAIAALSAARYLEPLK 305
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1768-2087 |
2.66e-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: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDR---VGGLLQYGIPTMKLSKEVVKRRVDLMAD---------EGIEFR 1835
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpyGGCVLSKALLGAAEAPEIASLWADLYKRkeevvkklnNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1836 TNVHV------GKDLKAEQLLQ------EYDAVLLTTGStWPRDLPLANRDLKGIHFA-----MEFLEAQQKkqlggknd 1898
Cdd:pfam07992 81 LGTEVvsidpgAKKVVLEELVDgdgetiTYDRLVIATGA-RPRLPPIPGVELNVGFLVrtldsAEALRLKLL-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1899 iisaaGKNVIIIGGGDTGCDCiATSLRQGAKSITTFEILPEPpqKRAQDNPWPQW-PKVFRvdygHEEVKLKWGkdprqy 1977
Cdd:pfam07992 152 -----PKRVVVVGGGYIGVEL-AAALAKLGKEVTLIEALDRL--LRAFDEEISAAlEKALE----KNGVEVRLG------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1978 cTTTKEFVGENGAIKgvntvevewTKTETGQwrmqevagsekYFPADLILLAMGFlGPEKTVPSELGLELDPRGNIKAsN 2057
Cdd:pfam07992 214 -TSVKEIIGDGDGVE---------VILKDGT-----------EIDADLVVVAIGR-RPNTELLEAAGLELDERGGIVV-D 270
|
330 340 350
....*....|....*....|....*....|.
gi 386771285 2058 GQYGTSNSKVFAAGDCRRGQ-SLVVWAITEG 2087
Cdd:pfam07992 271 EYLRTSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
1793-2113 |
2.64e-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: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1793 VTVFERNDRVGGLlQYGIPTM-----KLSKEVVKRRVDLMADEGIEFRTNVHVGK-DLKAEQLL------QEYDAVLLTT 1860
Cdd:COG0446 8 ITVIEKGPHHSYQ-PCGLPYYvgggiKDPEDLLVRTPESFERKGIDVRTGTEVTAiDPEAKTVTlrdgetLSYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1861 GStWPRDLPLANRDLKGIHFAMEFLEAQQKKQLggkndIISAAGKNVIIIGGGDTGCDcIATSLRQGAKSITTFEilpep 1940
Cdd:COG0446 87 GA-RPRPPPIPGLDLPGVFTLRTLDDADALREA-----LKEFKGKRAVVIGGGPIGLE-LAEALRKRGLKVTLVE----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1941 pqkrAQDNPWPQWPKVFrVDYGHEE-----VKLKWGkdprqycTTTKEFVGENGaikgvntVEVEWTKTETgqwrmqeva 2015
Cdd:COG0446 155 ----RAPRLLGVLDPEM-AALLEEElrehgVELRLG-------ETVVAIDGDDK-------VAVTLTDGEE--------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2016 gsekyFPADLILLAMGFlGPEKTVPSELGLELDPRGNIKAsNGQYGTSNSKVFAAGDCRR------GQSLVVW----AIT 2085
Cdd:COG0446 207 -----IPADLVVVAPGV-RPNTELAKDAGLALGERGWIKV-DETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasaANK 279
|
330 340
....*....|....*....|....*...
gi 386771285 2086 EGRQAARQvdsyLTGRPSGLPGPGGVIA 2113
Cdd:COG0446 280 QGRVAAEN----ILGGPAPFPGLGTFIS 303
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
1769-1933 |
1.40e-13 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 75.89 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1769 RVAIVGSGPSGLAASQQLNRA--GHFVTVFERNDRVGGLLQYGI-PTMKLSKEVVKRRVDLMADEGIEFRTNVHVGKDLK 1845
Cdd:PLN02852 28 HVCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1846 AEQLLQEYDAVLLTTGSTWPRDLPLANRDLKGIHFAMEFLEAQQKKQLGGKNDIISAAGKNVIIIGGGDTGCDCIATSLR 1925
Cdd:PLN02852 108 LSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNGHPDCVHLPPDLKSSDTAVVLGQGNVALDCARILLR 187
|
....*...
gi 386771285 1926 QGAKSITT 1933
Cdd:PLN02852 188 PTDELAST 195
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
1770-2098 |
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 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLL------QY-GIPTMKLSKEVVKRrvdlMADEGIEFRTNV---H 1839
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTttteveNYpGFPEGISGPELMEK----MKEQAVKFGAEIiyeE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1840 VGKDLKAEQLL-------QEY--DAVLLTTGSTwPRDLPLANRDlkgihfamEFLeaqqkkqlgGKNdiISAA------- 1903
Cdd:TIGR01292 78 VIKVDKSDRPFkvytgdgKEYtaKAVIIATGAS-ARKLGIPGED--------EFW---------GRG--VSYCatcdgpf 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1904 --GKNVIIIGGGDTGCDcIATSLRQGAKSIT------TF---EILpeppQKRAQDNPwpqwpkvfrvdygheevklkwgK 1972
Cdd:TIGR01292 138 fkNKEVAVVGGGDSAIE-EALYLTRIAKKVTlvhrrdKFraeKIL----LDRLKKNP----------------------K 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1973 DPRQYCTTTKEFVGENGaikgVNTVEVEWTKTetgqwrmqevaGSEKYFPADLILLAMGFLGPEKTVPSELglELDPRGN 2052
Cdd:TIGR01292 191 IEFLWNSTVEEIVGDNK----VEGVKIKNTVT-----------GEEEELEVDGVFIAIGHEPNTELLKGLL--ELDENGY 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 386771285 2053 IKASNGQYgTSNSKVFAAGDCR-RGQSLVVWAITEGRQAARQVDSYL 2098
Cdd:TIGR01292 254 IVTDEGMR-TSVPGVFAAGDVRdKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1768-2108 |
7.80e-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: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHF--VTVF--ERN---DRVggLLQYGIPTMKLSKEVVKRRVDLMADEGIEFRTNVHV 1840
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDgeITVIgaEPHppyNRP--PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1841 GK-DLKAEQLL------QEYDAVLLTTGSTwPRDLPLANRDLKGIHF------AMEFLEAqqkkqlggkndiiSAAGKNV 1907
Cdd:COG1251 80 TAiDRAARTVTladgetLPYDKLVLATGSR-PRVPPIPGADLPGVFTlrtlddADALRAA-------------LAPGKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1908 IIIGGGDTGCDcIATSLRQGAKSITTFEilpeppqkrAQDNPWPQWpkvfrVDYG--------HEE--VKLKWGkdprqy 1977
Cdd:COG1251 146 VVIGGGLIGLE-AAAALRKRGLEVTVVE---------RAPRLLPRQ-----LDEEagallqrlLEAlgVEVRLG------ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1978 cTTTKEFVGEnGAIKGVntvevewtKTETGQWrmqevagsekyFPADLILLAMGflgpekTVPS-EL----GLELDpRGn 2052
Cdd:COG1251 205 -TGVTEIEGD-DRVTGV--------RLADGEE-----------LPADLVVVAIG------VRPNtELaraaGLAVD-RG- 255
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386771285 2053 IKAsNGQYGTSNSKVFAAGDC---------RRGQSLVVWAITEGRQAARQvdsyLTGRPSGLPGP 2108
Cdd:COG1251 256 IVV-DDYLRTSDPDIYAAGDCaehpgpvygRRVLELVAPAYEQARVAAAN----LAGGPAAYEGS 315
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
1768-1807 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQ 1807
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
|
|
| arch_gltB |
cd00981 |
Archaeal-type gltB domain. This domain shares sequence similarity with a region of unknown ... |
1368-1566 |
9.75e-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: 9.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1368 KSIDIFLEGSAGQSFCAFLArGVNVTLKGDANDYVGKGLCGGNVVImpqdtvpfesHLNVivGNVCLYGATEGTAYFRGI 1447
Cdd:cd00981 45 GNVRINIYGVPGNDLGAFMS-GPTIIVYGNAQDDVGNTMNDGKIVI----------HGSA--GDVLGYAMRGGKIFIRGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1448 ASERFCVR----NSGVTAVVEG--VGDHGCEYMTGGVVVILGL------TGRNFAAGMSGGIAYVydldgsfKPKVNPE- 1514
Cdd:cd00981 112 AGYRVGIHmkeyKDKVPVLVIGgtAGDFLGEYMAGGVIIVLGLgtdeepVGRYIGTGMHGGVIYI-------RGKVERSk 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386771285 1515 -SVELLPLEI-EKDVLLVKELLADFIEKTGSKVAKELldnwaeaQGKFVKVFPY 1566
Cdd:cd00981 185 lGKEVPKFELtEEDLEFIEKYIEEFCKEFGYDKAEIL-------DEEFTKLKPK 231
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
1769-1806 |
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 386771285 1769 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLL 1806
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLA 38
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1770-2094 |
1.28e-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: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERnDRVGG------------LL-------------QYGIPTMKLS---KEVVK 1821
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskaLLhaaevahearhaaEFGISAGAPSvdwAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1822 RR-----------VDLMADEGIEF----------RTnVHV--GKDLKAeqllqeyDAVLLTTGSTwPRDLPLANRDLKGI 1878
Cdd:COG1249 85 RKdkvvdrlrggvEELLKKNGVDVirgrarfvdpHT-VEVtgGETLTA-------DHIVIATGSR-PRVPPIPGLDEVRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1879 HFAMEFLEAQQkkqlggkndiisaAGKNVIIIGGGDTGCDcIATSLRQ-GAKsITTFE----ILP-EPPQ--KRAQdnpw 1950
Cdd:COG1249 156 LTSDEALELEE-------------LPKSLVVIGGGYIGLE-FAQIFARlGSE-VTLVErgdrLLPgEDPEisEALE---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1951 pqwpKVFRvdygHEEVKLkwgkdprqyctttkefvgengaIKGVNTVEVEwtKTETGQWRMQEVAGSEKYFPADLILLAM 2030
Cdd:COG1249 217 ----KALE----KEGIDI----------------------LTGAKVTSVE--KTGDGVTVTLEDGGGEEAVEADKVLVAT 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 2031 GF------LGPEKTvpselGLELDPRGNIKAsNGQYGTSNSKVFAAGDCRRGQSLVVWAITEGRQAARQV 2094
Cdd:COG1249 265 GRrpntdgLGLEAA-----GVELDERGGIKV-DEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENI 328
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
1765-1804 |
1.90e-08 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 59.16 E-value: 1.90e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 386771285 1765 RTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
1772-1804 |
3.42e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 52.15 E-value: 3.42e-08
10 20 30
....*....|....*....|....*....|...
gi 386771285 1772 IVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
1768-1804 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
1766-1804 |
7.32e-08 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 57.05 E-value: 7.32e-08
10 20 30
....*....|....*....|....*....|....*....
gi 386771285 1766 TGKRVAIVGSGPSGLAASQQLNRAgHFVTVFERNDRVGG 1804
Cdd:COG2907 2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
1766-1878 |
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 386771285 1766 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGllqygiptmKLSKEVVKRRVDLMADEGIEFRTNVHVgKDLK 1845
Cdd:COG0446 123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---------VLDPEMAALLEEELREHGVELRLGETV-VAID 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 386771285 1846 AEQLLQ---------EYDAVLLTTG----STWPRDLPLANRDLKGI 1878
Cdd:COG0446 193 GDDKVAvtltdgeeiPADLVVVAPGvrpnTELAKDAGLALGERGWI 238
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1769-1840 |
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 386771285 1769 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGllqygiptmKLSKEVVKRRVDLMADEGIEFRTNVHV 1840
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
1768-1804 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1762-1929 |
2.05e-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: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1762 PEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG-----------------LLQY------GIPTMKLSKE 1818
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpshLYSLpffpnwSDDPDFPTGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1819 VVK-------RRVDLMADegIEFRTNVHVGKDLKAEQLLQ---------EYDAVLLTTGSTW-PRdLPlanrDLKGIH-F 1880
Cdd:COG2072 81 EILayleayaDKFGLRRP--IRFGTEVTSARWDEADGRWTvttddgetlTARFVVVATGPLSrPK-IP----DIPGLEdF 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 386771285 1881 AMEFLEAQQKK---QLggkndiisaAGKNVIIIGGGDTGCDCIATSLRQGAK 1929
Cdd:COG2072 154 AGEQLHSADWRnpvDL---------AGKRVLVVGTGASAVQIAPELARVAAH 196
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
1766-1861 |
2.85e-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: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1766 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLqygipTMKLSKEVVKRrvdlMADEGIEFRTNVHV----G 1841
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAF-----DEEISAALEKA----LEKNGVEVRLGTSVkeiiG 221
|
90 100
....*....|....*....|....*
gi 386771285 1842 KDLKAEQLLQE-----YDAVLLTTG 1861
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 386771285 252 YICSLSDRTVVYKGLFTSDQLWDYYtDLkdPEFETYLALVHTRFSTNTFPSWERAHPLRV----LAHNGEINTLRGNVNL 327
Cdd:cd01907 46 FVYSSGKDMEVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGSNREY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 328 MKaREGV---MQSD------LFGDQLKKLYPVVEpnlsdsgsfdcvlefltmasdrsLPESVMTMVPEAWQNDKTMPQEK 398
Cdd:cd01907 123 LE-RFGYkfeTETDteviayYLDLLLRKGGLPLE-----------------------YYKHIIRMPEEERELLLALRLTY 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 386771285 399 R--DFyqwaacvmepwDGP-ALISFTDGRYIGAVlDRNGLRPSRFYVTKENVlVMASEV 454
Cdd:cd01907 179 RlaDL-----------DGPfTIIVGTPDGFIVIR-DRIKLRPAVVAETDDYV-AIASEE 224
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
1766-1808 |
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 386771285 1766 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQY 1808
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| FwdC |
COG2218 |
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion]; |
1357-1520 |
1.35e-06 |
|
Formylmethanofuran dehydrogenase subunit C [Energy production and conversion];
Pssm-ID: 441820 [Multi-domain] Cd Length: 264 Bit Score: 52.12 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1357 CKYGEAGLPAGKsidIFLEGSAGqSFCAFLARGVNVTLKGDANDYVGKGLCGGNVVIMpqdtvpfeshlnvivGNV---- 1432
Cdd:COG2218 72 VKRIGAGMTAGE---IIVEGDVG-MYLGAGMKGGKITVNGNAGSFAGAEMKGGEIEIN---------------GNAgdfl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1433 --CLYGA----TEGTAYFRGIASERFCVRNSGVTAVVEG-VGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYDLDG 1505
Cdd:COG2218 133 gaAYRGDwrgmSGGTIIVKGNAGDRLGDRMRRGTIIIEGdAGDFAGSRMIAGTIIVKGNAGRRPGYGMKRGTIVVAGKPE 212
|
170
....*....|....*
gi 386771285 1506 SFKPKVNPESVELLP 1520
Cdd:COG2218 213 ELLPTFVDCGTHELV 227
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
1768-2107 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNR--AGHFVTVFERNDR-----------VGG---------------LLQYGIpTMKLSKEV 1819
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRlnKELEITVYEKTDIvsfgacglpyfVGGffddpntmiartpeeFIKSGI-DVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1820 VKrrvdlmadegIEFRTNVHVGKDLKAEQLLQE-YDAVLLTTGSTwPRDLPLANRDLKGIHFAMEFLEAQQKKQLGGKND 1898
Cdd:PRK09564 80 VK----------VDAKNKTITVKNLKTGSIFNDtYDKLMIATGAR-PIIPPIKNINLENVYTLKSMEDGLALKELLKDEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1899 IisaagKNVIIIGGGDTGCDcIATSLRQGAKSITTFE----ILPEPPQKRAQDnpwpqwpkVFRVDYGHEEVKLKWGKdp 1974
Cdd:PRK09564 149 I-----KNIVIIGAGFIGLE-AVEAAKHLGKNVRIIQledrILPDSFDKEITD--------VMEEELRENGVELHLNE-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1975 rqyctTTKEFVGENGaIKGVNTvevewtktetgqwrmqevagSEKYFPADLILLAMGFlGPEKTVPSELGLELDPRGNIK 2054
Cdd:PRK09564 213 -----FVKSLIGEDK-VEGVVT--------------------DKGEYEADVVIVATGV-KPNTEFLEDTGLKTLKNGAII 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386771285 2055 ASngQYG-TSNSKVFAAGDCRrgqslVVWAITEGRQA-----------ARQVDSYLTGRPSGLPG 2107
Cdd:PRK09564 266 VD--EYGeTSIENIYAAGDCA-----TIYNIVSNKNVyvplattanklGRMVGENLAGRHVSFKG 323
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
1759-1840 |
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 386771285 1759 PEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGL---LQYGIPTMKLSKEVVKRRV-DLMADEGIEF 1834
Cdd:COG1148 132 LEPIKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEPLIaEVEANPNITV 211
|
....*.
gi 386771285 1835 RTNVHV 1840
Cdd:COG1148 212 YTGAEV 217
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
1766-1804 |
3.39e-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: 3.39e-06
10 20 30
....*....|....*....|....*....|....*....
gi 386771285 1766 TGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
1768-1805 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGL 1805
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
1758-1807 |
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 386771285 1758 KPEIPEVRTGKRVAIVGSGPSGLAASQQLNRA-GHFVTVFERNDRVGGLLQ 1807
Cdd:PLN02576 3 IAEGSAAASSKDVAVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGGNIT 53
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1768-2102 |
5.41e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 50.90 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1768 KRVAIVGSGPSGLAASQQLNR---AGHFVTVFERNDR--VGGLLqYGIPTMKLSKEVVKRRV-DLMADEGIEFR----TN 1837
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYhlFQPLL-PEVAAGTLSPDDIAIPLrELLRRAGVRFIqgevTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1838 VHV---------GKDLkaeqllqEYDAVLLTTGSTwPRDLPLAN-----RDLKGIHFAMEF-------LEAQQKKQLGgk 1896
Cdd:COG1252 81 IDPeartvtladGRTL-------SYDYLVIATGSV-TNFFGIPGlaehaLPLKTLEDALALrerllaaFERAERRRLL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1897 ndiisaagkNVIIIGGGDTGCD---CIATSLRQGAK---------SITTFE----ILPE-PP--QKRAQdnpwpqwpKVF 1957
Cdd:COG1252 151 ---------TIVVVGGGPTGVElagELAELLRKLLRypgidpdkvRITLVEagprILPGlGEklSEAAE--------KEL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1958 RvDYGheeVKLKWGkdprqycTTTKEfVGENGAIkgvntvevewtkTETGQWrmqevagsekyFPADLILLAMGFLGPEk 2037
Cdd:COG1252 214 E-KRG---VEVHTG-------TRVTE-VDADGVT------------LEDGEE-----------IPADTVIWAAGVKAPP- 257
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386771285 2038 tVPSELGLELDPRGNIKASNGQYGTSNSKVFAAGDC-----RRGQSL---VVWAITEGRQAARQVDSYLTGRP 2102
Cdd:COG1252 258 -LLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCaavpdPDGKPVpktAQAAVQQAKVLAKNIAALLRGKP 329
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
1769-1874 |
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 386771285 1769 RVAIVGSGPSGLAASQQLNRAGHF-VTVFERNDRVGGLLQYGIPTMKLSKEVVKRRVDL-MADEGIEFRTNVHVGKDLKA 1846
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHERVkVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDPvFLSPNYRFFGNVHVGVDLKM 120
|
90 100
....*....|....*....|....*...
gi 386771285 1847 EQLLQEYDAVLLTTGSTwPRDLPLANRD 1874
Cdd:PTZ00188 121 EELRNHYNCVIFCCGAS-EVSIPIGQQD 147
|
|
| FwdC/FmdC |
cd00980 |
FwdC/FmdC. This domain of unknown function is found in the subunit C of formylmethanofuran ... |
1358-1520 |
9.34e-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: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1358 KYGEAGLPAGKsidIFLEGSAGQsFCAFLARGVNVTLKGDANDYVGKGLCGGNVVImpqdtvpfESHLNVIVGnvCLY-- 1435
Cdd:cd00980 31 KRIGARMTAGE---IVVEGDVGM-YVGAGMKGGKLVVEGNAGSWAGCEMKGGEITI--------KGNAGDYVG--SAYrg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1436 ---GATEGTAYFRGIASERFCVRNSGVTAVVEG-VGDHGCEYMTGGVVVILGLTGRNFAAGMSGGIAYVYDLDGSFKPKV 1511
Cdd:cd00980 97 dwrGMSGGTITIEGNAGDRLGERMRRGEILIKGdAGIFAGIRMNGGTIIVRGDAGAHPGYEMKRGTIVIGGEIEELLPTF 176
|
....*....
gi 386771285 1512 NPESVELLP 1520
Cdd:cd00980 177 KEEGTEEDV 185
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
1768-1951 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHF---VTVFERNDRVGGLLQYGI--PTMKLSkeVVKRRVDLMADEGIEF-----RTN 1837
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRAPEplrITLFEPRPELGRGVAYSTdsPEHLLN--VPAGRMSAFPDDPDHFlrwlrENG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1838 VHVGKDLKAEQ-----LLQEY-----------------------------------------------DAVLLTTGSTWP 1865
Cdd:COG4529 84 ARAAPAIDPDAfvprrLFGEYlrerlaealarapagvrlrhiraevvdlerddggyrvtladgetlraDAVVLATGHPPP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1866 RDLPLANRDLKGIH---FAMEFLEaqqkkqlggknDIisAAGKNVIIIGGGDTGCDCIATSLRQGAK-SITTFE---ILP 1938
Cdd:COG4529 164 APPPGLAAGSPRYIadpWPPGALA-----------RI--PPDARVLIIGTGLTAIDVVLSLAARGHRgPITALSrrgLLP 230
|
250
....*....|...
gi 386771285 1939 EPpqkRAQDNPWP 1951
Cdd:COG4529 231 RA---HPPGAPLP 240
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1768-1861 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLlqygiptmkLSKEVVKRRVDLMADEgIEFRTNVHV-----GK 1842
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL---------EDPEVSKQAQKILSKE-FKIKLGAKVtsvekSG 239
|
90 100
....*....|....*....|....*.
gi 386771285 1843 DLKAEQLLQ-------EYDAVLLTTG 1861
Cdd:PRK06292 240 DEKVEELEKggktetiEADYVLVATG 265
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
1769-1803 |
3.30e-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: 3.30e-05
10 20 30
....*....|....*....|....*....|....*
gi 386771285 1769 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVG 1803
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
1769-1855 |
3.60e-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: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1769 RVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVG--------GLLQYGIPTM------KLSKEVVKRRVDLMADEGIE- 1833
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLRYLepselaRLALEALDLWEELEEELGIDc 80
|
90 100
....*....|....*....|....*
gi 386771285 1834 -FRTN--VHVGKDLKAEQLLQEYDA 1855
Cdd:pfam01266 81 gFRRCgvLVLARDEEEEALEKLLAA 105
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1732-1871 |
3.69e-05 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 48.21 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1732 GISEPAVTIKNIECAI-----IDHAFEQGwikpeipEVRTGKRVAIVGSGPSG----LAASQQLNRAGHF---------V 1793
Cdd:COG1252 116 GLAEHALPLKTLEDALalrerLLAAFERA-------ERRRLLTIVVVGGGPTGvelaGELAELLRKLLRYpgidpdkvrI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1794 TVFERNDRVGGllqygiptmKLSKEVVKRRVDLMADEGIEFRTNVHVgKDLKAEQLL------QEYDAVLLTTG---STW 1864
Cdd:COG1252 189 TLVEAGPRILP---------GLGEKLSEAAEKELEKRGVEVHTGTRV-TEVDADGVTledgeeIPADTVIWAAGvkaPPL 258
|
....*..
gi 386771285 1865 PRDLPLA 1871
Cdd:COG1252 259 LADLGLP 265
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
1767-1804 |
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 386771285 1767 GKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
1757-1839 |
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 386771285 1757 IKPEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLqygiptmkLSKEVVKRRVDLMADEGIEFRT 1836
Cdd:PLN03000 174 IKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRV--------YTKKMEANRVGAAADLGGSVLT 245
|
...
gi 386771285 1837 NVH 1839
Cdd:PLN03000 246 GTL 248
|
|
| Amino_oxidase |
pfam01593 |
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ... |
1778-1804 |
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 386771285 1778 SGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:pfam01593 2 AGLAAARELLRAGHDVTVLEARDRVGG 28
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
1770-2073 |
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 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERND------RVG-----GLL-------------QYGIPTMKLS---KEVVKR 1822
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclNVGcipskALIaaaeafheakhaeEFGIHADGPKidfKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1823 RvdlmaDEGIEFRTNvHVGKDLK---AEQLLQEY------------------DAVLLTTGSTWPRDLPLANRDLKGIHFA 1881
Cdd:PRK06292 86 V-----RRERDRFVG-GVVEGLEkkpKIDKIKGTarfvdpntvevngerieaKNIVIATGSRVPPIPGVWLILGDRLLTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1882 MEFLEaqQKKQlggkndiisaaGKNVIIIGGGDTGCDcIATSL-RQGAKsITTFE----ILP-EPP--QKRAQDnpwpQW 1953
Cdd:PRK06292 160 DDAFE--LDKL-----------PKSLAVIGGGVIGLE-LGQALsRLGVK-VTVFErgdrILPlEDPevSKQAQK----IL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1954 PKVFRVDYGHEEVKlkwgkdprqyctttkefvgengaIKGVNTVEVEWTktetgqwrmqEVAGSEKYFPADLILLAMG-- 2031
Cdd:PRK06292 221 SKEFKIKLGAKVTS-----------------------VEKSGDEKVEEL----------EKGGKTETIEADYVLVATGrr 267
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 386771285 2032 ----FLGPEKTvpselGLELDPRGNIKAsNGQYGTSNSKVFAAGDC 2073
Cdd:PRK06292 268 pntdGLGLENT-----GIELDERGRPVV-DEHTQTSVPGIYAAGDV 307
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
1768-1807 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNRAG--HFVTVFERNDRVGGLLQ 1807
Cdd:PRK11883 1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQ 42
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
1767-1870 |
3.92e-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: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1767 GKRVAIVGSGPSGLAASQQLNRAGHFVTVFErndrvggllqygiptmklSKEVVKRRVDLMADEGIEFRTNVHvgkdlkA 1846
Cdd:COG0771 4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSD------------------DRPAPELAAAELEAPGVEVVLGEH------P 59
|
90 100
....*....|....*....|....
gi 386771285 1847 EQLLQEYDAVLLTTGstWPRDLPL 1870
Cdd:COG0771 60 EELLDGADLVVKSPG--IPPDHPL 81
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
2013-2073 |
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 386771285 2013 EVAGSEKYFPADLILLAMG------FLGPEKTvpselGLELDPRGNIKAsNGQYGTSNSKVFAAGDC 2073
Cdd:PRK06370 250 DCNGGAPEITGSHILVAVGrvpntdDLGLEAA-----GVETDARGYIKV-DDQLRTTNPGIYAAGDC 310
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
1770-1882 |
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 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLQYG-----IPTMKLSKEVVKRRVD-----LMADEGIEFRT--- 1836
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSGlvgpdMGFYLNKEQVVGGIARefrqrLRARGGLPGPYglr 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 386771285 1837 ------NVHVGKDLkAEQLLQEYDAVLLTtgSTWPRDLPLANRDLKGIHFAM 1882
Cdd:pfam12831 82 ggwvpfDPEVAKAV-LDEMLAEAGVTVLL--HTRVVGVVKEGGRITGVTVET 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1763-1868 |
6.22e-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: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1763 EVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGGLLqygiptmkLSKEVVKRRVDLMADEGIEFRTNVHVgk 1842
Cdd:COG1251 138 ALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ--------LDEEAGALLQRLLEALGVEVRLGTGV-- 207
|
90 100
....*....|....*....|....*...
gi 386771285 1843 dlkaEQLLQEYD--AVLLTTGSTWPRDL 1868
Cdd:COG1251 208 ----TEIEGDDRvtGVRLADGEELPADL 231
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
1071-1195 |
9.65e-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: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1071 PHHDIYSIEDLAELIYDLKCSNPNARISVKLvSEVGVGVVASGVAKGKAEhIVISGHDGGTGASSwtgiknaglpwelGV 1150
Cdd:cd04722 91 HGAVGYLAREDLELIRELREAVPDVKVVVKL-SPTGELAAAAAEEAGVDE-VGLGNGGGGGGGRD-------------AV 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 386771285 1151 AETHQVLVLNNLRSRVIVQADGQLRTGFDVVVAALLGADEFGFST 1195
Cdd:cd04722 156 PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
1769-1857 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771285 1769 RVAIVGSGPSGLAASQQLNRAGHFVTVFERND-------RVGGLLQYGIPTM------KLSKEVVKRRVDLMADEGI--E 1833
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRpgsgasgRNAGQLRPGLAALadralvRLAREALDLWRELAAELGIdcD 83
|
90 100
....*....|....*....|....*.
gi 386771285 1834 FRTN--VHVGKDLKAEQLLQEYDAVL 1857
Cdd:COG0665 84 FRRTgvLYLARTEAELAALRAEAEAL 109
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1760-1840 |
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 386771285 1760 EIPEvrtgkRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVggllqygiptmkLSKE------VVKrrvDLMADEGIE 1833
Cdd:PRK06370 169 ELPE-----HLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL------------LPREdedvaaAVR---EILEREGID 228
|
....*..
gi 386771285 1834 FRTNVHV 1840
Cdd:PRK06370 229 VRLNAEC 235
|
|
| proto_IX_ox |
TIGR00562 |
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ... |
1768-1833 |
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 386771285 1768 KRVAIVGSGPSGLAASQQLNR----AGHFVTVFERNDRVGG----------LLQYGIPTMKLSKEVVkrrVDLMADEGIE 1833
Cdd:TIGR00562 3 KHVVIIGGGISGLCAAYYLEKeipeLPVELTLVEASDRVGGkiqtvkedgyLIERGPDSFLERKKSA---PDLVKDLGLE 79
|
|
| PLN02529 |
PLN02529 |
lysine-specific histone demethylase 1 |
1759-1804 |
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 386771285 1759 PEIPEVRTGKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:PLN02529 152 SPIPEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
1770-1802 |
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 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRV 1802
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
1770-1840 |
5.80e-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: 5.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386771285 1770 VAIVGSGPSGLAASQQLNRAGHF-VTVFERNDRVGGLLQYGipTMKLSKEVVKRRVDLMADE-GI---EFRTNVHV 1840
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAKNRGLkVAIIERSVSPGGGAWLG--GQLFSAMVVRKPAHLFLDEfGIpyeDEGDYVVV 93
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
1767-1840 |
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 386771285 1767 GKRVAIVGSGPSGLAASQQLNRAGHFVTVFERNDrvggllqygipTMKLSKEVVKRrvdLMADEGIEFRTNVHV 1840
Cdd:COG0492 141 GKDVVVVGGGDSALEEALYLTKFASKVTLIHRRD-----------ELRASKILVER---LRANPKIEVLWNTEV 200
|
|
| PLN02268 |
PLN02268 |
probable polyamine oxidase |
1770-1804 |
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 386771285 1770 VAIVGSGPSGLAASQQLNRAGHFVTVFERNDRVGG 1804
Cdd:PLN02268 3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
|
|
| |
