|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
75-1164 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1104.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 75 KQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLP 154
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 155 ELgdYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQ 232
Cdd:PRK11750 82 KN--YAVGMVFLnqDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 233 VFVLRKRAShELIKPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVL 312
Cdd:PRK11750 160 LFIARRRIE-KRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 313 AHNGEINTLRGNVNLMKAREGVMQSDLFGDqLKKLYPVVEPNLSDSGSFDCVLEFLtMASDRSLPESVMTMVPEAWQNDK 392
Cdd:PRK11750 239 AHNGEINTITGNRQWARARAYKFQTPLIPD-LQEAAPFVNETGSDSSSLDNMLELL-LAGGMDLFRAMRLLVPPAWQNNP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 393 TMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKP 472
Cdd:PRK11750 317 DMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 473 GRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQkitldeirnaNVLNTPPVDELAKLPASERGiFDPRL-----SLFG 547
Cdd:PRK11750 397 GELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEK----------NVRRLVPFEELPDEQVGSRE-LDDDTlksyqKQFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 548 YSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQP 627
Cdd:PRK11750 466 YSFEELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 628 SAQQVHRIWLTNPILSIPD-TQLLKRNTHrGWRTKVLDITfqYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 706
Cdd:PRK11750 546 TEGHAHRVIFKSPVLSYSDfKQLTTLDEE-HYRADTLDLN--YDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIA 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 707 iDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVNdk 786
Cdd:PRK11750 623 -KGRLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYR-- 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 787 QIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKAT 866
Cdd:PRK11750 700 QVMLNYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARK 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 867 PdtriLRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTtLDSVKKCALRGQLEFVTDRQSIDISEVEPA 946
Cdd:PRK11750 780 P----IDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKL-VNERPVATLRDLLALKPADNPIPLDEVEPA 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 947 SEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVTASYLANAD 1026
Cdd:PRK11750 855 EELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAE 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1027 DLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGV 1106
Cdd:PRK11750 930 VLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGV 1009
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 442632933 1107 GVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:PRK11750 1010 GTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHK 1067
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
73-1164 |
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: 1057.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 73 PGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVT 152
Cdd:COG0067 8 PAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 153 LPELGDYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFE 230
Cdd:COG0067 88 LPEPGEYAVGMVFLpqDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 231 RQVFVLRKRASHELIKPG---RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAH 307
Cdd:COG0067 168 RKLYVARKRIEKAIRALGlddEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 308 PLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEA 387
Cdd:COG0067 248 PFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVL-GGRSLPHAMMMLIPEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 388 WQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLK 467
Cdd:COG0067 327 WENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 468 SRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWL-QQKITLDEIRNANVLNTPPVDELAKlpasergifdpRLSLF 546
Cdd:COG0067 407 GRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLkENRIRLEDLPEPEEEPAPDDDLLLR-----------RQQAF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 547 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQ 626
Cdd:COG0067 476 GYTEEEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 627 PSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 706
Cdd:COG0067 556 EEEEARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 707 IDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELA-QALRDDGVIAPEVND 785
Cdd:COG0067 636 DSDAAPAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALElLLDGLLLGLEDAAAA 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 786 KQIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 865
Cdd:COG0067 716 AAAKKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEP 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 866 TPDT--RILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEV 943
Cdd:COG0067 796 GGLLlgLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 944 EPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRylnqDPNNSRRSAIKQVASGRFGVTASYLA 1023
Cdd:COG0067 876 EEEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1024 NADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSE 1103
Cdd:COG0067 952 AAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVA 1031
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632933 1104 VGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:COG0067 1032 AAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLL 1092
|
|
| 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 442632933 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:pfam00310 81 qDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 246 KPG--RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRG 323
Cdd:pfam00310 161 VEGgdKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 324 NVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASdRSLPESVMTMVPEAWQNDKTMPQEKRDFYQ 403
Cdd:pfam00310 241 NRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGG-RSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 404 WAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEK 483
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 442632933 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 442632933 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:cd00713 81 rDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 246 KPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRGNV 325
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 326 NLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEAWQNDKTMPQEKRDFYQWA 405
Cdd:cd00713 241 NWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVR-SGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 406 ACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEKKL 485
Cdd:cd00713 320 SSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRI 399
|
410
....*....|....
gi 442632933 486 IQDIELKAKIAKSR 499
Cdd:cd00713 400 LDDEEIKDQLAKRH 413
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| gltB |
PRK11750 |
glutamate synthase subunit alpha; Provisional |
75-1164 |
0e+00 |
|
glutamate synthase subunit alpha; Provisional
Pssm-ID: 236968 [Multi-domain] Cd Length: 1485 Bit Score: 1104.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 75 KQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLP 154
Cdd:PRK11750 2 HMGLYDPSLERDNCGFGLIAHMEGEPSHKLVRTAIHALARMTHRGGIAADGKTGDGCGLLLQKPDRFFRAVAEEAGWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 155 ELgdYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQ 232
Cdd:PRK11750 82 KN--YAVGMVFLnqDPELAAAARRILEEELQRETLSVVGWREVPTNPSVLGEIALSSLPRIEQVFVNAPAGWRERDFERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 233 VFVLRKRAShELIKPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVL 312
Cdd:PRK11750 160 LFIARRRIE-KRLADDKDFYVCSLSNLVIIYKGLMMPADLPRFYLDLADLRLESAICVFHQRFSTNTLPRWPLAQPFRYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 313 AHNGEINTLRGNVNLMKAREGVMQSDLFGDqLKKLYPVVEPNLSDSGSFDCVLEFLtMASDRSLPESVMTMVPEAWQNDK 392
Cdd:PRK11750 239 AHNGEINTITGNRQWARARAYKFQTPLIPD-LQEAAPFVNETGSDSSSLDNMLELL-LAGGMDLFRAMRLLVPPAWQNNP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 393 TMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKP 472
Cdd:PRK11750 317 DMDPDLRAFYEFNSMHMEPWDGPAGIVMTDGRYAACNLDRNGLRPARYVITKDKLITLASEVGIWDYQPDEVVEKGRVGP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 473 GRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQkitldeirnaNVLNTPPVDELAKLPASERGiFDPRL-----SLFG 547
Cdd:PRK11750 397 GELLVIDTRTGRILHSAEIDNDLKSRHPYKEWLEK----------NVRRLVPFEELPDEQVGSRE-LDDDTlksyqKQFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 548 YSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQP 627
Cdd:PRK11750 466 YSFEELDQVIRVLAENGQEAVGSMGDDTPMAVLSSQPRSIYDYFRQQFAQVTNPPIDPLREAHVMSLATCIGREMNVFCE 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 628 SAQQVHRIWLTNPILSIPD-TQLLKRNTHrGWRTKVLDITfqYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 706
Cdd:PRK11750 546 TEGHAHRVIFKSPVLSYSDfKQLTTLDEE-HYRADTLDLN--YDPEETGLEAAIKRLCDEAEQAVRDGTVLLVLSDRNIA 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 707 iDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVNdk 786
Cdd:PRK11750 623 -KGRLPIPAAMAVGAVQHRLVDKGLRCDANIIVETASARDPHHFAVLLGFGATAVYPYLAYETLGDLVDTGEILKDYR-- 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 787 QIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKAT 866
Cdd:PRK11750 700 QVMLNYRKGINKGLYKIMSKMGISTIASYRGSQLFEAVGLHDDVVDLCFKGVVSRIGGASFEDFEQDQKNLSKRAWLARK 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 867 PdtriLRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTtLDSVKKCALRGQLEFVTDRQSIDISEVEPA 946
Cdd:PRK11750 780 P----IDQGGLLKYVHGGEYHAYNPDVVNTLQKAVQSGDYSDYQEYAKL-VNERPVATLRDLLALKPADNPIPLDEVEPA 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 947 SEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVTASYLANAD 1026
Cdd:PRK11750 855 EELFKRFDSAAMSIGALSPEAHEALAIAMNRLGGRSNSGEGGEDPARY-----GTEKVSKIKQVASGRFGVTPAYLVNAE 929
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1027 DLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGV 1106
Cdd:PRK11750 930 VLQIKVAQGAKPGEGGQLPGDKVNPLIARLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKALVSVKLVSEPGV 1009
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 442632933 1107 GVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:PRK11750 1010 GTIATGVAKAYADLITISGYDGGTGASPLTSVKYAGSPWELGLAETHQALVANGLRHK 1067
|
|
| GltB1 |
COG0067 |
Glutamate synthase domain 1 [Amino acid transport and metabolism]; Glutamate synthase domain 1 ... |
73-1164 |
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: 1057.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 73 PGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVT 152
Cdd:COG0067 8 PAAQGLYDPAFEHDACGVGFVAHIKGRKSHDIVEDALEALENLEHRGAVGADGKTGDGAGILIQIPDAFFRAEAAELGIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 153 LPELGDYATGIFYL--DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFE 230
Cdd:COG0067 88 LPEPGEYAVGMVFLpqDEAARAAARAIIEEILAEEGLTVLGWRDVPVDPSVLGETARATEPVIEQVFVARPDGLDGDAFE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 231 RQVFVLRKRASHELIKPG---RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAH 307
Cdd:COG0067 168 RKLYVARKRIEKAIRALGlddEDFYICSLSSRTIVYKGMLTPEQLGEFYPDLQDPRFESALALVHQRFSTNTFPSWPLAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 308 PLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEA 387
Cdd:COG0067 248 PFRYLAHNGEINTLRGNRNWMRAREALLASPLFGDDLEKLLPIVNPGGSDSASLDNVLELLVL-GGRSLPHAMMMLIPEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 388 WQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLK 467
Cdd:COG0067 327 WENNPDMDPERRAFYEYHSALMEPWDGPAAIVFTDGRQIGATLDRNGLRPARYVVTKDGLVILASEVGVLDIPPEDIVEK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 468 SRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWL-QQKITLDEIRNANVLNTPPVDELAKlpasergifdpRLSLF 546
Cdd:COG0067 407 GRLQPGKMLLVDLEEGRIIDDEEIKAELAAAHPYGEWLkENRIRLEDLPEPEEEPAPDDDLLLR-----------RQQAF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 547 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLLQ 626
Cdd:COG0067 476 GYTEEEELLLLLPMAAGGEEEGGSGGDDDPAALLSSSRLLLYYYFFQFFAQVTNPPPDIIREEVVSSLLTTGGGGNNLLL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 627 PSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGAG 706
Cdd:COG0067 556 EEEEARRRLLLLPPPLLNELLLLLLRLLDGDFKSTTTITLLDLADGAGGGAAAAAAAAEAAAAAAAAAVLLILIIDLSDD 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 707 IDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELA-QALRDDGVIAPEVND 785
Cdd:COG0067 636 DSDAAPAPLAAAAAAHHHHLHLLRRRTRLLVVVEVEAVEHHHHHLLLGGGGAAAAAAALYLALElLLDGLLLGLEDAAAA 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 786 KQIYAAYAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 865
Cdd:COG0067 716 AAAKKKKKKKKGKLKKKKMSGIISSSSGSYGAAAIFGALGLVVVVFFTFTTTTGGGGGGGGLDEEAEEEAARAAAAAAEP 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 866 TPDT--RILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEV 943
Cdd:COG0067 796 GGLLlgLGGGGGGEYGRRREGELHLLLQAATAAAAAAYRAYKYYRFARYTALLDLLRLLLLLLLLLFEEEEEEEEPEEEE 875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 944 EPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRylnqDPNNSRRSAIKQVASGRFGVTASYLA 1023
Cdd:COG0067 876 EEEESSAIAAASSAAASAAASAAAAAAAAGAGGGGGGGGGGGGGGGEGRR----ASGGSGSSSSASVAAAGGGVVVGAGA 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1024 NADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSE 1103
Cdd:COG0067 952 AAAEGGGGGGGGGGGGGGGGGGGGGGVPGIAPPPPHPPPPGIILPPPPHDIIIIIILLLLILLLLALVAVAAAVAVVVVA 1031
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442632933 1104 VGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:COG0067 1032 AAAGVAAAAAAAAAAAAVGSSGGGGGGGGGGGGSGAAGALGALGLLGLLLLLLLLLLLLLL 1092
|
|
| 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 442632933 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:pfam00310 1 CGVGFIAHIKGKPSHKIVEDALEALENMEHRGACGADPDTGDGAGILTQIPDEFFRKEAKELGIELPEAGQYAVGMVFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:pfam00310 81 qDEAKRAEAKKIFEEIAEEEGLEVLGWREVPTNNSVLGEAALESEPQIEQVFVGSPAGKSEDDFERKLYVARKRIEKEIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 246 KPG--RRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRG 323
Cdd:pfam00310 161 VEGgdKDFYICSLSSRTIVYKGMLTPEQLGQFYLDLQDPRFESAFALVHSRFSTNTFPSWPLAQPMRFLAHNGEINTLRG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 324 NVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASdRSLPESVMTMVPEAWQNDKTMPQEKRDFYQ 403
Cdd:pfam00310 241 NRNWMRAREALLKSELFGDDLDKLLPIVNPGGSDSASLDNVLELLVLGG-RSLPEALMMLIPEAWQNNPSMDPEKRAFYE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 404 WAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEK 483
Cdd:pfam00310 320 YHSGLMEPWDGPALIVFTDGRYVGATLDRNGLRPARYYITKDGLIILASEVGVLDIPPERVVEKGRLGPGRMLLVDLEEG 399
|
410 420
....*....|....*....|.
gi 442632933 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 442632933 88 CGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALAKQGVTLPELGDYATGIFYL- 166
Cdd:cd00713 1 CGVGFVANIDGKPSHDIVQDALEALERMEHRGGVGADGKTGDGAGILIQIPHEFFREELAEAGIELPEAGEYAVGMLFLp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 167 -DEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDEKAFERQVFVLRKRASHELI 245
Cdd:cd00713 81 rDEEAREAAKAIIEEELEAEGLRVLGWRDVPVDNSVLGPTARATEPLIEQVFVGAPSGDDGEAFERKLYLLRKRIEKAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 246 KPGRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLRVLAHNGEINTLRGNV 325
Cdd:cd00713 161 AADEDFYVCSLSSRTIVYKGMLLPEQLGQFYPDLQDPRFESAFALVHSRFSTNTFPSWPLAQPFRYLAHNGEINTIRGNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 326 NLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMaSDRSLPESVMTMVPEAWQNDKTMPQEKRDFYQWA 405
Cdd:cd00713 241 NWMRAREGLLKSPLFGEDLKKLKPIINPGGSDSASLDNVLELLVR-SGRSLPEAMMMLIPEAWQNNPTMDPELRAFYEYH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 406 ACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTLKSRLKPGRMLLVDTKEKKL 485
Cdd:cd00713 320 SSLMEPWDGPAAIAFTDGRQVGASLDRNGLRPARYVITKDGLLIMSSEVGVVDVPPEKVVEKGRLGPGEMLLVDLEEGRI 399
|
410
....*....|....
gi 442632933 486 IQDIELKAKIAKSR 499
Cdd:cd00713 400 LDDEEIKDQLAKRH 413
|
|
| GltB3 |
COG0070 |
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ... |
68-1164 |
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: 612.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 68 MPWEAPGKQGLYDPQNEHEACGVGFIVAIDGKRSHKILRDAQTLSERMNHRGACACDNDTGDGAGVLASIPHGLYSKALA 147
Cdd:COG0070 7 MGAAAAAGGGGGGGGAGGDGLGGGGGGAAALGGGLGALAAAGAAGGAGAGGGGAGAGGGTGGGGGGGGGGGGGGGLGALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 148 KQGVTLPELGDYATGIF-YLDEAQHAAAEKEFDDLAKSLGLEVIAWRTVPSNQSAIGVVARKSEPLSRQVFVRRPAGSDE 226
Cdd:COG0070 87 AGGGAFFAAGLAAGLLAlAAAVEAEAEEAEEDEEEEERVLLLVLLEAETLVVLLALGVRAAALARREAELSELAARRRLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 227 KAFERQVFVLRKRASHELikpgRRFYICSLSDRTVVYKGLFTSDQLWDYYTDLKDPEFETYLALVHTRFSTNTFPSWERA 306
Cdd:COG0070 167 LRRLALLRRRRRRRRREF----RRRSSSSLSSSSSSLYSLLLLVLLLLLLLLLLLLLLLLLFLSFLSRFTTTTTSSLTLF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 307 HPLRVLAHNGEINTLRGNVNLMKAREGVMQSDLFGDQLKKLYPVVEPNLSDSGSFDCVLEFLTMASDRSLPESVMTMVPE 386
Cdd:COG0070 243 FAPRTLAANNNNNNNNNNNNNNNRNAILNLSSRLEALSLELLPPLLPLLSDSSSDDLLLLLLLLLLLLLLLLLLMALAAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 387 AWQNDKTMPQEKRDFYQWAACVMEPWDGPALISFTDGRYIGAVLDRNGLRPSRFYVTKENVLVMASEVGVYDVDPSQVTL 466
Cdd:COG0070 323 APAPRAAAPPAAAAAFAAAADLYAAAAAAAAAAAGGDGDGGGLGLGGGRRRRRRLLRDRRLVRALSILVGLLILIEVVGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 467 KSRLKPGRMLLVDTKEKKLIQDIELKAKIAKSRPHSEWLQQKITLDEIRNANVLNTPPVDElaklpasergiFDPRLSLF 546
Cdd:COG0070 403 GRELPGGGLLVGGGGGGLLDDEEEDAEELEELLPELQDLLLLLKLLLLLEEEEELLLLEEE-----------LLQEREAE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 547 GYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPEANLL- 625
Cdd:COG0070 472 LEQELLLLLLLLLAEALEEEEESGGAGAAAAALDLLDLLLLLDFQFLLLFFQQPPPPVVFPPIVLLLEPPPLLLLLLLLl 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 626 QPSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFQYNEGVQGYIDAIDRICREGYAAAQAGYQLLVISDRGA 705
Cdd:COG0070 552 LLLLLEELLLLELLLLLLALALLLLLLLLLLLLGDATTLAAALEAAGGGGALAALLLAAEAAAAAAAAAVAAILAASIRD 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 706 GIDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGVIAPEVND 785
Cdd:COG0070 632 SALLLALLPALLALLLLHHHLLRALGRVLVLLVEALLRERVVHVAALLAGAAAAAAAALAALAAAAALLLLAYALLGLLE 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 786 KQIYAAYAQAIdTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAKCFRGTQSRIGGVTLEILAKEGLQRYQLTYGKA 865
Cdd:COG0070 712 AAAYKAKAALK-AGVKKKLKIGGSSISSSSGGGIIEGAGGGLGLLLELGGTTTTVGEGGGGGEILGEGGAARHAAAADAA 790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 866 TPDTRILRNPGQYHWRHGGEAHINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEVEP 945
Cdd:COG0070 791 AAAALALGGGGGGGRGGGGEGHHGGHYHHLLQQLAARTAAALYDDYYAYEDRADELVNERLRLLLLFLLRPPIPIEEVEP 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 946 ASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYLNQDPNNSRRSAIKQVASGRFGVTASYLANA 1025
Cdd:COG0070 871 EEEIVKRFATGAMSGGSSSSEAHEELAIAMNRIGGKSNGGGGGEEEGREDPLRNGDSRRSAIKQVASGRFGVTSEYLVNA 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1026 DDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVG 1105
Cdd:COG0070 951 DEIQIKMAQGAKPGEGGQLPGHKVYPWIARLRHSTPGVGLISPPPHHDIYSIEDLAQLIFDLKNANPAARISVKLVSEVG 1030
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 442632933 1106 VGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:COG0070 1031 VGTIAAGVAKAAADVILISGHDGGTGASPLSSIKHAGLPWELGLAETQQTLVLNNLRRR 1089
|
|
| GltB2 |
COG0069 |
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ... |
717-1164 |
4.80e-175 |
|
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: 532.52 E-value: 4.80e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 717 LALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGviAPEVNDKQIYAAYAQAI 796
Cdd:COG0069 1 LAAAAHHHLLRRKGRRTVSLIVVEGEERRVHHHAALLGGGGAAANPPYLAEEILDLLRRGG--LLGLDLEEAVKNYIKAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 797 DTGIAKVMAKMGISTLQSYKSAQIFEAVGLGSDLVAkcfrgtqsriggVTLEilakEGLQRYQLTYgkatpdTRILRNPG 876
Cdd:COG0069 79 EKGLLKIMSKMGISTLASYRGAQIFEAVGLSRELVD------------IGIA----DVLTQHRHAI------LRNLPVGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 877 QYHWRH--------------GGEAHINEPSSIGSLQEAAvnKNLDAFEAFKkTTLD--SVKKCALRGQLEFVTDRQSIDI 940
Cdd:COG0069 137 RYRYRFesigpeirqyffesDGEEHPFNRETRSLLYQAA--KNEEDYKPFG-TLVDyqPGYEWTLRSLFPFKADRPPIPI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 941 SE-VEPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSNTGEGGEDSDRYlnqdpNNSRRSAIKQVASGRFGVT- 1018
Cdd:COG0069 214 GEpVEPPYSIVSRFNISAMSFGALSAEAHEALAIGMNRIGGKSNTGEGGESPYHL-----GDGGGDAIKQIASGRFGVRd 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1019 --ASYLANADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARI 1096
Cdd:COG0069 289 edGEYLPNAKMIEIKLAQGAKPGEGGQLPGAKVTPEIARIRGSTPGVDLISPPPHHDIYSIEDLAQLIFDLRELNPGAPV 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442632933 1097 SVKLVSEVGV----GVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:COG0069 369 GVKLVSGAGVgtiaACKGVAKTGAYADFITIDGGEGGTGAAPLESIKHAGLPWELGLAEVHQTLVGNGLRDR 440
|
|
| Glu_syn_central |
pfam04898 |
Glutamate synthase central domain; The central domain of glutamate synthase connects the amino ... |
542-827 |
1.29e-146 |
|
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: 441.43 E-value: 1.29e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 542 RLSLFGYSTETVNMLLIPMFKNKKEALGSMGNDAPLACLSNFQPIPYEYFKQLFAQVTNPPIDPFREKVVMSMQCPLGPE 621
Cdd:pfam04898 2 RQKAFGYTQEDLEMLLKPMAETGKEPIGSMGDDTPLAVLSDKPRLLYDYFKQLFAQVTNPPIDPIREEIVMSLRTYLGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 622 ANLLQPSAQQVHRIWLTNPILSIPDTQLLKRNTHRGWRTKVLDITFqynegvQGYIDAIDRICREGYAAAQAGYQLLVIS 701
Cdd:pfam04898 82 GNLLEETPEHCRRLELPSPILTNEELEKLRSLKGPGFKVATLDITF------DGLEAALERLCEEAEEAVRDGANILILS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 702 DRGAGiDGKVAVSALLALGALHHHLIETLQRMKVGIVVETAEAREVHHICVLLGYGADAICPYLAFELAQALRDDGviAP 781
Cdd:pfam04898 156 DRGVD-ADRAPIPSLLAVSAVHHHLVREGLRTKVSLVVESGEAREVHHFAVLLGYGADAVNPYLAFETIRDLIREG--KG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 442632933 782 EVNDKQIYAA---YAQAIDTGIAKVMAKMGISTLQSYKSAQIFEAVGLG 827
Cdd:pfam04898 233 KLTDEDLEEAvknYRKAIEKGLLKIMSKMGISTLQSYRGAQIFEAIGLS 281
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
887-1164 |
2.26e-123 |
|
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: 383.99 E-value: 2.26e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 887 HINEPSSIGSLQEAAVNKNLDAFEAFKKTTLDSVKKCALRGQLEFVTDRQSIDISEVEPASEIVKRFATGAMSFGSISLE 966
Cdd:pfam01645 1 HRNEPEFIKTLQIAVQVESYPSYDKYREPLNERVPIGALRDLLEFDFAEDPIPLEEVEPALEIKTRFCTGAMSYGALSEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 967 AHQTLSITMNRIGGKSNTGEGGEDSDRYLNQDpnnsrRSAIKQVASGRFGVTASYLANADDLQIKMAQGAKPGEGGELPG 1046
Cdd:pfam01645 81 AHEALAKAMNRLGTKSNTGEGGEDPERLKYAD-----NIAIKQVASGRFGVTPEYLNNADAIEIKIAQGAKPGEGGHLPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1047 YKVTKDIAKTRKSVPGVGLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGVGVVASGVAKGKAEHIVISGH 1126
Cdd:pfam01645 156 EKVSPEIARIRGSPPGVGLISPPPHHDIYSIEDLAQLIYDLKEINPKAPISVKLVSGHGVGTIAAGVAKAGADIILIDGY 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 442632933 1127 DGGTGASSWTGIKNAGLPWELGVAETHQVLVLNNLRSR 1164
Cdd:pfam01645 236 DGGTGASPKTSIKHAGLPWELALAEAHQTLKENGLRDR 273
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
917-1164 |
8.37e-107 |
|
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: 340.67 E-value: 8.37e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 917 LDSVKKCALRGQLEFVTDRQSIDISE-------------VEPASEIVKRFATGAMSFGSISLEAHQTLSITMNRIGGKSN 983
Cdd:cd02808 31 SRGRPFGTLRDLLEFGAQLAKHPLEPdeevddrvtigpnAEKPLKLDSPFNISAMSFGALSKEAKEALAIGAALAGTASN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 984 TGEGGEDSDRYLNqdpnnsRRSAIKQVASGRFGVTASYLANADDLQIKMAQGAKPGEGGELPGYKVTKDIAKTRKSVPGV 1063
Cdd:cd02808 111 TGEGGELPEEREG------GGDIIKQVASGRFGVRPEYLNKADAIEIKIGQGAKPGEGGHLPGEKVTEEIAKIRGIPPGV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 1064 GLISPPPHHDIYSIEDLAELIYDLKCSNPNARISVKLVSEVGVGVVASGVAKGKAEHIVISGHDGGTGASSWTGIKNAGL 1143
Cdd:cd02808 185 DLISPPPHHDIYSIEDLAQLIEDLREATGGKPIGVKLVAGHGEGDIAAGVAAAGADFITIDGAEGGTGAAPLTFIDHVGL 264
|
250 260
....*....|....*....|.
gi 442632933 1144 PWELGVAETHQVLVLNNLRSR 1164
Cdd:cd02808 265 PTELGLARAHQALVKNGLRDR 285
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
274-476 |
4.20e-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: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 274 DYYTDLKDPEFETYLALVHTRFSTNTFPSWERAHPLR------VLAHNGEINTLRGNVNLMKAREGVMQSDlfgdqlkkl 347
Cdd:cd00352 56 DVALDLLDEPLKSGVALGHVRLATNGLPSEANAQPFRsedgriALVHNGEIYNYRELREELEARGYRFEGE--------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 348 ypvvepnlSDSGSFDCVLEFLTMASDrsLPESVMTMVPEawqndktmpqekrdfyqwaacvmepWDGPALISFTDG--RY 425
Cdd:cd00352 127 --------SDSEVILHLLERLGREGG--LFEAVEDALKR-------------------------LDGPFAFALWDGkpDR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442632933 426 IGAVLDRNGLRPSRFYVTKENVLVMASEVGVydVDPSQVTLKSRLKPGRML 476
Cdd:cd00352 172 LFAARDRFGIRPLYYGITKDGGLVFASEPKA--LLALPFKGVRRLPPGELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
252-454 |
2.64e-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: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 252 YICSLSDRTVVYKGLFTSDQLWDYYtDLkdPEFETYLALVHTRFSTNTFPSWERAHPLRV----LAHNGEINTLRGNVNL 327
Cdd:cd01907 46 FVYSSGKDMEVFKGVGYPEDIARRY-DL--EEYKGYHWIAHTRQPTNSAVWWYGAHPFSIgdiaVVHNGEISNYGSNREY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632933 328 MKaREGV---MQSD------LFGDQLKKLYPVVEpnlsdsgsfdcvlefltmasdrsLPESVMTMVPEAWQNDKTMPQEK 398
Cdd:cd01907 123 LE-RFGYkfeTETDteviayYLDLLLRKGGLPLE-----------------------YYKHIIRMPEEERELLLALRLTY 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442632933 399 R--DFyqwaacvmepwDGP-ALISFTDGRYIGAVlDRNGLRPSRFYVTKENVlVMASEV 454
Cdd:cd01907 179 RlaDL-----------DGPfTIIVGTPDGFIVIR-DRIKLRPAVVAETDDYV-AIASEE 224
|
|
| |
