|
Name |
Accession |
Description |
Interval |
E-value |
| PurF |
COG0034 |
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ... |
1-503 |
0e+00 |
|
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439804 [Multi-domain] Cd Length: 464 Bit Score: 561.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 1 MAELHHECGVAAIYhlpglvesplaprqGASHTSWHMPRLLLEIQNRGQLAAGMTSYDPESaqiLETHKDVGTVSEVFDI 80
Cdd:COG0034 1 MDKLHEECGVFGIY--------------GHEDVAQLTYYGLYALQHRGQESAGIATSDGGR---FHLHKGMGLVSDVFDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 81 QHqdrylplMQRLKGPAAIGHVRYATCGKEDRCYAHPFERTHieKNKWFSFAFNGQIANYTQLMEEIQaKREFHLARQTD 160
Cdd:COG0034 64 ED-------LERLKGNIAIGHVRYSTTGSSSLENAQPFYVNS--PFGSIALAHNGNLTNAEELREELE-EEGAIFQTTSD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 161 TEILMHLISQQLSGDrrpSLVELLTELSKKLDGAYNIVFLNAlGEMFVARDPLGLRPLCYAIEGPMFAAASESVALSNLG 240
Cdd:COG0034 134 TEVILHLIARELTKE---DLEEAIKEALRRVKGAYSLVILTG-DGLIAARDPNGIRPLVLGKLEDGYVVASESCALDILG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 241 FrnENIHTLAPGHAVIIQNNQIEVKKFAESPKTAHCFFEWIYFANVASTLDDRSVYLSRKALGEELAALEDIErGDdlIV 320
Cdd:COG0034 210 A--EFVRDVEPGEIVVIDEDGLRSRQFAEKPRPAPCIFEYVYFARPDSVIDGRSVYEARKRMGRELAREAPVD-AD--VV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 321 VPVPDTSKAAADAMAYKLGVPSLEGLIRNRYIGRTFIEG--KDRADKARLKYTPLREVLEGKRVLLVEDTIVRSTTMQVL 398
Cdd:COG0034 285 IPVPDSGRPAAIGYAEESGIPYEEGLIKNRYVGRTFIQPtqELRELGVRLKLNPIREVVKGKRVVLVDDSIVRGTTSRRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 399 ISQLRErGGAKEVHVRVACPPIVAPCFYGIDMSSISELFAprfiqsnAELTTEvqaEMARVLGADSLRYLPLPAIARSLG 478
Cdd:COG0034 365 VKMLRE-AGAKEVHFRIASPPIRYPCYYGIDTPTREELIA-------ANRSVE---EIREYIGADSLGYLSLEGLIEAVG 433
|
490 500
....*....|....*....|....*
gi 502874553 479 MSEGKLCRGCLTGEYPTPMGEQLYQ 503
Cdd:COG0034 434 EPIEGFCTACFTGDYPTGIPDEEKK 458
|
|
| purF |
TIGR01134 |
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ... |
8-494 |
3.94e-135 |
|
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273461 [Multi-domain] Cd Length: 442 Bit Score: 399.00 E-value: 3.94e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 8 CGVAAIYhlpglVESPLAPRQgaSHTSwhmprlLLEIQNRGQLAAGMTSYDPESaqiLETHKDVGTVSEVFDIQHqdryl 87
Cdd:TIGR01134 1 CGVVGIY-----GQEEVAASL--TYYG------LYALQHRGQESAGISVFDGNR---FRLHKGNGLVSDVFNEEH----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 88 plMQRLKGPAAIGHVRYATCGKEDRCYAHPFERThiEKNKWFSFAFNGQIANYTQLMEEIQAKReFHLARQTDTEILMHL 167
Cdd:TIGR01134 60 --LQRLKGNVGIGHVRYSTAGSSGLENAQPFVVN--SPYGGLALAHNGNLVNADELRRELEEEG-RHFNTTSDSEVLLHL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 168 ISQQLSGDrrPSLVELLTELSKKLDGAYNIVFLNALGeMFVARDPLGLRPLCYAIEGPMFAAASESVALSNLGFrnENIH 247
Cdd:TIGR01134 135 LAHNDESK--DDLFDAVARVLERVRGAYALVLMTEDG-LVAVRDPHGIRPLVLGRRGDGYVVASESCALDILGA--EFVR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 248 TLAPGHAVIIQNNQIEVKKFAESPkTAHCFFEWIYFANVASTLDDRSVYLSRKALGEELAALEDIErGDdlIVVPVPDTS 327
Cdd:TIGR01134 210 DVEPGEVVVIFDGGLESRQCARRP-RAPCVFEYVYFARPDSVIDGISVYYARKRMGKELARESPVE-AD--VVVPVPDSG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 328 KAAADAMAYKLGVPSLEGLIRNRYIGRTFIE--GKDRADKARLKYTPLREVLEGKRVLLVEDTIVRSTTMQVLISQLREr 405
Cdd:TIGR01134 286 RSAALGFAQASGIPYREGLIKNRYVGRTFIMptQELRELSVRLKLNPVRAVFEGKRVVLVDDSIVRGTTSRQIVEMLRD- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 406 GGAKEVHVRVACPPIVAPCFYGIDMSSISELFAPRfiqsnaelttEVQAEMARVlGADSLRYLPLPAIARSLGMSEGKLC 485
Cdd:TIGR01134 365 AGAKEVHVRIASPPIRYPCYYGIDMPTREELIAAR----------RTVEEIRKI-GADSLAYLSLEGLKEAVGNPESDLC 433
|
....*....
gi 502874553 486 RGCLTGEYP 494
Cdd:TIGR01134 434 LACFTGEYP 442
|
|
| PRK05793 |
PRK05793 |
amidophosphoribosyltransferase; Provisional |
4-504 |
3.13e-115 |
|
amidophosphoribosyltransferase; Provisional
Pssm-ID: 235611 [Multi-domain] Cd Length: 469 Bit Score: 349.33 E-value: 3.13e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 4 LHHECGVAAIYhlpglvesPLAPRQGASHTSWHmprlLLEIQNRGQLAAGMTSYDPESAQIletHKDVGTVSEVFDIQhq 83
Cdd:PRK05793 11 FKEECGVFGVF--------SKNNIDVASLTYYG----LYALQHRGQESAGIAVSDGEKIKV---HKGMGLVSEVFSKE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 84 drylpLMQRLKGPAAIGHVRYATCGKEDRCYAHPFERTHieKNKWFSFAFNGQIANYTQLMEEIQ-AKREFHLArqTDTE 162
Cdd:PRK05793 74 -----KLKGLKGNSAIGHVRYSTTGASDLDNAQPLVANY--KLGSIAIAHNGNLVNADVIRELLEdGGRIFQTS--IDSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 163 ILMHLISQQLsgdrRPSLVELLTELSKKLDGAYNIVFLnALGEMFVARDPLGLRPLCYAIEGPMFAAASESVALSNLGfr 242
Cdd:PRK05793 145 VILNLIARSA----KKGLEKALVDAIQAIKGSYALVIL-TEDKLIGVRDPHGIRPLCLGKLGDDYILSSESCALDTIG-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 243 NENIHTLAPGHAVIIQNNQIEVKKFAESPKTAHCFFEWIYFANVASTLDDRSVYLSRKALGEELAALEDIErGDdlIVVP 322
Cdd:PRK05793 218 AEFIRDVEPGEIVIIDEDGIKSIKFAEKTKCQTCAFEYIYFARPDSVIDGISVYESRVRAGRQLYKEYPVD-AD--IVIG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 323 VPDTSKAAADAMAYKLGVPSLEGLIRNRYIGRTFIEGK--DRADKARLKYTPLREVLEGKRVLLVEDTIVRSTTMQVLIS 400
Cdd:PRK05793 295 VPDSGIPAAIGYAEASGIPYGIGFIKNKYVGRTFIAPSqeLRERAVRVKLNPLKVNVEGKRVVLIDDSIVRGTTSKRLVE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 401 QLReRGGAKEVHVRVACPPIVAPCFYGIDMSSISELFAprfiqsnAELTTEvqaEMARVLGADSLRYLPLPAIARSLGMS 480
Cdd:PRK05793 375 LLR-KAGAKEVHFRVSSPPVKYPCYFGIDTPYRKELIG-------ANMSVE---EIREMIGADSLGYLSIEGLLESLNGD 443
|
490 500
....*....|....*....|....*.
gi 502874553 481 EGkLCRGCLTGEYP--TPMGEQLYQL 504
Cdd:PRK05793 444 KG-FCLGCFNGVYPvsAPKEGPKYLL 468
|
|
| PLN02440 |
PLN02440 |
amidophosphoribosyltransferase |
7-496 |
9.31e-112 |
|
amidophosphoribosyltransferase
Pssm-ID: 215241 [Multi-domain] Cd Length: 479 Bit Score: 340.50 E-value: 9.31e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 7 ECGVAAIYhlpglvESPLAPRQgaSHTSWHMprllleIQNRGQLAAGMTSYDPEsaqILETHKDVGTVSEVFDIQHqdry 86
Cdd:PLN02440 1 ECGVVGIF------GDPEASRL--CYLGLHA------LQHRGQEGAGIVTVDGN---RLQSITGNGLVSDVFDESK---- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 87 lplMQRLKGPAAIGHVRYATCGKEDRCYAHPFERTHieKNKWFSFAFNGQIANYTQLMEEIQAKREfHLARQTDTEILMH 166
Cdd:PLN02440 60 ---LDQLPGDIAIGHVRYSTAGASSLKNVQPFVANY--RFGSIGVAHNGNLVNYEELRAKLEENGS-IFNTSSDTEVLLH 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 167 LISQQLSgdrRPsLVELLTELSKKLDGAYNIVFLNAlGEMFVARDPLGLRPLCYAI-EGPMFAAASESVALSNLGFrnEN 245
Cdd:PLN02440 134 LIAISKA---RP-FFSRIVDACEKLKGAYSMVFLTE-DKLVAVRDPHGFRPLVMGRrSNGAVVFASETCALDLIGA--TY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 246 IHTLAPGHAVIIQNNQIEVKKFAE-SPKTAHCFFEWIYFANVASTLDDRSVYLSRKALGEELA--ALEDIErgddlIVVP 322
Cdd:PLN02440 207 EREVNPGEVIVVDKDKGVSSQCLMpHPEPKPCIFEHIYFARPNSIVFGRSVYESRLEFGEILAteIPVDCD-----VVIP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 323 VPDTSKAAADAMAYKLGVPSLEGLIRNRYIGRTFIE--GKDRADKARLKYTPLREVLEGKRVLLVEDTIVRSTTMQVLIS 400
Cdd:PLN02440 282 VPDSGRVAALGYAAKLGVPFQQGLIRSHYVGRTFIEpsQKIRDFSVKLKLNPVRSVLEGKRVVVVDDSIVRGTTSSKIVR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 401 QLRErGGAKEVHVRVACPPIVAPCFYGIDMSSISELFAPRfiqsnaeLTTEvqaEMARVLGADSLRYLPLPAIARSLGMS 480
Cdd:PLN02440 362 MLRE-AGAKEVHMRIASPPIIASCYYGVDTPSREELISNR-------MSVE---EIRKFIGCDSLAFLPLEDLKKSLGEE 430
|
490
....*....|....*.
gi 502874553 481 EGKLCRGCLTGEYPTP 496
Cdd:PLN02440 431 SPRFCYACFSGDYPVL 446
|
|
| GPATase_N |
cd00715 |
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ... |
45-284 |
6.02e-59 |
|
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.
Pssm-ID: 238367 [Multi-domain] Cd Length: 252 Bit Score: 195.76 E-value: 6.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 45 QNRGQLAAGMTSYDPESaqiLETHKDVGTVSEVFDIQHqdrylplMQRLKGPAAIGHVRYATCGKEDRCYAHPFERTHie 124
Cdd:cd00715 24 QHRGQESAGIATSDGKR---FHTHKGMGLVSDVFDEEK-------LRRLPGNIAIGHVRYSTAGSSSLENAQPFVVNS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 125 KNKWFSFAFNGQIANYTQLMEEIqAKREFHLARQTDTEILMHLISQQLsgdRRPSLVELLTELSKKLDGAYNIVFLNALG 204
Cdd:cd00715 92 PLGGIALAHNGNLVNAKELREEL-EEEGRIFQTTSDSEVILHLIARSL---AKDDLFEAIIDALERVKGAYSLVIMTADG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 205 eMFVARDPLGLRPLCYA-IEGPMFAAASESVALSNLGFrnENIHTLAPGHAVIIQNNQIEVKKFAESPKTAHCFFEWIYF 283
Cdd:cd00715 168 -LIAVRDPHGIRPLVLGkLEGDGYVVASESCALDIIGA--EFVRDVEPGEIVVIDDDGLESSQRAPKPKPAPCIFEYVYF 244
|
.
gi 502874553 284 A 284
Cdd:cd00715 245 A 245
|
|
| Gn_AT_II |
cd00352 |
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ... |
8-255 |
1.49e-40 |
|
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: 146.05 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 8 CGVAAIYHLPGlvesplaprqGASHTSWHMPRLLLEIQNRGQLAAGMTSYDPESaqiLETHKDVGTVSEVFDiqhqdryL 87
Cdd:cd00352 1 CGIFGIVGADG----------AASLLLLLLLRGLAALEHRGPDGAGIAVYDGDG---LFVEKRAGPVSDVAL-------D 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 88 PLMQRLKGPAAIGHVRYATCGKEDRCYAHPFertHIEKNKWFsFAFNGQIANYTQLMEEIQAKReFHLARQTDTEILMHL 167
Cdd:cd00352 61 LLDEPLKSGVALGHVRLATNGLPSEANAQPF---RSEDGRIA-LVHNGEIYNYRELREELEARG-YRFEGESDSEVILHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 168 ISQQLSGDRrpsLVELLTELSKKLDGAYNIVFLNAL-GEMFVARDPLGLRPLCYAI-EGPMFAAASESVALSNLGFRneN 245
Cdd:cd00352 136 LERLGREGG---LFEAVEDALKRLDGPFAFALWDGKpDRLFAARDRFGIRPLYYGItKDGGLVFASEPKALLALPFK--G 210
|
250
....*....|
gi 502874553 246 IHTLAPGHAV 255
Cdd:cd00352 211 VRRLPPGELL 220
|
|
| GlxB |
cd01907 |
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ... |
8-257 |
2.63e-18 |
|
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: 84.63 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 8 CGVAAIYHLPGLvesplaPRQGAShtswhMPRLLLEIQNRG-QLAAGMTSYDPESAQI------LETHKDVGT---VSEV 77
Cdd:cd01907 1 CGIFGIMSKDGE------PFVGAL-----LVEMLDAMQERGpGDGAGFALYGDPDAFVyssgkdMEVFKGVGYpedIARR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 78 FDIQhqdrylplmqRLKGPAAIGHVRYATCGKEDRCYAHPFERTHIeknkwfSFAFNGQIANYTQLMEEIQAKReFHLAR 157
Cdd:cd01907 70 YDLE----------EYKGYHWIAHTRQPTNSAVWWYGAHPFSIGDI------AVVHNGEISNYGSNREYLERFG-YKFET 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 158 QTDTEILMHLISQQLS-----------------GDRRPSLVELLTELSKKLDGAYNIVFlnAL-GEMFVARDPLGLRPLC 219
Cdd:cd01907 133 ETDTEVIAYYLDLLLRkgglpleyykhiirmpeEERELLLALRLTYRLADLDGPFTIIV--GTpDGFIVIRDRIKLRPAV 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 502874553 220 YAIEGPMFAAASESVALSNLGFR-NENIHTLAPGHAVII 257
Cdd:cd01907 211 VAETDDYVAIASEECAIREIPDRdNAKVWEPRPGEYVIW 249
|
|
| GFAT |
cd00714 |
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ... |
42-236 |
1.01e-17 |
|
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.
Pssm-ID: 238366 [Multi-domain] Cd Length: 215 Bit Score: 82.11 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 42 LEiqNRGQLAAGMTSYDPESaqiLETHKDVGTVSEVfdiqhqDRYLPLMQrLKGPAAIGHVRYATCGKEDRCYAHPfert 121
Cdd:cd00714 23 LE--YRGYDSAGIAVIGDGS---LEVVKAVGKVANL------EEKLAEKP-LSGHVGIGHTRWATHGEPTDVNAHP---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 122 HIEKNKWFSFAFNGQIANYTQLMEEIQAK-REFHlaRQTDTEILMHLISQQLsgDRRPSLVELLTELSKKLDGAYNIVFL 200
Cdd:cd00714 87 HRSCDGEIAVVHNGIIENYAELKEELEAKgYKFE--SETDTEVIAHLIEYYY--DGGLDLLEAVKKALKRLEGAYALAVI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502874553 201 NAL--GEMFVARD--PL--GLRPLCYAIegpmfaaASESVAL 236
Cdd:cd00714 163 SKDepDEIVAARNgsPLviGIGDGENFV-------ASDAPAL 197
|
|
| GATase_6 |
pfam13522 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
95-232 |
3.74e-17 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.
Pssm-ID: 433279 [Multi-domain] Cd Length: 130 Bit Score: 77.73 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 95 GPAAIGHVRYATCGKEDRCyAHPFERThiekNKWFSFAFNGQIANYTQLMEEIQAKReFHLARQTDTEILMHLISqqlsg 174
Cdd:pfam13522 10 GGVALGHVRLAIVDLPDAG-NQPMLSR----DGRLVLVHNGEIYNYGELREELADLG-HAFRSRSDTEVLLALYE----- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 502874553 175 drrpslvELLTELSKKLDGAYNIVF-LNALGEMFVARDPLGLRPLCYAIEGPMFAAASE 232
Cdd:pfam13522 79 -------EWGEDCLERLRGMFAFAIwDRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
302-416 |
4.22e-16 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 74.74 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 302 LGEELAALEDIERGDDLIVVPVPDTSKAAADAMAYKLGVPSLEGLIRNRYIGRTFIEGKDradkarlKYTPLREVLEGKR 381
Cdd:cd06223 1 AGRLLAEEIREDLLEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYG-------LELPLGGDVKGKR 73
|
90 100 110
....*....|....*....|....*....|....*
gi 502874553 382 VLLVEDTIVRSTTMQVLISQLRERgGAKEVHVRVA 416
Cdd:cd06223 74 VLLVDDVIATGGTLLAAIELLKEA-GAKVVGVAVL 107
|
|
| PTZ00295 |
PTZ00295 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
44-238 |
3.33e-14 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 240349 [Multi-domain] Cd Length: 640 Bit Score: 75.44 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 44 IQNRGQLAAGMTSYDPESAQILETHKDVGTVSEVFDIQHQDrylpLMQRLKGPA-AIGHVRYATCGKEDRCYAHPfertH 122
Cdd:PTZ00295 47 LQNRGYDSCGISTISSGGELKTTKYASDGTTSDSIEILKEK----LLDSHKNSTiGIAHTRWATHGGKTDENAHP----H 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 123 IEKNKWFSFAFNGQIANYTQLMEEIQAKReFHLARQTDTEILMHLISQQLsgDRRPSLVELLTELSKKLDGAYNIVFL-- 200
Cdd:PTZ00295 119 CDYKKRIALVHNGTIENYVELKSELIAKG-IKFRSETDSEVIANLIGLEL--DQGEDFQEAVKSAISRLQGTWGLCIIhk 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 502874553 201 NALGEMFVARDPlglRPLCYAIEGPMFAAASESVALSN 238
Cdd:PTZ00295 196 DNPDSLIVARNG---SPLLVGIGDDSIYVASEPSAFAK 230
|
|
| AsnB |
cd00712 |
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ... |
95-267 |
4.80e-14 |
|
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.
Pssm-ID: 238364 [Multi-domain] Cd Length: 220 Bit Score: 71.43 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 95 GPAAIGHVRYATCgkeDRCYAH-PF----ERTHIeknkwfsfAFNGQIANYTQLMEEIQAK-REFHlaRQTDTEILMHLI 168
Cdd:cd00712 40 EGVALGHRRLSII---DLSGGAqPMvsedGRLVL--------VFNGEIYNYRELRAELEALgHRFR--THSDTEVILHLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 169 sqQLSGdrrpslvellTELSKKLDGAYNIVFLNAL-GEMFVARDPLGLRPLCYAIEGPMFAAASE--------------- 232
Cdd:cd00712 107 --EEWG----------EDCLERLNGMFAFALWDKRkRRLFLARDRFGIKPLYYGRDGGGLAFASElkallalpgvpreld 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502874553 233 SVALSNLGFRN---------ENIHTLAPGHAVIIQNNQIEVKKF 267
Cdd:cd00712 175 EAALAEYLAFQyvpaprtifKGIRKLPPGHYLTVDPGGVEIRRY 218
|
|
| glmS |
TIGR01135 |
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ... |
93-273 |
6.92e-13 |
|
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273462 [Multi-domain] Cd Length: 607 Bit Score: 71.13 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 93 LKGPAAIGHVRYATCGKEDRCYAHPfertHIEKNKWFSFAFNGQIANYTQLMEEIQAK-REFHlaRQTDTEILMHLISQQ 171
Cdd:TIGR01135 62 LPGGVGIGHTRWATHGKPTDENAHP----HTDEGGRIAVVHNGIIENYAELREELEARgHVFS--SDTDTEVIAHLIEEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 172 LsgDRRPSLVELLTELSKKLDGAYNIVFLNA--LGEMFVAR--DPL--GLRplcyaiEGPMFaAASESVALsnLGFRNEN 245
Cdd:TIGR01135 136 L--REGGDLLEAVQKALKQLRGAYALAVLHAdhPETLVAARsgSPLivGLG------DGENF-VASDVTAL--LPYTRRV 204
|
170 180
....*....|....*....|....*...
gi 502874553 246 IhTLAPGHAVIIQNNQIEVKKFAESPKT 273
Cdd:TIGR01135 205 I-YLEDGDIAILTKDGVEIYNFEGAPVQ 231
|
|
| YafJ |
COG0121 |
Predicted glutamine amidotransferase YafJ [General function prediction only]; |
82-260 |
7.26e-13 |
|
Predicted glutamine amidotransferase YafJ [General function prediction only];
Pssm-ID: 439891 [Multi-domain] Cd Length: 248 Bit Score: 68.45 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 82 HQDRYLPLMQR-LKGPAAIGHVRYATCGKEDRCYAHPFerTHIEknkWFsFAFNGQIANY----TQLMEEIQAKREFHLA 156
Cdd:COG0121 62 WSDPNLRLLARpIKSRLVIAHVRKATVGPVSLENTHPF--RGGR---WL-FAHNGQLDGFdrlrRRLAEELPDELYFQPV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 157 RQTDTEILMHLISQQLS---GDRRPSLVELLTELSK--KLDGAYNIVFLNalGE-MFVAR--DPLGLRPLCYAI----EG 224
Cdd:COG0121 136 GTTDSELAFALLLSRLRdggPDPAEALAEALRELAElaRAPGRLNLLLSD--GErLYATRytSDDPYPTLYYLTrttpDD 213
|
170 180 190
....*....|....*....|....*....|....*.
gi 502874553 225 PMFAAASESValsnlgFRNENIHTLAPGHAVIIQNN 260
Cdd:COG0121 214 RVVVVASEPL------TDDEGWTEVPPGELLVVRDG 243
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
57-268 |
1.28e-12 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 70.07 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 57 YDpeSAQI-------LETHKDVGTVSEVfdiqhqDRYLPLmQRLKGPAAIGHVRYATCGKEDRCYAHPfertHIEKNKWF 129
Cdd:PRK00331 29 YD--SAGIavlddggLEVRKAVGKVANL------EAKLEE-EPLPGTTGIGHTRWATHGKPTERNAHP----HTDCSGRI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 130 SFAFNGQIANYTQLMEEIQAK-REFHlaRQTDTEILMHLISQQLSGDrrPSLVELLTELSKKLDGAYNIVFLNAL--GEM 206
Cdd:PRK00331 96 AVVHNGIIENYAELKEELLAKgHVFK--SETDTEVIAHLIEEELKEG--GDLLEAVRKALKRLEGAYALAVIDKDepDTI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502874553 207 FVARD--PLglrplcyAI---EGPMFaAASESVALsnLGFRNEnIHTLAPGHAVIIQNNQIEVKKFA 268
Cdd:PRK00331 172 VAARNgsPL-------VIglgEGENF-LASDALAL--LPYTRR-VIYLEDGEIAVLTRDGVEIFDFD 227
|
|
| GATase_7 |
pfam13537 |
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ... |
129-236 |
1.81e-12 |
|
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.
Pssm-ID: 433289 [Multi-domain] Cd Length: 123 Bit Score: 64.08 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 129 FSFAFNGQIANYTQLMEEIQAKReFHLARQTDTEILMHLISQqlsgdrrpslvELLTELSKKLDGAYNIVFLNAL-GEMF 207
Cdd:pfam13537 24 YVIVFNGEIYNYRELRAELEAKG-YRFRTHSDTEVILHLYEA-----------EWGEDCVDRLNGMFAFAIWDRRrQRLF 91
|
90 100 110
....*....|....*....|....*....|
gi 502874553 208 VARDPLGLRPLCYA-IEGPMFAAASESVAL 236
Cdd:pfam13537 92 LARDRFGIKPLYYGrDDGGRLLFASELKAL 121
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
57-273 |
2.37e-12 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 69.27 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 57 YDpeSAQI-------LETHKDVGTVSEVfdiqhqDRYLPLmQRLKGPAAIGHVRYATCGKEDRCYAHPfertHIEKNKWF 129
Cdd:COG0449 29 YD--SAGIavlddggLEVRKAVGKLANL------EEKLAE-EPLSGTIGIGHTRWATHGAPSDENAHP----HTSCSGRI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 130 SFAFNGQIANYTQLMEEIQAK-REFHlaRQTDTEILMHLISQQLsgDRRPSLVELLTELSKKLDGAYNIVFLNAL--GEM 206
Cdd:COG0449 96 AVVHNGIIENYAELREELEAKgHTFK--SETDTEVIAHLIEEYL--KGGGDLLEAVRKALKRLEGAYALAVISADepDRI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502874553 207 FVAR-DPlglrPLCYAI-EGPMFaAASESVALsnLGFRNENIHtLAPGHAVIIQNNQIEVKKFAESPKT 273
Cdd:COG0449 172 VAARkGS----PLVIGLgEGENF-LASDVPAL--LPYTRRVIY-LEDGEIAVLTRDGVEIYDLDGEPVE 232
|
|
| AsnB |
COG0367 |
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ... |
132-267 |
2.21e-11 |
|
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis
Pssm-ID: 440136 [Multi-domain] Cd Length: 558 Bit Score: 66.40 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 132 AFNGQIANYTQLMEEIQAK-REFHlaRQTDTEILMHLISQQlsGdrrpslvellTELSKKLDGAYNIVFLNA-LGEMFVA 209
Cdd:COG0367 72 VFNGEIYNYRELRAELEALgHRFR--THSDTEVILHAYEEW--G----------EDCLERLNGMFAFAIWDRrERRLFLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 210 RDPLGLRPLCYAIEGPMFAAASE---------------SVALSN-LGFRN--------ENIHTLAPGHAVIIQNN-QIEV 264
Cdd:COG0367 138 RDRFGIKPLYYAEDGGGLAFASElkallahpgvdreldPEALAEyLTLGYvpaprtifKGIRKLPPGHYLTVDAGgELEI 217
|
...
gi 502874553 265 KKF 267
Cdd:COG0367 218 RRY 220
|
|
| YafJ |
cd01908 |
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ... |
92-260 |
1.30e-09 |
|
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those 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 YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.
Pssm-ID: 238889 [Multi-domain] Cd Length: 257 Bit Score: 58.94 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 92 RLKGPAAIGHVRYATCGKEDRCYAHPFERTHIeknkwfSFAFNGQIANYTQLMEEIQAKREFHLARQTDTEILMHLISQQ 171
Cdd:cd01908 77 PIKSPLVLAHVRAATVGPVSLENCHPFTRGRW------LFAHNGQLDGFRLLRRRLLRLLPRLPVGTTDSELAFALLLSR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 172 L---SGDRRPSLVELLTELSKKLDGAYNIVFLNAL---GEMFVA-------------RDPLGLRPLCYAIEGPMfaAASE 232
Cdd:cd01908 151 LlerDPLDPAELLDAILQTLRELAALAPPGRLNLLlsdGEYLIAtryasapslyyltRRAPFGCARLLFRSVTT--PNDD 228
|
170 180
....*....|....*....|....*....
gi 502874553 233 SVAL-SNLGFRNENIHTLAPGHAVIIQNN 260
Cdd:cd01908 229 GVVVaSEPLTDDEGWTEVPPGELVVVSEG 257
|
|
| PTZ00077 |
PTZ00077 |
asparagine synthetase-like protein; Provisional |
97-267 |
1.04e-08 |
|
asparagine synthetase-like protein; Provisional
Pssm-ID: 185431 [Multi-domain] Cd Length: 586 Bit Score: 57.80 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 97 AAIGHVRYATCGKEDRcyAHPFerthIEKNKWFSFAFNGQIANYTQLMEEIQaKREFHLARQTDTEILMHLISQQLSGDr 176
Cdd:PTZ00077 49 NILAHERLAIVDLSDG--KQPL----LDDDETVALMQNGEIYNHWEIRPELE-KEGYKFSSNSDCEIIGHLYKEYGPKD- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 177 rpslvellteLSKKLDGAYNIVFLNAL-GEMFVARDPLGLRPLC--YAIEGPMFaAASESVALSNlgfRNENIHTLAPGH 253
Cdd:PTZ00077 121 ----------FWNHLDGMFATVIYDMKtNTFFAARDHIGIIPLYigYAKDGSIW-FSSELKALHD---QCVEVKQFPPGH 186
|
170
....*....|....
gi 502874553 254 AVIIQNNQIEVKKF 267
Cdd:PTZ00077 187 YYDQTKEKGEFVRY 200
|
|
| asnB |
PRK09431 |
asparagine synthetase B; Provisional |
132-253 |
1.44e-07 |
|
asparagine synthetase B; Provisional
Pssm-ID: 236513 [Multi-domain] Cd Length: 554 Bit Score: 54.14 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 132 AFNGQIANYTQLMEEIQAKREFHlaRQTDTEILMHLISqqlsgdrrpslvELLTELSKKLDGAYNIVFLNA-LGEMFVAR 210
Cdd:PRK09431 73 AVNGEIYNHQELRAELGDKYAFQ--TGSDCEVILALYQ------------EKGPDFLDDLDGMFAFALYDSeKDAYLIAR 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 502874553 211 DPLGLRPLCYAI-EGPMFAAASESVALSNLgfrNENIHTLAPGH 253
Cdd:PRK09431 139 DPIGIIPLYYGYdEHGNLYFASEMKALVPV---CKTIKEFPPGH 179
|
|
| Hpt1 |
COG2236 |
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine ... |
331-418 |
2.81e-07 |
|
Hypoxanthine phosphoribosyltransferase [Coenzyme transport and metabolism]; Hypoxanthine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 441837 [Multi-domain] Cd Length: 153 Bit Score: 50.23 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 331 ADAMAYKLGVPSLEGLIRNRYIGrtfieGKDRADKARLKYtPLREVLEGKRVLLVEDTIVRSTTMQVLISQLRERGGAKe 410
Cdd:COG2236 46 ARILADALGVPDLASIRVSSYTG-----TAKRLEEPVVKG-PLDEDLAGKRVLIVDDVADTGRTLEAVRDLLKEAGPAE- 118
|
....*...
gi 502874553 411 vhVRVACP 418
Cdd:COG2236 119 --VRTAVL 124
|
|
| PTZ00394 |
PTZ00394 |
glucosamine-fructose-6-phosphate aminotransferase; Provisional |
69-195 |
5.29e-07 |
|
glucosamine-fructose-6-phosphate aminotransferase; Provisional
Pssm-ID: 173585 [Multi-domain] Cd Length: 670 Bit Score: 52.57 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 69 KDVGTVSE----VFDIQHQDRYLPLMQRLKGPAAIGHVRYATCGKEDRCYAHPfertHIEKNKWFSFAFNGQIANYTQLM 144
Cdd:PTZ00394 67 RSVGNISQlrekVFSEAVAATLPPMDATTSHHVGIAHTRWATHGGVCERNCHP----QQSNNGEFTIVHNGIVTNYMTLK 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 502874553 145 EEIQAkREFHLARQTDTEILMHLISQQLSGDRRPSLVELLTELSKKLDGAY 195
Cdd:PTZ00394 143 ELLKE-EGYHFSSDTDTEVISVLSEYLYTRKGIHNFADLALEVSRMVEGSY 192
|
|
| PLN02549 |
PLN02549 |
asparagine synthase (glutamine-hydrolyzing) |
125-253 |
7.05e-07 |
|
asparagine synthase (glutamine-hydrolyzing)
Pssm-ID: 178164 [Multi-domain] Cd Length: 578 Bit Score: 52.07 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 125 KNKWFSFAFNGQIANYtqlmEEIQAKREFHLAR-QTDTEILMHLISqqlsgdrrpslvELLTELSKKLDGAYNIVFLNAL 203
Cdd:PLN02549 66 EDKTIVVTANGEIYNH----KELREKLKLHKFRtGSDCEVIAHLYE------------EHGEEFVDMLDGMFSFVLLDTR 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 502874553 204 GE-MFVARDPLGLRPL--CYAIEGPMFaAASESVALSNlgfRNENIHTLAPGH 253
Cdd:PLN02549 130 DNsFIAARDHIGITPLyiGWGLDGSVW-FASEMKALCD---DCERFEEFPPGH 178
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
299-417 |
9.77e-06 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 45.43 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 299 RKALGEELAA--LEDIERGDDlIVVPVPDTSKAAADAMAYKLGVPsLEGLIRNRYIGRTFIEgkdradkarLKYTPLREV 376
Cdd:pfam00156 11 ILKAVARLAAqiNEDYGGKPD-VVVGILRGGLPFAGILARRLDVP-LAFVRKVSYNPDTSEV---------MKTSSALPD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 502874553 377 LEGKRVLLVEDTIVRSTTMQVLISQLRERgGAKEVHVRVAC 417
Cdd:pfam00156 80 LKGKTVLIVDDILDTGGTLLKVLELLKNV-GPKEVKIAVLI 119
|
|
| PLN02981 |
PLN02981 |
glucosamine:fructose-6-phosphate aminotransferase |
97-199 |
3.52e-04 |
|
glucosamine:fructose-6-phosphate aminotransferase
Pssm-ID: 215531 [Multi-domain] Cd Length: 680 Bit Score: 43.20 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 97 AAIGHVRYATCGKEDRCYAHPfeRTHIEKNKwFSFAFNGQIANYtQLMEEIQAKREFHLARQTDTEI---LMHLISQQLS 173
Cdd:PLN02981 88 AGIAHTRWATHGPPAPRNSHP--QSSGPGNE-FLVVHNGIITNY-EVLKETLLRHGFTFESDTDTEVipkLAKFVFDKLN 163
|
90 100
....*....|....*....|....*..
gi 502874553 174 GDRRP-SLVELLTELSKKLDGAYNIVF 199
Cdd:PLN02981 164 EEEGDvTFSQVVMEVMRQLEGAYALIF 190
|
|
| Gn_AT_II_novel |
cd03766 |
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its ... |
131-244 |
5.17e-04 |
|
Gn_AT_II_novel. This asparagine synthase-related domain is present in eukaryotes but its function has not yet been determined. 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: 239735 [Multi-domain] Cd Length: 181 Bit Score: 41.12 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 131 FAFNGQIanYTQLMEEIQakrefhlarQTDTEILMHLISQQLSGDRRpslvelLTELSKKLDGAYNIVFLNALGE-MFVA 209
Cdd:cd03766 76 LQWNGEL--YNIDGVEDE---------ENDTEVIFELLANCSSESQD------ILDVLSSIEGPFAFIYYDASENkLYFG 138
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90 100 110
....*....|....*....|....*....|....*..
gi 502874553 210 RDPLGLRPLCYAIEGPMFAAASESVA--LSNLGFRNE 244
Cdd:cd03766 139 RDCLGRRSLLYKLDPNGFELSISSVSgsSSGSGFQEV 175
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| HptA |
COG0634 |
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; ... |
373-413 |
1.00e-03 |
|
Hypoxanthine-guanine phosphoribosyltransferase [Nucleotide transport and metabolism]; Hypoxanthine-guanine phosphoribosyltransferase is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440399 Cd Length: 176 Bit Score: 40.01 E-value: 1.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 502874553 373 LREVLEGKRVLLVEDtIVRS-TTMQVLISQLRERgGAKEVHV 413
Cdd:COG0634 85 LDEDIEGRDVLIVED-IIDTgLTLSYLLELLKSR-GPASVKI 124
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| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
299-417 |
1.19e-03 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 40.14 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502874553 299 RKALGEELA-ALEDIERGDDLIVVPvpdTSKA---AAdAMAYKLGVPSLeglirnrYIGRtfiEGKDRADKARLKytplR 374
Cdd:COG0461 46 LELLGEALAeLIKELGPEFDAVAGP---ATGGiplAA-AVARALGLPAI-------FVRK---EAKDHGTGGQIE----G 107
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90 100 110 120
....*....|....*....|....*....|....*....|...
gi 502874553 375 EVLEGKRVLLVEDTIVRSTTMQVLISQLRERGGakEVhVRVAC 417
Cdd:COG0461 108 GLLPGERVLVVEDVITTGGSVLEAVEALREAGA--EV-VGVAV 147
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| PLN02238 |
PLN02238 |
hypoxanthine phosphoribosyltransferase |
366-408 |
1.65e-03 |
|
hypoxanthine phosphoribosyltransferase
Pssm-ID: 215132 Cd Length: 189 Bit Score: 39.64 E-value: 1.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 502874553 366 ARLKYTPLREVLEGKRVLLVEDTIVRSTTMQVLISQLRERGGA 408
Cdd:PLN02238 84 AKVSGADLKIDVKGKHVLLVEDIVDTGNTLSALVAHLEAKGAA 126
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