|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09522 |
PRK09522 |
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
1-531 |
0e+00 |
|
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD;
Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 1118.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPI 80
Cdd:PRK09522 1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHD 160
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPANTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV 240
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 241 SMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSD 320
Cdd:PRK09522 241 SMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 321 LLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
Cdd:PRK09522 321 LLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 401 IAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKG 480
Cdd:PRK09522 401 IAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKG 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446686165 481 DAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG 531
Cdd:PRK09522 481 DAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG 531
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
4-531 |
1.81e-160 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 466.89 E-value: 1.81e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQL-RSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIG 82
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIgELGPEEIEVVRND---EITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVG--SNIPAGLTINAHF-NGMVMAVRH 159
Cdd:PRK14607 79 VCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVeeASLPECLEVTAKSdDGEIMGIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 160 DADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPantlQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAAL 239
Cdd:PRK14607 159 KEHPIFGVQFHPESILTEEGKRILKNFLNYQREEIDI----KSYLKKLVEGEDLSFEEAEDVMEDITDGNATDAQIAGFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 240 VSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSS 319
Cdd:PRK14607 235 TALRMKGETADELAGFASVMREKSRHIPAPSPRTVDTCGTGGDGFGTFNISTTSAFVVAAAGVPVAKHGNRAVSSKSGSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 320 DLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVL 399
Cdd:PRK14607 315 DVLEALGVKLEMTPEEAASVLRETGFSFLFAPLFHPAMKHAAPARRELGIRTAFNLLGPLTNPARVKYQIVGVFDPSYAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 400 PIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQG 478
Cdd:PRK14607 395 PLAQALQRLGTERAMVVSGiDGYDEISTCGPTQILELEDGEIVTYTFDPEELGLKRVDPEELKGGDPQENYRLAEDVLKG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446686165 479 KGDAAHEAAVAANVAMLMRLHGHED-LQANAQTVLEVLRSGSAY---DRVTALAARG 531
Cdd:PRK14607 475 EPRRPQRDAVALNAGAALYLVGEADsIKEGVGKALDLIDDGRAYkklEEVMDLSKTL 531
|
|
| trpD |
PRK00188 |
anthranilate phosphoribosyltransferase; Provisional |
198-529 |
2.90e-157 |
|
anthranilate phosphoribosyltransferase; Provisional
Pssm-ID: 234682 [Multi-domain] Cd Length: 339 Bit Score: 451.45 E-value: 2.90e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 198 NTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYlFADIV 277
Cdd:PRK00188 1 MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVPDPDD-AVDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 278 GTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGF 357
Cdd:PRK00188 80 GTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEVGIGFLFAPLYHPAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 358 RHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVH-SGGMDEVSLHAPTIVAELH 436
Cdd:PRK00188 160 KHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRLGSKRALVVHgSDGLDEISLTGPTTVAELK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 437 DGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGH-EDLQANAQTVLEVL 515
Cdd:PRK00188 240 DGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQGKGPGAARDAVLLNAAAALYVAGKaDDLKEGVELAREAI 319
|
330
....*....|....
gi 446686165 516 RSGSAYDRVTALAA 529
Cdd:PRK00188 320 DSGAALAKLEELVA 333
|
|
| trpD |
TIGR01245 |
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, ... |
204-529 |
1.32e-151 |
|
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, Thermotoga maritima, and Archaeoglobus fulgidus, this enzymatic domain (anthranilate phosphoribosyltransferase) is found C-terminal to glutamine amidotransferase; the fusion protein is designated anthranilate synthase component II (EC 4.1.3.27) [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 273522 [Multi-domain] Cd Length: 330 Bit Score: 436.70 E-value: 1.32e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 204 LEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFP-RPDYLFADIVGTGGD 282
Cdd:TIGR01245 1 LEKLIDGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPgRPPEDLVDIVGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 283 GSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMP 362
Cdd:TIGR01245 81 GANTINISTASAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLGPEKVARSLEETGIGFLFAPLYHPAMKHVAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 363 VRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTIVAELHDGEIK 441
Cdd:TIGR01245 161 VRRELGVRTVFNLLGPLTNPARPKYQVIGVYDPDLVEVMAEALKNLGVKRALVVHGdDGLDEISLTGPTTVAELKDGEIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 442 SYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHE-DLQANAQTVLEVLRSGSA 520
Cdd:TIGR01245 241 EYTLDPEDFGLPRAPLEELAGGSPEENAEILRDILRGKGSGAKRDIVALNAAAALYVAGRAsDLKEGVELALEAIDSGAA 320
|
....*....
gi 446686165 521 YDRVTALAA 529
Cdd:TIGR01245 321 AEKLEELVA 329
|
|
| TrpD |
COG0547 |
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ... |
199-524 |
5.40e-139 |
|
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and metabolism]; Anthranilate phosphoribosyltransferase, glycosyltransferase domain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440313 [Multi-domain] Cd Length: 327 Bit Score: 404.46 E-value: 5.40e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 199 TLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVG 278
Cdd:COG0547 1 MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPLPDGDVVDIVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 279 TGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFR 358
Cdd:COG0547 81 TGGDGANTFNISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEAGIGFLFAPLFHPAMK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 359 HAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTIVAELHD 437
Cdd:COG0547 161 HVAPVRKELGVRTIFNLLGPLTNPAGPKRQLLGVYHPELVEPLAEVLQLLGVKRALVVHGlDGLDEISLTGPTKVAELRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 438 GEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRS 517
Cdd:COG0547 241 GEIEEYTLDPEDFGLPRAPLEDLRGGDAEENAEILRAVLAGEGGPARDAVLLNAAAALYVAGKADSLAEGVELAREAIDS 320
|
....*..
gi 446686165 518 GSAYDRV 524
Cdd:COG0547 321 GAALAKL 327
|
|
| Glycos_transf_3 |
pfam00591 |
Glycosyl transferase family, a/b domain; This family includes anthranilate ... |
270-521 |
3.85e-113 |
|
Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 459860 [Multi-domain] Cd Length: 253 Bit Score: 335.80 E-value: 3.85e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 270 DYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLF 349
Cdd:pfam00591 1 LGDLVDIVGTGGDGDNTFNISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEALGINLDLTPEQVRKLLDEVGVGFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 350 APKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAP 429
Cdd:pfam00591 81 APNYHPAMKHVAPVRRELGIRTVFNLLGPLINPARVKRQVLGVYSKELAEGLAEVLKDLGRERAAVVHGDGLDEASLLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 430 TIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHG-HEDLQANA 508
Cdd:pfam00591 161 TTVAELKDGEITEYTLTPEDFGLGRATLEALEGGSPKENADILKGVLGGKGSAAHRDLVALNAGAALYLAGkADSLKEGV 240
|
250
....*....|...
gi 446686165 509 QTVLEVLRSGSAY 521
Cdd:pfam00591 241 AKALEVIDSGKAL 253
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
3-191 |
4.43e-108 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 320.15 E-value: 4.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 3 DILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLAtmsNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIG 82
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALN---PDAIVLSPGPGTPAEAGISLELIREFAGKVPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVG--SNIPAGLTINAH-FNGMVMAVRH 159
Cdd:PRK05670 78 VCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAWtDDGEIMGVRH 157
|
170 180 190
....*....|....*....|....*....|..
gi 446686165 160 DADRVCGFQFHPESILTTQGARLLEQTLAWAQ 191
Cdd:PRK05670 158 KELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
4-192 |
5.14e-92 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 279.23 E-value: 5.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRND---EITLEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGS--NIPAGLTINAHF-NGMVMAVRHD 160
Cdd:COG0512 78 CLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDreTLPDELEVTAWTeDGEIMGIRHR 157
|
170 180 190
....*....|....*....|....*....|..
gi 446686165 161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQ 192
Cdd:COG0512 158 ELPIEGVQFHPESILTEHGHQLLANFLELAGE 189
|
|
| PLN02641 |
PLN02641 |
anthranilate phosphoribosyltransferase |
199-478 |
1.01e-81 |
|
anthranilate phosphoribosyltransferase
Pssm-ID: 215345 [Multi-domain] Cd Length: 343 Bit Score: 258.12 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 199 TLQPILEKLYQAQTLSQQESHQLFSAVVRGElKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFP-RPDYLfaDIV 277
Cdd:PLN02641 3 SFRQLIESLIQGTDLTEEEAEAALDFLLDDA-DEAQISAFLVLLRAKGETFEEIAGLARAMIKRARKVDgLVDAV--DIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 278 GTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGF 357
Cdd:PLN02641 80 GTGGDGANTVNISTGSSILAAACGAKVAKQGNRSSSSACGSADVLEALGVAIDLGPEGVKRCVEEVGIGFMMAPKYHPAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 358 RHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHD 437
Cdd:PLN02641 160 KIVAPVRKKLKVKTVFNILGPMLNPARVPHAVVGVYHESLVEKMAKALQRFGMKRALVVHSEGLDEMSPLGPGDVLEVTP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446686165 438 GEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQG 478
Cdd:PLN02641 240 EKIEEFSFDPLDFGIPRCTLEDLRGGDPDYNAKVLRDVLSG 280
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
4-187 |
8.30e-78 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 242.44 E-value: 8.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERlatMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELEL---LNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAG---LTINAHFNGMVMAVRHD 160
Cdd:cd01743 78 CLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPdllEVTASTEDGVIMALRHR 157
|
170 180
....*....|....*....|....*..
gi 446686165 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:cd01743 158 DLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
5-184 |
1.68e-56 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 187.06 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 5 LLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATmsnpVLMLSPGPGVPSEAGCMPELLTRLRG-KLPIIGI 83
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPD----GIILSGGPGSPGAAGGAIEAIREARElKIPILGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAG-EILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSN--IPAGLTINAH--FNGMVMAVR 158
Cdd:pfam00117 77 CLGHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTATseNDGTIMGIR 156
|
170 180
....*....|....*....|....*.
gi 446686165 159 HDADRVCGFQFHPESILTTQGARLLE 184
Cdd:pfam00117 157 HKKLPIFGVQFHPESILTPHGPEILF 182
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
4-183 |
5.40e-55 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 183.07 E-value: 5.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMsnpVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPL---LIVISPGPCTPNEAGISLEAIRHFAGKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA--HFNGMVMAVRH 159
Cdd:TIGR00566 79 CLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAweEENIEIMAIRH 158
|
170 180
....*....|....*....|....
gi 446686165 160 DADRVCGFQFHPESILTTQGARLL 183
Cdd:TIGR00566 159 RDLPLEGVQFHPESILSEQGHQLL 182
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
4-185 |
2.56e-54 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 181.54 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRND---EVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINAHFN-GMVMAVRHD 160
Cdd:PRK07649 79 CLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIvkKETLPDCLEVTSWTEeGEIMAIRHK 158
|
170 180
....*....|....*....|....*
gi 446686165 161 ADRVCGFQFHPESILTTQGARLLEQ 185
Cdd:PRK07649 159 TLPIEGVQFHPESIMTSHGKELLQN 183
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
4-188 |
3.26e-48 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 166.38 E-value: 3.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLmLSPGPGVPSEAG-CMPELLTRLRGKLPIIG 82
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFDGVL-LSPGPGTPERAGaSIDMVRACAAAGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSL--VGSNIPAGLTINAHF-NGMVMAVRH 159
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLtiLPETLPAELEVTARTdSGVIMAVRH 161
|
170 180
....*....|....*....|....*....
gi 446686165 160 DADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:PRK07765 162 RELPIHGVQFHPESVLTEGGHRMLANWLT 190
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
4-187 |
2.83e-47 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 162.98 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLatmsNPV-LMLSPGPGVPSEAGCMPELLTRLRGKLPIIG 82
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNL----NIRhIIISPGPGHPRDSGISLDVISSYAPYIPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINAHF-NGMVMAVRH 159
Cdd:CHL00101 78 VCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIidPLNLPSPLEITAWTeDGLIMACRH 157
|
170 180
....*....|....*....|....*....
gi 446686165 160 DADRVC-GFQFHPESILTTQGARLLEQTL 187
Cdd:CHL00101 158 KKYKMLrGIQFHPESLLTTHGQQILRNFL 186
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
4-187 |
2.45e-46 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 160.41 E-value: 2.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSnpvLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSH---LVISPGPCTPNEAGISLAVIRHFADKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA--HFNGMV---MA 156
Cdd:PRK06774 79 CLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLViaADSLPGCFELTAwsERGGEMdeiMG 158
|
170 180 190
....*....|....*....|....*....|.
gi 446686165 157 VRHDADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:PRK06774 159 IRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
4-187 |
1.07e-45 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 158.54 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipAQTLIErLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRND--ALTLAD-IDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLV--GSNIPAGLTINA-HFNGMVMAVRHD 160
Cdd:PRK08007 79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVvePDSLPACFEVTAwSETREIMGIRHR 158
|
170 180
....*....|....*....|....*..
gi 446686165 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:PRK08007 159 QWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
4-188 |
7.32e-44 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 153.88 E-value: 7.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLatmsNPV-LMLSPGPGVPSEAGCMPELLTRLRGKLPIIG 82
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEAL----NPThLVISPGPCTPNEAGISLQAIEHFAGKLPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSN--IPAGLTINA---HFNGM---V 154
Cdd:PRK08857 78 VCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNdtLPECFELTAwteLEDGSmdeI 157
|
170 180 190
....*....|....*....|....*....|....
gi 446686165 155 MAVRHDADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:PRK08857 158 MGFQHKTLPIEAVQFHPESIKTEQGHQLLANFLA 191
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
4-192 |
5.13e-42 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 160.08 E-value: 5.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRnHIPAQTLIERLatmsNP-VLMLSPGPGVPSEAGCmPELLTRLRGK-LPII 81
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVR-YGFAEEMLDRV----NPdLVVLSPGPGRPSDFDC-KATIDAALARnLPIF 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 82 GICLGHQAIVEAYGGYVGQAGEILHGKASSIE-HDGQAMFAGLTNPLPVARYHSLVG--SNIPAGLTINAHF-NGMVMAV 157
Cdd:PRK13566 603 GVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFAdpETLPDELLVTAETeDGVIMAI 682
|
170 180 190
....*....|....*....|....*....|....*...
gi 446686165 158 RHDADRVCGFQFHPESILTTQ---GARLLEQTLAWAQQ 192
Cdd:PRK13566 683 EHKTLPVAAVQFHPESIMTLGgdvGLRIIENVVRLLAG 720
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
8-188 |
5.18e-42 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 148.64 E-value: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 8 DNIDSFTYNLADQLRSNGH--NVVIYRNhipAQTLIERLATmsNP-VLMLSPGPGVPS---EAGCMPELLTRLRGKLPII 81
Cdd:NF041322 3 DNFDSFTYNLVEYVSEQREhaETTVLKN---TASLAEVRAV--DPdAIVISPGPGHPKndrDVGVTADVLRELSPEVPTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 82 GICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINA----HFNGMVMAV 157
Cdd:NF041322 78 GVCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTAttdhDGEELVMGI 157
|
170 180 190
....*....|....*....|....*....|.
gi 446686165 158 RHDADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:NF041322 158 RHREHPIECVQFHPESVLTGVGHDVIENFLA 188
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
4-184 |
1.51e-40 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 146.10 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHipaQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGI 83
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRND---ELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQAGE-ILHGKASSIEHD---GQAMFAGLTNPLPVARYHSLVGS--NIPA-GLTINAHF-NGMVM 155
Cdd:PLN02335 98 CMGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEkdTFPSdELEVTAWTeDGLIM 177
|
170 180 190
....*....|....*....|....*....|
gi 446686165 156 AVRHDADR-VCGFQFHPESILTTQGARLLE 184
Cdd:PLN02335 178 AARHRKYKhIQGVQFHPESIITTEGKTIVR 207
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
1-188 |
6.22e-39 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 141.14 E-value: 6.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIErlatmSNPVLM-LSPGPGVPSEAGCMPELLTRLRGKLP 79
Cdd:PRK05637 1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILA-----ANPDLIcLSPGPGHPRDAGNMMALIDRTLGQIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 80 IIGICLGHQAIVEAYGGYVGQAGEIlHGKASSIEHDGQA----MFAGLT------NP------LPVARYHSLVGSNIPAG 143
Cdd:PRK05637 76 LLGICLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLAtdvepdHPeipgrkVPIARYHSLGCVVAPDG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446686165 144 L----TINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:PRK05637 155 MeslgTCSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVE 203
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
1-188 |
3.05e-24 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 99.81 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 1 MADILLLDNIDSFTYNLADQLRSNGhnvviyrnhIPAQTL-IERL---ATMSNPVLMLSPGPGVPSEAGCMPELLTRLRG 76
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIRKLG---------VPMQVVnVEDLdldEVENFSHILISPGPDVPRAYPQLFAMLERYHQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASS-IEHDGQAMFAGLTNPLPVARYHSLVGS--NIPAGLTINAHFN-G 152
Cdd:PRK06895 72 HKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPlKVRSNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVCDeN 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 446686165 153 MVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:PRK06895 152 VVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWLA 187
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
4-184 |
6.40e-22 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 93.15 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMsNPV-LMLSPGPGVPSEAGCmPELLTR-LRGKLPII 81
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELG----VYSELVPNTTPLEEIREK-NPKgIILSGGPSSVYAENA-PRADEKiFELGVPVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 82 GICLGHQAIVEAYGGYVGQAGEILHGKAS-SIEHDGqAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHF-NGMVMAVRH 159
Cdd:TIGR00888 75 GICYGMQLMAKQLGGEVGRAEKREYGKAElEILDED-DLFRGLPDESTVWMSHGDKVKELPEGFKVLATSdNCPVAAMAH 153
|
170 180
....*....|....*....|....*
gi 446686165 160 DADRVCGFQFHPESILTTQGARLLE 184
Cdd:TIGR00888 154 EEKPIYGVQFHPEVTHTEYGNELLE 178
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
5-184 |
1.35e-21 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 99.15 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 5 LLLDNIDSFTYNLADQLRS-NGHNVVIYRN-----HIPAQTLIERLAtMSNPVLmlSPGPGVPSEA---GCMPELLTRLR 75
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELSIvNGVPPVVVRNdewtwEEVYHYLYEEKA-FDNIVI--SPGPGSPTCPadiGICLRLLLECR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 76 gKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMF----AGLTNPLPVARYHSLV--------------- 136
Cdd:PLN02889 162 -DIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVidaeslpkelvpiaw 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 137 -----------------------------GSNIPAGLTIN-------AHFNGM-----VMAVRHDADRVCGFQFHPESIL 175
Cdd:PLN02889 241 tsssdtlsflesqksglvpdayesqigqsGSSDPFSSKLKngtswpsSHSERMqngkiLMGIMHSTRPHYGLQFHPESIA 320
|
....*....
gi 446686165 176 TTQGARLLE 184
Cdd:PLN02889 321 TCYGRQIFK 329
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
4-183 |
5.22e-19 |
|
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate.
Pssm-ID: 273821 [Multi-domain] Cd Length: 742 Bit Score: 90.74 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLAD---QLRSNGHNVVIYRNHIPAQTLIERLATMSnpVLMLSPGPGVPSEA---GCMPELLT-RLRG 76
Cdd:TIGR01823 8 VLFIDSYDSFTYNVVRlleQQTDISVHVTTVHSDTFQDQLLELLPLFD--AIVVGPGPGNPNNAqdmGIISELWElANLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNpLPVARYHSLVGSNIP-----AGLTINAHFN 151
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtllPLCLTEDEEG 164
|
170 180 190
....*....|....*....|....*....|..
gi 446686165 152 GMVMAVRHDADRVCGFQFHPESILTTQGARLL 183
Cdd:TIGR01823 165 IILMSAQTKKKPWFGVQYHPESCCSELGSGKL 196
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
4-184 |
3.64e-16 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 76.42 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLMLSPGP------GVPSeagCMPELLTrlrGK 77
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELG----VYSEILPNTTPLEEIKLKNPKGIILSGGPssvyeeDAPR---VDPEIFE---LG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 78 LPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHF-NGMVMA 156
Cdd:cd01742 71 VPVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSdNCPVAA 150
|
170 180
....*....|....*....|....*...
gi 446686165 157 VRHDADRVCGFQFHPESILTTQGARLLE 184
Cdd:cd01742 151 IANEEKKIYGVQFHPEVTHTEKGKEILK 178
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
4-172 |
2.03e-15 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 75.37 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNID---SFTYNLADQLRSNGHNVVIYRnhIPAQTLIERLATMSNP-VLMLSPGP-GVPSEAGCMPELLTRLRG-- 76
Cdd:COG0518 2 ILILDHDPfggQYPGLIARRLREAGIELDVLR--VYAGEILPYDPDLEDPdGLILSGGPmSVYDEDPWLEDEPALIREaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 77 --KLPIIGICLGHQAIVEAYGGYVGQAG--EIlhGKAsSIE-HDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAH-F 150
Cdd:COG0518 80 elGKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWA-PVElTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASsD 156
|
170 180
....*....|....*....|..
gi 446686165 151 NGMVMAVRHDaDRVCGFQFHPE 172
Cdd:COG0518 157 NCPNQAFRYG-RRVYGVQFHPE 177
|
|
| Glycos_trans_3N |
pfam02885 |
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ... |
201-263 |
5.29e-15 |
|
Glycosyl transferase family, helical bundle domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.
Pssm-ID: 460737 [Multi-domain] Cd Length: 63 Bit Score: 69.33 E-value: 5.29e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446686165 201 QPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENA 263
Cdd:pfam02885 1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
|
|
| PRK09071 |
PRK09071 |
glycosyl transferase family protein; |
210-447 |
2.02e-14 |
|
glycosyl transferase family protein;
Pssm-ID: 181637 [Multi-domain] Cd Length: 323 Bit Score: 74.18 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 210 AQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLE-NAAPFPRPD---------------YLF 273
Cdd:PRK09071 18 RRSLTREEARQAMGMILDGEVEDDQLGAFLMLLRVKEETAEELAGFVEAIRErLQAPPLAVDldwpsyagkrrhlpwYLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 274 AdivgtggdgsnsinistasAFVAAACGLKVAKHGNRSVSSKSGSS-DLLAAFGINLDMNADKSRQALDELGVCFL---- 348
Cdd:PRK09071 98 A-------------------AKLLAQNGYRVLLHGGGGHTAGRLYTeQLLEALGIPIARSWQEAEQALEEHNIAYLpled 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 349 FAPKYHTgfrhAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVH-SGGMDEVSLH 427
Cdd:PRK09071 159 FAPQLQR----MIDLRNTLGLRSPINTLARLLNPLNAKASLQGIFHPGYQQLHREAARLLGDQNALVFKgEGGESERNPD 234
|
250 260
....*....|....*....|
gi 446686165 428 APTIVAELHDGEIKSYQLTA 447
Cdd:PRK09071 235 VSTTLYGSRNGEAWDEEWPA 254
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
4-184 |
7.69e-14 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 69.88 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERlatmsNPVLMLSPGPGVpSEAGCMPELLTRLrgKLPIIGI 83
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAF-----EDGLILSGGPDI-ERAGNCPEYLKEL--DVPILGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 84 CLGHQAIVEAYGGYVGQA--GEILHGKASSIEHDGqaMFAGLTNPLPVARYHSLVGSNIPAGLTINAHF-NGMVMAVRHD 160
Cdd:PRK00758 74 CLGHQLIAKAFGGEVGRGeyGEYALVEVEILDEDD--ILKGLPPEIRVWASHADEVKELPDGFEILARSdICEVEAMKHK 151
|
170 180
....*....|....*....|....
gi 446686165 161 ADRVCGFQFHPESILTTQGARLLE 184
Cdd:PRK00758 152 EKPIYGVQFHPEVAHTEYGEEIFK 175
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
74-184 |
2.19e-13 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 72.39 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 74 LRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAH-FNG 152
Cdd:PRK00074 72 FELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIAStENC 151
|
90 100 110
....*....|....*....|....*....|..
gi 446686165 153 MVMAVRHDADRVCGFQFHPESILTTQGARLLE 184
Cdd:PRK00074 152 PIAAIANEERKFYGVQFHPEVTHTPQGKKLLE 183
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
15-173 |
1.13e-09 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 57.51 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 15 YNLADQLRSNGHNVVIyrnhIPAQTLIERLATMsNP-VLMLSPGPGVPSEAgcmPELLTRLR----GKLPIIGICLGHQA 89
Cdd:cd01744 10 HNILRELLKRGCEVTV----VPYNTDAEEILKL-DPdGIFLSNGPGDPALL---DEAIKTVRkllgKKIPIFGICLGHQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 90 IVEAYG--------GYVGQ---AGEILHGKA--SSIEHdGQAmfagltnplpvaryhsLVGSNIPAGLTINaHFN---GM 153
Cdd:cd01744 82 LALALGaktykmkfGHRGSnhpVKDLITGRVyiTSQNH-GYA----------------VDPDSLPGGLEVT-HVNlndGT 143
|
170 180
....*....|....*....|
gi 446686165 154 VMAVRHDADRVCGFQFHPES 173
Cdd:cd01744 144 VEGIRHKDLPVFSVQFHPEA 163
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
15-96 |
1.91e-08 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 56.10 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 15 YNLADQLRSNGHNVVIYrnhiPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAY 94
Cdd:TIGR01368 184 RNILRRLVKRGCEVTVV----PYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAF 259
|
..
gi 446686165 95 GG 96
Cdd:TIGR01368 260 GA 261
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
73-172 |
3.96e-08 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 53.40 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 73 RLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIE--HDGQAM--FAGLTNPLPVARYHSLVGSNIPAGLTI-- 146
Cdd:cd01741 77 ALAAGKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTltEAGKADplFAGLPDEFPVFHWHGDTVVELPPGAVLla 156
|
90 100
....*....|....*....|....*..
gi 446686165 147 -NAHFNGMVMAVRhdaDRVCGFQFHPE 172
Cdd:cd01741 157 sSEACPNQAFRYG---DRALGLQFHPE 180
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
4-187 |
4.38e-08 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 55.85 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFTYNLADQLRSNGhnvvIYRNHIPAQTLIERLATMSNPVLMLSPGP------GVPSeagcMPELLTRL--R 75
Cdd:PLN02347 13 VLILDYGSQYTHLITRRVRELG----VYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPT----VPEGFFDYcrE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 76 GKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARY--HSLVGSNIPAGLTINAH-FNG 152
Cdd:PLN02347 85 RGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQTVWmsHGDEAVKLPEGFEVVAKsVQG 164
|
170 180 190
....*....|....*....|....*....|....*
gi 446686165 153 MVMAVRHDADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:PLN02347 165 AVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-96 |
7.01e-08 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 51.06 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFT---YNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSnpVLMLSPGPGVPSEAGCMPELLTRLR----G 76
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDDYD--GLILPGGPGTPDDLARDEALLALLReaaaA 78
|
90 100
....*....|....*....|
gi 446686165 77 KLPIIGICLGHQAIVEAYGG 96
Cdd:cd01653 79 GKPILGICLGAQLLVLGVQF 98
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
16-96 |
1.29e-07 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 53.74 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 16 NLADQLRSNGHNVVIYrnhiPAQTLIERLATMSNPVLMLSPGPGVPSEagcMPELLTRLRGK---LPIIGICLGHQAIVE 92
Cdd:PRK12838 180 SILRSLSKRGCKVTVL----PYDTSLEEIKNLNPDGIVLSNGPGDPKE---LQPYLPEIKKLissYPILGICLGHQLIAL 252
|
....
gi 446686165 93 AYGG 96
Cdd:PRK12838 253 ALGA 256
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
15-173 |
1.91e-07 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 53.44 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 15 YNLADQLRSNGHNVVIYRNHIPAQTLIErlatMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAY 94
Cdd:PLN02771 252 HNILRRLASYGCKITVVPSTWPASEALK----MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 95 GGYVGQAGEILHGKassiEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTInAHFN---GMVMAVRHDADRVCGFQFHP 171
Cdd:PLN02771 328 GGKTFKMKFGHHGG----NHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEV-THVNlndGSCAGLAFPALNVMSLQYHP 402
|
..
gi 446686165 172 ES 173
Cdd:PLN02771 403 EA 404
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-90 |
7.46e-07 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 47.20 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 4 ILLLDNIDSFT---YNLADQLRSNGHNVVIYRNHIPAQTLIERLAtmSNPVLMLSPGPGVPSEAGCMPELLTRLR----G 76
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLD--DYDGLILPGGPGTPDDLAWDEALLALLReaaaA 78
|
90
....*....|....
gi 446686165 77 KLPIIGICLGHQAI 90
Cdd:cd03128 79 GKPVLGICLGAQLL 92
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
35-96 |
1.53e-05 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 47.38 E-value: 1.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446686165 35 IPAQTLIERLATMsNP-VLMLSPGPGVPSEAGCMPELLTRL-RGKLPIIGICLGHQAIVEAYGG 96
Cdd:PRK12564 205 VPATTTAEEILAL-NPdGVFLSNGPGDPAALDYAIEMIRELlEKKIPIFGICLGHQLLALALGA 267
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
15-96 |
7.63e-05 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 45.17 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 15 YNLADQLRSNGHNVVIyrnhIPAQTLIERLATMSNPVLMLSPGPGVPSEAG-CMPELLTRLRGKLPIIGICLGHQAIVEA 93
Cdd:CHL00197 204 YNILRRLKSFGCSITV----VPATSPYQDILSYQPDGILLSNGPGDPSAIHyGIKTVKKLLKYNIPIFGICMGHQILSLA 279
|
...
gi 446686165 94 YGG 96
Cdd:CHL00197 280 LEA 282
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
15-96 |
1.26e-04 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 44.24 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 15 YNLADQLRSNGHNVVIYrnhiPAQTLIERLATMsNPV-LMLSPGPGVPSEagcMPELLTRLRG----KLPIIGICLGHQA 89
Cdd:COG0505 188 RNILRELAERGCRVTVV----PATTSAEEILAL-NPDgVFLSNGPGDPAA---LDYAIETIREllgkGIPIFGICLGHQL 259
|
....*..
gi 446686165 90 IVEAYGG 96
Cdd:COG0505 260 LALALGA 266
|
|
| PRK08136 |
PRK08136 |
glycosyl transferase family protein; Provisional |
210-409 |
7.47e-04 |
|
glycosyl transferase family protein; Provisional
Pssm-ID: 236160 [Multi-domain] Cd Length: 317 Bit Score: 41.77 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 210 AQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGS-NSIN 288
Cdd:PRK08136 17 ARDLDRDTARALYGAMLDGRVPDLELGAILIALRIKGESEAEMLGFLDAMQAHTIPLTPPAGRPMPVVIPSYNGArKQAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 289 ISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLK 368
Cdd:PRK08136 97 LTPLLALLLAREGVPVLVHGVSEDPTRVTSAEIFEALGIPPTLHADQAQAKLAEGQPAFIPVGVLCPPLARLLALRWRMG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446686165 369 TRTLFNVLGPLINP--AHPPLALIGVYSPELVLPIAETLRVLG 409
Cdd:PRK08136 177 VRNSAHTLAKLATPfaEGAALRLSSYTHPEYRDRLAEFFSDIG 219
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
73-172 |
4.16e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 38.77 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 73 RLRGKLPIIGICLGHQAIVEAYGG--YVGQAGEI--------LHGKASSIEHdgqamfagLTNPLPVARYHslvGS--NI 140
Cdd:PRK07053 79 RLAAGLPTLGICLGAQLIARALGArvYPGGQKEIgwapltltDAGRASPLRH--------LGAGTPVLHWH---GDtfDL 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 446686165 141 PAGLTINAHfngmVMAVRHDA----DRVCGFQFHPE 172
Cdd:PRK07053 148 PEGATLLAS----TPACRHQAfawgNHVLALQFHPE 179
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
75-172 |
6.22e-03 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 38.39 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446686165 75 RGKlPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDgQAMFAGLTNPLPVA---RYHSLVGSNIPA--------- 142
Cdd:pfam07722 104 RGK-PILGICRGFQLLNVALGGTLYQDIQEQPGFTDHREHC-QVAPYAPSHAVNVEpgsLLASLLGSEEFRvnslhhqai 181
|
90 100 110
....*....|....*....|....*....|....*...
gi 446686165 143 -----GLTINAHFN-GMVMAVRHDADR--VCGFQFHPE 172
Cdd:pfam07722 182 drlapGLRVEAVAPdGTIEAIESPNAKgfALGVQWHPE 219
|
|
| |
