|
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: 1053.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 1 MADILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLGTMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPI 80
Cdd:PRK09522 1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNIPAGLTINANFNGMVMAVRHD 160
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 161 ADRVCGFQFHPESILTTQGARLLEQTLAWALQKLEHTNTLQPILEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAALV 240
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 241 SMKVRGEQPQEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSD 320
Cdd:PRK09522 241 SMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 321 LLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
Cdd:PRK09522 321 LLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 401 IAETLRVLGYQRAAVVHSGGMDEVSLHAPTVVAELHAGEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQGKG 480
Cdd:PRK09522 401 IAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKG 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 556281144 481 EAAHEAAVAANVAMLMRLHGHEDLKANAQQVLDVLHSGAAYDRVTALAARG 531
Cdd:PRK09522 481 DAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG 531
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
4-531 |
6.91e-159 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 463.03 E-value: 6.91e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQL-RANGHNVVIYRNSVPAQALIERLgtmdNPV-LMLSPGPGTPSEAGCMPELLTRMRGKLPII 81
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIgELGPEEIEVVRNDEITIEEIEAL----NPShIVISPGPGRPEEAGISVEVIRHFSGKVPIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 82 GICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVG--SNIPAGLTINA-NFNGMVMAVR 158
Cdd:PRK14607 78 GVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVeeASLPECLEVTAkSDDGEIMGIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 159 HDADRVCGFQFHPESILTTQGARLLEQTLAWALQKLEhtntLQPILEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAA 238
Cdd:PRK14607 158 HKEHPIFGVQFHPESILTEEGKRILKNFLNYQREEID----IKSYLKKLVEGEDLSFEEAEDVMEDITDGNATDAQIAGF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 239 LVSMKVRGEQPQEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGS 318
Cdd:PRK14607 234 LTALRMKGETADELAGFASVMREKSRHIPAPSPRTVDTCGTGGDGFGTFNISTTSAFVVAAAGVPVAKHGNRAVSSKSGS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 319 SDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELV 398
Cdd:PRK14607 314 ADVLEALGVKLEMTPEEAASVLRETGFSFLFAPLFHPAMKHAAPARRELGIRTAFNLLGPLTNPARVKYQIVGVFDPSYA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 399 LPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTVVAELHAGEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQ 477
Cdd:PRK14607 394 EPLAQALQRLGTERAMVVSGiDGYDEISTCGPTQILELEDGEIVTYTFDPEELGLKRVDPEELKGGDPQENYRLAEDVLK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 556281144 478 GKGEAAHEAAVAANVAMLMRLHGHED-LKANAQQVLDVLHSGAAY---DRVTALAARG 531
Cdd:PRK14607 474 GEPRRPQRDAVALNAGAALYLVGEADsIKEGVGKALDLIDDGRAYkklEEVMDLSKTL 531
|
|
| trpD |
PRK00188 |
anthranilate phosphoribosyltransferase; Provisional |
198-529 |
2.91e-155 |
|
anthranilate phosphoribosyltransferase; Provisional
Pssm-ID: 234682 [Multi-domain] Cd Length: 339 Bit Score: 446.45 E-value: 2.91e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 198 NTLQPILEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLENAAPFPRPDYlFADIV 277
Cdd:PRK00188 1 MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVPDPDD-AVDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 278 GTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGF 357
Cdd:PRK00188 80 GTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEVGIGFLFAPLYHPAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 358 RHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVH-SGGMDEVSLHAPTVVAELH 436
Cdd:PRK00188 160 KHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRLGSKRALVVHgSDGLDEISLTGPTTVAELK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 437 AGEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHGH-EDLKANAQQVLDVL 515
Cdd:PRK00188 240 DGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQGKGPGAARDAVLLNAAAALYVAGKaDDLKEGVELAREAI 319
|
330
....*....|....
gi 556281144 516 HSGAAYDRVTALAA 529
Cdd:PRK00188 320 DSGAALAKLEELVA 333
|
|
| trpD |
TIGR01245 |
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, ... |
204-529 |
2.05e-145 |
|
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: 420.91 E-value: 2.05e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 204 LEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLENAAPFP-RPDYLFADIVGTGGD 282
Cdd:TIGR01245 1 LEKLIDGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPgRPPEDLVDIVGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 283 GSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGFRHAMP 362
Cdd:TIGR01245 81 GANTINISTASAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLGPEKVARSLEETGIGFLFAPLYHPAMKHVAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 363 VRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTVVAELHAGEIK 441
Cdd:TIGR01245 161 VRRELGVRTVFNLLGPLTNPARPKYQVIGVYDPDLVEVMAEALKNLGVKRALVVHGdDGLDEISLTGPTTVAELKDGEIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 442 SYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHGHE-DLKANAQQVLDVLHSGAA 520
Cdd:TIGR01245 241 EYTLDPEDFGLPRAPLEELAGGSPEENAEILRDILRGKGSGAKRDIVALNAAAALYVAGRAsDLKEGVELALEAIDSGAA 320
|
....*....
gi 556281144 521 YDRVTALAA 529
Cdd:TIGR01245 321 AEKLEELVA 329
|
|
| TrpD |
COG0547 |
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ... |
199-524 |
1.55e-135 |
|
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: 395.60 E-value: 1.55e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 199 TLQPILEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLENAAPFPRPDYLFADIVG 278
Cdd:COG0547 1 MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPLPDGDVVDIVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 279 TGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGFR 358
Cdd:COG0547 81 TGGDGANTFNISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEAGIGFLFAPLFHPAMK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 359 HAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTVVAELHA 437
Cdd:COG0547 161 HVAPVRKELGVRTIFNLLGPLTNPAGPKRQLLGVYHPELVEPLAEVLQLLGVKRALVVHGlDGLDEISLTGPTKVAELRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 438 GEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHGHEDLKANAQQVLDVLHS 517
Cdd:COG0547 241 GEIEEYTLDPEDFGLPRAPLEDLRGGDAEENAEILRAVLAGEGGPARDAVLLNAAAALYVAGKADSLAEGVELAREAIDS 320
|
....*..
gi 556281144 518 GAAYDRV 524
Cdd:COG0547 321 GAALAKL 327
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
3-191 |
5.23e-109 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 322.46 E-value: 5.23e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 3 DILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLgtmDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIG 82
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEAL---NPDAIVLSPGPGTPAEAGISLELIREFAGKVPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVG--SNIPAGLTINA-NFNGMVMAVRH 159
Cdd:PRK05670 78 VCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAwTDDGEIMGVRH 157
|
170 180 190
....*....|....*....|....*....|..
gi 556281144 160 DADRVCGFQFHPESILTTQGARLLEQTLAWAL 191
Cdd:PRK05670 158 KELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| Glycos_transf_3 |
pfam00591 |
Glycosyl transferase family, a/b domain; This family includes anthranilate ... |
270-521 |
5.24e-109 |
|
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: 325.01 E-value: 5.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 270 DYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLF 349
Cdd:pfam00591 1 LGDLVDIVGTGGDGDNTFNISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEALGINLDLTPEQVRKLLDEVGVGFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 350 APKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAP 429
Cdd:pfam00591 81 APNYHPAMKHVAPVRRELGIRTVFNLLGPLINPARVKRQVLGVYSKELAEGLAEVLKDLGRERAAVVHGDGLDEASLLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 430 TVVAELHAGEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHG-HEDLKANA 508
Cdd:pfam00591 161 TTVAELKDGEITEYTLTPEDFGLGRATLEALEGGSPKENADILKGVLGGKGSAAHRDLVALNAGAALYLAGkADSLKEGV 240
|
250
....*....|...
gi 556281144 509 QQVLDVLHSGAAY 521
Cdd:pfam00591 241 AKALEVIDSGKAL 253
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
4-190 |
7.36e-93 |
|
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: 281.16 E-value: 7.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERlgtMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEITLEEIEA---LAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGS--NIPAGLTINA-NFNGMVMAVRHD 160
Cdd:COG0512 78 CLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDreTLPDELEVTAwTEDGEIMGIRHR 157
|
170 180 190
....*....|....*....|....*....|
gi 556281144 161 ADRVCGFQFHPESILTTQGARLLEQTLAWA 190
Cdd:COG0512 158 ELPIEGVQFHPESILTEHGHQLLANFLELA 187
|
|
| PLN02641 |
PLN02641 |
anthranilate phosphoribosyltransferase |
197-478 |
4.22e-81 |
|
anthranilate phosphoribosyltransferase
Pssm-ID: 215345 [Multi-domain] Cd Length: 343 Bit Score: 256.58 E-value: 4.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 197 TNTLQPILEKLYQAETLSQQESHQLFSAVVRGEVkPEQLAAALVSMKVRGEQPQEIAGAATALLENAAPFP-RPDYLfaD 275
Cdd:PLN02641 1 IASFRQLIESLIQGTDLTEEEAEAALDFLLDDAD-EAQISAFLVLLRAKGETFEEIAGLARAMIKRARKVDgLVDAV--D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 276 IVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHT 355
Cdd:PLN02641 78 IVGTGGDGANTVNISTGSSILAAACGAKVAKQGNRSSSSACGSADVLEALGVAIDLGPEGVKRCVEEVGIGFMMAPKYHP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 356 GFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTVVAEL 435
Cdd:PLN02641 158 AMKIVAPVRKKLKVKTVFNILGPMLNPARVPHAVVGVYHESLVEKMAKALQRFGMKRALVVHSEGLDEMSPLGPGDVLEV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 556281144 436 HAGEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQG 478
Cdd:PLN02641 238 TPEKIEEFSFDPLDFGIPRCTLEDLRGGDPDYNAKVLRDVLSG 280
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
4-187 |
2.73e-79 |
|
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: 246.29 E-value: 2.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERlgtMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELEL---LNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNIPAG---LTINANFNGMVMAVRHD 160
Cdd:cd01743 78 CLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPdllEVTASTEDGVIMALRHR 157
|
170 180
....*....|....*....|....*..
gi 556281144 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:cd01743 158 DLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
5-184 |
1.97e-56 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 187.06 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 5 LLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIErlgtMDNPVLMLSPGPGTPSEAGCMPELLTRMRG-KLPIIGI 83
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILE----ENPDGIILSGGPGSPGAAGGAIEAIREARElKIPILGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAG-EILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSN--IPAGLTINA--NFNGMVMAVR 158
Cdd:pfam00117 77 CLGHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTAtsENDGTIMGIR 156
|
170 180
....*....|....*....|....*.
gi 556281144 159 HDADRVCGFQFHPESILTTQGARLLE 184
Cdd:pfam00117 157 HKKLPIFGVQFHPESILTPHGPEILF 182
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
4-185 |
6.80e-55 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 183.08 E-value: 6.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLgtmdNP-VLMLSPGPGTPSEAGCMPELLTRMRGKLPIIG 82
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRNDEVTISDIENM----KPdFLMISPGPCSPNEAGISMEVIRYFAGKIPIFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLV--GSNIPAGLTINA-NFNGMVMAVRH 159
Cdd:PRK07649 78 VCLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIvkKETLPDCLEVTSwTEEGEIMAIRH 157
|
170 180
....*....|....*....|....*.
gi 556281144 160 DADRVCGFQFHPESILTTQGARLLEQ 185
Cdd:PRK07649 158 KTLPIEGVQFHPESIMTSHGKELLQN 183
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
4-183 |
2.17e-54 |
|
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: 181.52 E-value: 2.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLGTMdnpVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPL---LIVISPGPCTPNEAGISLEAIRHFAGKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLV--GSNIPAGLTINA--NFNGMVMAVRH 159
Cdd:TIGR00566 79 CLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAweEENIEIMAIRH 158
|
170 180
....*....|....*....|....
gi 556281144 160 DADRVCGFQFHPESILTTQGARLL 183
Cdd:TIGR00566 159 RDLPLEGVQFHPESILSEQGHQLL 182
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
4-188 |
8.00e-48 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 165.22 E-value: 8.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLGTMDNPVLmLSPGPGTPSEAG-CMPELLTRMRGKLPIIG 82
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFDGVL-LSPGPGTPERAGaSIDMVRACAAAGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSL--VGSNIPAGLTINANF-NGMVMAVRH 159
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLtiLPETLPAELEVTARTdSGVIMAVRH 161
|
170 180
....*....|....*....|....*....
gi 556281144 160 DADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:PRK07765 162 RELPIHGVQFHPESVLTEGGHRMLANWLT 190
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
4-187 |
4.15e-47 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 162.39 E-value: 4.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLGTMDnpvLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQK---IVISPGPCTPDEAGISLDVIRHYAGRLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLV--GSNIPAGLTINA-NFNGMVMAVRHD 160
Cdd:PRK08007 79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVvePDSLPACFEVTAwSETREIMGIRHR 158
|
170 180
....*....|....*....|....*..
gi 556281144 161 ADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:PRK08007 159 QWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
4-187 |
4.38e-47 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 162.21 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLgtmdNPV-LMLSPGPGTPSEAGCMPELLTRMRGKLPIIG 82
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNL----NIRhIIISPGPGHPRDSGISLDVISSYAPYIPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLV--GSNIPAGLTINA-NFNGMVMAVRH 159
Cdd:CHL00101 78 VCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIidPLNLPSPLEITAwTEDGLIMACRH 157
|
170 180
....*....|....*....|....*....
gi 556281144 160 DADRVC-GFQFHPESILTTQGARLLEQTL 187
Cdd:CHL00101 158 KKYKMLrGIQFHPESLLTTHGQQILRNFL 186
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
4-187 |
4.77e-47 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 162.34 E-value: 4.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLGTMDnpvLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSH---LVISPGPCTPNEAGISLAVIRHFADKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLV--GSNIPAGLTINA--NFNGMV---MA 156
Cdd:PRK06774 79 CLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLViaADSLPGCFELTAwsERGGEMdeiMG 158
|
170 180 190
....*....|....*....|....*....|.
gi 556281144 157 VRHDADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:PRK06774 159 IRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
4-188 |
4.27e-45 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 157.35 E-value: 4.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLgtmdNPV-LMLSPGPGTPSEAGCMPELLTRMRGKLPIIG 82
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRNDEIDIDGIEAL----NPThLVISPGPCTPNEAGISLQAIEHFAGKLPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSN--IPAGLTINA---NFNGM---V 154
Cdd:PRK08857 78 VCLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNdtLPECFELTAwteLEDGSmdeI 157
|
170 180 190
....*....|....*....|....*....|....
gi 556281144 155 MAVRHDADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:PRK08857 158 MGFQHKTLPIEAVQFHPESIKTEQGHQLLANFLA 191
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
8-188 |
2.06e-44 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 155.19 E-value: 2.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 8 DNIDSFTYNLADQL--RANGHNVVIYRNSvpaqALIERLGTMDNPVLMLSPGPGTPS---EAGCMPELLTRMRGKLPIIG 82
Cdd:NF041322 3 DNFDSFTYNLVEYVseQREHAETTVLKNT----ASLAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNIPAGLTINA----NFNGMVMAVR 158
Cdd:NF041322 79 VCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTAttdhDGEELVMGIR 158
|
170 180 190
....*....|....*....|....*....|
gi 556281144 159 HDADRVCGFQFHPESILTTQGARLLEQTLA 188
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLA 188
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
4-192 |
6.02e-43 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 162.78 E-value: 6.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAqaliERLGTMDNPVLMLSPGPGTPSEAGCmPELLTRMRGK-LPIIG 82
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVRYGFAE----EMLDRVNPDLVVLSPGPGRPSDFDC-KATIDAALARnLPIFG 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIE-HDGQAMFAGLANPLPVARYHSLVG--SNIPAGLTINA-NFNGMVMAVR 158
Cdd:PRK13566 604 VCLGLQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFAdpETLPDELLVTAeTEDGVIMAIE 683
|
170 180 190
....*....|....*....|....*....|....*..
gi 556281144 159 HDADRVCGFQFHPESILTTQ---GARLLEQTLAWALQ 192
Cdd:PRK13566 684 HKTLPVAAVQFHPESIMTLGgdvGLRIIENVVRLLAG 720
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
4-184 |
1.53e-40 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 146.10 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSvpaQALIERLGTMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRND---ELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQAGE-ILHGKASSIEHD---GQAMFAGLANPLPVARYHSLVGS--NIPA-GLTINA-NFNGMVM 155
Cdd:PLN02335 98 CMGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEkdTFPSdELEVTAwTEDGLIM 177
|
170 180 190
....*....|....*....|....*....|
gi 556281144 156 AVRHDADR-VCGFQFHPESILTTQGARLLE 184
Cdd:PLN02335 178 AARHRKYKhIQGVQFHPESIITTEGKTIVR 207
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
1-192 |
6.19e-40 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 143.83 E-value: 6.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 1 MADILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPaqalIERLGTMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPI 80
Cdd:PRK05637 1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVP----VEEILAANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 81 IGICLGHQAIVEAYGGYVGQAGEIlHGKASSIEHDGQA----MFAGLA------NP------LPVARYHSLVGSNIPAGL 144
Cdd:PRK05637 77 LGICLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLAtdvepdHPeipgrkVPIARYHSLGCVVAPDGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556281144 145 ----TINANFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWALQ 192
Cdd:PRK05637 156 eslgTCSSEIGPVIMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLLA 207
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
1-188 |
4.51e-25 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 102.12 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 1 MADILLLDNIDSFTYNLADQLRanghnvviyRNSVPAQAL-IERL--GTMDN-PVLMLSPGPGTPSEAGCMPELLTRMRG 76
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIR---------KLGVPMQVVnVEDLdlDEVENfSHILISPGPDVPRAYPQLFAMLERYHQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASS-IEHDGQAMFAGLANPLPVARYHSLVGS--NIPAGLTINANFN-G 152
Cdd:PRK06895 72 HKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPlKVRSNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVCDeN 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 556281144 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 |
1.13e-21 |
|
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: 92.38 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGhnvvIYRNSVPAQALIERLGTMDNPVLMLSPGPGTPSEAGCmPELLTRM-RGKLPIIG 82
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELG----VYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENA-PRADEKIfELGVPVLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 83 ICLGHQAIVEAYGGYVGQAGEILHGKAS-SIEHDGqAMFAGLANPLPVARYHSLVGSNIPAGLTINA-NFNGMVMAVRHD 160
Cdd:TIGR00888 76 ICYGMQLMAKQLGGEVGRAEKREYGKAElEILDED-DLFRGLPDESTVWMSHGDKVKELPEGFKVLAtSDNCPVAAMAHE 154
|
170 180
....*....|....*....|....
gi 556281144 161 ADRVCGFQFHPESILTTQGARLLE 184
Cdd:TIGR00888 155 EKPIYGVQFHPEVTHTEYGNELLE 178
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
5-184 |
1.49e-21 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 98.77 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 5 LLLDNIDSFTYNLADQLRA-NG-HNVVIYRNSVPAQALIERL---GTMDNPVLmlSPGPGTPSEA---GCMPELLTRMRg 76
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELSIvNGvPPVVVRNDEWTWEEVYHYLyeeKAFDNIVI--SPGPGSPTCPadiGICLRLLLECR- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMF----AGLANPLPVARYHSLV--GSNIP--------- 141
Cdd:PLN02889 162 DIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFddipSGRNSGFKVVRYHSLVidAESLPkelvpiawt 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 142 -------------AGLTINANFNGM--------------------------------VMAVRHDADRVCGFQFHPESILT 176
Cdd:PLN02889 242 sssdtlsflesqkSGLVPDAYESQIgqsgssdpfssklkngtswpsshsermqngkiLMGIMHSTRPHYGLQFHPESIAT 321
|
....*...
gi 556281144 177 TQGARLLE 184
Cdd:PLN02889 322 CYGRQIFK 329
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
4-183 |
4.13e-20 |
|
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: 94.20 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRA---NGHNVVIYRNSVPAQALIERLGTMDnpVLMLSPGPGTPSEA---GCMPELLT-RMRG 76
Cdd:TIGR01823 8 VLFIDSYDSFTYNVVRLLEQqtdISVHVTTVHSDTFQDQLLELLPLFD--AIVVGPGPGNPNNAqdmGIISELWElANLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANpLPVARYHSLVGSNIP-----AGLTINANFN 151
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtllPLCLTEDEEG 164
|
170 180 190
....*....|....*....|....*....|..
gi 556281144 152 GMVMAVRHDADRVCGFQFHPESILTTQGARLL 183
Cdd:TIGR01823 165 IILMSAQTKKKPWFGVQYHPESCCSELGSGKL 196
|
|
| PRK09071 |
PRK09071 |
glycosyl transferase family protein; |
210-447 |
1.80e-16 |
|
glycosyl transferase family protein;
Pssm-ID: 181637 [Multi-domain] Cd Length: 323 Bit Score: 80.34 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 210 AETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLE-NAAPFPRPD---------------YLF 273
Cdd:PRK09071 18 RRSLTREEARQAMGMILDGEVEDDQLGAFLMLLRVKEETAEELAGFVEAIRErLQAPPLAVDldwpsyagkrrhlpwYLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 274 AdivgtggdgsnsinistasAFVAAACGLKVAKHGNRSVSSKSGSS-DLLAAFGINLDMNADKSRAALDELGVCFL---- 348
Cdd:PRK09071 98 A-------------------AKLLAQNGYRVLLHGGGGHTAGRLYTeQLLEALGIPIARSWQEAEQALEEHNIAYLpled 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 349 FAPKYHTgfrhAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVhSGGMDEVSLHa 428
Cdd:PRK09071 159 FAPQLQR----MIDLRNTLGLRSPINTLARLLNPLNAKASLQGIFHPGYQQLHREAARLLGDQNALVF-KGEGGESERN- 232
|
250 260
....*....|....*....|..
gi 556281144 429 PTVVAELH---AGEIKSYQLTA 447
Cdd:PRK09071 233 PDVSTTLYgsrNGEAWDEEWPA 254
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
4-184 |
1.20e-15 |
|
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: 74.88 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERlgtmdNPV-LMLSPGPGTPSEAG---CMPELLTrmrGKLP 79
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLK-----NPKgIILSGGPSSVYEEDaprVDPEIFE---LGVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 80 IIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNIPAGLTINANF-NGMVMAVR 158
Cdd:cd01742 73 VLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSdNCPVAAIA 152
|
170 180
....*....|....*....|....*.
gi 556281144 159 HDADRVCGFQFHPESILTTQGARLLE 184
Cdd:cd01742 153 NEEKKIYGVQFHPEVTHTEKGKEILK 178
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
4-210 |
1.26e-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: 76.14 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNID---SFTYNLADQLRANGHNVVIYRnsVPAQALIERLGTMDNP-VLMLSPGPGTP-SEAGCMPELLTRMRG-- 76
Cdd:COG0518 2 ILILDHDPfggQYPGLIARRLREAGIELDVLR--VYAGEILPYDPDLEDPdGLILSGGPMSVyDEDPWLEDEPALIREaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 77 --KLPIIGICLGHQAIVEAYGGYVGQAG--EIlhGKAsSIE-HDGQAMFAGLANPLPVARYHSLVGSNIPAGLTINA-NF 150
Cdd:COG0518 80 elGKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWA-PVElTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLAsSD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556281144 151 NGMVMAVRHDaDRVCGFQFHPE------SILTTQGARLLEQTLAWAlQKLEHTNTLQPILEKLYQA 210
Cdd:COG0518 157 NCPNQAFRYG-RRVYGVQFHPEvthtmmEAWLEERADELAAEELLA-EASLHDPELREAGRRLLRN 220
|
|
| Glycos_trans_3N |
pfam02885 |
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ... |
201-263 |
1.84e-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: 70.87 E-value: 1.84e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556281144 201 QPILEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLENA 263
Cdd:pfam02885 1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
4-184 |
1.10e-13 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 69.50 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERlgtmdNPVLMLSPGPgTPSEAGCMPELLTRMrgKLPIIGI 83
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKAF-----EDGLILSGGP-DIERAGNCPEYLKEL--DVPILGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 84 CLGHQAIVEAYGGYVGQA--GEILHGKASSIEHDGqaMFAGLANPLPVARYHSLVGSNIPAGLTINANF-NGMVMAVRHD 160
Cdd:PRK00758 74 CLGHQLIAKAFGGEVGRGeyGEYALVEVEILDEDD--ILKGLPPEIRVWASHADEVKELPDGFEILARSdICEVEAMKHK 151
|
170 180
....*....|....*....|....
gi 556281144 161 ADRVCGFQFHPESILTTQGARLLE 184
Cdd:PRK00758 152 EKPIYGVQFHPEVAHTEYGEEIFK 175
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
35-184 |
1.54e-12 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 69.69 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 35 VPAQALIERLGTMdNPV-LMLSPGPGTPSEAG---CMPELLtrmRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKAS 110
Cdd:PRK00074 33 VPYDISAEEIRAF-NPKgIILSGGPASVYEEGaprADPEIF---ELGVPVLGICYGMQLMAHQLGGKVERAGKREYGRAE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556281144 111 SIEHDGQAMFAGLANPLPVARYHSLVGSNIPAGLTINA-NFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLE 184
Cdd:PRK00074 109 LEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIAsTENCPIAAIANEERKFYGVQFHPEVTHTPQGKKLLE 183
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
15-173 |
1.91e-10 |
|
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: 59.82 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 15 YNLADQLRANGHNVVIyrnsVPAQALIERLGTMDNPVLMLSPGPGTPSEAgcmPELLTRMR----GKLPIIGICLGHQAI 90
Cdd:cd01744 10 HNILRELLKRGCEVTV----VPYNTDAEEILKLDPDGIFLSNGPGDPALL---DEAIKTVRkllgKKIPIFGICLGHQLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 91 VEAYG--------GYVGQ---AGEILHGKA--SSIEHdGQAmfaglanplpvaryhsLVGSNIPAGLT---INANfNGMV 154
Cdd:cd01744 83 ALALGaktykmkfGHRGSnhpVKDLITGRVyiTSQNH-GYA----------------VDPDSLPGGLEvthVNLN-DGTV 144
|
170
....*....|....*....
gi 556281144 155 MAVRHDADRVCGFQFHPES 173
Cdd:cd01744 145 EGIRHKDLPVFSVQFHPEA 163
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
15-96 |
4.37e-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: 55.32 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 15 YNLADQLRANGHNVVIyrnsVPAQALIERLGTMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGICLGHQAIVEAY 94
Cdd:TIGR01368 184 RNILRRLVKRGCEVTV----VPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAF 259
|
..
gi 556281144 95 GG 96
Cdd:TIGR01368 260 GA 261
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-96 |
4.71e-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: 51.45 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFT---YNLADQLRANGHNVVIYRNSVPAQALIERLGTMDnpVLMLSPGPGTPSEAGCMPELLTRMR----G 76
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDDYD--GLILPGGPGTPDDLARDEALLALLReaaaA 78
|
90 100
....*....|....*....|
gi 556281144 77 KLPIIGICLGHQAIVEAYGG 96
Cdd:cd01653 79 GKPILGICLGAQLLVLGVQF 98
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
16-96 |
5.36e-08 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 54.90 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 16 NLADQLRANGHNVVIyrnsVPAQALIERLGTMDNPVLMLSPGPGTPSEagcMPELLTRMRGK---LPIIGICLGHQAIVE 92
Cdd:PRK12838 180 SILRSLSKRGCKVTV----LPYDTSLEEIKNLNPDGIVLSNGPGDPKE---LQPYLPEIKKLissYPILGICLGHQLIAL 252
|
....
gi 556281144 93 AYGG 96
Cdd:PRK12838 253 ALGA 256
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
4-187 |
6.48e-08 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 55.08 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFTYNLADQLRANGhnvvIYRNSVPAQALIERLGTMDNPVLMLSPGPGTPSEAGC--MPELLTRM--RGKLP 79
Cdd:PLN02347 13 VLILDYGSQYTHLITRRVRELG----VYSLLLSGTASLDRIASLNPRVVILSGGPHSVHVEGAptVPEGFFDYcrERGVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 80 IIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARY--HSLVGSNIPAGLTINA-NFNGMVMA 156
Cdd:PLN02347 89 VLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQTVWmsHGDEAVKLPEGFEVVAkSVQGAVVA 168
|
170 180 190
....*....|....*....|....*....|.
gi 556281144 157 VRHDADRVCGFQFHPESILTTQGARLLEQTL 187
Cdd:PLN02347 169 IENRERRIYGLQYHPEVTHSPKGMETLRHFL 199
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
15-173 |
2.62e-07 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 53.06 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 15 YNLADQLRANGHNVVIYRNSVPAQALIErlgtMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGICLGHQAIVEAY 94
Cdd:PLN02771 252 HNILRRLASYGCKITVVPSTWPASEALK----MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 95 GGYVGQAGEILHGKassiEHDGQAMFAGLANPLPVARYHSLVGSNIPAGLTI-NANFN-GMVMAVRHDADRVCGFQFHPE 172
Cdd:PLN02771 328 GGKTFKMKFGHHGG----NHPVRNNRTGRVEISAQNHNYAVDPASLPEGVEVtHVNLNdGSCAGLAFPALNVMSLQYHPE 403
|
.
gi 556281144 173 S 173
Cdd:PLN02771 404 A 404
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
77-172 |
2.69e-07 |
|
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: 51.09 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIE--HDGQAM--FAGLANPLPVARYHSLVGSNIPAGLTI---NAN 149
Cdd:cd01741 81 GKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTltEAGKADplFAGLPDEFPVFHWHGDTVVELPPGAVLlasSEA 160
|
90 100
....*....|....*....|...
gi 556281144 150 FNGMVMAVRhdaDRVCGFQFHPE 172
Cdd:cd01741 161 CPNQAFRYG---DRALGLQFHPE 180
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-90 |
6.08e-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: 47.58 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 4 ILLLDNIDSFT---YNLADQLRANGHNVVIYRNSVPAQALIERLGTMDnpVLMLSPGPGTPSEAGCMPELLTRMR----G 76
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDDYD--GLILPGGPGTPDDLAWDEALLALLReaaaA 78
|
90
....*....|....
gi 556281144 77 KLPIIGICLGHQAI 90
Cdd:cd03128 79 GKPVLGICLGAQLL 92
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
35-96 |
3.56e-05 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 46.22 E-value: 3.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556281144 35 VPAQALIERLGTMdNP-VLMLSPGPGTPSEAGCMPELLTR-MRGKLPIIGICLGHQAIVEAYGG 96
Cdd:PRK12564 205 VPATTTAEEILAL-NPdGVFLSNGPGDPAALDYAIEMIRElLEKKIPIFGICLGHQLLALALGA 267
|
|
| PRK08136 |
PRK08136 |
glycosyl transferase family protein; Provisional |
210-409 |
7.42e-05 |
|
glycosyl transferase family protein; Provisional
Pssm-ID: 236160 [Multi-domain] Cd Length: 317 Bit Score: 44.85 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 210 AETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLENAAPFPRPDYLFADIVGTGGDGS-NSIN 288
Cdd:PRK08136 17 ARDLDRDTARALYGAMLDGRVPDLELGAILIALRIKGESEAEMLGFLDAMQAHTIPLTPPAGRPMPVVIPSYNGArKQAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 289 ISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGFRHAMPVRQQLK 368
Cdd:PRK08136 97 LTPLLALLLAREGVPVLVHGVSEDPTRVTSAEIFEALGIPPTLHADQAQAKLAEGQPAFIPVGVLCPPLARLLALRWRMG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556281144 369 TRTLFNVLGPLINP--AHPPLALIGVYSPELVLPIAETLRVLG 409
Cdd:PRK08136 177 VRNSAHTLAKLATPfaEGAALRLSSYTHPEYRDRLAEFFSDIG 219
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
15-96 |
3.74e-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: 42.70 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 15 YNLADQLRANGHNVVIyrnsVPAQALIERLGTMdNPV-LMLSPGPGTPSEagcMPELLTRMRG----KLPIIGICLGHQA 89
Cdd:COG0505 188 RNILRELAERGCRVTV----VPATTSAEEILAL-NPDgVFLSNGPGDPAA---LDYAIETIREllgkGIPIFGICLGHQL 259
|
....*..
gi 556281144 90 IVEAYGG 96
Cdd:COG0505 260 LALALGA 266
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
15-96 |
5.14e-04 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 42.48 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 15 YNLADQLRANGHNVVIyrnsVPAQALIERLGTMDNPVLMLSPGPGTPSEAG-CMPELLTRMRGKLPIIGICLGHQAIVEA 93
Cdd:CHL00197 204 YNILRRLKSFGCSITV----VPATSPYQDILSYQPDGILLSNGPGDPSAIHyGIKTVKKLLKYNIPIFGICMGHQILSLA 279
|
...
gi 556281144 94 YGG 96
Cdd:CHL00197 280 LEA 282
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
73-172 |
5.60e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 38.39 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 73 RMRGKLPIIGICLGHQAIVEAYGG--YVGQAGEI--------LHGKASSIEHdgqamfagLANPLPVARYHslvGS--NI 140
Cdd:PRK07053 79 RLAAGLPTLGICLGAQLIARALGArvYPGGQKEIgwapltltDAGRASPLRH--------LGAGTPVLHWH---GDtfDL 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 556281144 141 PAGLTINANfngmVMAVRHDA----DRVCGFQFHPE 172
Cdd:PRK07053 148 PEGATLLAS----TPACRHQAfawgNHVLALQFHPE 179
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
78-172 |
6.50e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 38.40 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556281144 78 LPIIGICLGHQAIVEAYGGYVG------QAGEI---LHGKASSiehdgQAMFAGLANPLPVARYHSLVGSNIPAGLTINA 148
Cdd:PRK09065 89 MPLLGICYGHQLLAHALGGEVGynpagrESGTVtveLHPAAAD-----DPLFAGLPAQFPAHLTHLQSVLRLPPGAVVLA 163
|
90 100
....*....|....*....|....*.
gi 556281144 149 nFNGM--VMAVRHdADRVCGFQFHPE 172
Cdd:PRK09065 164 -RSAQdpHQAFRY-GPHAWGVQFHPE 187
|
|
| |
