|
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: 1061.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 1 MADILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPI 80
Cdd:PRK09522 1 MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGSNIPAGLTINASFEGMVMAVRHD 160
Cdd:PRK09522 81 IGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLEQTLDWALQKLEQTNTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV 240
Cdd:PRK09522 161 ADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 241 SMKVRGESPQEIAGAATALLENAAPFPRPDYPFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSD 320
Cdd:PRK09522 241 SMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 321 LLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
Cdd:PRK09522 321 LLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 401 IAETLRVLGYQRAAVVHSGGMDEVSLHAPTLVAELNNGEVLNYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQGKG 480
Cdd:PRK09522 401 IAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKG 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 515953640 481 EAAHEAAVAANVAMLMRLHGEEDLKANAQKVLDVLRSGAAYDRVTALAARG 531
Cdd:PRK09522 481 DAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG 531
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
4-531 |
1.27e-158 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 462.26 E-value: 1.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVViyRNHVPAQTLIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK14607 2 IILIDNYDSFTYNIYQYIGELGPEEI--EVVRNDEITIEEIEALNPSHIVISPGPGRPEEAGISVEVIRHFSGKVPILGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVG--SNIPAGLTINA-SFEGMVMAVRHD 160
Cdd:PRK14607 80 CLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKGLFRGIPNPTVATRYHSLVVeeASLPECLEVTAkSDDGEIMGIRHK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLEQTLDWALQKLEqtntLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALV 240
Cdd:PRK14607 160 EHPIFGVQFHPESILTEEGKRILKNFLNYQREEID----IKSYLKKLVEGEDLSFEEAEDVMEDITDGNATDAQIAGFLT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 241 SMKVRGESPQEIAGAATALLENAAPFPRPDYPFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSD 320
Cdd:PRK14607 236 ALRMKGETADELAGFASVMREKSRHIPAPSPRTVDTCGTGGDGFGTFNISTTSAFVVAAAGVPVAKHGNRAVSSKSGSAD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 321 LLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLP 400
Cdd:PRK14607 316 VLEALGVKLEMTPEEAASVLRETGFSFLFAPLFHPAMKHAAPARRELGIRTAFNLLGPLTNPARVKYQIVGVFDPSYAEP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 401 IAETLRVLGYQRAAVVHS-GGMDEVSLHAPTLVAELNNGEVLNYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQGK 479
Cdd:PRK14607 396 LAQALQRLGTERAMVVSGiDGYDEISTCGPTQILELEDGEIVTYTFDPEELGLKRVDPEELKGGDPQENYRLAEDVLKGE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953640 480 GEAAHEAAVAANVAMLMRLHGEED-LKANAQKVLDVLRSGAAY---DRVTALAARG 531
Cdd:PRK14607 476 PRRPQRDAVALNAGAALYLVGEADsIKEGVGKALDLIDDGRAYkklEEVMDLSKTL 531
|
|
| trpD |
PRK00188 |
anthranilate phosphoribosyltransferase; Provisional |
198-529 |
3.77e-154 |
|
anthranilate phosphoribosyltransferase; Provisional
Pssm-ID: 234682 [Multi-domain] Cd Length: 339 Bit Score: 443.37 E-value: 3.77e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 198 NTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKVRGESPQEIAGAATALLENAAPFPRPDYpFADIV 277
Cdd:PRK00188 1 MTMKELLEKLVEGEDLSEEEAEELMDAIMSGEATPAQIAAFLTALRVKGETVDEIAGAARAMREHAVPVPDPDD-AVDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 278 GTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSDLLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTGF 357
Cdd:PRK00188 80 GTGGDGANTFNISTAAAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEVGIGFLFAPLYHPAM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 358 RHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVH-SGGMDEVSLHAPTLVAELN 436
Cdd:PRK00188 160 KHVAPVRKELGIRTIFNLLGPLTNPARPKRQLIGVYSPDLLEPMAEVLKRLGSKRALVVHgSDGLDEISLTGPTTVAELK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 437 NGEVLNYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHG-EEDLKANAQKVLDVL 515
Cdd:PRK00188 240 DGEIREYTLTPEDFGLPRAPLEDLRGGDPEENAAILRAVLQGKGPGAARDAVLLNAAAALYVAGkADDLKEGVELAREAI 319
|
330
....*....|....
gi 515953640 516 RSGAAYDRVTALAA 529
Cdd:PRK00188 320 DSGAALAKLEELVA 333
|
|
| trpD |
TIGR01245 |
anthranilate phosphoribosyltransferase; In many widely different species, including E. coli, ... |
204-529 |
1.10e-144 |
|
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: 418.98 E-value: 1.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 204 LEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKVRGESPQEIAGAATALLENAAPFP-RPDYPFADIVGTGGD 282
Cdd:TIGR01245 1 LEKLIDGKDLSRDEAEQLMKEIMSGEASPAQIAAILTALRIKGETPEEITGFAKAMREHAVKVPgRPPEDLVDIVGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 283 GSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSDLLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTGFRHAMP 362
Cdd:TIGR01245 81 GANTINISTASAFVAAAAGVKVAKHGNRSVSSKSGSADVLEALGVNLDLGPEKVARSLEETGIGFLFAPLYHPAMKHVAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 363 VRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTLVAELNNGEVL 441
Cdd:TIGR01245 161 VRRELGVRTVFNLLGPLTNPARPKYQVIGVYDPDLVEVMAEALKNLGVKRALVVHGdDGLDEISLTGPTTVAELKDGEIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 442 NYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHG-EEDLKANAQKVLDVLRSGAA 520
Cdd:TIGR01245 241 EYTLDPEDFGLPRAPLEELAGGSPEENAEILRDILRGKGSGAKRDIVALNAAAALYVAGrASDLKEGVELALEAIDSGAA 320
|
....*....
gi 515953640 521 YDRVTALAA 529
Cdd:TIGR01245 321 AEKLEELVA 329
|
|
| TrpD |
COG0547 |
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ... |
199-524 |
1.76e-136 |
|
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: 397.91 E-value: 1.76e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 199 TLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKVRGESPQEIAGAATALLENAAPFPRPDYPFADIVG 278
Cdd:COG0547 1 MMKELLKKLAEGKDLTREEAREAMRQIMSGEATPAQIGAFLTALRMKGETVEEIAGFADAMRELAVPVPLPDGDVVDIVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 279 TGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSDLLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTGFR 358
Cdd:COG0547 81 TGGDGANTFNISTAAAFVAAAAGVPVAKHGNRSVSSKSGSADVLEALGVNLDLSPEQVARCLEEAGIGFLFAPLFHPAMK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 359 HAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHS-GGMDEVSLHAPTLVAELNN 437
Cdd:COG0547 161 HVAPVRKELGVRTIFNLLGPLTNPAGPKRQLLGVYHPELVEPLAEVLQLLGVKRALVVHGlDGLDEISLTGPTKVAELRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 438 GEVLNYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHGEEDLKANAQKVLDVLRS 517
Cdd:COG0547 241 GEIEEYTLDPEDFGLPRAPLEDLRGGDAEENAEILRAVLAGEGGPARDAVLLNAAAALYVAGKADSLAEGVELAREAIDS 320
|
....*..
gi 515953640 518 GAAYDRV 524
Cdd:COG0547 321 GAALAKL 327
|
|
| Glycos_transf_3 |
pfam00591 |
Glycosyl transferase family, a/b domain; This family includes anthranilate ... |
270-521 |
2.67e-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: 325.78 E-value: 2.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 270 DYPFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSDLLAAFGINLDMNAERSREALDDLGVCFLF 349
Cdd:pfam00591 1 LGDLVDIVGTGGDGDNTFNISTAAAIVAAACGVKVAKHGNRSVSSKSGSADVLEALGINLDLTPEQVRKLLDEVGVGFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 350 APKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAP 429
Cdd:pfam00591 81 APNYHPAMKHVAPVRRELGIRTVFNLLGPLINPARVKRQVLGVYSKELAEGLAEVLKDLGRERAAVVHGDGLDEASLLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 430 TLVAELNNGEVLNYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHGE-EDLKANA 508
Cdd:pfam00591 161 TTVAELKDGEITEYTLTPEDFGLGRATLEALEGGSPKENADILKGVLGGKGSAAHRDLVALNAGAALYLAGKaDSLKEGV 240
|
250
....*....|...
gi 515953640 509 QKVLDVLRSGAAY 521
Cdd:pfam00591 241 AKALEVIDSGKAL 253
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
3-191 |
8.15e-109 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 322.08 E-value: 8.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 3 DILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLAtmqNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIG 82
Cdd:PRK05670 1 MILLIDNYDSFTYNLVQYLGELGAEVVVYRNDEITLEEIEALN---PDAIVLSPGPGTPAEAGISLELIREFAGKVPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVG--SNIPAGLTINA-SFEGMVMAVRH 159
Cdd:PRK05670 78 VCLGHQAIGEAFGGKVVRAKEIMHGKTSPIEHDGSGIFAGLPNPFTVTRYHSLVVdrESLPDCLEVTAwTDDGEIMGVRH 157
|
170 180 190
....*....|....*....|....*....|..
gi 515953640 160 DADRVCGMQFHPESILTSNGARLLEQTLDWAL 191
Cdd:PRK05670 158 KELPIYGVQFHPESILTEHGHKLLENFLELAR 189
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
4-190 |
1.38e-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: 283.08 E-value: 1.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAqtlIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:COG0512 1 ILLIDNYDSFTYNLVQYLGELGAEVVVVRNDEIT---LEEIEALAPDGIVLSPGPGTPEEAGISLEVIRAFAGKIPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGS--NIPAGLTINASFE-GMVMAVRHD 160
Cdd:COG0512 78 CLGHQAIGEAFGGKVVRAPEPMHGKTSPITHDGSGLFAGLPNPFTATRYHSLVVDreTLPDELEVTAWTEdGEIMGIRHR 157
|
170 180 190
....*....|....*....|....*....|
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLEQTLDWA 190
Cdd:COG0512 158 ELPIEGVQFHPESILTEHGHQLLANFLELA 187
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
4-187 |
4.60e-81 |
|
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: 250.91 E-value: 4.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRlatMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:cd01743 1 ILLIDNYDSFTYNLVQYLRELGAEVVVVRNDEITLEELEL---LNPDAIVISPGPGHPEDAGISLEIIRALAGKVPILGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGSNIPAG---LTINASFEGMVMAVRHD 160
Cdd:cd01743 78 CLGHQAIAEAFGGKVVRAPEPMHGKTSEIHHDGSGLFKGLPQPFTVGRYHSLVVDPDPLPdllEVTASTEDGVIMALRHR 157
|
170 180
....*....|....*....|....*..
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLEQTL 187
Cdd:cd01743 158 DLPIYGVQFHPESILTEYGLRLLENFL 184
|
|
| PLN02641 |
PLN02641 |
anthranilate phosphoribosyltransferase |
197-478 |
1.67e-79 |
|
anthranilate phosphoribosyltransferase
Pssm-ID: 215345 [Multi-domain] Cd Length: 343 Bit Score: 252.73 E-value: 1.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 197 TNTLQPILEKLYQAQTLSQQESHQLFSAVVRGElKPEQLAAALVSMKVRGESPQEIAGAATALLENAAPFPRPDyPFADI 276
Cdd:PLN02641 1 IASFRQLIESLIQGTDLTEEEAEAALDFLLDDA-DEAQISAFLVLLRAKGETFEEIAGLARAMIKRARKVDGLV-DAVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 277 VGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSRSGSSDLLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTG 356
Cdd:PLN02641 79 VGTGGDGANTVNISTGSSILAAACGAKVAKQGNRSSSSACGSADVLEALGVAIDLGPEGVKRCVEEVGIGFMMAPKYHPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 357 FRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTLVAELN 436
Cdd:PLN02641 159 MKIVAPVRKKLKVKTVFNILGPMLNPARVPHAVVGVYHESLVEKMAKALQRFGMKRALVVHSEGLDEMSPLGPGDVLEVT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 515953640 437 NGEVLNYQLEAADFGLTPYHQDALAGGTPEENRDILTRLLQG 478
Cdd:PLN02641 239 PEKIEEFSFDPLDFGIPRCTLEDLRGGDPDYNAKVLRDVLSG 280
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
4-188 |
1.69e-57 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 190.02 E-value: 1.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHvpaQTLIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK07649 2 ILMIDNYDSFTFNLVQFLGELGQELVVKRND---EVTISDIENMKPDFLMISPGPCSPNEAGISMEVIRYFAGKIPIFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLV--GSNIPAGLTINASF-EGMVMAVRHD 160
Cdd:PRK07649 79 CLGHQSIAQVFGGEVVRAERLMHGKTSLMHHDGKTIFSDIPNPFTATRYHSLIvkKETLPDCLEVTSWTeEGEIMAIRHK 158
|
170 180
....*....|....*....|....*...
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLEQTLD 188
Cdd:PRK07649 159 TLPIEGVQFHPESIMTSHGKELLQNFIR 186
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
5-184 |
2.85e-56 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 186.67 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 5 LLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLATmqnpVLMLSPGPGAPSEAGCMPELLTRMRG-KLPIIGI 83
Cdd:pfam00117 1 LLIDNGDSFTYNLARALRELGVEVTVVPNDTPAEEILEENPD----GIILSGGPGSPGAAGGAIEAIREARElKIPILGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAG-EILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGSN--IPAGLTINA--SFEGMVMAVR 158
Cdd:pfam00117 77 CLGHQLLALAFGGKVVKAKkFGHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYAVDPdtLPDGLEVTAtsENDGTIMGIR 156
|
170 180
....*....|....*....|....*.
gi 515953640 159 HDADRVCGMQFHPESILTSNGARLLE 184
Cdd:pfam00117 157 HKKLPIFGVQFHPESILTPHGPEILF 182
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
4-183 |
1.20e-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: 184.99 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLATMqnpVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:TIGR00566 2 VLMIDNYDSFTYNLVQYFCELGAEVVVKRNDSLTLQEIEALLPL---LIVISPGPCTPNEAGISLEAIRHFAGKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLV--GSNIPAGLTINASFE--GMVMAVRH 159
Cdd:TIGR00566 79 CLGHQAMGQAFGGDVVRANTVMHGKTSEIEHNGAGIFRGLFNPLTATRYHSLVvePETLPTCFPVTAWEEenIEIMAIRH 158
|
170 180
....*....|....*....|....
gi 515953640 160 DADRVCGMQFHPESILTSNGARLL 183
Cdd:TIGR00566 159 RDLPLEGVQFHPESILSEQGHQLL 182
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
4-183 |
6.84e-50 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 170.62 E-value: 6.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLATMQNPVLmLSPGPGAPSEAG-CMPELLTRMRGKLPIIG 82
Cdd:PRK07765 3 ILVVDNYDSFVFNLVQYLGQLGVEAEVWRNDDPRLADEAAVAAQFDGVL-LSPGPGTPERAGaSIDMVRACAAAGTPLLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSL--VGSNIPAGLTINASFE-GMVMAVRH 159
Cdd:PRK07765 82 VCLGHQAIGVAFGATVDRAPELLHGKTSSVHHTGVGVLAGLPDPFTATRYHSLtiLPETLPAELEVTARTDsGVIMAVRH 161
|
170 180
....*....|....*....|....
gi 515953640 160 DADRVCGMQFHPESILTSNGARLL 183
Cdd:PRK07765 162 RELPIHGVQFHPESVLTEGGHRML 185
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
4-188 |
2.43e-48 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 165.67 E-value: 2.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLatmqNPV-LMLSPGPGAPSEAGCMPELLTRMRGKLPIIG 82
Cdd:CHL00101 2 ILIIDNYDSFTYNLVQSLGELNSDVLVCRNDEIDLSKIKNL----NIRhIIISPGPGHPRDSGISLDVISSYAPYIPILG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLV--GSNIPAGLTINA-SFEGMVMAVRH 159
Cdd:CHL00101 78 VCLGHQSIGYLFGGKIIKAPKPMHGKTSKIYHNHDDLFQGLPNPFTATRYHSLIidPLNLPSPLEITAwTEDGLIMACRH 157
|
170 180 190
....*....|....*....|....*....|
gi 515953640 160 DADRVC-GMQFHPESILTSNGARLLEQTLD 188
Cdd:CHL00101 158 KKYKMLrGIQFHPESLLTTHGQQILRNFLS 187
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
4-187 |
2.00e-47 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 163.16 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLATMQnpvLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK08007 2 ILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQK---IVISPGPCTPDEAGISLDVIRHYAGRLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLV--GSNIPAGLTINA-SFEGMVMAVRHD 160
Cdd:PRK08007 79 CLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVvePDSLPACFEVTAwSETREIMGIRHR 158
|
170 180
....*....|....*....|....*..
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLEQTL 187
Cdd:PRK08007 159 QWDLEGVQFHPESILSEQGHQLLANFL 185
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
4-192 |
6.51e-46 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 171.25 E-value: 6.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRnHVPAQTLIDRlatmQNP-VLMLSPGPGAPSEAGCmPELLTRMRGK-LPII 81
Cdd:PRK13566 529 VLLVDHEDSFVHTLANYFRQTGAEVTTVR-YGFAEEMLDR----VNPdLVVLSPGPGRPSDFDC-KATIDAALARnLPIF 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 82 GICLGHQAIVEAYGGYVGQAGEILHGKASSIE-HDGQAMFAGLPNPLPVARYHSLVG--SNIPAGLTINASFE-GMVMAV 157
Cdd:PRK13566 603 GVCLGLQAIVEAFGGELGQLAYPMHGKPSRIRvRGPGRLFSGLPEEFTVGRYHSLFAdpETLPDELLVTAETEdGVIMAI 682
|
170 180 190
....*....|....*....|....*....|....*...
gi 515953640 158 RHDADRVCGMQFHPESILT---SNGARLLEQTLDWALQ 192
Cdd:PRK13566 683 EHKTLPVAAVQFHPESIMTlggDVGLRIIENVVRLLAG 720
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
4-187 |
2.00e-45 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 158.10 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRLATMQnpvLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK06774 2 LLLIDNYDSFTYNLYQYFCELGTEVMVKRNDELQLTDIEQLAPSH---LVISPGPCTPNEAGISLAVIRHFADKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLV--GSNIPAGLTINASFE-----GMVMA 156
Cdd:PRK06774 79 CLGHQALGQAFGARVVRARQVMHGKTSAICHSGQGVFRGLNQPLTVTRYHSLViaADSLPGCFELTAWSErggemDEIMG 158
|
170 180 190
....*....|....*....|....*....|.
gi 515953640 157 VRHDADRVCGMQFHPESILTSNGARLLEQTL 187
Cdd:PRK06774 159 IRHRTLPLEGVQFHPESILSEQGHQLLDNFL 189
|
|
| Anth_synII_Halo |
NF041322 |
anthranilate synthase component II; |
8-188 |
1.18e-44 |
|
anthranilate synthase component II;
Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 155.96 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 8 DNIDSFTYNLADQL--RANGHNVVIYRNHVPaqtlIDRLATMQNPVLMLSPGPGAPS---EAGCMPELLTRMRGKLPIIG 82
Cdd:NF041322 3 DNFDSFTYNLVEYVseQREHAETTVLKNTAS----LAEVRAVDPDAIVISPGPGHPKndrDVGVTADVLRELSPEVPTLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 83 ICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGSNIPAGLTINAS----FEGMVMAVR 158
Cdd:NF041322 79 VCLGLEAAVYAYGGTVGRAPEPVHGKAFPVDHDGEGVFAGLEQGFQAGRYHSLVATEVPDCFEVTATtdhdGEELVMGIR 158
|
170 180 190
....*....|....*....|....*....|
gi 515953640 159 HDADRVCGMQFHPESILTSNGARLLEQTLD 188
Cdd:NF041322 159 HREHPIECVQFHPESVLTGVGHDVIENFLA 188
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
4-183 |
4.92e-43 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 151.57 E-value: 4.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHvpaQTLIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PRK08857 2 LLMIDNYDSFTYNLYQYFCELGAQVKVVRND---EIDIDGIEALNPTHLVISPGPCTPNEAGISLQAIEHFAGKLPILGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGSN--IPAGLTINASFEGM------VM 155
Cdd:PRK08857 79 CLGHQAIAQVFGGQVVRARQVMHGKTSPIRHTGRSVFKGLNNPLTVTRYHSLVVKNdtLPECFELTAWTELEdgsmdeIM 158
|
170 180
....*....|....*....|....*...
gi 515953640 156 AVRHDADRVCGMQFHPESILTSNGARLL 183
Cdd:PRK08857 159 GFQHKTLPIEAVQFHPESIKTEQGHQLL 186
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
4-184 |
1.02e-41 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 149.18 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHvpaQTLIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGI 83
Cdd:PLN02335 21 IIVIDNYDSFTYNLCQYMGELGCHFEVYRND---ELTVEELKRKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQAGE-ILHGKASSIEHD---GQAMFAGLPNPLPVARYHSLVGS--NIPA-GLTINASFE-GMVM 155
Cdd:PLN02335 98 CMGLQCIGEAFGGKIVRSPFgVMHGKSSPVHYDekgEEGLFSGLPNPFTAGRYHSLVIEkdTFPSdELEVTAWTEdGLIM 177
|
170 180 190
....*....|....*....|....*....|
gi 515953640 156 AVRHDADR-VCGMQFHPESILTSNGARLLE 184
Cdd:PLN02335 178 AARHRKYKhIQGVQFHPESIITTEGKTIVR 207
|
|
| PRK05637 |
PRK05637 |
anthranilate synthase component II; Provisional |
1-192 |
1.44e-40 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 145.76 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 1 MADILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDrlatMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPI 80
Cdd:PRK05637 1 MTHVVLIDNHDSFVYNLVDAFAVAGYKCTVFRNTVPVEEILA----ANPDLICLSPGPGHPRDAGNMMALIDRTLGQIPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 81 IGICLGHQAIVEAYGGYVGQAGEIlHGKASSIEHDGQA----MFAGLP------NP------LPVARYHSLVGSNIPAGL 144
Cdd:PRK05637 77 LGICLGFQALLEHHGGKVEPCGPV-HGTTDNMILTDAGvqspVFAGLAtdvepdHPeipgrkVPIARYHSLGCVVAPDGM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953640 145 TINASFEGMV----MAVRHDADRVCGMQFHPESILTSNGARLLEQTLDWALQ 192
Cdd:PRK05637 156 ESLGTCSSEIgpviMAAETTDGKAIGLQFHPESVLSPTGPIILSRCVEQLLA 207
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
1-187 |
2.55e-26 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 105.97 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 1 MADILLLDNIDSFTYNLADQLRANGhnvviyrnhVPAQTL----IDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRG 76
Cdd:PRK06895 1 ATKLLIINNHDSFTFNLVDLIRKLG---------VPMQVVnvedLDLDEVENFSHILISPGPDVPRAYPQLFAMLERYHQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASS-IEHDGQAMFAGLPNPLPVARYHSLVGS--NIPAGLTINASF-EG 152
Cdd:PRK06895 72 HKSILGVCLGHQTLCEFFGGELYNLNNVRHGQQRPlKVRSNSPLFDGLPEEFNIGLYHSWAVSeeNFPTPLEITAVCdEN 151
|
170 180 190
....*....|....*....|....*....|....*
gi 515953640 153 MVMAVRHDADRVCGMQFHPESILTSNGARLLEQTL 187
Cdd:PRK06895 152 VVMAMQHKTLPIYGVQFHPESYISEFGEQILRNWL 186
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
4-184 |
4.26e-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: 93.92 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGhnvvIYRNHVPAQTLIDRLATMQNPVLMLSPGPGAPSEAGCmPELLTRM-RGKLPIIG 82
Cdd:TIGR00888 1 ILVLDFGSQYTQLIARRLRELG----VYSELVPNTTPLEEIREKNPKGIILSGGPSSVYAENA-PRADEKIfELGVPVLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 83 ICLGHQAIVEAYGGYVGQAGEILHGKAS-SIEHDGqAMFAGLPNPLPVARYHSLVGSNIPAGLTINASFEGM-VMAVRHD 160
Cdd:TIGR00888 76 ICYGMQLMAKQLGGEVGRAEKREYGKAElEILDED-DLFRGLPDESTVWMSHGDKVKELPEGFKVLATSDNCpVAAMAHE 154
|
170 180
....*....|....*....|....
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLE 184
Cdd:TIGR00888 155 EKPIYGVQFHPEVTHTEYGNELLE 178
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
5-184 |
4.79e-21 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 97.23 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 5 LLLDNIDSFTYNLADQLRA-NGHNVVIYRN-----HVPAQTLIDRLAtMQNPVLmlSPGPGAPSEA---GCMPELLTRMR 75
Cdd:PLN02889 85 LLIDNYDSYTYNIYQELSIvNGVPPVVVRNdewtwEEVYHYLYEEKA-FDNIVI--SPGPGSPTCPadiGICLRLLLECR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 76 gKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLP----NPLPVARYHSLVGSN-------IPAGL 144
Cdd:PLN02889 162 -DIPILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHNGCRLFDDIPsgrnSGFKVVRYHSLVIDAeslpkelVPIAW 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 145 TI--------------------------NASF------------------EGM-----VMAVRHDADRVCGMQFHPESIL 175
Cdd:PLN02889 241 TSssdtlsflesqksglvpdayesqigqSGSSdpfssklkngtswpsshsERMqngkiLMGIMHSTRPHYGLQFHPESIA 320
|
....*....
gi 515953640 176 TSNGARLLE 184
Cdd:PLN02889 321 TCYGRQIFK 329
|
|
| PabB-fungal |
TIGR01823 |
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
4-197 |
2.30e-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: 91.89 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRA---NGHNVVIYRNHVPAQTLIDRLatMQNPVLMLSPGPGAPSEA---GCMPELLT-RMRG 76
Cdd:TIGR01823 8 VLFIDSYDSFTYNVVRLLEQqtdISVHVTTVHSDTFQDQLLELL--PLFDAIVVGPGPGNPNNAqdmGIISELWElANLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNpLPVARYHSLVGSNIP-----AGLTINASFE 151
Cdd:TIGR01823 86 EVPVLGICLGFQSLCLAQGADISRLPTPKHGQVYEMHTNDAAIFCGLFS-VKSTRYHSLYANPEGidtllPLCLTEDEEG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515953640 152 GMVMAVRHDADRVCGMQFHPESILTSNGA-RLLEQTLDWALQKLEQT 197
Cdd:TIGR01823 165 IILMSAQTKKKPWFGVQYHPESCCSELGSgKLVSNFLKLAFINNVKT 211
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
4-184 |
1.95e-17 |
|
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: 80.27 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDRlatmqNPV-LMLSPGP------GAPSeagCMPELLTrmrG 76
Cdd:cd01742 1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEEIKLK-----NPKgIILSGGPssvyeeDAPR---VDPEIFE---L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARYHSLVGSNIPAGLTINASFEG-MVM 155
Cdd:cd01742 70 GVPVLGICYGMQLIAKALGGKVERGDKREYGKAEIEIDDSSPLFEGLPDEQTVWMSHGDEVVKLPEGFKVIASSDNcPVA 149
|
170 180
....*....|....*....|....*....
gi 515953640 156 AVRHDADRVCGMQFHPESILTSNGARLLE 184
Cdd:cd01742 150 AIANEEKKIYGVQFHPEVTHTEKGKEILK 178
|
|
| PRK09071 |
PRK09071 |
glycosyl transferase family protein; |
210-447 |
7.45e-17 |
|
glycosyl transferase family protein;
Pssm-ID: 181637 [Multi-domain] Cd Length: 323 Bit Score: 81.50 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 210 AQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKVRGESPQEIAGAATALLEnAAPFPRPDypfADIvgtggDGSnsini 289
Cdd:PRK09071 18 RRSLTREEARQAMGMILDGEVEDDQLGAFLMLLRVKEETAEELAGFVEAIRE-RLQAPPLA---VDL-----DWP----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 290 STA-----------SAFVAAACGLKVAKHGNRSVSSRSGSS-DLLAAFGINLDMNAERSREALDDLGVCFL----FAPKY 353
Cdd:PRK09071 84 SYAgkrrhlpwyllAAKLLAQNGYRVLLHGGGGHTAGRLYTeQLLEALGIPIARSWQEAEQALEEHNIAYLpledFAPQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 354 HTgfrhAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVH-SGGMDEVSLHAPTLV 432
Cdd:PRK09071 164 QR----MIDLRNTLGLRSPINTLARLLNPLNAKASLQGIFHPGYQQLHREAARLLGDQNALVFKgEGGESERNPDVSTTL 239
|
250
....*....|....*
gi 515953640 433 AELNNGEVLNYQLEA 447
Cdd:PRK09071 240 YGSRNGEAWDEEWPA 254
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
4-172 |
2.48e-16 |
|
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: 78.06 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNID---SFTYNLADQLRANGHNVVIYRnhVPAQTLIDRLATMQNP-VLMLSPGP-GAPSEAGCMPELLTRMRG-- 76
Cdd:COG0518 2 ILILDHDPfggQYPGLIARRLREAGIELDVLR--VYAGEILPYDPDLEDPdGLILSGGPmSVYDEDPWLEDEPALIREaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 77 --KLPIIGICLGHQAIVEAYGGYVGQAG--EIlhGKAsSIE-HDGQAMFAGLPNPLPVARYHSLVGSNIPAGLTINASFE 151
Cdd:COG0518 80 elGKPVLGICYGAQLLAHALGGKVEPGPgrEI--GWA-PVElTEADPLFAGLPDEFTVWMSHGDTVTELPEGAEVLASSD 156
|
170 180
....*....|....*....|..
gi 515953640 152 G-MVMAVRHDaDRVCGMQFHPE 172
Cdd:COG0518 157 NcPNQAFRYG-RRVYGVQFHPE 177
|
|
| Glycos_trans_3N |
pfam02885 |
Glycosyl transferase family, helical bundle domain; This family includes anthranilate ... |
201-263 |
7.73e-16 |
|
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: 71.64 E-value: 7.73e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953640 201 QPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKVRGESPQEIAGAATALLENA 263
Cdd:pfam02885 1 KELIKKLRDGEDLTREEARAAMDGIMSGEATDAQIAAFLMALRMKGETAEEIAGLARAMRESG 63
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
4-184 |
8.25e-15 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 72.58 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGHNVVIYRNHVPAQTLIDrlatmQNPVLMLSPGPGApSEAGCMPELLTRMrgKLPIIGI 83
Cdd:PRK00758 2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEIKA-----FEDGLILSGGPDI-ERAGNCPEYLKEL--DVPILGI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 84 CLGHQAIVEAYGGYVGQA--GEILHGKASSIEHDGqaMFAGLPNPLPVARYHSLVGSNIPAGLTINASFEGM-VMAVRHD 160
Cdd:PRK00758 74 CLGHQLIAKAFGGEVGRGeyGEYALVEVEILDEDD--ILKGLPPEIRVWASHADEVKELPDGFEILARSDICeVEAMKHK 151
|
170 180
....*....|....*....|....
gi 515953640 161 ADRVCGMQFHPESILTSNGARLLE 184
Cdd:PRK00758 152 EKPIYGVQFHPEVAHTEYGEEIFK 175
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
35-184 |
2.54e-14 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 75.47 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 35 VPAQTLIDRLATMqNPV-LMLSPGP------GAPSeagCMPELLtrmRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHG 107
Cdd:PRK00074 33 VPYDISAEEIRAF-NPKgIILSGGPasvyeeGAPR---ADPEIF---ELGVPVLGICYGMQLMAHQLGGKVERAGKREYG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953640 108 KASSIEHDGQAMFAGLPNPLPVARYHSLVGSNIPAGLTINASFEGM-VMAVRHDADRVCGMQFHPESILTSNGARLLE 184
Cdd:PRK00074 106 RAELEVDNDSPLFKGLPEEQDVWMSHGDKVTELPEGFKVIASTENCpIAAIANEERKFYGVQFHPEVTHTPQGKKLLE 183
|
|
| PLN02347 |
PLN02347 |
GMP synthetase |
4-192 |
6.02e-10 |
|
GMP synthetase
Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 61.62 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFTYNLADQLRANGhnvvIYRNHVPAQTLIDRLATMQNPVLMLSPGP------GAPSeagcMPELLTRM--R 75
Cdd:PLN02347 13 VLILDYGSQYTHLITRRVRELG----VYSLLLSGTASLDRIASLNPRVVILSGGPhsvhveGAPT----VPEGFFDYcrE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 76 GKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLPNPLPVARY--HSLVGSNIPAGLTINA-SFEG 152
Cdd:PLN02347 85 RGVPVLGICYGMQLIVQKLGGEVKPGEKQEYGRMEIRVVCGSQLFGDLPSGETQTVWmsHGDEAVKLPEGFEVVAkSVQG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515953640 153 MVMAVRHDADRVCGMQFHPESILTSNGARLLEQTL--------DWALQ 192
Cdd:PLN02347 165 AVVAIENRERRIYGLQYHPEVTHSPKGMETLRHFLfdvcgvtaDWKMQ 212
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
15-173 |
3.34e-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: 56.35 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 15 YNLADQLRANGHNVVIyrnhVPAQTLIDRLATMQNPVLMLSPGPGAPSEAgcmPELLTRMR----GKLPIIGICLGHQAI 90
Cdd:cd01744 10 HNILRELLKRGCEVTV----VPYNTDAEEILKLDPDGIFLSNGPGDPALL---DEAIKTVRkllgKKIPIFGICLGHQLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 91 VEAYG--------GYVGQ---AGEILHGKA--SSIEHdGQAMFA-GLPNPLPVarYHslvgsnipagltINA---SFEGM 153
Cdd:cd01744 83 ALALGaktykmkfGHRGSnhpVKDLITGRVyiTSQNH-GYAVDPdSLPGGLEV--TH------------VNLndgTVEGI 147
|
170 180
....*....|....*....|
gi 515953640 154 vmavRHDADRVCGMQFHPES 173
Cdd:cd01744 148 ----RHKDLPVFSVQFHPEA 163
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
15-96 |
6.12e-09 |
|
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: 57.64 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 15 YNLADQLRANGHNVVIyrnhVPAQTLIDRLATMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGICLGHQAIVEAY 94
Cdd:TIGR01368 184 RNILRRLVKRGCEVTV----VPYDTDAEEIKKYNPDGIFLSNGPGDPAAVEPAIETIRKLLEKIPIFGICLGHQLLALAF 259
|
..
gi 515953640 95 GG 96
Cdd:TIGR01368 260 GA 261
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
77-178 |
8.23e-09 |
|
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: 55.33 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 77 KLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIE--HDGQAM--FAGLPNPLPVARYHSLVGSNIPAGLTINASFEG 152
Cdd:cd01741 81 GKPVLGICLGHQLLARALGGKVGRNPKGWEIGWFPVTltEAGKADplFAGLPDEFPVFHWHGDTVVELPPGAVLLASSEA 160
|
90 100
....*....|....*....|....*....
gi 515953640 153 ---MVMAVRhdaDRVCGMQFHPESILTSN 178
Cdd:cd01741 161 cpnQAFRYG---DRALGLQFHPEERLLRN 186
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
16-96 |
3.20e-08 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 55.67 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 16 NLADQLRANGHNVVIyrnhVPAQTLIDRLATMQNPVLMLSPGPGAPSEagcMPELLTRMRGK---LPIIGICLGHQAIVE 92
Cdd:PRK12838 180 SILRSLSKRGCKVTV----LPYDTSLEEIKNLNPDGIVLSNGPGDPKE---LQPYLPEIKKLissYPILGICLGHQLIAL 252
|
....
gi 515953640 93 AYGG 96
Cdd:PRK12838 253 ALGA 256
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-96 |
2.34e-07 |
|
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: 49.52 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFT---YNLADQLRANGHNVVIYRNHVPAQTLIDRLATMQnpVLMLSPGPGAPSEAGCMPELLTRMR----G 76
Cdd:cd01653 1 VAVLLFPGFEElelASPLDALREAGAEVDVVSPDGGPVESDVDLDDYD--GLILPGGPGTPDDLARDEALLALLReaaaA 78
|
90 100
....*....|....*....|
gi 515953640 77 KLPIIGICLGHQAIVEAYGG 96
Cdd:cd01653 79 GKPILGICLGAQLLVLGVQF 98
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
15-173 |
2.45e-06 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 49.98 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 15 YNLADQLRANGHNVVIYRNHVPAQTLIDrlatMQNPVLMLSPGPGAPSEAGCMPELLTRMRGKLPIIGICLGHQAIVEAY 94
Cdd:PLN02771 252 HNILRRLASYGCKITVVPSTWPASEALK----MKPDGVLFSNGPGDPSAVPYAVETVKELLGKVPVFGICMGHQLLGQAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 95 GGYV-----GQAG------EILHGKA--SSIEHDGQAMFAGLPNPLPVARYHSLVGSNipAGLtinaSFEGMvmavrhda 161
Cdd:PLN02771 328 GGKTfkmkfGHHGgnhpvrNNRTGRVeiSAQNHNYAVDPASLPEGVEVTHVNLNDGSC--AGL----AFPAL-------- 393
|
170
....*....|..
gi 515953640 162 dRVCGMQFHPES 173
Cdd:PLN02771 394 -NVMSLQYHPEA 404
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-90 |
2.68e-06 |
|
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: 45.65 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 4 ILLLDNIDSFT---YNLADQLRANGHNVVIYRNHVPAQTLIDRLAtmQNPVLMLSPGPGAPSEAGCMPELLTRMR----G 76
Cdd:cd03128 1 VAVLLFGGSEElelASPLDALREAGAEVDVVSPDGGPVESDVDLD--DYDGLILPGGPGTPDDLAWDEALLALLReaaaA 78
|
90
....*....|....
gi 515953640 77 KLPIIGICLGHQAI 90
Cdd:cd03128 79 GKPVLGICLGAQLL 92
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
35-96 |
3.97e-06 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 48.92 E-value: 3.97e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515953640 35 VPAQTLIDRLATMqNP-VLMLSPGPGAPSEAGCMPELLTR-MRGKLPIIGICLGHQAIVEAYGG 96
Cdd:PRK12564 205 VPATTTAEEILAL-NPdGVFLSNGPGDPAALDYAIEMIRElLEKKIPIFGICLGHQLLALALGA 267
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
15-96 |
6.75e-05 |
|
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: 45.01 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 15 YNLADQLRANGHNVVIyrnhVPAQTLIDRLATMqNPV-LMLSPGPGAPSEagcMPELLTRMRG----KLPIIGICLGHQA 89
Cdd:COG0505 188 RNILRELAERGCRVTV----VPATTSAEEILAL-NPDgVFLSNGPGDPAA---LDYAIETIREllgkGIPIFGICLGHQL 259
|
....*..
gi 515953640 90 IVEAYGG 96
Cdd:COG0505 260 LALALGA 266
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
15-96 |
8.63e-05 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 44.79 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 15 YNLADQLRANGHNVVIyrnhVPAQTLIDRLATMQNPVLMLSPGPGAPSEAG-CMPELLTRMRGKLPIIGICLGHQAIVEA 93
Cdd:CHL00197 204 YNILRRLKSFGCSITV----VPATSPYQDILSYQPDGILLSNGPGDPSAIHyGIKTVKKLLKYNIPIFGICMGHQILSLA 279
|
...
gi 515953640 94 YGG 96
Cdd:CHL00197 280 LEA 282
|
|
| PRK07053 |
PRK07053 |
glutamine amidotransferase; Provisional |
73-172 |
4.90e-04 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 235919 [Multi-domain] Cd Length: 234 Bit Score: 41.85 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 73 RMRGKLPIIGICLGHQAIVEAYGG--YVGQAGEI--------LHGKASSIEHdgqamfagLPNPLPVARYHslvGS--NI 140
Cdd:PRK07053 79 RLAAGLPTLGICLGAQLIARALGArvYPGGQKEIgwapltltDAGRASPLRH--------LGAGTPVLHWH---GDtfDL 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 515953640 141 PAGLTINASFEgmvmAVRHDA----DRVCGMQFHPE 172
Cdd:PRK07053 148 PEGATLLASTP----ACRHQAfawgNHVLALQFHPE 179
|
|
| PRK08136 |
PRK08136 |
glycosyl transferase family protein; Provisional |
210-409 |
6.71e-04 |
|
glycosyl transferase family protein; Provisional
Pssm-ID: 236160 [Multi-domain] Cd Length: 317 Bit Score: 41.77 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 210 AQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKVRGESPQEIAGAATALLENAAPFPRPDYPFADIVGTGGDGS-NSIN 288
Cdd:PRK08136 17 ARDLDRDTARALYGAMLDGRVPDLELGAILIALRIKGESEAEMLGFLDAMQAHTIPLTPPAGRPMPVVIPSYNGArKQAN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 289 ISTASAFVAAACGLKVAKHGNRSVSSRSGSSDLLAAFGINLDMNAERSREALDDLGVCFLFAPKYHTGFRHAMPVRQQLK 368
Cdd:PRK08136 97 LTPLLALLLAREGVPVLVHGVSEDPTRVTSAEIFEALGIPPTLHADQAQAKLAEGQPAFIPVGVLCPPLARLLALRWRMG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515953640 369 TRTLFNVLGPLINP--AHPPLALIGVYSPELVLPIAETLRVLG 409
Cdd:PRK08136 177 VRNSAHTLAKLATPfaEGAALRLSSYTHPEYRDRLAEFFSDIG 219
|
|
| PRK09065 |
PRK09065 |
glutamine amidotransferase; Provisional |
78-172 |
1.09e-03 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 40.72 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953640 78 LPIIGICLGHQAIVEAYGGYVG------QAGEI---LHGKASSiehdgQAMFAGLPNPLPVARYHSLVGSNIPAGLTINA 148
Cdd:PRK09065 89 MPLLGICYGHQLLAHALGGEVGynpagrESGTVtveLHPAAAD-----DPLFAGLPAQFPAHLTHLQSVLRLPPGAVVLA 163
|
90 100
....*....|....*....|....*.
gi 515953640 149 S--FEGmVMAVRHdADRVCGMQFHPE 172
Cdd:PRK09065 164 RsaQDP-HQAFRY-GPHAWGVQFHPE 187
|
|
| |
