|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
6-545 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 709.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILARNLEGD 85
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 86 EKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGEI 165
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 166 SQDLRNRFALKAFEHTADYDAAISDFFRKQYSE---------GKAQLPLRYGCNPHQRpAQAYITQQEELP----FKVLC 232
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEkeprqfnlnFTKKQTLRYGENPHQK-AAFYVTQNVKEGsvatAEQLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 233 G-TPGYINLLDALNSWPLVKELSaslnLPAAASFKHVSPAGAAVGLPLSDverqvyfvndmedlsplacAYARARGADRM 311
Cdd:TIGR00355 240 GkELSYNNIADADAALEIVKEFD----EPAAVIVKHANPCGVALGKTILD-------------------AYDRAFGADPT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 312 SSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNGKYCILQIDPNYVPGQmESREVFGVTLQQKRND 391
Cdd:TIGR00355 297 SAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPEL-DFKRVNGGLLVQDRDD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 392 AIINQSTFKeIVSKnKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLGAGQQSRIHCTRLAGDKTDnwwlrqhpk 471
Cdd:TIGR00355 376 GMVDQSTLK-VVTK-RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKAD--------- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323056 472 vlnmkwAKGIKRADKSNAIDLFVTGQ-RIEGPEKVDYESKFEevPEPFTKEERLEWLSKLNNVSLSSDAFFPFPD 545
Cdd:TIGR00355 445 ------DEGLEAKGSSLASDAFFPFRdGVEEAAAAGITCIIQ--PGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
202-591 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 654.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 202 QLPLRYGCNPHQRPAQAYItQQEELPFKVLCGTPGYINLLDALNSWPLVKELSASLNLPAAASFKHVSPAGAAVGLPLSD 281
Cdd:PRK07106 3 ELELKYGCNPNQKPARIFM-KEGELPIEVLNGRPGYINFLDALNSWQLVKELKEATGLPAAASFKHVSPAGAAVGLPLSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 282 VERQVYFVNDMEdLSPLACAYARARGADRMSSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNGKY 361
Cdd:PRK07106 82 TLKKIYFVDDME-LSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALEILKAKKKGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 362 CILQIDPNYVPGQMESREVFGVTLQQKRNDAIINQSTFKEIVSKNKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVV 441
Cdd:PRK07106 161 NIIKIDPNYEPAPIETKDVFGITFEQGRNELKIDEDLLKNIVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDGQAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 442 GLGAGQQSRIHCTRLAGDKTDNWWLRQHPKVLNMKWAKGIKRADKSNAIDLFVTGQRIEGPEKVDYESKFEEVPEPFTKE 521
Cdd:PRK07106 241 GIGAGQQSRIHCTRLAGNKADIWYLRQHPKVLNLPFKEGIRRPDRDNAIDVYLSDDYMDVLADGVWQQFFTEKPEPLTRE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 522 ERLEWLSKLNNVSLSSDAFFPFPDNVYRAVQSGVKFITAPSGSVMDKVVFQAADSFDIVYVENPIRLFHH 591
Cdd:PRK07106 321 EKRAWLATLTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
6-591 |
1.52e-168 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 489.15 E-value: 1.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILA-RNLEG 84
Cdd:COG0138 4 KRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILArRDNPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 85 DEKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGE 164
Cdd:COG0138 84 HVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKANGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 165 ISQDLRNRFALKAFEHTADYDAAISDFFRKQYSEG-----------KAQlPLRYGCNPHQRpAQAYITQQEE---LPFKV 230
Cdd:COG0138 164 TSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEEefpetltlsfeKVQ-DLRYGENPHQK-AAFYRDPGAEgglATAEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 231 LCGTP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGLPLSDverqvyfvndmedlsplacAYARARGAD 309
Cdd:COG0138 242 LQGKElSYNNILDADAALELVKEFDE----PAVVIVKHANPCGVAVGDTLAE-------------------AYEKAYACD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 310 RMSSFGDFIALSNIVDVATAKIISK---EVsdgVIAPGYEPEALNILSKKKNGKycILQI-DPNYVPGQMESREVFGVTL 385
Cdd:COG0138 299 PVSAFGGIIAFNRPVDAATAEAIAKiflEV---IIAPDFSPEALEILAKKKNLR--LLELgGLDPPAPGLDVKSVSGGLL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 386 QQKRNDAIINQSTFKeIVSKNKAlTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLGAGQQSRIHCTRLAgdktdnww 465
Cdd:COG0138 374 VQDRDLGLIDPADLK-VVTKRAP-TEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIA-------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 466 lrqhpkvlnmkwakgIKRAdksnaidlfvtGQRIEGpekvdyeskfeevpepftkeerlewlsklnnVSLSSDAFFPFPD 545
Cdd:COG0138 444 ---------------LEKA-----------GERAKG-------------------------------SVLASDAFFPFRD 466
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 6323056 546 NVYRAVQSGVKFITAPSGSVMDKVVFQAADSFDIVYVENPIRLFHH 591
Cdd:COG0138 467 GVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-460 |
1.26e-134 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 394.94 E-value: 1.26e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 136 AAKNHSRVTILSDPNDYSIFLQDLSKDGEISQDLRNRFALKAFEHTADYDAAISDFFRKQYSE---------GKAQLPLR 206
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASefpetltlsFEKKQDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 207 YGCNPHQRpAQAYITQQEE---LPFKVLCGTP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGlplsdv 282
Cdd:smart00798 81 YGENPHQK-AAFYTDPDALggiATAKQLQGKElSYNNILDADAALELVKEFDE----PACVIVKHANPCGVAVG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 283 erqvyfvndmedlSPLACAYARARGADRMSSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNGKyc 362
Cdd:smart00798 150 -------------DTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLR-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 363 ILQIDPNYVPGQMESREVFGVTLQQKRNDAIINQSTFKeIVSKnKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVG 442
Cdd:smart00798 215 LLECGPLPDPDGLEFKSVSGGLLVQDRDNGGIDPEDLK-VVTK-RQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVG 292
|
330
....*....|....*...
gi 6323056 443 LGAGQQSRIHCTRLAGDK 460
Cdd:smart00798 293 IGAGQMSRVDSARIAAEK 310
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-460 |
3.29e-131 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 385.99 E-value: 3.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 136 AAKNHSRVTILSDPNDYSIFLQDLSKDGEISQDLRNRFALKAFEHTADYDAAISDFFR-KQYSE-----GKAQLPLRYGC 209
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAgKEFPEtltlsFEKVQDLRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 210 NPHQRpAQAYITQQEE---LPFKVLCG-TPGYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGlplsdverq 285
Cdd:pfam01808 81 NPHQK-AAFYRDPGPAgglATAEQLQGkELSYNNILDADAALELVKEFDE----PAAVIVKHANPCGVAVG--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 286 vyfvndmedlSPLACAYARARGADRMSSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNgkYCILQ 365
Cdd:pfam01808 147 ----------DTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKN--LRLLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 366 IDPNY-VPGQMESREVFGVTLQQKRNDAIINQSTFKeIVSKnKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLG 444
Cdd:pfam01808 215 IDPLYpPPPGLEFRSVSGGLLVQDRDDALIDPDDLK-VVTK-RAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIG 292
|
330
....*....|....*.
gi 6323056 445 AGQQSRIHCTRLAGDK 460
Cdd:pfam01808 293 AGQMSRVDSARIAIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
6-192 |
3.81e-109 |
|
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production.
Pssm-ID: 238709 [Multi-domain] Cd Length: 187 Bit Score: 324.94 E-value: 3.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILARNLEGD 85
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 86 EKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGEI 165
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGSI 160
|
170 180
....*....|....*....|....*..
gi 6323056 166 SQDLRNRFALKAFEHTADYDAAISDFF 192
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
6-545 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 709.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILARNLEGD 85
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 86 EKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGEI 165
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 166 SQDLRNRFALKAFEHTADYDAAISDFFRKQYSE---------GKAQLPLRYGCNPHQRpAQAYITQQEELP----FKVLC 232
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEkeprqfnlnFTKKQTLRYGENPHQK-AAFYVTQNVKEGsvatAEQLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 233 G-TPGYINLLDALNSWPLVKELSaslnLPAAASFKHVSPAGAAVGLPLSDverqvyfvndmedlsplacAYARARGADRM 311
Cdd:TIGR00355 240 GkELSYNNIADADAALEIVKEFD----EPAAVIVKHANPCGVALGKTILD-------------------AYDRAFGADPT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 312 SSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNGKYCILQIDPNYVPGQmESREVFGVTLQQKRND 391
Cdd:TIGR00355 297 SAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPEL-DFKRVNGGLLVQDRDD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 392 AIINQSTFKeIVSKnKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLGAGQQSRIHCTRLAGDKTDnwwlrqhpk 471
Cdd:TIGR00355 376 GMVDQSTLK-VVTK-RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKAD--------- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323056 472 vlnmkwAKGIKRADKSNAIDLFVTGQ-RIEGPEKVDYESKFEevPEPFTKEERLEWLSKLNNVSLSSDAFFPFPD 545
Cdd:TIGR00355 445 ------DEGLEAKGSSLASDAFFPFRdGVEEAAAAGITCIIQ--PGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
202-591 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 654.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 202 QLPLRYGCNPHQRPAQAYItQQEELPFKVLCGTPGYINLLDALNSWPLVKELSASLNLPAAASFKHVSPAGAAVGLPLSD 281
Cdd:PRK07106 3 ELELKYGCNPNQKPARIFM-KEGELPIEVLNGRPGYINFLDALNSWQLVKELKEATGLPAAASFKHVSPAGAAVGLPLSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 282 VERQVYFVNDMEdLSPLACAYARARGADRMSSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNGKY 361
Cdd:PRK07106 82 TLKKIYFVDDME-LSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALEILKAKKKGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 362 CILQIDPNYVPGQMESREVFGVTLQQKRNDAIINQSTFKEIVSKNKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVV 441
Cdd:PRK07106 161 NIIKIDPNYEPAPIETKDVFGITFEQGRNELKIDEDLLKNIVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDGQAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 442 GLGAGQQSRIHCTRLAGDKTDNWWLRQHPKVLNMKWAKGIKRADKSNAIDLFVTGQRIEGPEKVDYESKFEEVPEPFTKE 521
Cdd:PRK07106 241 GIGAGQQSRIHCTRLAGNKADIWYLRQHPKVLNLPFKEGIRRPDRDNAIDVYLSDDYMDVLADGVWQQFFTEKPEPLTRE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 522 ERLEWLSKLNNVSLSSDAFFPFPDNVYRAVQSGVKFITAPSGSVMDKVVFQAADSFDIVYVENPIRLFHH 591
Cdd:PRK07106 321 EKRAWLATLTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
6-591 |
1.52e-168 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 489.15 E-value: 1.52e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILA-RNLEG 84
Cdd:COG0138 4 KRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILArRDNPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 85 DEKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGE 164
Cdd:COG0138 84 HVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKANGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 165 ISQDLRNRFALKAFEHTADYDAAISDFFRKQYSEG-----------KAQlPLRYGCNPHQRpAQAYITQQEE---LPFKV 230
Cdd:COG0138 164 TSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEEefpetltlsfeKVQ-DLRYGENPHQK-AAFYRDPGAEgglATAEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 231 LCGTP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGLPLSDverqvyfvndmedlsplacAYARARGAD 309
Cdd:COG0138 242 LQGKElSYNNILDADAALELVKEFDE----PAVVIVKHANPCGVAVGDTLAE-------------------AYEKAYACD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 310 RMSSFGDFIALSNIVDVATAKIISK---EVsdgVIAPGYEPEALNILSKKKNGKycILQI-DPNYVPGQMESREVFGVTL 385
Cdd:COG0138 299 PVSAFGGIIAFNRPVDAATAEAIAKiflEV---IIAPDFSPEALEILAKKKNLR--LLELgGLDPPAPGLDVKSVSGGLL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 386 QQKRNDAIINQSTFKeIVSKNKAlTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLGAGQQSRIHCTRLAgdktdnww 465
Cdd:COG0138 374 VQDRDLGLIDPADLK-VVTKRAP-TEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIA-------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 466 lrqhpkvlnmkwakgIKRAdksnaidlfvtGQRIEGpekvdyeskfeevpepftkeerlewlsklnnVSLSSDAFFPFPD 545
Cdd:COG0138 444 ---------------LEKA-----------GERAKG-------------------------------SVLASDAFFPFRD 466
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 6323056 546 NVYRAVQSGVKFITAPSGSVMDKVVFQAADSFDIVYVENPIRLFHH 591
Cdd:COG0138 467 GVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
6-591 |
9.65e-168 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 486.91 E-value: 9.65e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILA-RNLEG 84
Cdd:PRK00881 5 KRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILArRDNPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 85 DEKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGE 164
Cdd:PRK00881 85 HVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKANGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 165 ISQDLRNRFALKAFEHTADYDAAISDFFRKQYSEG----------KAQlPLRYGCNPHQRpAQAYITQQEELP---FKVL 231
Cdd:PRK00881 165 TTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEEfpetlnlsfeKKQ-DLRYGENPHQK-AAFYRDPNAEGGvatAEQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 232 CG-TPGYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGLPLSDverqvyfvndmedlsplacAYARARGADR 310
Cdd:PRK00881 243 QGkELSYNNIADADAALELVKEFDE----PACVIVKHANPCGVAVGDTILE-------------------AYDKAYACDP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 311 MSSFGDFIALSNIVDVATAKIISK---EVsdgVIAPGYEPEALNILSKKKNGKycILQIdPNYVPGQMESREVFGVTLQQ 387
Cdd:PRK00881 300 VSAFGGIIAFNREVDAETAEAIHKiflEV---IIAPSFSEEALEILAKKKNLR--LLEC-PFPGGWEGDFKSVSGGLLVQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 388 KRNDAIINQSTFKeIVSKNKAlTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLGAGQQSRIHCTRLAgdktdnwwlr 467
Cdd:PRK00881 374 DRDLGMVDPADLK-VVTKRQP-TEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIA---------- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 468 qhpkvlnmkwakgIKRAdksnaidlfvtgqriegpekvdyeskfeevpepftKEERLEwlskLNNVSLSSDAFFPFPDNV 547
Cdd:PRK00881 442 -------------IEKA-----------------------------------GDAGLD----LKGAVLASDAFFPFRDGV 469
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 6323056 548 YRAVQSGVKFITAPSGSVMDKVVFQAADSFDIVYVENPIRLFHH 591
Cdd:PRK00881 470 EAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-460 |
1.26e-134 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 394.94 E-value: 1.26e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 136 AAKNHSRVTILSDPNDYSIFLQDLSKDGEISQDLRNRFALKAFEHTADYDAAISDFFRKQYSE---------GKAQLPLR 206
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASefpetltlsFEKKQDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 207 YGCNPHQRpAQAYITQQEE---LPFKVLCGTP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGlplsdv 282
Cdd:smart00798 81 YGENPHQK-AAFYTDPDALggiATAKQLQGKElSYNNILDADAALELVKEFDE----PACVIVKHANPCGVAVG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 283 erqvyfvndmedlSPLACAYARARGADRMSSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNGKyc 362
Cdd:smart00798 150 -------------DTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLR-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 363 ILQIDPNYVPGQMESREVFGVTLQQKRNDAIINQSTFKeIVSKnKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVG 442
Cdd:smart00798 215 LLECGPLPDPDGLEFKSVSGGLLVQDRDNGGIDPEDLK-VVTK-RQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVG 292
|
330
....*....|....*...
gi 6323056 443 LGAGQQSRIHCTRLAGDK 460
Cdd:smart00798 293 IGAGQMSRVDSARIAAEK 310
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-460 |
3.29e-131 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 385.99 E-value: 3.29e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 136 AAKNHSRVTILSDPNDYSIFLQDLSKDGEISQDLRNRFALKAFEHTADYDAAISDFFR-KQYSE-----GKAQLPLRYGC 209
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAgKEFPEtltlsFEKVQDLRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 210 NPHQRpAQAYITQQEE---LPFKVLCG-TPGYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGlplsdverq 285
Cdd:pfam01808 81 NPHQK-AAFYRDPGPAgglATAEQLQGkELSYNNILDADAALELVKEFDE----PAAVIVKHANPCGVAVG--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 286 vyfvndmedlSPLACAYARARGADRMSSFGDFIALSNIVDVATAKIISKEVSDGVIAPGYEPEALNILSKKKNgkYCILQ 365
Cdd:pfam01808 147 ----------DTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKN--LRLLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 366 IDPNY-VPGQMESREVFGVTLQQKRNDAIINQSTFKeIVSKnKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLG 444
Cdd:pfam01808 215 IDPLYpPPPGLEFRSVSGGLLVQDRDDALIDPDDLK-VVTK-RAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIG 292
|
330
....*....|....*.
gi 6323056 445 AGQQSRIHCTRLAGDK 460
Cdd:pfam01808 293 AGQMSRVDSARIAIEK 308
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
6-192 |
3.81e-109 |
|
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production.
Pssm-ID: 238709 [Multi-domain] Cd Length: 187 Bit Score: 324.94 E-value: 3.81e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILARNLEGD 85
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 86 EKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGEI 165
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGSI 160
|
170 180
....*....|....*....|....*..
gi 6323056 166 SQDLRNRFALKAFEHTADYDAAISDFF 192
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
6-591 |
7.18e-102 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 319.04 E-value: 7.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 6 KTAILSVYDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPEMLGGRVKTLHPAVHAGILA-RNLEG 84
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILArRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 85 DEKDLKEQHIDKVDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVTLLRAAAKNHSRVTILSDPNDYSIFLQDLSKDGE 164
Cdd:PLN02891 103 HMEALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 165 ISQDLRNRFALKAFEHTADYDAAISDFFRKQYSEGKAQLP-----------LRYGCNPHQrPAQAYITqqeelpfKVLCG 233
Cdd:PLN02891 183 DQQDFRRKLAWKAFQHVASYDSAVSEWLWKQINGGGKFPPsltvpltlkssLRYGENPHQ-KAAFYVD-------KSLSE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 234 TPG---------------YINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGLPLSDverqvyfvndmedlspl 298
Cdd:PLN02891 255 VNAggiataiqhhgkemsYNNYLDADAAWNCVSEFSN----PTCVVVKHTNPCGVASRGDILE----------------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 299 acAYARARGADRMSSFGDFIALSNIVDVATAKIIS--KEVSDG--------VIAPGYEPEALNILsKKKNGKYCILQIDP 368
Cdd:PLN02891 314 --AYRLAVRADPVSAFGGIVAFNCEVDEDLAREIRefRSPTDGetrmfyeiVVAPKYTEKGLEVL-KGKSKTLRILEAKP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 369 NyVPGQMESREVFGVTLQQKRNDAIINQSTFKeiVSKNKALTEQAVIDLTVATLVLKYTQSNSVCYAKNGMVVGLGAGQQ 448
Cdd:PLN02891 391 R-KKGRLSLRQVGGGWLAQDSDDLTPEDITFT--VVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 449 SRIHCTRLAgdktdnwwlrqhpkvlnmkwakgIKRAdksnaidlfvtGQRIEGpekvdyeskfeevpepftkeerlewls 528
Cdd:PLN02891 468 NRVESLRIA-----------------------LEKA-----------GEEAKG--------------------------- 486
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323056 529 klnnVSLSSDAFFPFP--DNVYRAVQSGVKFITAPSGSVMDKVVFQAADSFDIVYVENPIRLFHH 591
Cdd:PLN02891 487 ----AALASDAFFPFAwnDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
17-131 |
4.33e-24 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 96.40 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 17 GLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHAPeMLGGRVKtlhpavhagilarnlegDEKDLKEQHIdk 96
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRVQ-----------------IGDLIKNGEI-- 60
|
90 100 110
....*....|....*....|....*....|....*
gi 6323056 97 vDFVVCNLYPFKETVAKiGVTVQEAVEEIDIGGVT 131
Cdd:pfam02142 61 -DLVINTLYPFKATVHD-GYAIRRAAENIDIPGPT 93
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
17-131 |
4.39e-23 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 93.69 E-value: 4.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 17 GLLDLAKGLVENNVRILASGGTANMVREAGFPVddvssithapemlggrVKTLHPAVHAGILArnlegdekDLKEQHIDK 96
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQ--------ILDLIKNGE 56
|
90 100 110
....*....|....*....|....*....|....*
gi 6323056 97 VDFVVCNLYPFKETVAKIGVTVQEAVEEIDIGGVT 131
Cdd:smart00851 57 IDLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
8-153 |
2.09e-13 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 66.77 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 8 AILSVYD--KTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSIThapemlggrvKTLHPAVHAGILARNlegd 85
Cdd:cd00532 2 VFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRH----------EDGEPTVDAAIAEKG---- 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323056 86 ekdlkeqhidKVDFVVCNLYPFKEtvakigvtvqeavEEIDIGGVTLLRAAAKNHSRVTilSDPNDYS 153
Cdd:cd00532 68 ----------KFDVVINLRDPRRD-------------RCTDEDGTALLRLARLYKIPVT--TPNATAM 110
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
7-58 |
9.14e-06 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 44.78 E-value: 9.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6323056 7 TAILSV--YDKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSITHA 58
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG 55
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
5-62 |
3.69e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 47.01 E-value: 3.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323056 5 TKTAILSVY--DKTGLLDLAKGLVENNVRILASGGTANMVREAGFPVDDVSSIT----HAPEML 62
Cdd:PRK05294 937 SGTVFLSVRdrDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHegrpHIVDLI 1000
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
5-91 |
2.82e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 44.00 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323056 5 TKTAILSVYDKT--GLLDLAKGLVENNVRILASGGTANMVREAGFPVDdvssithapemlggRVKTLHPA-VHAGILARN 81
Cdd:PLN02735 972 SGTVFISLNDLTkpHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVE--------------RVLKLHEGrPHAGDMLAN 1037
|
90
....*....|....*....
gi 6323056 82 LE---------GDEKDLKE 91
Cdd:PLN02735 1038 GQiqlmvitssGDALDQKD 1056
|
|
| |
