|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
6-546 |
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: 789.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILARDIDSD 85
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 86 EKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGEI 165
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 166 SQDLRNRLALKAFEHTADYDAAISDFFRKQYSE---------GQAQITLRYGANPHQKpAQAYVSQQDSLP----FKVLC 232
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEkeprqfnlnFTKKQTLRYGENPHQK-AAFYVTQNVKEGsvatAEQLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 233 G-SPGYINLLDALNSWPLVKELSaslnLPAAASFKHVSPAGAAVGIPLSDvekqvyfvadienlsplacAYARARGADRM 311
Cdd:TIGR00355 240 GkELSYNNIADADAALEIVKEFD----EPAAVIVKHANPCGVALGKTILD-------------------AYDRAFGADPT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 312 SSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKYCILQIDPNYVPEAVeRRQVYGVTLEQKRND 391
Cdd:TIGR00355 297 SAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELD-FKRVNGGLLVQDRDD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 392 AIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQSRIHCTRLAGDKADnwwfrqhpr 471
Cdd:TIGR00355 376 GMVDQSTLK-VVTK-RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKAD--------- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323768 472 vleikwAKGVKRPEKSNAIDLFVTGQIPTEEPELSEYQSKFEeiPKPFTPEERKEWLSKLTNVSLSSDAFFPFPD 546
Cdd:TIGR00355 445 ------DEGLEAKGSSLASDAFFPFRDGVEEAAAAGITCIIQ--PGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
202-592 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 651.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 202 QITLRYGANPHQKPAQAYVSQQDsLPFKVLCGSPGYINLLDALNSWPLVKELSASLNLPAAASFKHVSPAGAAVGIPLSD 281
Cdd:PRK07106 3 ELELKYGCNPNQKPARIFMKEGE-LPIEVLNGRPGYINFLDALNSWQLVKELKEATGLPAAASFKHVSPAGAAVGLPLSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 282 VEKQVYFVADIEnLSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKY 361
Cdd:PRK07106 82 TLKKIYFVDDME-LSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALEILKAKKKGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 362 CILQIDPNYVPEAVERRQVYGVTLEQKRNDAIINQSTFKEIVSQNKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVV 441
Cdd:PRK07106 161 NIIKIDPNYEPAPIETKDVFGITFEQGRNELKIDEDLLKNIVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDGQAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 442 GLGAGQQSRIHCTRLAGDKADNWWFRQHPRVLEIKWAKGVKRPEKSNAIDLFVTGQIpTEEPELSEYQSKFEEIPKPFTP 521
Cdd:PRK07106 241 GIGAGQQSRIHCTRLAGNKADIWYLRQHPKVLNLPFKEGIRRPDRDNAIDVYLSDDY-MDVLADGVWQQFFTEKPEPLTR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323768 522 EERKEWLSKLTNVSLSSDAFFPFPDNVYRAVKSGVKYIAAPSGSVMDKVVFSAADSFDLVYVENPIRLFHH 592
Cdd:PRK07106 320 EEKRAWLATLTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
6-576 |
2.52e-172 |
|
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: 498.78 E-value: 2.52e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILA-RDIDS 84
Cdd:COG0138 4 KRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILArRDNPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 85 DEKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGE 164
Cdd:COG0138 84 HVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKANGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 165 ISQDLRNRLALKAFEHTADYDAAISDFFRKQYSE----------GQAQITLRYGANPHQKpAQAYVSQQDS---LPFKVL 231
Cdd:COG0138 164 TSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEeefpetltlsFEKVQDLRYGENPHQK-AAFYRDPGAEgglATAEQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 232 CGSP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGIPLSDvekqvyfvadienlsplacAYARARGADR 310
Cdd:COG0138 243 QGKElSYNNILDADAALELVKEFDE----PAVVIVKHANPCGVAVGDTLAE-------------------AYEKAYACDP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 311 MSSFGDWIALSNIVDVPTAKIISR---EVsdgVIAPGYEPEALAILSKKKGGKycILQI-DPNYVPEAVERRQVYGVTLE 386
Cdd:COG0138 300 VSAFGGIIAFNRPVDAATAEAIAKiflEV---IIAPDFSPEALEILAKKKNLR--LLELgGLDPPAPGLDVKSVSGGLLV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 387 QKRNDAIINQSTFKeIVSQNKnLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQSRIHCTRLAGDKAdnwwf 466
Cdd:COG0138 375 QDRDLGLIDPADLK-VVTKRA-PTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKA----- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 467 rqhprvleikwakgvkrpeksnaidlfvtgqipteepelseyqskfeeipkpftpEERkewlskLTNVSLSSDAFFPFPD 546
Cdd:COG0138 448 -------------------------------------------------------GER------AKGSVLASDAFFPFRD 466
|
570 580 590
....*....|....*....|....*....|
gi 6323768 547 NVYRAVKSGVKYIAAPSGSVMDKVVFSAAD 576
Cdd:COG0138 467 GVEAAAKAGITAIIQPGGSIRDEEVIAAAD 496
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-461 |
1.12e-135 |
|
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: 397.63 E-value: 1.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 136 AAKNHARVTILSDPKDYSEFLSELSSNGEISQDLRNRLALKAFEHTADYDAAISDFFRKQYSE---------GQAQITLR 206
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASefpetltlsFEKKQDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 207 YGANPHQKpAQAYVSQQDS---LPFKVLCGSP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGiplsdv 282
Cdd:smart00798 81 YGENPHQK-AAFYTDPDALggiATAKQLQGKElSYNNILDADAALELVKEFDE----PACVIVKHANPCGVAVG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 283 ekqvyfvadienlSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKyc 362
Cdd:smart00798 150 -------------DTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLR-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 363 ILQIDPNYVPEAVERRQVYGVTLEQKRNDAIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVG 442
Cdd:smart00798 215 LLECGPLPDPDGLEFKSVSGGLLVQDRDNGGIDPEDLK-VVTK-RQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVG 292
|
330
....*....|....*....
gi 6323768 443 LGAGQQSRIHCTRLAGDKA 461
Cdd:smart00798 293 IGAGQMSRVDSARIAAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-460 |
7.27e-132 |
|
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: 387.91 E-value: 7.27e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 136 AAKNHARVTILSDPKDYSEFLSELSSNGEISQDLRNRLALKAFEHTADYDAAISDFFR-KQYSE-----GQAQITLRYGA 209
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAgKEFPEtltlsFEKVQDLRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 210 NPHQKpAQAYVSQQDS---LPFKVLCG-SPGYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGiplsdvekq 285
Cdd:pfam01808 81 NPHQK-AAFYRDPGPAgglATAEQLQGkELSYNNILDADAALELVKEFDE----PAAVIVKHANPCGVAVG--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 286 vyfvadienlSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKggKYCILQ 365
Cdd:pfam01808 147 ----------DTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKK--NLRLLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 366 IDPNY-VPEAVERRQVYGVTLEQKRNDAIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLG 444
Cdd:pfam01808 215 IDPLYpPPPGLEFRSVSGGLLVQDRDDALIDPDDLK-VVTK-RAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIG 292
|
330
....*....|....*.
gi 6323768 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 |
1.25e-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: 326.09 E-value: 1.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILARDIDSD 85
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 86 EKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGEI 165
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGSI 160
|
170 180
....*....|....*....|....*..
gi 6323768 166 SQDLRNRLALKAFEHTADYDAAISDFF 192
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
6-546 |
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: 789.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILARDIDSD 85
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 86 EKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGEI 165
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 166 SQDLRNRLALKAFEHTADYDAAISDFFRKQYSE---------GQAQITLRYGANPHQKpAQAYVSQQDSLP----FKVLC 232
Cdd:TIGR00355 161 SLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEkeprqfnlnFTKKQTLRYGENPHQK-AAFYVTQNVKEGsvatAEQLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 233 G-SPGYINLLDALNSWPLVKELSaslnLPAAASFKHVSPAGAAVGIPLSDvekqvyfvadienlsplacAYARARGADRM 311
Cdd:TIGR00355 240 GkELSYNNIADADAALEIVKEFD----EPAAVIVKHANPCGVALGKTILD-------------------AYDRAFGADPT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 312 SSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKYCILQIDPNYVPEAVeRRQVYGVTLEQKRND 391
Cdd:TIGR00355 297 SAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELD-FKRVNGGLLVQDRDD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 392 AIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQSRIHCTRLAGDKADnwwfrqhpr 471
Cdd:TIGR00355 376 GMVDQSTLK-VVTK-RQPTEQELIDLLFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKAD--------- 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323768 472 vleikwAKGVKRPEKSNAIDLFVTGQIPTEEPELSEYQSKFEeiPKPFTPEERKEWLSKLTNVSLSSDAFFPFPD 546
Cdd:TIGR00355 445 ------DEGLEAKGSSLASDAFFPFRDGVEEAAAAGITCIIQ--PGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
202-592 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 651.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 202 QITLRYGANPHQKPAQAYVSQQDsLPFKVLCGSPGYINLLDALNSWPLVKELSASLNLPAAASFKHVSPAGAAVGIPLSD 281
Cdd:PRK07106 3 ELELKYGCNPNQKPARIFMKEGE-LPIEVLNGRPGYINFLDALNSWQLVKELKEATGLPAAASFKHVSPAGAAVGLPLSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 282 VEKQVYFVADIEnLSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKY 361
Cdd:PRK07106 82 TLKKIYFVDDME-LSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALEILKAKKKGNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 362 CILQIDPNYVPEAVERRQVYGVTLEQKRNDAIINQSTFKEIVSQNKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVV 441
Cdd:PRK07106 161 NIIKIDPNYEPAPIETKDVFGITFEQGRNELKIDEDLLKNIVTENKELPDEAKRDLIIALITLKYTQSNSVCYAKDGQAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 442 GLGAGQQSRIHCTRLAGDKADNWWFRQHPRVLEIKWAKGVKRPEKSNAIDLFVTGQIpTEEPELSEYQSKFEEIPKPFTP 521
Cdd:PRK07106 241 GIGAGQQSRIHCTRLAGNKADIWYLRQHPKVLNLPFKEGIRRPDRDNAIDVYLSDDY-MDVLADGVWQQFFTEKPEPLTR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323768 522 EERKEWLSKLTNVSLSSDAFFPFPDNVYRAVKSGVKYIAAPSGSVMDKVVFSAADSFDLVYVENPIRLFHH 592
Cdd:PRK07106 320 EEKRAWLATLTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
6-576 |
2.52e-172 |
|
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: 498.78 E-value: 2.52e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILA-RDIDS 84
Cdd:COG0138 4 KRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILArRDNPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 85 DEKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGE 164
Cdd:COG0138 84 HVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKANGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 165 ISQDLRNRLALKAFEHTADYDAAISDFFRKQYSE----------GQAQITLRYGANPHQKpAQAYVSQQDS---LPFKVL 231
Cdd:COG0138 164 TSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEeefpetltlsFEKVQDLRYGENPHQK-AAFYRDPGAEgglATAEQL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 232 CGSP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGIPLSDvekqvyfvadienlsplacAYARARGADR 310
Cdd:COG0138 243 QGKElSYNNILDADAALELVKEFDE----PAVVIVKHANPCGVAVGDTLAE-------------------AYEKAYACDP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 311 MSSFGDWIALSNIVDVPTAKIISR---EVsdgVIAPGYEPEALAILSKKKGGKycILQI-DPNYVPEAVERRQVYGVTLE 386
Cdd:COG0138 300 VSAFGGIIAFNRPVDAATAEAIAKiflEV---IIAPDFSPEALEILAKKKNLR--LLELgGLDPPAPGLDVKSVSGGLLV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 387 QKRNDAIINQSTFKeIVSQNKnLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQSRIHCTRLAGDKAdnwwf 466
Cdd:COG0138 375 QDRDLGLIDPADLK-VVTKRA-PTEEELADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKA----- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 467 rqhprvleikwakgvkrpeksnaidlfvtgqipteepelseyqskfeeipkpftpEERkewlskLTNVSLSSDAFFPFPD 546
Cdd:COG0138 448 -------------------------------------------------------GER------AKGSVLASDAFFPFRD 466
|
570 580 590
....*....|....*....|....*....|
gi 6323768 547 NVYRAVKSGVKYIAAPSGSVMDKVVFSAAD 576
Cdd:COG0138 467 GVEAAAKAGITAIIQPGGSIRDEEVIAAAD 496
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
6-592 |
1.72e-168 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 488.83 E-value: 1.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILA-RDIDS 84
Cdd:PRK00881 5 KRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILArRDNPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 85 DEKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGE 164
Cdd:PRK00881 85 HVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKANGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 165 ISQDLRNRLALKAFEHTADYDAAISDFFRKQYSEG----------QAQiTLRYGANPHQKpAQAYVsqqDSLP------F 228
Cdd:PRK00881 165 TTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEEfpetlnlsfeKKQ-DLRYGENPHQK-AAFYR---DPNAeggvatA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 229 KVLCGSP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGiplsdvekqvyfvADIENlsplacAYARARG 307
Cdd:PRK00881 240 EQLQGKElSYNNIADADAALELVKEFDE----PACVIVKHANPCGVAVG-------------DTILE------AYDKAYA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 308 ADRMSSFGDWIALSNIVDVPTAKIISR---EVsdgVIAPGYEPEALAILSKKKGGKycILQIDPNYVPEAvERRQVYGVT 384
Cdd:PRK00881 297 CDPVSAFGGIIAFNREVDAETAEAIHKiflEV---IIAPSFSEEALEILAKKKNLR--LLECPFPGGWEG-DFKSVSGGL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 385 LEQKRNDAIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQSRIHCTRLAGDKAdnw 464
Cdd:PRK00881 371 LVQDRDLGMVDPADLK-VVTK-RQPTEQELKDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKA--- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 465 wfrqhprvleikwakgvkrpeKSNAIDlfvtgqipteepelseyqskfeeipkpftpeerkewlskLTNVSLSSDAFFPF 544
Cdd:PRK00881 446 ---------------------GDAGLD---------------------------------------LKGAVLASDAFFPF 465
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 6323768 545 PDNVYRAVKSGVKYIAAPSGSVMDKVVFSAADSFDLVYVENPIRLFHH 592
Cdd:PRK00881 466 RDGVEAAAKAGITAIIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-461 |
1.12e-135 |
|
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: 397.63 E-value: 1.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 136 AAKNHARVTILSDPKDYSEFLSELSSNGEISQDLRNRLALKAFEHTADYDAAISDFFRKQYSE---------GQAQITLR 206
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASefpetltlsFEKKQDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 207 YGANPHQKpAQAYVSQQDS---LPFKVLCGSP-GYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGiplsdv 282
Cdd:smart00798 81 YGENPHQK-AAFYTDPDALggiATAKQLQGKElSYNNILDADAALELVKEFDE----PACVIVKHANPCGVAVG------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 283 ekqvyfvadienlSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKGGKyc 362
Cdd:smart00798 150 -------------DTLAEAYRKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLR-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 363 ILQIDPNYVPEAVERRQVYGVTLEQKRNDAIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVG 442
Cdd:smart00798 215 LLECGPLPDPDGLEFKSVSGGLLVQDRDNGGIDPEDLK-VVTK-RQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVG 292
|
330
....*....|....*....
gi 6323768 443 LGAGQQSRIHCTRLAGDKA 461
Cdd:smart00798 293 IGAGQMSRVDSARIAAEKA 311
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
136-460 |
7.27e-132 |
|
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: 387.91 E-value: 7.27e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 136 AAKNHARVTILSDPKDYSEFLSELSSNGEISQDLRNRLALKAFEHTADYDAAISDFFR-KQYSE-----GQAQITLRYGA 209
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAgKEFPEtltlsFEKVQDLRYGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 210 NPHQKpAQAYVSQQDS---LPFKVLCG-SPGYINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGiplsdvekq 285
Cdd:pfam01808 81 NPHQK-AAFYRDPGPAgglATAEQLQGkELSYNNILDADAALELVKEFDE----PAAVIVKHANPCGVAVG--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 286 vyfvadienlSPLACAYARARGADRMSSFGDWIALSNIVDVPTAKIISREVSDGVIAPGYEPEALAILSKKKggKYCILQ 365
Cdd:pfam01808 147 ----------DTLAEAYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKK--NLRLLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 366 IDPNY-VPEAVERRQVYGVTLEQKRNDAIINQSTFKeIVSQnKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLG 444
Cdd:pfam01808 215 IDPLYpPPPGLEFRSVSGGLLVQDRDDALIDPDDLK-VVTK-RAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIG 292
|
330
....*....|....*.
gi 6323768 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 |
1.25e-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: 326.09 E-value: 1.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILARDIDSD 85
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 86 EKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGEI 165
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGSI 160
|
170 180
....*....|....*....|....*..
gi 6323768 166 SQDLRNRLALKAFEHTADYDAAISDFF 192
Cdd:cd01421 161 SEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
6-592 |
4.33e-104 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 324.82 E-value: 4.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 6 KTAILSVYDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPEMLGGRVKTLHPAVHGGILA-RDIDS 84
Cdd:PLN02891 23 KQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILArRDQEH 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 85 DEKDLKEQHIEKVDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVTLLRAAAKNHARVTILSDPKDYSEFLSELSSNGE 164
Cdd:PLN02891 103 HMEALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 165 ISQDLRNRLALKAFEHTADYDAAISDFFRKQYSEGQA-----------QITLRYGANPHQKpAQAYVSqqdslpfKVLCG 233
Cdd:PLN02891 183 DQQDFRRKLAWKAFQHVASYDSAVSEWLWKQINGGGKfppsltvpltlKSSLRYGENPHQK-AAFYVD-------KSLSE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 234 SPG---------------YINLLDALNSWPLVKELSAslnlPAAASFKHVSPAGAAVGiplsdvekqvyfvADIENlspl 298
Cdd:PLN02891 255 VNAggiataiqhhgkemsYNNYLDADAAWNCVSEFSN----PTCVVVKHTNPCGVASR-------------GDILE---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 299 acAYARARGADRMSSFGDWIALSNIVDVPTAKIIS--REVSDG--------VIAPGYEPEALAILsKKKGGKYCILQIDP 368
Cdd:PLN02891 314 --AYRLAVRADPVSAFGGIVAFNCEVDEDLAREIRefRSPTDGetrmfyeiVVAPKYTEKGLEVL-KGKSKTLRILEAKP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 369 NyVPEAVERRQVYGVTLEQKRNDAIINQSTFKeiVSQNKNLTEQAIIDLTVATIAIKYTQSNSVCYARNGMVVGLGAGQQ 448
Cdd:PLN02891 391 R-KKGRLSLRQVGGGWLAQDSDDLTPEDITFT--VVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQP 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 449 SRIHCTRLAGDKADNwwfrqhprvlEIKWAkgvkrpeksnaidlfvtgqipteepelseyqskfeeipkpftpeerkewl 528
Cdd:PLN02891 468 NRVESLRIALEKAGE----------EAKGA-------------------------------------------------- 487
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323768 529 skltnvSLSSDAFFPFP--DNVYRAVKSGVKYIAAPSGSVMDKVVFSAADSFDLVYVENPIRLFHH 592
Cdd:PLN02891 488 ------ALASDAFFPFAwnDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
17-131 |
1.80e-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: 214855 [Multi-domain] Cd Length: 91 Bit Score: 97.54 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 17 GLLDLARGLIEKNVRILASGGTARMIRDAGFPIedvsaithapemlggrVKTLHPAVHGGILArdidsdekDLKEQHIEK 96
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQ--------ILDLIKNGE 56
|
90 100 110
....*....|....*....|....*....|....*
gi 6323768 97 VDYVVCNLYPFKETVAKVGVTIPEAVEEIDIGGVT 131
Cdd:smart00851 57 IDLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
17-131 |
5.17e-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: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 17 GLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHAPeMLGGRVktlhpavhggilardidSDEKDLKEQHIek 96
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRV-----------------QIGDLIKNGEI-- 60
|
90 100 110
....*....|....*....|....*....|....*
gi 6323768 97 vDYVVCNLYPFKETVAKvGVTIPEAVEEIDIGGVT 131
Cdd:pfam02142 61 -DLVINTLYPFKATVHD-GYAIRRAAENIDIPGPT 93
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
8-153 |
2.05e-14 |
|
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: 69.46 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323768 8 AILSVYD--KTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAIThapemlggrvKTLHPAVHGGILARdidsd 85
Cdd:cd00532 2 VFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRH----------EDGEPTVDAAIAEK----- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323768 86 ekdlkeqhiEKVDYVVCNLYPFKEtvakvgvtipeavEEIDIGGVTLLRAAAKNHarVTILSDPKDYS 153
Cdd:cd00532 67 ---------GKFDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK--IPVTTPNATAM 110
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
7-58 |
9.06e-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: 9.06e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6323768 7 TAILSV--YDKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAITHA 58
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEG 55
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
5-62 |
6.56e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 46.24 E-value: 6.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323768 5 TKTAILSVY--DKTGLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAIT----HAPEML 62
Cdd:PRK05294 937 SGTVFLSVRdrDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHegrpHIVDLI 1000
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
5-62 |
3.82e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 43.61 E-value: 3.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323768 5 TKTAILSVYDKT--GLLDLARGLIEKNVRILASGGTARMIRDAGFPIEDVSAI----THAPEML 62
Cdd:PLN02735 972 SGTVFISLNDLTkpHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLhegrPHAGDML 1035
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