|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
6-569 |
0e+00 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 761.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 6 VGILGGGQLGRMIVEAANRLNIKTVILD-AENSPAKQISNsnDHVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKNL 84
Cdd:PLN02948 25 VGVLGGGQLGRMLCQAASQMGIKVKVLDpLEDCPASSVAA--RHVVGSFDDRAAVREFAKRCDVLTVEIEHVDVDTLEAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 85 QVKhpKLKIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVeqASETSLLNVGRDLGFPFVLKSRTLAYDGRGNFVVKN 164
Cdd:PLN02948 103 EKQ--GVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEI--DDLESAEKAGDLFGYPLMLKSRRLAYDGRGNAVAKT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 165 KEMIPEALEVL--KDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAEN 242
Cdd:PLN02948 179 EEDLSSAVAALggFERGLYAEKWAPFVKELAVMVARSRDGSTRCYPVVETIHKDNICHVVEAPANVPWKVAKLATDVAEK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 243 AIKSFPGCGIFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMpknfTSFSTITTNAIMLNVL 322
Cdd:PLN02948 259 AVGSLEGAGVFGVELFLLKDGQILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPL----GDTSMKVPAAIMYNIL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 323 GDKhtkDKEL------ETCERALATPGSSVYLYGK-ESRPNRKVGHINIIASSMAECEQRLNYITGRTDIPikisvaqkL 395
Cdd:PLN02948 335 GED---EGEAgfrlahQLMGRALNIPGASVHWYGKpEMRKQRKMGHITVVGPSAAEVEARLDQLLAEESAD--------P 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 396 DLEAMVKPLVGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMV 475
Cdd:PLN02948 404 DALPKGTPLVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGLQVIIAGAGGAAHLPGMV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 476 AAMTPLPVIGVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEVLVK 555
Cdd:PLN02948 484 ASMTPLPVIGVPVKTSHLDGLDSLLSIVQMPRGVPVATVAIGNATNAGLLAVRMLGASDPDLLDKMEAYQEDMRDMVLEK 563
|
570
....*....|....
gi 398365279 556 AQKLETVGYEAYLE 569
Cdd:PLN02948 564 AEKLEELGWEEYLN 577
|
|
| purK |
TIGR01161 |
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ... |
5-368 |
9.66e-180 |
|
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273473 [Multi-domain] Cd Length: 352 Bit Score: 510.73 E-value: 9.66e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 5 TVGILGGGQLGRMIVEAANRLNIKTVILDA-ENSPAKQISNSNdhVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKN 83
Cdd:TIGR01161 1 TVGILGGGQLGRMLALAARPLGIKVHVLDPdANSPAVQVADHV--VLAPFFDPAAIRELAESCDVITFEFEHVDVEALEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 84 LQVKHpkLKIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQasETSLLNVGRDLGFPFVLKSRTLAYDGRGNFVVK 163
Cdd:TIGR01161 79 LEARG--VKLFPSPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKD--EEELDAALQELGFPVVLKARTGGYDGRGQYRIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 164 NKEMIPEALEVLKDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENA 243
Cdd:TIGR01161 155 NEADLPQAAKELGDRECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGILRYVVAPAAVPDAIQARAEEIARRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 244 IKSFPGCGIFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMPKnftsfSTITTNAIMLNVLG 323
Cdd:TIGR01161 235 MEELGYVGVLAVEMFVLPDGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGS-----TELLLPSVMVNLLG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398365279 324 dkhTKDKELETCERALATPGSSVYLYGK-ESRPNRKVGHINIIASS 368
Cdd:TIGR01161 310 ---TEDDVIPLWEEILALPGAKLHWYGKaEVRPGRKVGHVNLVGSD 352
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
13-377 |
4.45e-149 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 432.58 E-value: 4.45e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 13 QLGRMIVEAANRLNIKTVILD-AENSPAKQISNsnDHVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKNLQvkhPKL 91
Cdd:COG0026 1 QLGRMLALAAKRLGYRVHVLDpDPDSPAAQVAD--EHIVADYDDEEALREFAERCDVVTFEFENVPAEALEALE---AEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 92 KIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASEtsLLNVGRDLGFPFVLKSRTLAYDGRGNFVVKNKEMIPEA 171
Cdd:COG0026 76 PVRPGPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGYDGKGQVVIKSAADLEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 172 LEVLKDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENAIKSFPGCG 251
Cdd:COG0026 154 WAALGGGPCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARISEALAAEAEEIAKRIAEALDYVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 252 IFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMPKnftsfSTITTNAIMLNVLGDkhtkDKE 331
Cdd:COG0026 234 VLAVEFFVTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGD-----TELLSPAVMVNLLGD----DWE 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 398365279 332 LETCERALATPGSSVYLYGK-ESRPNRKVGHINIIASSMAECEQRLN 377
Cdd:COG0026 305 DPGWEALLALPGAHLHLYGKkEARPGRKMGHVTVLGDDLEEALERAR 351
|
|
| AIRC |
pfam00731 |
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ... |
405-551 |
7.43e-87 |
|
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 459917 Cd Length: 147 Bit Score: 265.39 E-value: 7.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 405 VGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLPVI 484
Cdd:pfam00731 1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGLKVIIAGAGGAAHLPGMVAALTTLPVI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365279 485 GVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEE 551
Cdd:pfam00731 81 GVPVKSSALDGLDSLLSIVQMPSGVPVATVAIGGAKNAALLAAQILALSDPELAEKLKEYREEMAEK 147
|
|
| AIRC |
smart01001 |
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ... |
403-552 |
2.43e-76 |
|
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 214965 Cd Length: 152 Bit Score: 238.59 E-value: 2.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 403 PLVGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLP 482
Cdd:smart01001 1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGIKVIIAGAGGAAHLPGVVAALTTLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365279 483 VIGVPVKGSCLDGVDSLHSIVQMPRGVPVATVAIN--NSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEV 552
Cdd:smart01001 81 VIGVPVSSGYLGGLDSLLSIVQMPSGIPVATVAIGidGAFNAALLAAQILALNDPELAAKLAAYRINQTEEV 152
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
13-63 |
1.45e-03 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 40.83 E-value: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398365279 13 QLGRMIVEAANRLNIKTVILDAENSPAKQISNSND----HVNGSFSNPLDIEKLA 63
Cdd:cd19968 16 YMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENaiaqGVDGIIVSPIDVKALV 70
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02948 |
PLN02948 |
phosphoribosylaminoimidazole carboxylase |
6-569 |
0e+00 |
|
phosphoribosylaminoimidazole carboxylase
Pssm-ID: 178534 [Multi-domain] Cd Length: 577 Bit Score: 761.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 6 VGILGGGQLGRMIVEAANRLNIKTVILD-AENSPAKQISNsnDHVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKNL 84
Cdd:PLN02948 25 VGVLGGGQLGRMLCQAASQMGIKVKVLDpLEDCPASSVAA--RHVVGSFDDRAAVREFAKRCDVLTVEIEHVDVDTLEAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 85 QVKhpKLKIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVeqASETSLLNVGRDLGFPFVLKSRTLAYDGRGNFVVKN 164
Cdd:PLN02948 103 EKQ--GVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPEFMEI--DDLESAEKAGDLFGYPLMLKSRRLAYDGRGNAVAKT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 165 KEMIPEALEVL--KDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAEN 242
Cdd:PLN02948 179 EEDLSSAVAALggFERGLYAEKWAPFVKELAVMVARSRDGSTRCYPVVETIHKDNICHVVEAPANVPWKVAKLATDVAEK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 243 AIKSFPGCGIFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMpknfTSFSTITTNAIMLNVL 322
Cdd:PLN02948 259 AVGSLEGAGVFGVELFLLKDGQILLNEVAPRPHNSGHYTIEACYTSQFEQHLRAVLGLPL----GDTSMKVPAAIMYNIL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 323 GDKhtkDKEL------ETCERALATPGSSVYLYGK-ESRPNRKVGHINIIASSMAECEQRLNYITGRTDIPikisvaqkL 395
Cdd:PLN02948 335 GED---EGEAgfrlahQLMGRALNIPGASVHWYGKpEMRKQRKMGHITVVGPSAAEVEARLDQLLAEESAD--------P 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 396 DLEAMVKPLVGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMV 475
Cdd:PLN02948 404 DALPKGTPLVGIIMGSDSDLPTMKDAAEILDSFGVPYEVTIVSAHRTPERMFSYARSAHSRGLQVIIAGAGGAAHLPGMV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 476 AAMTPLPVIGVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEVLVK 555
Cdd:PLN02948 484 ASMTPLPVIGVPVKTSHLDGLDSLLSIVQMPRGVPVATVAIGNATNAGLLAVRMLGASDPDLLDKMEAYQEDMRDMVLEK 563
|
570
....*....|....
gi 398365279 556 AQKLETVGYEAYLE 569
Cdd:PLN02948 564 AEKLEELGWEEYLN 577
|
|
| purK |
TIGR01161 |
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole ... |
5-368 |
9.66e-180 |
|
phosphoribosylaminoimidazole carboxylase, PurK protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, N5-carboxyaminoimidazole ribonucleotide synthetase, which hydrolyzes ATP and converts AIR to N5-CAIR. PurE converts N5-CAIR to CAIR. In the presence of high concentrations of bicarbonate, PurE is reported able to convert AIR to CAIR directly and without ATP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273473 [Multi-domain] Cd Length: 352 Bit Score: 510.73 E-value: 9.66e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 5 TVGILGGGQLGRMIVEAANRLNIKTVILDA-ENSPAKQISNSNdhVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKN 83
Cdd:TIGR01161 1 TVGILGGGQLGRMLALAARPLGIKVHVLDPdANSPAVQVADHV--VLAPFFDPAAIRELAESCDVITFEFEHVDVEALEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 84 LQVKHpkLKIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQasETSLLNVGRDLGFPFVLKSRTLAYDGRGNFVVK 163
Cdd:TIGR01161 79 LEARG--VKLFPSPDALAIIQDRLTQKQFLQKLGLPVPPFLVIKD--EEELDAALQELGFPVVLKARTGGYDGRGQYRIR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 164 NKEMIPEALEVLKDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENA 243
Cdd:TIGR01161 155 NEADLPQAAKELGDRECIVEEFVPFERELSVIVARSADGETAFYPVVENIHQDGILRYVVAPAAVPDAIQARAEEIARRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 244 IKSFPGCGIFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMPKnftsfSTITTNAIMLNVLG 323
Cdd:TIGR01161 235 MEELGYVGVLAVEMFVLPDGRLLINELAPRVHNSGHYTLDGCSTSQFEQHLRAILGLPLGS-----TELLLPSVMVNLLG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 398365279 324 dkhTKDKELETCERALATPGSSVYLYGK-ESRPNRKVGHINIIASS 368
Cdd:TIGR01161 310 ---TEDDVIPLWEEILALPGAKLHWYGKaEVRPGRKVGHVNLVGSD 352
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
13-377 |
4.45e-149 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 432.58 E-value: 4.45e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 13 QLGRMIVEAANRLNIKTVILD-AENSPAKQISNsnDHVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKNLQvkhPKL 91
Cdd:COG0026 1 QLGRMLALAAKRLGYRVHVLDpDPDSPAAQVAD--EHIVADYDDEEALREFAERCDVVTFEFENVPAEALEALE---AEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 92 KIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASEtsLLNVGRDLGFPFVLKSRTLAYDGRGNFVVKNKEMIPEA 171
Cdd:COG0026 76 PVRPGPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLED--LEAAIAELGLPAVLKTRRGGYDGKGQVVIKSAADLEAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 172 LEVLKDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENAIKSFPGCG 251
Cdd:COG0026 154 WAALGGGPCILEEFVPFERELSVIVARSPDGEVATYPVVENVHRNGILDESIAPARISEALAAEAEEIAKRIAEALDYVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 252 IFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMPKnftsfSTITTNAIMLNVLGDkhtkDKE 331
Cdd:COG0026 234 VLAVEFFVTKDGELLVNEIAPRPHNSGHWTIEACVTSQFEQHLRAVCGLPLGD-----TELLSPAVMVNLLGD----DWE 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 398365279 332 LETCERALATPGSSVYLYGK-ESRPNRKVGHINIIASSMAECEQRLN 377
Cdd:COG0026 305 DPGWEALLALPGAHLHLYGKkEARPGRKMGHVTVLGDDLEEALERAR 351
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
5-376 |
1.00e-145 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 424.95 E-value: 1.00e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 5 TVGILGGGQLGRMIVEAANRLNIKTVILD-AENSPAKQISNsnDHVNGSFSNPLDIEKLAEKCDVLTIEIEHVDVPTLKN 83
Cdd:PRK06019 4 TIGIIGGGQLGRMLALAAAPLGYKVIVLDpDPDSPAAQVAD--EVIVADYDDVAALRELAEQCDVITYEFENVPAEALDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 84 LQVKHPklkIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASEtsLLNVGRDLGFPFVLKSRTLAYDGRGNFVVK 163
Cdd:PRK06019 82 LAARVP---VPPGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAED--LEAALADLGLPAVLKTRRGGYDGKGQWVIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 164 NKEMIPEALEVLKDRPLYAEKWAPFTKELAVMIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENA 243
Cdd:PRK06019 157 SAEDLEAAWALLGSVPCILEEFVPFEREVSVIVARGRDGEVVFYPLVENVHRNGILRTSIAPARISAELQAQAEEIASRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 244 IKSFPGCGIFGVEMFYLETGELLINEIAPRPHNSGHYTIDACVTSQFEAHLRSILDLPMPKnftsfSTITTNAIMLNVLG 323
Cdd:PRK06019 237 AEELDYVGVLAVEFFVTGDGELLVNEIAPRPHNSGHWTIEACSTSQFEQHLRAILGLPLGT-----TRLLSPAVMVNLLG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 398365279 324 DKHTKDKEletcERALATPGSSVYLYGK-ESRPNRKVGHINIIASSMAECEQRL 376
Cdd:PRK06019 312 DDWLEPRW----DALLALPGAHLHLYGKaEARPGRKMGHVTVLGDDVEALLAKL 361
|
|
| PurE |
COG0041 |
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ... |
403-563 |
3.09e-97 |
|
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439811 Cd Length: 161 Bit Score: 292.73 E-value: 3.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 403 PLVGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLP 482
Cdd:COG0041 1 PKVGIIMGSDSDWPTMKKAAKILDEFGIPYEVRVVSAHRTPDRLFEYAKTAEERGLKVIIAGAGGAAHLPGMVAAKTTLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 483 VIGVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEVLVKAQKLETV 562
Cdd:COG0041 81 VIGVPVKSKALDGLDSLLSIVQMPPGVPVATVAIGGAKNAALLAAQILALKDPELAEKLKAYREEQTEKVLAKDEELQEK 160
|
.
gi 398365279 563 G 563
Cdd:COG0041 161 L 161
|
|
| AIRC |
pfam00731 |
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ... |
405-551 |
7.43e-87 |
|
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 459917 Cd Length: 147 Bit Score: 265.39 E-value: 7.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 405 VGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLPVI 484
Cdd:pfam00731 1 VGIIMGSDSDLPVMKKAAKILKEFGIPYEVRVVSAHRTPERLLEYAKEAEERGLKVIIAGAGGAAHLPGMVAALTTLPVI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398365279 485 GVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEE 551
Cdd:pfam00731 81 GVPVKSSALDGLDSLLSIVQMPSGVPVATVAIGGAKNAALLAAQILALSDPELAEKLKEYREEMAEK 147
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
115-284 |
3.17e-86 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 264.89 E-value: 3.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 115 KNGIAVTQSVPVEQASEtsLLNVGRDLGFPFVLKSRTLAYDGRGNFVVKNKEMIPEALEVLKDRPLYAEKWAPFTKELAV 194
Cdd:pfam02222 2 KLGLPTPRFMAAESLEE--LIEAGQELGYPCVVKARRGGYDGKGQYVVRSEADLPQAWEELGDGPVIVEEFVPFDRELSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 195 MIVRSVNGLVFSYPIVETIHKDNICDLCYAPARVPDSVQLKAKLLAENAIKSFPGCGIFGVEMFYLETGELLINEIAPRP 274
Cdd:pfam02222 80 LVVRSVDGETAFYPVVETIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGDLLINELAPRP 159
|
170
....*....|
gi 398365279 275 HNSGHYTIDA 284
Cdd:pfam02222 160 HNSGHYTLDG 169
|
|
| purE |
TIGR01162 |
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ... |
405-560 |
3.94e-79 |
|
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273474 Cd Length: 156 Bit Score: 245.99 E-value: 3.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 405 VGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLPVI 484
Cdd:TIGR01162 1 VGIIMGSDSDLPTMKKAADILEEFGIPYELRVVSAHRTPELMLEYAKTAEERGIKVIIAGAGGAAHLPGMVAALTPLPVI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398365279 485 GVPVKGSCLDGVDSLHSIVQMPRGVPVATVAINNSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEVLVKAQKLE 560
Cdd:TIGR01162 81 GVPVPSKALSGLDSLLSIVQMPSGVPVATVAIGNAGNAALLAAQILGIKDPELAEKLKEYRENQKEEVLKKNKKLE 156
|
|
| AIRC |
smart01001 |
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ... |
403-552 |
2.43e-76 |
|
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 214965 Cd Length: 152 Bit Score: 238.59 E-value: 2.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 403 PLVGIIMGSDSDLPVMSAACAVLKDFGVPFEVTIVSAHRTPHRMSAYAISASKRGIKTIIAGAGGAAHLPGMVAAMTPLP 482
Cdd:smart01001 1 PLVGIIMGSTSDLPVMEEAAKTLEEFGIPYEVGVASAHRTPDRLFEYAKEAEDRGIKVIIAGAGGAAHLPGVVAALTTLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365279 483 VIGVPVKGSCLDGVDSLHSIVQMPRGVPVATVAIN--NSTNAALLAVRLLGAYDSSYTTKMEQFLLKQEEEV 552
Cdd:smart01001 81 VIGVPVSSGYLGGLDSLLSIVQMPSGIPVATVAIGidGAFNAALLAAQILALNDPELAAKLAAYRINQTEEV 152
|
|
| PurT |
COG0027 |
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide ... |
3-360 |
3.56e-25 |
|
Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) [Nucleotide transport and metabolism]; Formate-dependent phosphoribosylglycinamide formyltransferase (GAR transformylase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439798 [Multi-domain] Cd Length: 393 Bit Score: 107.52 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 3 SRTVGILGGGQLGRMIVEAANRLNIKTVILDA-ENSPAKQISNSNdHVngsfSNPLD-------IEKlaEKCDVLTIEIE 74
Cdd:COG0027 12 ATKVMLLGSGELGKEVAIELQRLGVEVIAVDRyANAPAMQVAHRS-YV----IDMLDgdalralIER--EKPDFIVPEIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 75 HVDVPTLKNLQVKhpKLKIYPSPETIRLIQDKyiqkehlikNGI----AVTQSVPVEQ----ASETSLLNVGRDLGFPFV 146
Cdd:COG0027 85 AIATDALVELEAE--GFRVVPTARAVRLTMNR---------EGIrrlaAEELGLPTSPyrfaDSLEELRAAVEEIGYPCV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 147 LKSrTLAYDGRGNFVVKNKEMIPEALEvlkdrplYA-------------EKWAPFTKELAVMIVRSVNGLV-FSYPI--- 209
Cdd:COG0027 154 VKP-VMSSSGKGQSVVRSPADIEAAWE-------YAqeggrggagrvivEGFVDFDYEITLLTVRAVDGPThFCEPIghr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 210 ------VETIHkdnicdlcyaPARVPDSVQLKAKLLAENAIKSFPGCGIFGVEMFYleTG-ELLINEIAPRPHNSGhyti 282
Cdd:COG0027 226 qedgdyRESWQ----------PQPMSEAALAKAQEIAKKVTDALGGRGIFGVELFV--KGdEVYFSEVSPRPHDTG---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 283 daCVT------SQFEAHLRSILDLPMPkNFTSFSTITTNAImlnvLGDKHTKDKELETCERALATPGSSVYLYGK-ESRP 355
Cdd:COG0027 290 --MVTlisqdlSEFALHARAILGLPVP-EIRLVGPAASAVI----LAEGESWAPAFDGLAEALAVPGTDLRLFGKpEAYG 362
|
....*
gi 398365279 356 NRKVG 360
Cdd:COG0027 363 RRRMG 367
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
3-360 |
3.15e-24 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 104.83 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 3 SRTVGILGGGQLGRMIVEAANRLNIKTVILDA-ENSPAKQISNSNdHVnGSFSNPLDIEKL--AEKCDVLTIEIEHVDVP 79
Cdd:PRK09288 12 ATRVMLLGSGELGKEVAIEAQRLGVEVIAVDRyANAPAMQVAHRS-HV-IDMLDGDALRAVieREKPDYIVPEIEAIATD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 80 TLKNLQVKHpkLKIYPSPETIRLIQDKyiqkeHLIKNGIAVTQSVPVEQ----ASETSLLNVGRDLGFPFVLK----Srt 151
Cdd:PRK09288 90 ALVELEKEG--FNVVPTARATRLTMNR-----EGIRRLAAEELGLPTSPyrfaDSLEELRAAVEEIGYPCVVKpvmsS-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 152 layDGRGNFVVKNKEMIPEALEvlkdrplYA-------------EKWAPFTKELAVMIVRSVN-GLVFSYPI-------- 209
Cdd:PRK09288 161 ---SGKGQSVVRSPEDIEKAWE-------YAqeggrggagrvivEEFIDFDYEITLLTVRAVDgGTHFCAPIghrqedgd 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 210 -VETIHkdnicdlcyaPARVPDSVQLKAKLLAENAIKSFPGCGIFGVEMFyLETGELLINEIAPRPHNSGhytidaCVT- 287
Cdd:PRK09288 231 yRESWQ----------PQPMSPAALEEAQEIAKKVTDALGGRGLFGVELF-VKGDEVYFSEVSPRPHDTG------MVTl 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398365279 288 -----SQFEAHLRSILDLPMPkNFTSFSTITTNAImlnvLGDKHTKDKELETCERALATPGSSVYLYGK-ESRPNRKVG 360
Cdd:PRK09288 294 isqnlSEFELHARAILGLPIP-DIRLYSPAASAVI----LAEGESANPSFDGLAEALAVPGTDVRLFGKpEIRGGRRMG 367
|
|
| PurK_C |
pfam17769 |
Phosphoribosylaminoimidazole carboxylase C-terminal domain; This entry represents the ... |
316-375 |
9.63e-18 |
|
Phosphoribosylaminoimidazole carboxylase C-terminal domain; This entry represents the C-terminal domain of the PurK enzyme.
Pssm-ID: 436029 [Multi-domain] Cd Length: 56 Bit Score: 77.22 E-value: 9.63e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398365279 316 AIMLNVLGDKHTKDkeletCERALATPGSSVYLYGK-ESRPNRKVGHINIIASSMAECEQR 375
Cdd:pfam17769 1 AVMVNLLGEELGEG-----LEELLAIPGAHLHLYGKeEARPGRKMGHVTVVGDDLEELLER 56
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
94-275 |
1.05e-16 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 80.30 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 94 YPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASEtsLLNVGRDLGFPFVLKSRTLAyDGRGNFVVKNKEMIPEALE 173
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEE--ALAFAEEIGYPVVVKPADGA-GSRGVRVVRDEEELEAALA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 174 VLK--------DRPLYAEKWAPfTKELavmivrSVNGLVF--------------SYP-IVETIHkdnicdlcYAPARVPD 230
Cdd:COG0439 120 EARaeakagspNGEVLVEEFLE-GREY------SVEGLVRdgevvvcsitrkhqKPPyFVELGH--------EAPSPLPE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 398365279 231 SVQLKAKLLAENAIKSFP-GCGIFGVEMFYLETGELLINEIAPRPH 275
Cdd:COG0439 185 ELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINARLG 230
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
105-270 |
1.19e-08 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 56.65 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 105 DKYIQKEHLIKNGIAVTQSVPVEQASETSLLNVGRDLGFPFVLKSrtlAYDG--RGNFVVKNKEMIPEALEVLK--DRPL 180
Cdd:COG1181 95 DKALTKRVLAAAGLPTPPYVVLRRGELADLEAIEEELGLPLFVKP---AREGssVGVSKVKNAEELAAALEEAFkyDDKV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 181 YAEKWAPfTKELAVMIVRSVNGLVFsyPIVETIHKDNICD------------LCyaPARVPDSVQLKAKLLAENAIKSFp 248
Cdd:COG1181 172 LVEEFID-GREVTVGVLGNGGPRAL--PPIEIVPENGFYDyeakytdggteyIC--PARLPEELEERIQELALKAFRAL- 245
|
170 180
....*....|....*....|...
gi 398365279 249 GC-GIFGVEMFYLETGELLINEI 270
Cdd:COG1181 246 GCrGYARVDFRLDEDGEPYLLEV 268
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
95-177 |
4.37e-05 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 45.65 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 95 PSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASETSLLNVGRDLGFPFVLKSRtlayDG---RGNFVVKNKEMIPEA 171
Cdd:PRK12767 101 SSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELQFPLFVKPR----DGsasIGVFKVNDKEELEFL 176
|
....*.
gi 398365279 172 LEVLKD 177
Cdd:PRK12767 177 LEYVPN 182
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
117-274 |
5.18e-05 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 44.61 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 117 GIAVTQSVPVEQA-----SETSLLNVGRDLGFPFVLKSrtlAYDGR--GNFVVKNKEMIPEALEVL--KDRPLYAEKWAP 187
Cdd:pfam07478 6 GLPVVPFVTFTRAdwklnPKEWCAQVEEALGYPVFVKP---ARLGSsvGVSKVESREELQAAIEEAfqYDEKVLVEEGIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 188 fTKELAVMIVRSVNGLVFsyPIVETIHKDNICDlcYA------------PARVPDSVQLKAKLLAENAIKSFPGCGIFGV 255
Cdd:pfam07478 83 -GREIECAVLGNEDPEVS--PVGEIVPSGGFYD--YEakyiddsaqivvPADLEEEQEEQIQELALKAYKALGCRGLARV 157
|
170
....*....|....*....
gi 398365279 256 EMFYLETGELLINEIAPRP 274
Cdd:pfam07478 158 DFFLTEDGEIVLNEVNTIP 176
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
87-197 |
5.87e-04 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 42.42 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 87 KHPKLK-IYPSPETIRLIQDKYIQKEHLIKNGiavtqsVPVEQASETSLLNV------GRDLGFPFVLKSRTlAYDGRGN 159
Cdd:PRK08462 98 SHHNIKfIGPSVEVMALMSDKSKAKEVMKRAG------VPVIPGSDGALKSYeeakkiAKEIGYPVILKAAA-GGGGRGM 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 398365279 160 FVVKNKEMI--------PEALEVLKDRPLYAEKWAPFTKELAVMIV 197
Cdd:PRK08462 171 RVVEDESDLenlylaaeSEALSAFGDGTMYMEKFINNPRHIEVQIL 216
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
16-187 |
6.00e-04 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 41.85 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 16 RMIVEAANRLNIKTVILDAENspakqisnsnDHVNGSFSNPLDIEKLAEKCDVLTIEIehvdVPTLKNL----QVKHPKL 91
Cdd:COG0189 17 KALIEAAQRRGHEVEVIDPDD----------LTLDLGRAPELYRGEDLSEFDAVLPRI----DPPFYGLallrQLEAAGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 92 KIYPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEqaSETSLLNVGRDLGFPFVLKSRTlAYDGRGNFVVKNKEMIPEA 171
Cdd:COG0189 83 PVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTR--DPDDLRAFLEELGGPVVLKPLD-GSGGRGVFLVEDEDALESI 159
|
170
....*....|....*....
gi 398365279 172 LEVLK---DRPLYAEKWAP 187
Cdd:COG0189 160 LEALTelgSEPVLVQEFIP 178
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
13-63 |
1.45e-03 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 40.83 E-value: 1.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 398365279 13 QLGRMIVEAANRLNIKTVILDAENSPAKQISNSND----HVNGSFSNPLDIEKLA 63
Cdd:cd19968 16 YMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENaiaqGVDGIIVSPIDVKALV 70
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
20-60 |
1.82e-03 |
|
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380546 [Multi-domain] Cd Length: 268 Bit Score: 40.36 E-value: 1.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 398365279 20 EAANRLNIKTVILDAENSPAKQISNSNDHVNGSFS----NPLDIE 60
Cdd:cd06323 23 AEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDalliNPTDSD 67
|
|
| PGDH_like_3 |
cd12174 |
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
4-76 |
2.92e-03 |
|
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.
Pssm-ID: 240651 [Multi-domain] Cd Length: 305 Bit Score: 39.85 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365279 4 RTVGILGGGQLGRMIVEAANRLNIKTVILDAENSP--AKQISNSNDHVNgsfsnplDIEKLAEKCDVLTIeieHV 76
Cdd:cd12174 136 KTLGVIGLGNIGRLVANAALALGMKVIGYDPYLSVeaAWKLSVEVQRVT-------SLEELLATADYITL---HV 200
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
93-173 |
6.21e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 39.40 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 93 IYPSPETIRLIQDKYIQKEHLIKNGIAVtqsVP--------VEQASEtsllnVGRDLGFPFVLKSrTLAYDGRGNFVVKN 164
Cdd:PRK08591 103 IGPSAETIRLMGDKVTAKATMKKAGVPV---VPgsdgpvddEEEALA-----IAKEIGYPVIIKA-TAGGGGRGMRVVRT 173
|
....*....
gi 398365279 165 KEMIPEALE 173
Cdd:PRK08591 174 EAELEKAFS 182
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
94-177 |
9.76e-03 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 38.37 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365279 94 YPSPETIRLIQDKYIQKEHLIKNGIAVTQSVPVEQASETSllNVGRDLGFPFVLK-SRTLAYD------GRGNFVVKNKE 166
Cdd:COG3919 106 YPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLD--ALAEDLGFPVVVKpADSVGYDelsfpgKKKVFYVDDRE 183
|
90
....*....|.
gi 398365279 167 mipEALEVLKD 177
Cdd:COG3919 184 ---ELLALLRR 191
|
|
| |
