|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
5-655 |
0e+00 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 968.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 5 ARAFTAVLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLADYALVIFVSPNAIDRALAQYGAIWPN 84
Cdd:PRK06975 1 ARAFTVVVTRPDGQSAALAAQLAAAGLDVLDFPLLDIAPVADDAPLRAALARLSDYALVVFVSPNAVDRALARLDAIWPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 85 ALPVGVVGPGSVAALERHGIAAPAHRVIAPQAPADGGVPHYDSESLFACIEAVFGgvqALTGKRVLIVRGDGGREWLAER 164
Cdd:PRK06975 81 ALPVAVVGPGSVAALARHGIAAPAHRVIAPDAPADGGEARYDSEALFAEIDAAFG---ALAGKRVLIVRGDGGREWLAER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 165 LREAGADVTLVAAYRRVVPEPRVGAWERVHALLHGEPHAWLVTSSEGVRNLHELARAHLNDAEIDALKHALLVTPHPRIE 244
Cdd:PRK06975 158 LREAGAEVELVEAYRRVVPEPSIGAWERVHALLSGAPHAWLLTSSEAVRNLDELARAHLNPAEIDALKHAPLVAPHARIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 245 QTARSLGFDRITLTGAGDERIVRAFRTMADEAVQPATAAPVTKRMTDTNDSKSVA---SQPAAASAPPSRPAYMASEPPA 321
Cdd:PRK06975 238 EQARALGFDRITLTGAGDERIVRAFLTWADAAAQPATAAPAPSRMTDTNDSKSVTsqpAAAAAAPAPPPNPPATPPEPPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 322 RRG-GSAVLWFVVVVLGCAAGVGGYALNRKIDRLDGTFVTRQKALDAQTAETRLKTEQALASTHQVDTQLAQLDGKLADA 400
Cdd:PRK06975 318 RRGrGSAALWFVVVVLACAAAVGGYALNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 401 QSAQQALQQQYQDLSRNRDAWMLEEVDQMLSSASQQLQLTGNTQLALIALQNADARLATSQSAQAVTVRKALALDIEKLK 480
Cdd:PRK06975 398 QSAQQALEQQYQDLSRNRDDWMIAEVEQMLSSASQQLQLTGNVQLALIALQNADARLATSDSPQAVAVRKAIAQDIERLK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 481 AAPAADLTGLAIKLDDAIAKIDALPLSGEAIVPH----EAPKAAPADAASSAVAGEPRWKVWWHDFSAGLGQQLKGLVQV 556
Cdd:PRK06975 478 AAPSADLTGLAIKLDDAIAKIDALPLSGEALPPHatmaAAPAAAAAAAAAAAAAGEPRWKAWWRRFSAGVGEQLKQLVQV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 557 RRIDNADAMLASPDQGYFVRENVKLRLLTARLSLLARNDSAMKADLHAAQASLGKYFDQASKDTQTVEDLLKQVDGASLT 636
Cdd:PRK06975 558 RRIDNADAMLLSPDQGYFLRENLKLRLLNARLSLLSRNDAAFKSDLHAAQAALARYFDTASKDTQTVQDLLKQVDAASLT 637
|
650
....*....|....*....
gi 1834749349 637 VAVPNLNTSLNAVQQFKSR 655
Cdd:PRK06975 638 VAVPNLNTSLAAVQQFKKR 656
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
316-655 |
1.42e-74 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 243.72 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 316 ASEPPARrggsAVLWFVVVVLGCAAGVGGYALNRKIDRLDGT---FVTRQKALDAQTAETRLKTEQALASTHQVDTQLAQ 392
Cdd:COG2959 24 APAPPAL----WLALLALLLALAAGGGGYYLGWQQLQQQQAElaqLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 393 LDGKLADAQSAQQALQQQYQDLSR-NRDAWMLEEVDQMLSSASQQLQLTGNTQLALIALQNADARLATSQSAQAVTVRKA 471
Cdd:COG2959 100 LEQRLAELQQQLAALQQLLQSLSGsSRDDWLLAEAEYLLRLAGQQLQLEGDVKTALAALQSADARLARLNDPSLLPVRRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 472 LALDIEKLKAAPAADLTGLAIKLDDAIAKIDALPLSGEaivpheAPKAAPADAASSAVAGEPRWkvWWHDFSAGLGQQLK 551
Cdd:COG2959 180 IARDIARLRAVPQVDIDGIALRLDALANQVDNLPLASD------VAPAAAPAAAAAEASASISD--WQQNLWEKSWDELR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 552 GLVQVRRIDNADAMLASPDQGYFVRENVKLRLLTARLSLLARNDSAMKADLHAAQASLGKYFDQASKDTQTVEDLLKQVD 631
Cdd:COG2959 252 DLVRIRRRDQPVAPLLSPEQAFFLRENLRLRLLNARLALLRRQEELYQQSLAAAQTWLRRYFDTDSPATQAFLAELDQLQ 331
|
330 340
....*....|....*....|....
gi 1834749349 632 GASLTVAVPNLNTSLNAVQQFKSR 655
Cdd:COG2959 332 AQSISVELPDILESLAALRKLLAQ 355
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
11-268 |
1.83e-52 |
|
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole (linear) to uroporphyrinogen-III, the fourth step in the biosynthesis of heme. This ubiquitous enzyme is present in eukaryotes, bacteria and archaea. Mutations in the human uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria, a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 119440 [Multi-domain] Cd Length: 239 Bit Score: 180.58 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 11 VLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPaPLDAAFATLADYALVIFVSPNAID---RALAQYGAIWPNALP 87
Cdd:cd06578 2 LVTRPRPQADELAALLEALGAEVLELPLIEIEPLDDA-ELDAALADLDEYDWLIFTSPNAVEaffEALEELGLRALAGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 88 VGVVGPGSVAALERHGIAApahrVIAPQApadggvphYDSESLFACIEAvfggvQALTGKRVLIVRGDGGREWLAERLRE 167
Cdd:cd06578 81 IAAVGPKTAEALREAGLTA----DFVPEE--------GDSEGLLELLEL-----QDGKGKRILRPRGGRAREDLAEALRE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 168 AGADVTLVAAYRRVVPEPRVGAWErvhALLHGEPHAWLVTSSEGVRNLHELARAHLNdaeiDALKHALLVTPHPRIEQTA 247
Cdd:cd06578 144 RGAEVDEVEVYRTVPPDLDAELLE---LLEEGAIDAVLFTSPSTVRNLLELLGKEGR----ALLKNVKIAAIGPRTAEAL 216
|
250 260
....*....|....*....|..
gi 1834749349 248 RSLGFDR-ITLTGAGDERIVRA 268
Cdd:cd06578 217 RELGLKVvIVAESPTLEALLEA 238
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
21-255 |
3.14e-38 |
|
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 426866 [Multi-domain] Cd Length: 230 Bit Score: 141.30 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 21 ALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLADYALVIFVSPNAIDR---ALAQYGAI--WPNALPVGVVGPGS 95
Cdd:pfam02602 1 ELAELLEALGAEPLELPLIEIVPPEDRAELDEALKDLGEYDWLIFTSANAVRAffeALKLEGEDlrALANIKIAAVGPKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 96 VAALERHGIAApahrVIAPQAPadggvphYDSESLFACIeavfggVQALTGKRVLIVRGDGGREWLAERLREAGADVTLV 175
Cdd:pfam02602 81 ARALREAGLTP----DFVPSEE-------GTAEGLAEEL------AELLAGKRVLLLRGNIGRDDLAEALRERGAEVTEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 176 AAYRRVVPEPRVGAWERvhALLHGEPHAWLVTSSEGVRNLHELARahlnDAEIDALKHALLVTPHPRIEQTARSLGFDRI 255
Cdd:pfam02602 144 VVYRTVPPEELPEELRE--ALKDGEIDAVTFTSPSTVRNLLELLK----DEGLDWLKSVKAAAIGPTTAEALKELGLKVD 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
5-655 |
0e+00 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 968.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 5 ARAFTAVLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLADYALVIFVSPNAIDRALAQYGAIWPN 84
Cdd:PRK06975 1 ARAFTVVVTRPDGQSAALAAQLAAAGLDVLDFPLLDIAPVADDAPLRAALARLSDYALVVFVSPNAVDRALARLDAIWPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 85 ALPVGVVGPGSVAALERHGIAAPAHRVIAPQAPADGGVPHYDSESLFACIEAVFGgvqALTGKRVLIVRGDGGREWLAER 164
Cdd:PRK06975 81 ALPVAVVGPGSVAALARHGIAAPAHRVIAPDAPADGGEARYDSEALFAEIDAAFG---ALAGKRVLIVRGDGGREWLAER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 165 LREAGADVTLVAAYRRVVPEPRVGAWERVHALLHGEPHAWLVTSSEGVRNLHELARAHLNDAEIDALKHALLVTPHPRIE 244
Cdd:PRK06975 158 LREAGAEVELVEAYRRVVPEPSIGAWERVHALLSGAPHAWLLTSSEAVRNLDELARAHLNPAEIDALKHAPLVAPHARIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 245 QTARSLGFDRITLTGAGDERIVRAFRTMADEAVQPATAAPVTKRMTDTNDSKSVA---SQPAAASAPPSRPAYMASEPPA 321
Cdd:PRK06975 238 EQARALGFDRITLTGAGDERIVRAFLTWADAAAQPATAAPAPSRMTDTNDSKSVTsqpAAAAAAPAPPPNPPATPPEPPA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 322 RRG-GSAVLWFVVVVLGCAAGVGGYALNRKIDRLDGTFVTRQKALDAQTAETRLKTEQALASTHQVDTQLAQLDGKLADA 400
Cdd:PRK06975 318 RRGrGSAALWFVVVVLACAAAVGGYALNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 401 QSAQQALQQQYQDLSRNRDAWMLEEVDQMLSSASQQLQLTGNTQLALIALQNADARLATSQSAQAVTVRKALALDIEKLK 480
Cdd:PRK06975 398 QSAQQALEQQYQDLSRNRDDWMIAEVEQMLSSASQQLQLTGNVQLALIALQNADARLATSDSPQAVAVRKAIAQDIERLK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 481 AAPAADLTGLAIKLDDAIAKIDALPLSGEAIVPH----EAPKAAPADAASSAVAGEPRWKVWWHDFSAGLGQQLKGLVQV 556
Cdd:PRK06975 478 AAPSADLTGLAIKLDDAIAKIDALPLSGEALPPHatmaAAPAAAAAAAAAAAAAGEPRWKAWWRRFSAGVGEQLKQLVQV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 557 RRIDNADAMLASPDQGYFVRENVKLRLLTARLSLLARNDSAMKADLHAAQASLGKYFDQASKDTQTVEDLLKQVDGASLT 636
Cdd:PRK06975 558 RRIDNADAMLLSPDQGYFLRENLKLRLLNARLSLLSRNDAAFKSDLHAAQAALARYFDTASKDTQTVQDLLKQVDAASLT 637
|
650
....*....|....*....
gi 1834749349 637 VAVPNLNTSLNAVQQFKSR 655
Cdd:PRK06975 638 VAVPNLNTSLAAVQQFKKR 656
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
316-655 |
1.42e-74 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 243.72 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 316 ASEPPARrggsAVLWFVVVVLGCAAGVGGYALNRKIDRLDGT---FVTRQKALDAQTAETRLKTEQALASTHQVDTQLAQ 392
Cdd:COG2959 24 APAPPAL----WLALLALLLALAAGGGGYYLGWQQLQQQQAElaqLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 393 LDGKLADAQSAQQALQQQYQDLSR-NRDAWMLEEVDQMLSSASQQLQLTGNTQLALIALQNADARLATSQSAQAVTVRKA 471
Cdd:COG2959 100 LEQRLAELQQQLAALQQLLQSLSGsSRDDWLLAEAEYLLRLAGQQLQLEGDVKTALAALQSADARLARLNDPSLLPVRRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 472 LALDIEKLKAAPAADLTGLAIKLDDAIAKIDALPLSGEaivpheAPKAAPADAASSAVAGEPRWkvWWHDFSAGLGQQLK 551
Cdd:COG2959 180 IARDIARLRAVPQVDIDGIALRLDALANQVDNLPLASD------VAPAAAPAAAAAEASASISD--WQQNLWEKSWDELR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 552 GLVQVRRIDNADAMLASPDQGYFVRENVKLRLLTARLSLLARNDSAMKADLHAAQASLGKYFDQASKDTQTVEDLLKQVD 631
Cdd:COG2959 252 DLVRIRRRDQPVAPLLSPEQAFFLRENLRLRLLNARLALLRRQEELYQQSLAAAQTWLRRYFDTDSPATQAFLAELDQLQ 331
|
330 340
....*....|....*....|....
gi 1834749349 632 GASLTVAVPNLNTSLNAVQQFKSR 655
Cdd:COG2959 332 AQSISVELPDILESLAALRKLLAQ 355
|
|
| HemD |
COG1587 |
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III ... |
11-255 |
3.96e-57 |
|
Uroporphyrinogen-III synthase [Coenzyme transport and metabolism]; Uroporphyrinogen-III synthase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 441195 Cd Length: 229 Bit Score: 192.81 E-value: 3.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 11 VLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLADYALVIFVSPNAIDRALAQYGAIWP--NALPV 88
Cdd:COG1587 7 LVTRPAPQAEELAALLEALGAEVVELPLIEIEPLPDPAALRAALERLGDYDWVIFTSANAVRAFFEALEELGLrlAGLKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 89 GVVGPGSVAALERHGIAApahrVIAPqapadggvPHYDSESLFACIeavfggvQALTGKRVLIVRGDGGREWLAERLREA 168
Cdd:COG1587 87 AAVGPKTAAALRAAGLKV----DLVP--------EGFTSEGLLELL-------QALAGKRVLIPRGDGGREDLAETLRAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 169 GADVTLVAAYRRVVPEPRVGAWERvhALLHGEPHAWLVTSSEGVRNLHELARahlnDAEIDALKHALLVTPHPRIEQTAR 248
Cdd:COG1587 148 GAEVDEVEVYRTVPPDDLPEELLE--ALAAGEIDAVLFTSPSTVRNLLELAP----DAGLAALARVRIAAIGPRTAEAAR 221
|
....*..
gi 1834749349 249 SLGFDRI 255
Cdd:COG1587 222 ELGLKVV 228
|
|
| HemD |
cd06578 |
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole ... |
11-268 |
1.83e-52 |
|
Uroporphyrinogen-III synthase (HemD) catalyzes the asymmetrical cyclization of tetrapyrrole (linear) to uroporphyrinogen-III, the fourth step in the biosynthesis of heme. This ubiquitous enzyme is present in eukaryotes, bacteria and archaea. Mutations in the human uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria, a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 119440 [Multi-domain] Cd Length: 239 Bit Score: 180.58 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 11 VLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPaPLDAAFATLADYALVIFVSPNAID---RALAQYGAIWPNALP 87
Cdd:cd06578 2 LVTRPRPQADELAALLEALGAEVLELPLIEIEPLDDA-ELDAALADLDEYDWLIFTSPNAVEaffEALEELGLRALAGLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 88 VGVVGPGSVAALERHGIAApahrVIAPQApadggvphYDSESLFACIEAvfggvQALTGKRVLIVRGDGGREWLAERLRE 167
Cdd:cd06578 81 IAAVGPKTAEALREAGLTA----DFVPEE--------GDSEGLLELLEL-----QDGKGKRILRPRGGRAREDLAEALRE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 168 AGADVTLVAAYRRVVPEPRVGAWErvhALLHGEPHAWLVTSSEGVRNLHELARAHLNdaeiDALKHALLVTPHPRIEQTA 247
Cdd:cd06578 144 RGAEVDEVEVYRTVPPDLDAELLE---LLEEGAIDAVLFTSPSTVRNLLELLGKEGR----ALLKNVKIAAIGPRTAEAL 216
|
250 260
....*....|....*....|..
gi 1834749349 248 RSLGFDR-ITLTGAGDERIVRA 268
Cdd:cd06578 217 RELGLKVvIVAESPTLEALLEA 238
|
|
| hemD |
PRK05928 |
uroporphyrinogen-III synthase; Reviewed |
9-255 |
3.85e-39 |
|
uroporphyrinogen-III synthase; Reviewed
Pssm-ID: 235647 Cd Length: 249 Bit Score: 144.73 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 9 TAVLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDpAPLDAAFATLADYALVIFVSPNAIDRALAQY---GAIWPNA 85
Cdd:PRK05928 3 KILVTRPSPKAEELVELLRELGFVALHFPLIEIEPGRQ-LPQLAAQLAALGADWVIFTSKNAVEFLLSALkkkKLKWPKN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 86 LPVGVVGPGSVAALERHGIAApahrVIAPQApadggvphYDSESLFACIEAvfggvQALTGKRVLIVRGDGGREWLAERL 165
Cdd:PRK05928 82 KKYAAIGEKTALALKKLGGKV----VFVPED--------GESSELLLELPE-----LLLKGKRVLYLRGNGGREVLGDTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 166 REAGADVTLVAAYRRVVPEPRVGawERVHALLHGEPHAWLVTSSEGVRNLHELARAHlndAEIDALKHALLVTPHPRIEQ 245
Cdd:PRK05928 145 EERGAEVDECEVYERVPPKLDGA--ELLARLQSGEVDAVIFTSPSTVRAFFSLAPEL---GRREWLLSCKAVVIGERTAE 219
|
250
....*....|
gi 1834749349 246 TARSLGFDRI 255
Cdd:PRK05928 220 ALRELGIKVI 229
|
|
| HEM4 |
pfam02602 |
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD ... |
21-255 |
3.14e-38 |
|
Uroporphyrinogen-III synthase HemD; This family consists of uroporphyrinogen-III synthase HemD EC:4.2.1.75 also known as Hydroxymethylbilane hydrolyase (cyclizing) from eukaryotes, bacteria and archaea. This enzyme catalyzes the reaction: Hydroxymethylbilane <=> uroporphyrinogen-III + H(2)O. Some members of this family are multi-functional proteins possessing other enzyme activities related to porphyrin biosynthesis, such as Swiss:Q59294 with pfam00590, however the aligned region corresponds with the uroporphyrinogen-III synthase EC:4.2.1.75 activity only. Uroporphyrinogen-III synthase is the fourth enzyme in the heme pathway. Mutant forms of the Uroporphyrinogen-III synthase gene cause congenital erythropoietic porphyria in humans a recessive inborn error of metabolism also known as Gunther disease.
Pssm-ID: 426866 [Multi-domain] Cd Length: 230 Bit Score: 141.30 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 21 ALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLADYALVIFVSPNAIDR---ALAQYGAI--WPNALPVGVVGPGS 95
Cdd:pfam02602 1 ELAELLEALGAEPLELPLIEIVPPEDRAELDEALKDLGEYDWLIFTSANAVRAffeALKLEGEDlrALANIKIAAVGPKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 96 VAALERHGIAApahrVIAPQAPadggvphYDSESLFACIeavfggVQALTGKRVLIVRGDGGREWLAERLREAGADVTLV 175
Cdd:pfam02602 81 ARALREAGLTP----DFVPSEE-------GTAEGLAEEL------AELLAGKRVLLLRGNIGRDDLAEALRERGAEVTEV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 176 AAYRRVVPEPRVGAWERvhALLHGEPHAWLVTSSEGVRNLHELARahlnDAEIDALKHALLVTPHPRIEQTARSLGFDRI 255
Cdd:pfam02602 144 VVYRTVPPEELPEELRE--ALKDGEIDAVTFTSPSTVRNLLELLK----DEGLDWLKSVKAAAIGPTTAEALKELGLKVD 217
|
|
| HemX |
pfam04375 |
HemX, putative uroporphyrinogen-III C-methyltransferase; This is a family of bacterial ... |
418-655 |
2.77e-33 |
|
HemX, putative uroporphyrinogen-III C-methyltransferase; This is a family of bacterial putative uroporphyrinogen-III C-methyltransferase proteins. It forms one of the members of a complex of proteins involved in the biogenesis of the inner membrane in E.coli. Uroporphorphyrin-III C-methyltransferase (HemX) is a single spanning inner membrane protein that regulates the activity of NAD(P)H:glutamyl-tRNA reductase (HemA) in the tetrapyrrole biosynthesis pathway.
Pssm-ID: 427905 Cd Length: 236 Bit Score: 127.84 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 418 RDAWMLEEVDQMLSSASQQLQLTGNTQLALIALQNADARLATSQSAQAVTVRKALALDIEKLKAAPAADLTGLAIKLDDA 497
Cdd:pfam04375 2 RKDWLLAEADFLLKLAGRKLWLDQDVDTALALLKGADAVLAEQNDPSLIAVRRAIARDIEALRAVPQVDRDGIILRLNQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 498 IAKIDALPLSGEAIVPHEAPKAAPADAAssavaGEPRWKVW----WHDFsaglgqqLKGLVQVRRIDNADAMLASPDQGY 573
Cdd:pfam04375 82 AEQVDNLPLADNNFDESPMDADNAELSD-----SVSDWRQNleksAKSF-------MSHFIRIRRRDQSIKPLLAPNQDI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 574 FVRENVKLRLLTARLSLLARNDSAMKADLHAAQASLGKYFDQASKDTQTVEDLLKQVDGASLTVAVPNLNTSLNAVQQFK 653
Cdd:pfam04375 150 YLRENIRLRLEIAILAVPRQQNEVYKQSLETVQTWVRAYFDTDDPATQAFLKELDELAEQPISVDVPDQLQSLPALEKLL 229
|
..
gi 1834749349 654 SR 655
Cdd:pfam04375 230 NR 231
|
|
| PRK05752 |
PRK05752 |
uroporphyrinogen-III synthase; Validated |
12-255 |
2.49e-29 |
|
uroporphyrinogen-III synthase; Validated
Pssm-ID: 235590 Cd Length: 255 Bit Score: 117.13 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 12 LTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLADYALVIFVSPNAIDRALAQYGAIWPN--ALPVG 89
Cdd:PRK05752 8 LTRPAEECAALAASLAEAGIFSSSLPLLAIEPLPETPEQRALLLELDRYCAVIVVSKPAARLGLELLDRYWPQppQQPWF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 90 VVGPGSVAALERHGIAApahrviapQAPADGGvphyDSESLFACieAVFGGVQALTGKRVLIVRGDGGREWLAERLREAG 169
Cdd:PRK05752 88 SVGAATAAILQDYGLDV--------SYPEQGD----DSEALLAL--PALRQALAVPDPRVLIMRGEGGRELLAERLREQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 170 ADVTLVAAYRRVVPE------PRVGAWERVHALlhgephawLVTSSEGVRNLHELArahlnDAEIDALKHALLVTPHPRI 243
Cdd:PRK05752 154 ASVDYLELYRRCLPDypagtlLQRVEAERLNGL--------VVSSGQGFEHLQQLA-----GADWPELARLPLFVPSPRV 220
|
250
....*....|..
gi 1834749349 244 EQTARSLGFDRI 255
Cdd:PRK05752 221 AEQARAAGAQTV 232
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
318-641 |
1.58e-09 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 60.11 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 318 EPPARRGGSAVLWFVVVVLGCAAGVGGYalnrkidrldgtFVTRQKAlDAQTAETRLKTEQALASTHQVDTQLAQLDGKL 397
Cdd:PRK10920 28 EKKSKNRTGLVLSAVAIAIALAAGAGLY------------YHGKQQA-QNQTATNDALANQLTALQKAQESQKQELEGIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 398 ADAQSAQQALQQQYQDLSR-------------NRDA--WMLEEVDQMLSSASQQLQLTGNTQLALIALQNADARLATSQS 462
Cdd:PRK10920 95 KQQAKALDQANRQQAALAKqldelqqkvatisGSDAktWLLAQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMND 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 463 AQAVTVRKALALDIEKLKAAPAADLTGLAIKLDDAIAKIDALPLSGeaivpHEAPKAAPADAASSAVAGEPRWKV----W 538
Cdd:PRK10920 175 PSLITVRRAITDDIATLSAVSQVDYDGIILKLNQLSNQVDNLRLAD-----NDSDGSPMDSDSEELSSSLSEWRQnlskS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 539 WHDFsaglgqqLKGLVQVRRIDNADAMLASPDQGYFVRENVKLRLLTARLSLLARNDSAMKADLHAAQASLGKYFDQASK 618
Cdd:PRK10920 250 WHNF-------MDNFITIRRRDDTAEPLLAPNQDVYLRENIRSRLLVAAQAVPRHQEETYKQSLENVSTWVRAYFDTDDA 322
|
330 340
....*....|....*....|...
gi 1834749349 619 DTQTVEDLLKQVDGASLTVAVPN 641
Cdd:PRK10920 323 TTKAFLDEVDQLSQQNISMDLPE 345
|
|
| PRK08811 |
PRK08811 |
uroporphyrinogen-III synthase; Validated |
2-255 |
1.76e-08 |
|
uroporphyrinogen-III synthase; Validated
Pssm-ID: 181558 Cd Length: 266 Bit Score: 55.99 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 2 AGGARAFTAVLTRPDGQSGALASQLAEAGCDVLEFPLIDIAPVDDPAPLDAAFATLAdYALVIFVSPNAIDRALAQYGAI 81
Cdd:PRK08811 13 ATADAAWTLISLRPSGEHAPLRRAVARHGGRLLALSPWRLQRLDTAQARDALRQALA-APIVVFTSPAAVRAAHRLLPLQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 82 WPNALPVGVVGPGSVAALERHGIaapaHRVIAPQapadggvpHYDSESLFACIEAvfggvqALTGKRVLIVRGDGGREWL 161
Cdd:PRK08811 92 RPARAHWLSVGEGTARALQACGI----DEVVRPT--------RMDSEGLLALPLA------QAPLQAVGLITAPGGRGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 162 AERLREAGADVTLVAAYRRVVPEPRVgawERVHALLHGEPHAWL-VTSSEGVrnlhELARAHLNDAEIDALKHALLVTPH 240
Cdd:PRK08811 154 APTLQQRGARILRADVYQRVPLRLRA---STLAALSRAAPRSVLaLSSAEAL----TLILQQLPDALRRALQQRPVVASS 226
|
250
....*....|....*
gi 1834749349 241 PRIEQTARSLGFDRI 255
Cdd:PRK08811 227 DRLLDAAHAAGFIHV 241
|
|
| CoaBC |
COG0452 |
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ... |
128-228 |
1.35e-03 |
|
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440221 [Multi-domain] Cd Length: 399 Bit Score: 41.55 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 128 ESLFACIEAVFGGVQALTGKRVLIVRGdGGREW------------------LAERLREAGADVTLVAAYRRVVPEPRVga 189
Cdd:COG0452 169 EEIVEAIEALLAPKKDLAGKKVLITAG-PTREPidpvrfisnrssgkmgyaLAEAAAARGAEVTLVSGPVALPTPAGV-- 245
|
90 100 110
....*....|....*....|....*....|....*....
gi 1834749349 190 wERVHallhgephawlVTSSEgvrNLHELARAHLNDAEI 228
Cdd:COG0452 246 -ERID-----------VESAE---EMLEAVLAAFPDADI 269
|
|
| PRK05579 |
PRK05579 |
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated |
126-177 |
6.40e-03 |
|
bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated
Pssm-ID: 235513 [Multi-domain] Cd Length: 399 Bit Score: 39.35 E-value: 6.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834749349 126 DSESLFACIEAVFGGvQALTGKRVLIVRGdGGRE------------------WLAERLREAGADVTLVAA 177
Cdd:PRK05579 169 EPEEIVAAAERALSP-KDLAGKRVLITAG-PTREpidpvryitnrssgkmgyALARAAARRGADVTLVSG 236
|
|
| |
