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Conserved domains on  [gi|1513459651|gb|RNW01226|]
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uroporphyrinogen-III C-methyltransferase [Enterobacter asburiae]

Protein Classification

uroporphyrinogen-III C-methyltransferase( domain architecture ID 11485097)

uroporphyrinogen-III C-methyltransferase similar to Escherichia coli protein HemX

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
1-398 0e+00

putative uroporphyrinogen III C-methyltransferase; Provisional


:

Pssm-ID: 236795  Cd Length: 390  Bit Score: 607.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651   1 MTEHDKSSAVVEETRETVETTPQPETTEKTAEKKNGsnktsLALSAIAIAIALAAGVGLYGLVKQQGANQTSTSDALVNQ 80
Cdd:PRK10920    1 MTEQEKSSAVVEETREAVETTSQPVATEKKSKNRTG-----LVLSAVAIAIALAAGAGLYYHGKQQAQNQTATNDALANQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651  81 LTALQKAQETQKTELETVIKQQAAALAEANSKQEELAKQLGDVQQKVATISGTDAKTWLLSQADFLVKLAGRKLWSDQDV 160
Cdd:PRK10920   76 LTALQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 161 TTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVNQLSNQIDNLQLADNNDDDSPMDSDGTEL 240
Cdd:PRK10920  156 TTAAALLKSADASLADMNDPSLITVRRAITDDIATLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDSEEL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 241 SSSLSEWRINLQKSWQNFMDSFITIRRRDETAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEETYKQALDNVSTWVRA 320
Cdd:PRK10920  236 SSSLSEWRQNLSKSWHNFMDNFITIRRRDDTAEPLLAPNQDVYLRENIRSRLLVAAQAVPRHQEETYKQSLENVSTWVRA 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513459651 321 YYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNLLAQPGVPAEPTDgaaPAPAPAPESAPQGE 398
Cdd:PRK10920  316 YFDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQPILEKLMQTRVRNLLAQPAAGATEAK---APQADAPAAAPQGE 390
 
Name Accession Description Interval E-value
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
1-398 0e+00

putative uroporphyrinogen III C-methyltransferase; Provisional


Pssm-ID: 236795  Cd Length: 390  Bit Score: 607.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651   1 MTEHDKSSAVVEETRETVETTPQPETTEKTAEKKNGsnktsLALSAIAIAIALAAGVGLYGLVKQQGANQTSTSDALVNQ 80
Cdd:PRK10920    1 MTEQEKSSAVVEETREAVETTSQPVATEKKSKNRTG-----LVLSAVAIAIALAAGAGLYYHGKQQAQNQTATNDALANQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651  81 LTALQKAQETQKTELETVIKQQAAALAEANSKQEELAKQLGDVQQKVATISGTDAKTWLLSQADFLVKLAGRKLWSDQDV 160
Cdd:PRK10920   76 LTALQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 161 TTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVNQLSNQIDNLQLADNNDDDSPMDSDGTEL 240
Cdd:PRK10920  156 TTAAALLKSADASLADMNDPSLITVRRAITDDIATLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDSEEL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 241 SSSLSEWRINLQKSWQNFMDSFITIRRRDETAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEETYKQALDNVSTWVRA 320
Cdd:PRK10920  236 SSSLSEWRQNLSKSWHNFMDNFITIRRRDDTAEPLLAPNQDVYLRENIRSRLLVAAQAVPRHQEETYKQSLENVSTWVRA 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513459651 321 YYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNLLAQPGVPAEPTDgaaPAPAPAPESAPQGE 398
Cdd:PRK10920  316 YFDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQPILEKLMQTRVRNLLAQPAAGATEAK---APQADAPAAAPQGE 390
HemX pfam04375
HemX, putative uroporphyrinogen-III C-methyltransferase; This is a family of bacterial ...
134-369 1.47e-122

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: 354.34  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 134 DAKTWLLSQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVNQ 213
Cdd:pfam04375   1 DRKDWLLAEADFLLKLAGRKLWLDQDVDTALALLKGADAVLAEQNDPSLIAVRRAIARDIEALRAVPQVDRDGIILRLNQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 214 LSNQIDNLQLADNNDDDSPMDSDGTELSSSLSEWRINLQKSWQNFMDSFITIRRRDETAVPLLAPNQDIYLRENIRSRLL 293
Cdd:pfam04375  81 LAEQVDNLPLADNNFDESPMDADNAELSDSVSDWRQNLEKSAKSFMSHFIRIRRRDQSIKPLLAPNQDIYLRENIRLRLE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513459651 294 VAAQAVPRHQEETYKQALDNVSTWVRAYYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNL 369
Cdd:pfam04375 161 IAILAVPRQQNEVYKQSLETVQTWVRAYFDTDDPATQAFLKELDELAEQPISVDVPDQLQSLPALEKLLNRRVRSL 236
HemX COG2959
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ...
56-370 2.17e-117

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: 345.80  E-value: 2.17e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651  56 GVGLYGLVKQQGANQTSTSDALVNQLTALQ---KAQETQKTELETVIKQQAAALAEANSKQEELAKQLGDVQQKVATISG 132
Cdd:COG2959    44 GGGGYYLGWQQLQQQQAELAQLAQQLAALQqqaQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQQLLQSLSG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 133 TDAKTWLLSQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVN 212
Cdd:COG2959   124 SSRDDWLLAEAEYLLRLAGQQLQLEGDVKTALAALQSADARLARLNDPSLLPVRRAIARDIARLRAVPQVDIDGIALRLD 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 213 QLSNQIDNLQLADNNDDDSPMDSDGTELSSSLSEWRINL-QKSWQNfMDSFITIRRRDETAVPLLAPNQDIYLRENIRSR 291
Cdd:COG2959   204 ALANQVDNLPLASDVAPAAAPAAAAAEASASISDWQQNLwEKSWDE-LRDLVRIRRRDQPVAPLLSPEQAFFLRENLRLR 282
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513459651 292 LLVAAQAVPRHQEETYKQALDNVSTWVRAYYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNLL 370
Cdd:COG2959   283 LLNARLALLRRQEELYQQSLAAAQTWLRRYFDTDSPATQAFLAELDQLQAQSISVELPDILESLAALRKLLAQRVRALL 361
 
Name Accession Description Interval E-value
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
1-398 0e+00

putative uroporphyrinogen III C-methyltransferase; Provisional


Pssm-ID: 236795  Cd Length: 390  Bit Score: 607.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651   1 MTEHDKSSAVVEETRETVETTPQPETTEKTAEKKNGsnktsLALSAIAIAIALAAGVGLYGLVKQQGANQTSTSDALVNQ 80
Cdd:PRK10920    1 MTEQEKSSAVVEETREAVETTSQPVATEKKSKNRTG-----LVLSAVAIAIALAAGAGLYYHGKQQAQNQTATNDALANQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651  81 LTALQKAQETQKTELETVIKQQAAALAEANSKQEELAKQLGDVQQKVATISGTDAKTWLLSQADFLVKLAGRKLWSDQDV 160
Cdd:PRK10920   76 LTALQKAQESQKQELEGILKQQAKALDQANRQQAALAKQLDELQQKVATISGSDAKTWLLAQADFLVKLAGRKLWSDQDV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 161 TTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVNQLSNQIDNLQLADNNDDDSPMDSDGTEL 240
Cdd:PRK10920  156 TTAAALLKSADASLADMNDPSLITVRRAITDDIATLSAVSQVDYDGIILKLNQLSNQVDNLRLADNDSDGSPMDSDSEEL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 241 SSSLSEWRINLQKSWQNFMDSFITIRRRDETAVPLLAPNQDIYLRENIRSRLLVAAQAVPRHQEETYKQALDNVSTWVRA 320
Cdd:PRK10920  236 SSSLSEWRQNLSKSWHNFMDNFITIRRRDDTAEPLLAPNQDVYLRENIRSRLLVAAQAVPRHQEETYKQSLENVSTWVRA 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1513459651 321 YYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNLLAQPGVPAEPTDgaaPAPAPAPESAPQGE 398
Cdd:PRK10920  316 YFDTDDATTKAFLDEVDQLSQQNISMDLPETLQSQPILEKLMQTRVRNLLAQPAAGATEAK---APQADAPAAAPQGE 390
HemX pfam04375
HemX, putative uroporphyrinogen-III C-methyltransferase; This is a family of bacterial ...
134-369 1.47e-122

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: 354.34  E-value: 1.47e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 134 DAKTWLLSQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVNQ 213
Cdd:pfam04375   1 DRKDWLLAEADFLLKLAGRKLWLDQDVDTALALLKGADAVLAEQNDPSLIAVRRAIARDIEALRAVPQVDRDGIILRLNQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 214 LSNQIDNLQLADNNDDDSPMDSDGTELSSSLSEWRINLQKSWQNFMDSFITIRRRDETAVPLLAPNQDIYLRENIRSRLL 293
Cdd:pfam04375  81 LAEQVDNLPLADNNFDESPMDADNAELSDSVSDWRQNLEKSAKSFMSHFIRIRRRDQSIKPLLAPNQDIYLRENIRLRLE 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1513459651 294 VAAQAVPRHQEETYKQALDNVSTWVRAYYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNL 369
Cdd:pfam04375 161 IAILAVPRQQNEVYKQSLETVQTWVRAYFDTDDPATQAFLKELDELAEQPISVDVPDQLQSLPALEKLLNRRVRSL 236
HemX COG2959
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ...
56-370 2.17e-117

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: 345.80  E-value: 2.17e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651  56 GVGLYGLVKQQGANQTSTSDALVNQLTALQ---KAQETQKTELETVIKQQAAALAEANSKQEELAKQLGDVQQKVATISG 132
Cdd:COG2959    44 GGGGYYLGWQQLQQQQAELAQLAQQLAALQqqaQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQQLLQSLSG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 133 TDAKTWLLSQADFLVKLAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVN 212
Cdd:COG2959   124 SSRDDWLLAEAEYLLRLAGQQLQLEGDVKTALAALQSADARLARLNDPSLLPVRRAIARDIARLRAVPQVDIDGIALRLD 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 213 QLSNQIDNLQLADNNDDDSPMDSDGTELSSSLSEWRINL-QKSWQNfMDSFITIRRRDETAVPLLAPNQDIYLRENIRSR 291
Cdd:COG2959   204 ALANQVDNLPLASDVAPAAAPAAAAAEASASISDWQQNLwEKSWDE-LRDLVRIRRRDQPVAPLLSPEQAFFLRENLRLR 282
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1513459651 292 LLVAAQAVPRHQEETYKQALDNVSTWVRAYYNTDDATTTAFLEDIDKLSQQNITMNVPDKLASQPILEKLMQTRVRNLL 370
Cdd:COG2959   283 LLNARLALLRRQEELYQQSLAAAQTWLRRYFDTDSPATQAFLAELDQLQAQSISVELPDILESLAALRKLLAQRVRALL 361
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
75-350 2.02e-25

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 108.27  E-value: 2.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651  75 DALVNQLTALQKAQETQKTELETVIKQQAAALAEANSKQEELAKQLGDVQQKVATISGTDAK------TWLLSQADFLVK 148
Cdd:PRK06975  349 DRLDQELVQRQQANDAQTAELRVKTEQAQASVHQLDSQFAQLDGKLADAQSAQQALEQQYQDlsrnrdDWMIAEVEQMLS 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 149 LAGRKLWSDQDVTTAAALLKSADASLADMNDPSLITARRAITEDIASLSAVSQVDYDGIILKVNQLSNQIDNLQLADN-- 226
Cdd:PRK06975  429 SASQQLQLTGNVQLALIALQNADARLATSDSPQAVAVRKAIAQDIERLKAAPSADLTGLAIKLDDAIAKIDALPLSGEal 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1513459651 227 --NDDDSPMDSDGTELSSSLSE-----WRINLQKSWQNFMD---SFITIRRRDETAVPLLAPNQDIYLRENIRSRLLVAA 296
Cdd:PRK06975  509 ppHATMAAAPAAAAAAAAAAAAageprWKAWWRRFSAGVGEqlkQLVQVRRIDNADAMLLSPDQGYFLRENLKLRLLNAR 588
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1513459651 297 QAVPRHQEETYKQALDNVSTWVRAYYNTDDATTTAFLEDIDKLSQQNITMNVPD 350
Cdd:PRK06975  589 LSLLSRNDAAFKSDLHAAQAALARYFDTASKDTQTVQDLLKQVDAASLTVAVPN 642
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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