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Conserved domains on  [gi|2049544817|gb|QWH29241|]
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antibiotic biosynthesis monooxygenase [Bacillus mycoides]

Protein Classification

antibiotic biosynthesis monooxygenase family protein( domain architecture ID 10006366)

antibiotic biosynthesis monooxygenase family protein may be involved in the biosynthesis of several antibiotics; similar to Streptomyces tetracenomycin-F1 monooxygenase and deoxynogalonate monooxygenase

CATH:  3.30.70.100
EC:  1.-.-.-
Gene Ontology:  GO:0004497|GO:0017000|GO:0016491
PubMed:  31399587
SCOP:  4001439

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
HmoA COG2329
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ...
1-80 2.33e-15

Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism];


:

Pssm-ID: 441901  Cd Length: 98  Bit Score: 65.40  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTG-EGIIEKFEGFIDLSVLvkKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGHRAG 79
Cdd:COG2329     1 MIVVINRFRVKPGQEEEFEEAFAErRELLAEQPGFLGFELL--RSLEDPGEYLVVSYWESEEAFRAWFRSSEHRAAHAKG 78

                  .
gi 2049544817  80 R 80
Cdd:COG2329    79 R 79
 
Name Accession Description Interval E-value
HmoA COG2329
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ...
1-80 2.33e-15

Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism];


Pssm-ID: 441901  Cd Length: 98  Bit Score: 65.40  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTG-EGIIEKFEGFIDLSVLvkKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGHRAG 79
Cdd:COG2329     1 MIVVINRFRVKPGQEEEFEEAFAErRELLAEQPGFLGFELL--RSLEDPGEYLVVSYWESEEAFRAWFRSSEHRAAHAKG 78

                  .
gi 2049544817  80 R 80
Cdd:COG2329    79 R 79
PRK13315 PRK13315
heme oxygenase;
1-104 1.33e-11

heme oxygenase;


Pssm-ID: 237345  Cd Length: 107  Bit Score: 56.34  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTGEGIIEKFEGFIDLSVLVKKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGH-RAG 79
Cdd:PRK13315    1 MIVVTNRITVKKGFAAKMAPRFTKGGPLEELEGFHKVEVWLIDNDDEYDEMYVNMWWETEEDFEAWRNSDAFKEAHkRPS 80
                          90       100
                  ....*....|....*....|....*
gi 2049544817  80 RGKPKPDHIIKVEHGVYYVKSSKSA 104
Cdd:PRK13315   81 KTESDDSPIIGSEIVKSEVLSSLER 105
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
2-76 1.68e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 49.96  E-value: 1.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049544817   2 FIETKTFTVKEGTSNIVVERFTGE-GIIEKFEGFIDLSVLVKkvRRGDEEVVVMIRWESEEAWKNWETSEEHLAGH 76
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELvEATRNEPGCLSYELLRS--LEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
 
Name Accession Description Interval E-value
HmoA COG2329
Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and ...
1-80 2.33e-15

Heme-degrading monooxygenase HmoA and related ABM domain proteins [Coenzyme transport and metabolism];


Pssm-ID: 441901  Cd Length: 98  Bit Score: 65.40  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTG-EGIIEKFEGFIDLSVLvkKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGHRAG 79
Cdd:COG2329     1 MIVVINRFRVKPGQEEEFEEAFAErRELLAEQPGFLGFELL--RSLEDPGEYLVVSYWESEEAFRAWFRSSEHRAAHAKG 78

                  .
gi 2049544817  80 R 80
Cdd:COG2329    79 R 79
PRK13315 PRK13315
heme oxygenase;
1-104 1.33e-11

heme oxygenase;


Pssm-ID: 237345  Cd Length: 107  Bit Score: 56.34  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTGEGIIEKFEGFIDLSVLVKKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGH-RAG 79
Cdd:PRK13315    1 MIVVTNRITVKKGFAAKMAPRFTKGGPLEELEGFHKVEVWLIDNDDEYDEMYVNMWWETEEDFEAWRNSDAFKEAHkRPS 80
                          90       100
                  ....*....|....*....|....*
gi 2049544817  80 RGKPKPDHIIKVEHGVYYVKSSKSA 104
Cdd:PRK13315   81 KTESDDSPIIGSEIVKSEVLSSLER 105
PRK13314 PRK13314
heme oxygenase;
1-99 2.16e-10

heme oxygenase;


Pssm-ID: 183969  Cd Length: 107  Bit Score: 52.96  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTGEGIIEKFEGFIDLSVLVKKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGHrAGR 80
Cdd:PRK13314    1 MIIVTNTAKITKGNGHKLIDRFNKVGKVETMPGFLGLEVLLTQNTVDYDEVTISTRWNAKEDFQGWTKSPAFKAAH-SHQ 79
                          90
                  ....*....|....*....
gi 2049544817  81 GKpKPDHIIKVEHGVYYVK 99
Cdd:PRK13314   80 GG-MPDYILDNKISYYDVK 97
ABM pfam03992
Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the ...
2-76 1.68e-09

Antibiotic biosynthesis monooxygenase; This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.


Pssm-ID: 427635  Cd Length: 74  Bit Score: 49.96  E-value: 1.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2049544817   2 FIETKTFTVKEGTSNIVVERFTGE-GIIEKFEGFIDLSVLVKkvRRGDEEVVVMIRWESEEAWKNWETSEEHLAGH 76
Cdd:pfam03992   1 IVVVAEIRVKPGKAEEFEEALAELvEATRNEPGCLSYELLRS--LEDPDEYVVLEVWEDEAAFEAHLQSPHFKAAH 74
PRK13316 PRK13316
heme oxygenase IsdG;
1-82 7.74e-07

heme oxygenase IsdG;


Pssm-ID: 183970  Cd Length: 121  Bit Score: 44.36  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTGEG-------IIEKFEGFIDLSVLVKKVRRGD-EEVVVMIRWESEEAWKNWETSEEH 72
Cdd:PRK13316    1 MIIVTNTIKVEKGAAEHVIRQFTGANgdghptkDIAEVEGFLGFELWHSKPEDKDyEEVVVTSKWESEEAQRNWVKSDSF 80
                          90
                  ....*....|
gi 2049544817  73 LAGHraGRGK 82
Cdd:PRK13316   81 KKAH--GRTK 88
PRK13313 PRK13313
staphylobilin-forming heme oxygenase IsdI;
1-99 2.10e-06

staphylobilin-forming heme oxygenase IsdI;


Pssm-ID: 183968  Cd Length: 108  Bit Score: 42.62  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   1 MFIETKTFTVKEGTSNIVVERFTGEGIIEKFEGFIDLSVLVKKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGHRAGR 80
Cdd:PRK13313    1 MFMAENRLQLQKGSAEETIERFYNRQGIETIEGFQQMFVTKTLNTEDTDEVKILTIWESEDSFNNWLNSDVFKEAHKNVR 80
                          90       100
                  ....*....|....*....|....*...
gi 2049544817  81 GKPKPDH---------IIKVEHGVYYVK 99
Cdd:PRK13313   81 LKSDDDGqqspilsnkVFKYDIGYHYQK 108
PRK13312 PRK13312
staphylobilin-forming heme oxygenase IsdG;
2-82 3.00e-05

staphylobilin-forming heme oxygenase IsdG;


Pssm-ID: 139480  Cd Length: 107  Bit Score: 39.71  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049544817   2 FIETKTFTVKEGTSNIVVERFTGEGIIEKFEGFIDLSVLVKKVRRGDEEVVVMIRWESEEAWKNWETSEEHLAGHRAGRG 81
Cdd:PRK13312    3 FMAENRLTLTKGTAKDIIERFYTRHGIETLEGFDGMFVTQTLEQEDFDEVKILTVWKSKQAFTDWLKSDVFKAAHKHVRS 82

                  .
gi 2049544817  82 K 82
Cdd:PRK13312   83 K 83
COG3224 COG3224
Antibiotic biosynthesis monooxygenase (ABM) superfamily enzyme [General function prediction ...
29-71 1.41e-03

Antibiotic biosynthesis monooxygenase (ABM) superfamily enzyme [General function prediction only];


Pssm-ID: 442457  Cd Length: 183  Bit Score: 36.04  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2049544817  29 EKFEGFIDLSVLvkKVRRGDEEVVVMIRWESEEAWKNWETSEE 71
Cdd:COG3224    35 ARFPGFLGVGVI--RPSGGSDEWVILLRFDSEENLDAWLESPE 75
 
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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