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Conserved domains on  [gi|491296480|ref|WP_005154494|]
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MULTISPECIES: oxygenase MpaB family protein [unclassified Acinetobacter]

Protein Classification

oxygenase MpaB family protein( domain architecture ID 10561995)

oxygenase MpaB family protein similar to Penicillium ER-bound oxygenase mpaB/mpaB', which is part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), and Streptomyces rubber oxygenase

EC:  1.-.-.-
Gene Ontology:  GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPAB_Lcp_cat pfam09995
ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain; This is the catalytic domain ...
 132-357 3.42e-18

ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain; This is the catalytic domain found in the endoplasmic reticulum (ER) -bound oxygenases mpaB' (MPAB2) and mpaB (MPAB) from Penicillium roqueforti and Penicillium brevicompactum and in the rubber oxygenase (Lcp) from Streptomyces sp., which contains highly conserved arginine and histidine residues. Structural analysis from Lcp revealed that Arg164, Thr168 and His198 are crucial active site residues. The mpaB and mpaB' are part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA). Lcp (Latex clearing proteins) is a rubber oxygenase that catalyzes the extracellular cleavage of poly (cis-1,4-isoprene). This domain is also present in uncharacterized proteins from Mycobacterium sp. and hypothetical proteins, mainly from bacteria and fungi.


:

Pssm-ID: 462938  Cd Length: 223  Bit Score: 82.74  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491296480  132 SLMAGYMypGFNQPLVLTGA-----LKKQAGTRLAETTKWWVDITEQDGFErfskGFTSTIFVRFIHALVRHQLQKSEKW 206
Cdd:pfam09995  14 GLRALLL--QAAHPLVGAGVadhsnFRTDPWGRLRRTLTYVATVTFGTGEE----AEALAERVRRMHARVRGTDDSGRRY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491296480  207 DAetwglpINQYDQAMTNIAFSGVVLIGIRALGIFPSKQEVDSFLHFWKYAGWLMGVEEKWLVDHEADGWKLIYWMQFAH 286
Cdd:pfam09995  88 SA------LDPELLLWVHATLYASFLDAYERFGGPLTDAEADRYYAEWRRLGRLLGVPPRDWPATRAEFWAYWDDMLRPE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491296480  287 PQSDASSislgsslskepfeRKYRYLRSFQQKLAYKQHLEITQFFIGRKKMQKLGLAPQSASWFAYYLIGR 357
Cdd:pfam09995 162 LEVTPEA-------------RELAPVRFLPARPAGRLLRALTVGLLPPWARELLGLPWTARDRRRLRALAR 219
 
Name Accession Description Interval E-value
MPAB_Lcp_cat pfam09995
ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain; This is the catalytic domain ...
 132-357 3.42e-18

ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain; This is the catalytic domain found in the endoplasmic reticulum (ER) -bound oxygenases mpaB' (MPAB2) and mpaB (MPAB) from Penicillium roqueforti and Penicillium brevicompactum and in the rubber oxygenase (Lcp) from Streptomyces sp., which contains highly conserved arginine and histidine residues. Structural analysis from Lcp revealed that Arg164, Thr168 and His198 are crucial active site residues. The mpaB and mpaB' are part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA). Lcp (Latex clearing proteins) is a rubber oxygenase that catalyzes the extracellular cleavage of poly (cis-1,4-isoprene). This domain is also present in uncharacterized proteins from Mycobacterium sp. and hypothetical proteins, mainly from bacteria and fungi.


Pssm-ID: 462938  Cd Length: 223  Bit Score: 82.74  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491296480  132 SLMAGYMypGFNQPLVLTGA-----LKKQAGTRLAETTKWWVDITEQDGFErfskGFTSTIFVRFIHALVRHQLQKSEKW 206
Cdd:pfam09995  14 GLRALLL--QAAHPLVGAGVadhsnFRTDPWGRLRRTLTYVATVTFGTGEE----AEALAERVRRMHARVRGTDDSGRRY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491296480  207 DAetwglpINQYDQAMTNIAFSGVVLIGIRALGIFPSKQEVDSFLHFWKYAGWLMGVEEKWLVDHEADGWKLIYWMQFAH 286
Cdd:pfam09995  88 SA------LDPELLLWVHATLYASFLDAYERFGGPLTDAEADRYYAEWRRLGRLLGVPPRDWPATRAEFWAYWDDMLRPE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491296480  287 PQSDASSislgsslskepfeRKYRYLRSFQQKLAYKQHLEITQFFIGRKKMQKLGLAPQSASWFAYYLIGR 357
Cdd:pfam09995 162 LEVTPEA-------------RELAPVRFLPARPAGRLLRALTVGLLPPWARELLGLPWTARDRRRLRALAR 219
 
Name Accession Description Interval E-value
MPAB_Lcp_cat pfam09995
ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain; This is the catalytic domain ...
 132-357 3.42e-18

ER-bound oxygenase mpaB/B'/Rubber oxygenase, catalytic domain; This is the catalytic domain found in the endoplasmic reticulum (ER) -bound oxygenases mpaB' (MPAB2) and mpaB (MPAB) from Penicillium roqueforti and Penicillium brevicompactum and in the rubber oxygenase (Lcp) from Streptomyces sp., which contains highly conserved arginine and histidine residues. Structural analysis from Lcp revealed that Arg164, Thr168 and His198 are crucial active site residues. The mpaB and mpaB' are part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA). Lcp (Latex clearing proteins) is a rubber oxygenase that catalyzes the extracellular cleavage of poly (cis-1,4-isoprene). This domain is also present in uncharacterized proteins from Mycobacterium sp. and hypothetical proteins, mainly from bacteria and fungi.


Pssm-ID: 462938  Cd Length: 223  Bit Score: 82.74  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491296480  132 SLMAGYMypGFNQPLVLTGA-----LKKQAGTRLAETTKWWVDITEQDGFErfskGFTSTIFVRFIHALVRHQLQKSEKW 206
Cdd:pfam09995  14 GLRALLL--QAAHPLVGAGVadhsnFRTDPWGRLRRTLTYVATVTFGTGEE----AEALAERVRRMHARVRGTDDSGRRY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491296480  207 DAetwglpINQYDQAMTNIAFSGVVLIGIRALGIFPSKQEVDSFLHFWKYAGWLMGVEEKWLVDHEADGWKLIYWMQFAH 286
Cdd:pfam09995  88 SA------LDPELLLWVHATLYASFLDAYERFGGPLTDAEADRYYAEWRRLGRLLGVPPRDWPATRAEFWAYWDDMLRPE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491296480  287 PQSDASSislgsslskepfeRKYRYLRSFQQKLAYKQHLEITQFFIGRKKMQKLGLAPQSASWFAYYLIGR 357
Cdd:pfam09995 162 LEVTPEA-------------RELAPVRFLPARPAGRLLRALTVGLLPPWARELLGLPWTARDRRRLRALAR 219
 
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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