Fred_00020 Fred_00020   Fred_00040 Fred_00040

Fred_00030 : CDS information

close this sectionLocation

Organism
StrainATCC 49344
Entry nameFredericamycin
Contig
Start / Stop / Direction4,920 / 2,731 / - [in whole cluster]
4,920 / 2,731 / - [in contig]
Locationcomplement(2731..4920) [in whole cluster]
complement(2731..4920) [in contig]
TypeCDS
Length2,190 bp (729 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative multicopper oxidase
Product (GenBank)putative multicopper oxidase
Gene
Gene (GenBank)
EC number
Keyword
Note
  • This ORF is not involved in fredericamycins biosynthesis.
Note (GenBank)
  • Orf3
Reference
ACC
PmId
[16305230] Cloning, sequencing, analysis, and heterologous expression of the fredericamycin biosynthetic gene cluster from Streptomyces griseus. (J Am Chem Soc. , 2005)
comment
Fredericamycin(FDM) gene clusterの同定論文。

Orf3は、Mn(II)-oxidation-associated multicopper oxidaseとして知られるCumA(id26%)や、dihydrogeodin→geodinへの変換を担うdihydrogeodin oxidaseであるDHGO(id41%)に似ている。

fdm clusterの境界決定のため、orf1, 3, 33を遺伝子置換により不活化。
これらのmutantはFDM-A産生にあまり影響しない。
さらにこれらのgenesを除外したfdmC-fdmT3のfragmentをS.albusへ導入し、FDM-A産生に十分であることを確認している。
Related Reference
ACC
Q68UP9
PmId
[15293032] A cloned Bacillus halodurans multicopper oxidase exhibiting alkaline laccase activity. (Appl Microbiol Biotechnol. , 2004)
comment
Blast 88th, 31%, 2e-51, N末200aa以上余る。
Bacillus halodurans_lbh1
Alkaline laccase(EC 1.10.3.2)

Bacillus haloduransのmulticopper oxidaseがalkaline laccase activity(2,2'-azino-bis(3-ethylbenz-thiazoline-6-sulfonic acid), 2,6-dimethoxyphenol and syringaldazine (SGZ)の酸化)を示した。
ACC
Q9X3V2
PmId
[10103278] cumA, a gene encoding a multicopper oxidase, is involved in Mn2+ oxidation in Pseudomonas putida GB-1. (Appl Environ Microbiol. , 1999)
comment
Blast 137th, id30%, 2e-34, N末200aa以上余る。
Pseudomonas putida_cumA
CumA

Pseudomonas putida CumA_cumA nonoxidizing mutantの原因遺伝子としてmulticopper oxidaseをコードするcumAを同定。 Cu2+の添加により、Mn2+-oxidizing activityが上昇することを確認している。

close this sectionSequence

selected fasta
>putative multicopper oxidase [putative multicopper oxidase]
MVENLFEQNILWAVLTAVVWGCAARGARRLAIRPAAALRRRARLGLALLTVALLTLAVRA
GLALGLVATAGWLGGADYVLFGALPPVLAAVAVAALAVPAYLRVLRAAPAAGSDPDGSPL
PPGLRALAAGDRLVVPVQACCATTLLGAAGTLHPPAPPYTGPFLVHILLGGAVCGGLLLL
HRRRRAALEARGGRPVPRARQLVRATATVTGLAVLTAGGCTLAAGQSRLPDRTSASAHAH
SGTAPTRSVVDLTGDRSGEPDRRFTLTATDRTLRLASGEKVAALSFNNSLPGPELRVRRG
QLVEVVLVNRDVADGVTLHWHGVDVPNAEDGVAGVTQDAVPPGGHHVYRFRPDRAGTFWY
HSHQQSSIAVARGLFGALVVEEPSKDQRAPFDRTVVAHAWPVGTARNSPGGPHGGGALSG
TNGLGGTLRTAFGDDTRTRAEKVRAGTEVRLRLVNADNCPRTYSLAGTSFAVAAIDGTEV
QGASEVRGRLLRVAGGGRYDLTYRQPDGPVRLTVVGDANASADGQGFEGCGQDGAYGTGR
TETASLQLAPNPSAAGRVPAVSGPLFDPLHYGSAAGAGPLGRSPRFDRDFSLVLGNSLGF
HDGSPMVLWTVNNAVHPDIPALVVEEGDLVRTTFLNRSLDDHPMHLHGHRMLVLSRDGEP
ATGSPWWTDTLNVAPGERYEVAFRSDNPGLWMDHCHNLDHARDGMVLHLAYDGVTGPYES
GSSTGNVPE
selected fasta
>putative multicopper oxidase [putative multicopper oxidase]
ATGGTGGAGAACCTCTTCGAACAGAACATCCTCTGGGCCGTGTTGACGGCCGTCGTCTGG
GGGTGCGCGGCACGCGGGGCCAGACGGCTGGCCATCCGCCCCGCCGCCGCGCTCCGGCGC
CGGGCGCGGCTCGGACTGGCCTTGCTCACGGTCGCCCTGCTGACCCTGGCCGTCCGGGCA
GGCCTCGCCCTCGGGCTCGTCGCCACCGCCGGCTGGCTCGGGGGCGCGGACTACGTGCTG
TTCGGCGCGCTGCCCCCGGTCCTCGCCGCCGTCGCGGTGGCGGCACTGGCCGTTCCCGCG
TACCTGCGCGTCCTGCGCGCGGCACCGGCGGCCGGGTCGGACCCGGACGGCTCGCCGCTC
CCGCCCGGCCTGCGGGCGCTCGCCGCGGGCGACCGCCTCGTGGTCCCGGTACAGGCGTGC
TGCGCGACGACGCTGCTCGGAGCCGCGGGCACGCTGCACCCGCCGGCACCGCCGTACACC
GGCCCGTTCCTCGTCCACATCCTGCTGGGCGGCGCCGTCTGCGGTGGCCTGCTCCTGCTC
CACCGGCGCCGCCGGGCCGCCCTGGAGGCTCGTGGCGGACGGCCCGTCCCGCGTGCGCGG
CAGCTGGTGCGGGCCACCGCGACGGTCACCGGGCTCGCCGTCCTCACCGCCGGCGGCTGC
ACGCTCGCCGCCGGACAGAGCCGGCTGCCCGACCGGACCAGTGCCTCGGCGCACGCGCAC
TCCGGGACCGCCCCCACCCGCTCGGTCGTCGACCTGACCGGTGACCGCTCCGGTGAACCG
GACCGGCGGTTCACCCTCACGGCGACCGACCGCACCCTGCGCCTGGCGTCCGGCGAGAAG
GTGGCCGCCCTGTCCTTCAACAACAGCCTCCCCGGACCGGAGCTACGGGTCAGGCGCGGC
CAGCTGGTGGAGGTGGTGCTGGTCAACCGCGACGTGGCGGACGGCGTCACCCTGCACTGG
CACGGCGTCGACGTCCCCAACGCCGAGGACGGCGTGGCCGGGGTCACCCAGGACGCCGTC
CCGCCCGGAGGGCACCACGTGTACCGCTTCCGCCCCGACCGGGCCGGCACCTTCTGGTAC
CACTCCCACCAGCAGTCGAGCATCGCCGTGGCGCGCGGCCTGTTCGGGGCGCTGGTGGTC
GAGGAACCGTCGAAGGACCAACGGGCGCCGTTCGACCGGACCGTGGTCGCGCACGCCTGG
CCCGTGGGGACGGCCCGGAACTCCCCGGGCGGGCCGCACGGCGGCGGTGCCCTGAGCGGC
ACCAACGGCCTCGGCGGCACCCTGCGTACCGCCTTCGGCGACGACACGCGCACCCGCGCG
GAGAAGGTCCGGGCCGGGACCGAGGTGCGGCTGCGCCTGGTCAACGCGGACAACTGCCCG
CGTACGTACTCCCTCGCGGGGACCTCCTTCGCGGTCGCGGCGATCGACGGCACCGAAGTC
CAGGGAGCCTCCGAGGTGCGCGGCCGGCTGCTGAGGGTGGCGGGCGGCGGCCGGTACGAC
CTCACCTACCGTCAGCCGGACGGCCCGGTCCGGCTGACGGTCGTCGGCGACGCCAACGCC
TCCGCCGACGGCCAGGGCTTCGAGGGGTGCGGGCAGGACGGCGCCTACGGAACGGGCCGC
ACCGAGACCGCGTCCCTGCAGCTCGCCCCGAACCCCTCGGCCGCCGGCCGGGTCCCCGCC
GTCAGCGGGCCGCTCTTCGACCCGCTGCACTACGGCTCGGCGGCCGGCGCCGGTCCGCTC
GGCCGGTCCCCACGGTTCGACCGCGACTTCTCCCTGGTCCTCGGCAACAGCCTCGGCTTC
CACGACGGCAGCCCCATGGTGCTGTGGACCGTCAACAACGCGGTCCACCCCGACATCCCG
GCCCTCGTCGTCGAGGAGGGCGACCTGGTGCGCACGACCTTCCTCAACCGGAGCCTGGAC
GACCACCCGATGCATCTGCACGGCCACCGCATGCTCGTGCTGTCCAGGGACGGCGAACCG
GCCACCGGCAGCCCGTGGTGGACCGACACCCTCAACGTCGCCCCCGGCGAGCGCTACGAG
GTGGCCTTCCGTTCCGACAACCCCGGCCTGTGGATGGACCACTGCCACAATCTCGACCAC
GCACGCGACGGCATGGTGCTGCACCTCGCGTACGACGGCGTGACCGGCCCCTACGAGAGC
GGGAGCTCCACCGGCAACGTTCCGGAGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR002355 Multicopper oxidase, copper-binding site (Binding_site)
[694-705] PS00080
PS00080   MULTICOPPER_OXIDASE2
IPR008972 Cupredoxin (Domain)
[227-388] 4.39999001237725e-38 SSF49503 [584-714] 8.5000302480906e-34 SSF49503
SSF49503   Cupredoxin
[252-382] 4.70000000000003e-63 G3DSA:2.60.40.420 [436-503] 1.40000000000001e-61 G3DSA:2.60.40.420 [604-718] 1.40000000000001e-61 G3DSA:2.60.40.420
G3DSA:2.60.40.420   Cupredoxin
IPR011706 Multicopper oxidase, type 2 (Domain)
[612-710] 6.79999999999998e-25 PF07731
PF07731   Cu-oxidase_2
IPR011707 Multicopper oxidase, type 3 (Domain)
[270-384] 9.40000000000003e-31 PF07732
PF07732   Cu-oxidase_3
SignalP
[1-37] 0.361 Signal
Bacteria, Gram-positive   
[1-63] 0.867 Signal
Eukaryota   
TMHMM
[10-27] Transmembrane (o-i) [48-70] Transmembrane (i-o) [80-102] Transmembrane (o-i) [133-152] Transmembrane (i-o) [162-181] Transmembrane (o-i) [202-224] Transmembrane (i-o)
Transmembrane 6   
Fred_00020 Fred_00020   Fred_00040 Fred_00040
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